Prions: The beginning of our awareness.
INDEX
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747681/
Osong Public Health Res Perspect. 2013 Feb; 4(1): 57–66.
Jeongmin Lee, Su Yeon Kim, Kyu Jam Hwang,
Young Ran Ju, and Hee-Jong Wooa
2013 Feb 4
World Organization for Animal Health (Office International des Epizooties; OIE)
specific risk material (SRM)
Considering that the prevalence of BSE in the United Kingdom (UK) has much to do with sheep farming, this new cross-species epidemic appears to be related to the current conditions involving
- frequent human contact with animals,
- enlarged livestock markets,
- increasing interchange/trade, and
- global warming.
... many problems remain from both social and preventive medical perspectives since TSEs can spread through food and blood transfusions with very low concentrations of pathogenic prions, which current technologies cannot detect. In addition, since they have long incubation periods similar to other degenerative chronic diseases, more scientific investigations must be performed to identify the overall pathogeneses of BSE and vCJD, and to develop treatment strategies for them. ...
Prions, which were first proposed by Dr Prusiner at the University of California, San Francisco, became a hot topic since they do not have genes, unlike bacteria or viruses, and are able to replicate, unlike toxic elements. Eventually, he scientifically answered a number of questions and suggested that these gene-less proteins can replicate in the body, induce the disease, and be subsequently transmitted to other animals; he received a Nobel Prize for his work in 1997. This type of prion-only hypothesis is recognized as a new pathogenic mechanism of neurodegenerative disorders.
... Unlike bacteria or viruses, pathogenic PrPSc cannot be removed by regular alcohol or formalin sterilization processes, and cannot be decomposed by proteolytic enzymes. Moreover, it is resistant to heat, ultraviolet rays, and chemicals.
PrPSc (prion disease structures) in infected animals is concentrated in specific areas.
These areas are called specific risk material (SRM) and include the brain, eyes, spinal cord, skull, vertebral column, tonsils, and distal ileum; these are the most crucial areas for disease management and control. The disease is transmittable via surgical tools that came into contact with SRM and via blood transfusion. ... The amount required to induce the disease is very small; a scientific report submitted to the British Council in 2001 states that an amount as small as one speck of pepper may cause the disease. ... It is noteworthy that Payer’s patch tissue, which is the most essential factor for PrPSc absorption, is mostly on the ileum in humans; however, similar tissues are predominantly found in the whole intestine including mesentery in cattle.
Prion illnesses represent a parallel with past pandemics.
- they are sourced from a singular competitive commerce food commodity (sheep),
- mutation enhancing practices have been dominant in that industry for many decades,
- commercial products which can host such sources are transported globally,
- they will be endemic and multiple before efficient & effective testing is devised,
- they can appear harmless in a long undetected, untreatable incubation period,
- they are resistant to all common disease controls: chemicals, radiation, fire,
- they often multiply in form by mutation within hosts making detection more difficult,
- Their means of contagion will be denied until a majority of persons are infected.
By the time past recorded pandemics (of LESS virulent, LESS mutationally unstable, and MORE controllable) diminished, as much as 60% of the population were fatal victims. Like in the earlier instances, public awareness and political concern continues to be distracted by other human created urgencies, even though as many as a conservative estimate of 40% of some national populations may already be infected. Each time a large area pandemic has been recorded, the pathogen was a common lifeform developed by mutation in a commerce involving live animals in which a mutation provided an ability for it to transfer to a human host. This time, international travel and international commerce have amplified previous risks of contagion spread by more than 10,000% of the last pandemic.
With the potential decades long incubation period of the few currently (2019-06) defined prion diseases and the potential decades long palliative care responses currently undertaken ... national budgets, healthcare facilities, general levels of commerce, financial resources of individuals, and instigations of tribal/inter-group conflicts will increasingly be stressed to destructive levels of anarchy. This represents the first form of human species (previous examples have involved singular and localized cultures) Armageddon. This may become the wimpering variation of tragic death.
Prions: Diagnostic possibilities.
INDEX
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2851297/
A Case of Gerstmann-Sträussler-Scheinker Disease
Min Jeong Park, MD, Hee Young Jo, MD, Sang-Myung Cheon, MD,
Sun Seob Choi, MD, Yong-Sun Kim, MD, and Jae Woo Kim, MD
J Clin Neurol. 2010 Mar; 6(1): 46–50.
LINK 2: https://www.healthline.com/health/csf-analysis
Cerebrospinal fluid (CSF) analysis
LINK 3: https://www.healthline.com/health/csf-total-protein#complications
CSF protein test
LINK 4: https://www.invitae.com/en/physician/tests/03506/
Invitae Hereditary Prion Disease Test
LINK 5: GTR - Genetic Testing Registry
https://www.ncbi.nlm.nih.gov/gtr/conditions/C0017495/
LINK 6: NIND, NIH Factsheet.
https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/
Fact-Sheets/Creutzfeldt-Jakob-Disease-Fact-Sheet
Date last modified: Tue, 2019-05-14
Prepared by:
Office of Communications and Public Liaison
National Institute of Neurological Disorders and Stroke
National Institutes of Health
Bethesda, MD 20892
The physician’s first goal is to rule out other conditions that might be causing the dementia, especially because some causes of dementia are reversible, such as normal pressure hydrocephalus and vitamin B12 deficiency.
In general, the definitive diagnosis of a prion disease requires a brain biopsy or an autopsy with immunohistologic and genetic studies. Several ancillary tests are useful for this. EEG usually demonstrates generalized triphasic periodic sharp waves (PSW) in sporadic CJD. CSF (Cerebrospinal fluid) testing for the 14-3-3 protein can also be helpful. However, these methods are not sensitive for genetic TSE (transmissible spongiform encephalopathies).
Cerebrospinal fluid (CSF) analysis is a way of looking for conditions that affect your brain and spine.
It’s a series of laboratory tests performed on a sample of CSF.
CSF is the clear fluid that cushions and delivers nutrients to your central nervous system (CNS).
The CNS consists of the brain and spinal cord.
CSF is produced by the choroid plexus in the brain and then reabsorbed into your bloodstream.
The fluid is completely replaced every few hours. In addition to delivering nutrients, CSF flows around your brain and spinal column, providing protection and carrying away waste.
CSF is in direct contact with your brain and spine.
So CSF analysis is more effective than a blood test for understanding CNS symptoms.
However, it’s more difficult to obtain a spinal fluid sample than a blood sample. Entering the spinal canal with a needle requires expert knowledge of the spine’s anatomy and a clear understanding of any underlying brain or spinal conditions that might increase the risk of complications from the procedure.
People who take blood thinners have a heightened risk of bleeding.
Lumbar puncture is extremely dangerous for people who have clotting problems such as a low platelet count, which is called thrombocytopenia.
There are serious additional risks if you have a brain mass, tumor, or abscess.
These conditions put pressure on your brain stem. A lumbar puncture could then cause brain herniation to occur.
This can result in brain damage or even death.
Brain herniation is a shifting of structures of the brain. It’s usually accompanied by high intracranial pressure.
The condition eventually cuts off blood supply to your brain. This causes irreparable damage.
The test (is best avoided) if a brain mass is suspected.
Your doctor will order a CSF protein test if they suspect you have a central nervous system disease such as multiple sclerosis (MS) or an infectious condition such as meningitis. CSF protein tests are also helpful when looking for signs of injury, bleeding in the spinal fluid, or vasculitis. Vasculitis is another term for inflamed blood vessels.
High levels of protein in your CSF can also indicate:
- aseptic meningitis
- bacterial meningitis
- brain abscess
- brain tumor
- cerebral hemorrhage
- epilepsy
- neurosyphilis
Acute alcohol use disorder is another possible cause of high protein levels.
Different laboratories have different ranges they consider normal, which is due to the different ways each laboratory processes samples.
Electroencephalography (EEG), which records the brain’s electrical pattern, can be particularly valuable because it shows a specific type of abnormality in major but not all types of CJD.
Cerebrospinal fluid-based tests.
In April 2015, the National Prion Disease Pathology Surveillance Center began reporting a new diagnostic test for human prion diseases, called second generation Real Time-Quaking-Induced Conversion (RT-QuIC). RT-QuIC is based on an ultrasensitive detection of the pathogenic prion protein in the cerebrospinal fluid of individuals affected by CJD and other forms of human prion diseases. This new advanced test demonstrates a very high sensitivity and specificity of the disease. RT-QuIC differs from traditional surrogate markers of prion disease –14-3-3 and tau proteins -- in that it detects directly a disease-defining pathogenic prion protein as opposed to a surrogate marker of rapid neurodegeneration. Detection of these traditional surrogate marker proteins is accurate in approximately three-fourths of cases.
Magnetic resonance imaging (MRI) has recently been found to be accurate in about 90 percent of cases.
The only way to confirm a diagnosis of CJD is by brain biopsy or autopsy.
In a brain biopsy, a neurosurgeon removes a small piece of tissue from the person’s brain so that it can be examined by a neuropathologist. This procedure may be dangerous for the individual, and the operation does not always obtain tissue from the affected part of the brain. Because a correct diagnosis of CJD does not help the individual, a brain biopsy is discouraged unless it is needed to rule out a treatable disorder. In an autopsy, the whole brain is examined after death.
The Invitae Hereditary Prion Disease Test analyzes the PRNP gene, which is associated with a clinically heterogeneous spectrum of progressive neurodegenerative conditions characterized by dementia, ataxia, pyramidal and extrapyramidal features, sleep and sensory disturbances, and psychiatric manifestations. PRNP-related prion diseases include the genetic form of Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker syndrome, and fatal familial insomnia.
Individuals with clinical signs and symptoms of prion disease may benefit from diagnostic genetic testing to confirm the diagnosis, provide anticipatory guidance, and help determine which relatives are at risk.
In many cases, prion diseases have nonspecific or overlapping features with different types of dementia.
In these cases, clinicians may want to consider the Invitae Combined Dementia and Amyotrophic Lateral Sclerosis Panel, which includes genes associated with various forms of dementia (including early-onset Alzheimer’s disease and frontotemporal dementia), and ALS. Clinicians may also consider the Invitae Hereditary Parkinson’s Disease and Parkinsonism Panel, as there is some clinical overlap between prion disease and parkinsonism.
Prions: Structure, Transmission, Variability, Location.
INDEX
https://en.wikipedia.org/wiki/Prion
2019-05-25
Prions are misfolded proteins which characterize several fatal neurodegenerative diseases in humans and many other animals. It is not known what causes the normal protein to misfold; the abnormal three-dimensional structure is suspected of conferring infectious properties. The word prion derives from "proteinaceous infectious particle". Prions composed of the prion protein (PrP) are hypothesized (guessed to be) as the cause of transmissible spongiform encephalopathies (TSEs), including scrapie in sheep, chronic wasting disease (CWD) in deer, bovine spongiform encephalopathy (BSE) in cattle (commonly known as "mad cow disease"), and Creutzfeldt-Jakob disease (CJD) in humans.
A prion disease is a proteopathy.
In humans, prions are believed to be (NOT know definitively to be) the cause of Creutzfeldt–Jakob disease (CJD), its variant (vCJD), Gerstmann–Sträussler–Scheinker syndrome, fatal familial insomnia and kuru. All known prion diseases in mammals affect the structure of the brain or other neural tissue; all are progressive, have no known effective treatment and are always fatal. There is also evidence suggesting prions may play a part in the process of Alzheimer’s disease, and Parkinson's disease, and these have been termed prion-like diseases. Several yeast proteins have also been identified as having prionogenic properties.
The hypothesized role of a protein as an infectious agent stands in contrast to all other known infectious agents such as viruses, bacteria, fungi and parasites, all of which contain nucleic acids (DNA, RNA or both). Synthetic prions, created in the laboratory independent of any biological source, have little or no ability to cause infection with TSEs. However, when synthetic prions are administered in combination with cofactors, such as phosphatidylethanolamine and RNA molecules, then this can transmit TSEs.
Several scientific observations remain unexplained by the prion hypothesis:
It is known that mice with severe combined immunodeficiency do not develop scrapie following inoculation with brain tissue from animals infected with scrapie, suggesting that either the role of immunity in prion pathogenesis is incompletely understood or that there is some other flaw in current understanding of prion pathophysiology. More recently, it has been shown that scrapie and Creutzfeldt–Jakob disease may require agent-specific nucleic acids for transmission of infection. For these reasons, the prion/TSE hypothesis incompletely accounts for the observed data.
Prion aggregates are stable, accumulate in infected tissue and are associated with tissue damage and cell death.
This structural stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult. Prion structure varies slightly between species, but nonetheless prion replication is subject to epimutation and natural selection just like other forms of replication.
Structure.
The protein that prions are made of (PrP) is found throughout the body, even in healthy people and animals.
However, PrP found in infectious material has a different structure and is resistant to proteases, the enzymes in the body that can normally break down proteins. The normal form of the protein is called PrPC, while the infectious form is called PrPSc – the C refers to 'cellular' PrP, while the Sc refers to 'scrapie', the prototypic prion disease, occurring in sheep. While PrPC is structurally well-defined, PrPSc is certainly polydisperse and defined at a relatively poor level. PrP can be induced to fold into other more-or-less well-defined isoforms in vitro, and their relationship to the form(s) that are pathogenic in vivo is not yet clear.
Prions in plants.
In 2015, researchers at The University of Texas Health Science Center at Houston found that plants can be a vector for prions. When researchers fed hamsters grass that grew on ground where a deer that died with chronic wasting disease (CWD) was buried, the hamsters became ill with CWD, suggesting that prions can bind to plants, which then take them up into the leaf and stem structure, where they can be eaten by herbivores, thus completing the cycle. It is thus possible that there is a progressively accumulating number of prions in the environment.
Genetic factors.
A gene for the normal protein has been identified: the PRNP gene.
In all inherited cases of prion disease, there is a mutation in the PRNP gene.
Many different PRNP mutations have been identified and these proteins are more likely to fold into abnormal prion.
Although this discovery puts a hole in the general prion hypothesis, that prions can aggregate only proteins of identical amino acid make-up. These mutations can occur throughout the gene. Some mutations involve expansion of the octapeptide repeat region at the N-terminal of PrP. Other mutations that have been identified as a cause of inherited prion disease occur at positions 102, 117 & 198 (GSS), 200, 210 & 232 (CJD) and 178 (Fatal Familial Insomnia, FFI). The cause of prion disease can be sporadic, genetic, or infectious, or a combination of these factors. For example, to have scrapie, both an infectious agent and a susceptible genotype must be present.
Viral hypothesis
The protein-only hypothesis has been criticised by those maintaining that the simplest explanation of the evidence to date is viral.
For more than a decade, Yale University neuropathologist Laura Manuelidis has been proposing that prion diseases are caused instead by an unidentified slow virus. In January 2007, she and her colleagues published an article reporting to have found a virus in 10%, or less, of their scrapie-infected cells in culture. In 2016, Sotirios Botsios and Laura Manuelidis showed evidence that TSE specific nucleic acids may be required for infectious transmission of CJD and Scrapie.
Evidence in favor of a viral hypothesis (best current guess) includes:
Strain variation:
differences in prion infectivity, incubation, symptomology, and progression among species resembles that seen between viruses, especially RNA viruses
The long incubation and rapid onset of symptoms resembles lentiviruses, such as HIV-induced AIDS
Viral-like particles that do not appear to be composed of PrP have been found in some of the cells of scrapie- or CJD-infected cell lines.
Many viruses, including HIV which needs CD4 and CXCR4, need a receptor to attach to and enter into host cells.
The host prion, PrPc may be a receptor protein for an as yet undiscovered TSE virus, explaining why animals lacking host prion do not become infected with experimental prion disease.
A prion-like protein, called MAVS, has been shown to misfold as part of the innate immune response against pathogenic viruses, similarly the cellular prion, PrPC has been shown to have anti HIV properties, and it is hypothesized that the misfolding of the prion in TSEs may be an antiviral response against an unknown virus.
In 2016, studies have demonstrated susceptibility to nucleases under certain situations:
>99% of infectivity was destroyed, but there was no reduction of prion protein, suggesting the presence of a nucleic acid.
Studies propagating TSE infectivity in cell-free reactions and in purified component chemical reactions is thought to strongly suggest against TSE viral nature. However, some viruses, such as Poliovirus, have the ability to replicate in cell-free reactions.
The definition of a prion-like domain arises from the study of fungal prions.
In yeast, prionogenic proteins have a portable prion domain that is both necessary and sufficient for self-templating and protein aggregation. This has been shown by attaching the prion domain to a reporter protein, which then aggregates like a known prion. Similarly, removing the prion domain from a fungal prion protein inhibits prionogenesis. This modular view of prion behaviour has led to the hypothesis that similar prion domains are present in animal proteins, in addition to PrP.
These fungal prion domains have several characteristic sequence features.
They are typically enriched in asparagine, glutamine, tyrosine and glycine residues, with an asparagine bias being particularly conducive to the aggregative property of prions. Historically, prionogenesis has been seen as independent of sequence and only dependent on relative residue content. However, this has been shown to be false, with the spacing of prolines and charged residues having been shown to be critical in amyloid formation
Prions: Tissues in the Small Intestine play a Major Role in .. Prion Disease ..
INDEX
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542385/
The Gut-Associated Lymphoid Tissues in the Small Intestine, Not the Large Intestine,
Play a Major Role in Oral Prion Disease Pathogenesis.
David S. Donaldson, Kathryn J. Else, and Neil A. Mabbott -- B. Caughey, Editor
J Virol. 2015 Sep 15; 89(18): 9532–9547.
ABSTRACT
Prion diseases are infectious neurodegenerative disorders characterized by accumulations of abnormally folded cellular prion protein in affected tissues. Many natural prion diseases are acquired orally, and following exposure, the early replication of some prion isolates upon follicular dendritic cells (FDC) within gut-associated lymphoid tissues (GALT) is important for the efficient spread of disease to the brain (neuroinvasion). Prion detection within large intestinal GALT biopsy specimens has been used to estimate human and animal disease prevalence. However, the relative contributions of the small and large intestinal GALT to oral prion pathogenesis were unknown.
To address this issue, we created mice that specifically lacked FDC-containing GALT only in the small intestine.
Our data show that oral prion disease susceptibility was dramatically reduced in mice lacking small intestinal GALT.
Although these mice had FDC-containing GALT throughout their large intestines, these tissues were not early sites of prion accumulation or neuroinvasion. We also determined whether pathology specifically within the large intestine might influence prion pathogenesis. Congruent infection with the nematode parasite Trichuris muris in the large intestine around the time of oral prion exposure did not affect disease pathogenesis. Together, these data demonstrate that the small intestinal GALT are the major early sites of prion accumulation and neuroinvasion after oral exposure. This has important implications for our understanding of the factors that influence the risk of infection and the preclinical diagnosis of disease. ...
INTRODUCTION
Prion diseases (transmissible spongiform encephalopathies [TSEs]) are subacute neurodegenerative diseases affecting both animals and humans and are characterized by the accumulation of aggregations of PrPSc, abnormally folded isoforms of the cellular prion protein (PrPC), in affected tissues. Infectivity copurifies with PrPSc, and it appears to constitute the major, if not sole, component of the infectious agent (1). Many prion diseases, including natural sheep scrapie, bovine spongiform encephalopathy, chronic wasting disease (CWD) in mule deer and elk, and kuru and variant Creutzfeldt-Jakob disease (vCJD) in humans, are acquired peripherally by oral consumption of prion-contaminated food.
The gut-associated lymphoid tissues (GALT) comprise a collection of multifollicular structures, including the
tonsils, Peyer's patches, appendix, colonic and cecal patches,
and a number of smaller, single follicular structures termed isolated lymphoid follicles (ILF).
These tissues are situated throughout the gastrointestinal tract, and together with
the mesenteric lymph nodes (MLN),
they help protect the host from infection.
However, following oral exposure, some prion isolates exploit the GALT to infect the host (2,–4), where they replicate upon
follicular dendritic cells (FDC) in the B-cell follicles before spreading via enteric nerves to the central nervous system (CNS) (a process termed neuroinvasion) (2,–7). Once the prions have been amplified on the surfaces of FDC above the threshold required for neuroinvasion, they subsequently infect the enteric nerves within the intestine. The prions then spread through the peripheral nervous system (both sympathetic and parasympathetic) and infect the CNS, although hematogenous spread cannot be entirely excluded. Our previous data suggest that neuroinvasion after oral exposure occurs directly via GALT since neuroinvasion was blocked in mice that lacked GALT.
The ILF in the intestine can be classified as either immature ILF (individual primary B-cell follicles) or mature ILF containing a single organized B-cell-containing germinal center and an FDC network (12,–16). We have shown that FDC-containing mature ILF were a novel, previously unrecognized site of prion accumulation and neuroinvasion in the intestine. ...
Prions accumulate in both small intestinal (SI) and large intestinal (LI) GALT.
Accumulation within LI GALT, such as the rectoanal mucosa-associated lymphoid tissues (RAMALT) of scrapie- and CWD-affected species and the appendix of vCJD-affected humans, has received significant attention, as it has been used to identify preclinical infected animals and to gain insight into the possible prevalence of vCJD in the United Kingdom. ...
DISCUSSION
Here we show that the SI GALT are the major early sites of prion accumulation and neuroinvasion after oral exposure. ...
Our data show that Peyer's patches and mature ILF in the SI are each individually capable of supporting prion accumulation and neuroinvasion. ... In the absence of FDC-containing GALT in the SI, the gastrointestinal tract appears to act as a barrier against oral prion infection. Unfortunately, it is not currently possible to create mice with FDC-containing GALT exclusively in the SI.
After accumulating upon FDC, the prions are then amplified above the threshold required for neuroinvasion and spread to the enteric nervous system and the CNS, ultimately causing neurodegeneration and death. Infection can spread to enteric nerves in SI GALT within 21 days of exposure (9), potentially in association with classical dendritic cells. In the current study, no PrPSc was detected in the LI GALT by 15 weeks after oral exposure. Since the initial infection of enteric nerves occurs substantially before the detection of PrPSc in LI GALT, our data strongly support the conclusion that the LI GALT are not important early sites of prion neuroinvasion after oral exposure.
... influence(s) on the host's susceptibility to oral prion infection.
... dramatically reduced susceptibility of aged mice to oral prion infection ....
... chronic inflammation, ... may expand the tissue distribution of prions within infected hosts.
... damage to the LI mucosa and the associated immune pathology may also affect oral prion disease pathogenesis.
... S. Typhimurium infection can also have a dramatic effect on M cells and classical dendritic cells in the SI, which have key roles in oral prion pathogenesis. This may have significantly influenced prion uptake in the SI, enhancing disease susceptibility independent of the effects on the LI.
... Although LI GALT are not early sites of infection, the detection of PrPSc within the RAMALT and appendix has proved to be a useful method to detect prion-infected individuals during the preclinical phase and has been used in the United Kingdom to gain insight into the possible prevalence of vCJD in the human population. However, ... the time at which these tissues are sampled in relation to prion exposure may dramatically affect the sensitivity of these assays. For instance, humans with subclinical vCJD infection may have only minimal PrP deposition in appendiceal tissue. Together, these data show that analyses of such biopsy specimens may miss individuals in the early stages of oral prion infection and underestimate the disease prevalence. ...
Prions: Autopsy findings regarding Alzheimer's.
INDEX
https://www.sciencedaily.com/news/health_medicine/alzheimer's/
June 7, 2019
LINK 2: Neuropathy: Chapter 9 Degenerative Diseases, Alzheimer's Disease (AD)
http://neuropathology-web.org/chapter9/chapter9bAD.html
by Dimitri Agamanolis, M.D.
Updated: August, 2016
LINK 3: Rules Updated for Postmortem Dx of Alzheimer's.
https://www.medpagetoday.com/neurology/alzheimersdisease/30731
by John Gever, Senior Editor, MedPage Today
January 18, 2012
LINK 4: Alzheimer's Disease: How It’s Diagnosed.
https://www.webmd.com/alzheimers/guide/making-diagnosis-tests#1
WebMD Medical Reference Reviewed by Neil Lava, MD
May 19, 2019
Prion detection and diagnosis is largely considered impossible to confirm until an autopsy is done.
Not all prions are the same in structure. Prions are known to mutate. The genesis of prion structures is currently (2019-06) theoretical (best guess, rationalized projection, spurious associations). To keep the public from becoming alarmed at the apparent endemic outbreak of Alzheimer's disease amongst aging North Americans and its spread into other industrialized-commercialized economies writers and reporters have made efforts to distance Alzheimers's disease from prion diseases, often on the basis that the two develop at perceptually different rates, and, that each progresses from initial symptoms to fatality in different time durations. These expressed differences are little more than a smokescreen using variables as if they were known real specifics.
If we are going to focus on timing, symptoms, and development, let's consider the REALITY.
Alzheimer's victims can be sheltered from diagnosis for a decade or longer by family members in denial and afraid of the stigma and expectations attached to the label of Alzheimer's. Tragically, they more easily abuse their friend or loved one for becoming forgetful, acting senile, getting old, becoming paranoid, or not being careful and stumbling or dropping things ... than to acknowledge and admit that perhaps their loved one has a neurological DISEASE rather than a neurological decline. Persons diagnosed with Alzheimer's may die from the disease or complications or an accident within a few years, or, live for decades sheltered in full-time nursing or hospice care.
SYMPTOMS of Alzheimer's.
- loss of memory,
- awareness is diminished,
- mental deterioration,
- involuntary movement of the eyes,
- cognitive decline,
- clumsiness,
- behavioral changes,
- lack of coordination,
- unsteadiness,
- difficulty in walking,
- uncooperative,
- speech disturbance,
- a slowly progressive ataxic gait,
- lack of coordination in swallowing,
- weakness in the legs,
- weakness of extremities,
- poor reflexes,
- abnormal sensations,
- fidgeting,
- severe dementia,
- confused states,
- apparent deafness,
- coma,
- death.
The limited knowledge we have about Prion diseases is not surprising to a sincere researcher.
Currently, most research concerning prion diseases is acquired from autopsies.
Yet autopsies, in Canada, are governed by restrictions and regulations set forth by each province separately and subject to modification frequently by political forces which oversee medical associations. Autopsies cost money. Healthcare costs and budgets decrease if greater restrictions are imposed on medical procedures. In some provinces, the medical examiner (previously termed a coroner who had less restrictions) cannot rule that a death was caused by medical malpractice or error.
An autopsy is often not performed unless a homicide is expected, or, a socially prominent person has died.
If the family of the deceased acts quickly enough they can demand an autopsy which they agree to pay $3500 or more for.
The results will still be phrased in politically acceptable terms that hold as few persons responsible as possible ... especially not those employed by the government including doctors. If the deceased is designated as being under the care of a doctor, it is usually, automatically NOT a justification for an autopsy. Other nations and medical jurisdictions have other regulations and limitations on when, if, and who might be given an autopsy, what indicators will be checked for, the training of the medical examiner, how specific the results can be specified, and who may receive a copy of the autopsy. And, there is no easy or quick means of diagnosing the presence of prions in a laboratory.
Individuals who were cognitively normal at the time of death can nevertheless be diagnosed with Alzheimer's disease on the basis of autopsy findings alone, according to new guidelines (2012) endorsed by the National Institute on Aging (NIA) and the Alzheimer's Association.
The guidelines for postmortem assessment of Alzheimer's disease, which replace criteria issued in 1997, also call on pathologists to base diagnoses on an "ABC" risk score that combines assessments of beta-amyloid plaques, neurofibrillary tangles (prions?), and neuritic plaques.
The 1997 criteria had stipulated that patients whose brains had the plaques and tangles characteristic of Alzheimer's disease could not receive a formal postmortem diagnosis unless they also had had clinical dementia before death.
In contrast, the new guidelines are focused solely on histological and biochemical abnormalities found at autopsy, without reference to symptoms shown while patients were still living. ...
Key to the new attitude has been a raft of recent research documenting that plaques and tangles can infest patients' brains long before they develop clinical symptoms. This has been demonstrated from autopsy findings and from imaging studies in live patients using tracers that highlight beta-amyloid plaques.
The overall result is that we have an information climate in which many people don't want to know more details out of fear of social exclusion, abandonment, or, prejudice. We have others, politicians, who are terrified that the possibility of an epidemic of a costly, totally disabling, potentially sudden onset illness that cannot be controlled, diagnosed, nor treated is spreading through the population. Then we have a so-called scientific community composed mostly of institutionally employed laboratory technicians whose main concern is maintaining employment by following well-worn and limited testing procedures to look for something that is expected. Prions are NOT expected structures easily detected with routine test procedures. If they were we would know a lot more about them and understand them intensively.
We do know, or believe that we know, that prion diseases can suddenly appear (in our awareness).
They likely develop from one or more mutations of genes and cells, yet have no genes themselves and are suggestive of aggressive forms of combining and replicating chemicals or metals devoid of life. We have formulated that they can be acquired by exposure to contaminated liquids, tissues, or soils, or vegetation ... yet may rest dormantly in a body, often apparently in the small intestine, for as long as decades until they are triggered into invasive activity by some form of catalytic action. Then, depending upon which of the known human forms one acquires, when they acquire it, what they are exposed to in terms of experiences and substances, and what other ailments or immune distractions they may have ... an ACTIVE prion illness may result in a fatality within days, weeks, months, or years ... though not usually decades. These factors are not that different from Alzheimer's basics.
SYMPTOMS of Prion Diseases.
- loss of memory,
- awareness is diminished,
- mental deterioration,
- involuntary movement of the eyes,
- cognitive decline,
- clumsiness,
- behavioral changes,
- lack of coordination,
- unsteadiness,
- difficulty in walking,
- uncooperative,
- speech disturbance,
- a slowly progressive ataxic gait,
- lack of coordination in swallowing,
- weakness in the legs,
- weakness of extremities,
- poor reflexes,
- abnormal sensations,
- fidgeting,
- severe dementia,
- confused states,
- apparent deafness,
- coma,
- death.
Consider the similarity about the symptoms of each.
Based on clinical evaluations, 13% of persons over 65 years and 45% of those over 85 have AD in the USA (2016).
AD is driven by two processes: extracellular deposition of beta amyloid-Aß and intracellular accumulation of tau protein.
Both these compounds are insoluble. Aß is the main component of senile plaques and tau is the component of neurofibrillary tangles. Aß deposition is specific for AD and is thought to be primary. Tau accumulation is also seen in other degenerative diseases and is thought to be secondary.
BETA AMYLOID.
Aß is a 36 to 43 amino acid peptide, which is part of a larger protein, the Amyloid Precursor Protein (APP).
APP is a transmembrane protein, made by neurons and other brain cells.
It is also found in extraneural tissues and is especially abundant in platelets. Its function is unknown.
The Aß amyloid residue includes part of the transmembrane domain of APP and is derived from cleavage of APP by the enzymes ß-and ?-secretase. Aß monomers and oligomers are further degraded by other enzymes. Defective clearance of Aß from aberrant cleavage of APP and other mechanisms results in its accumulation. Aß monomers polymerize initially into soluble oligomers and then into larger insoluble fragments such as Aß42, which precipitate as amyloid fibrils.
Aß is toxic to neurons.
In brain slice preparations, it causes loss of long term potentiation, damages synapses, and kills neurons.
Moreover, it shows selective neurotoxicity for the hippocampus and entorhinal cortex (areas that are severely affected in AD) while sparing cerebellar neurons. This damage is mediated by free radicals, which are generated when soluble Aß is complexed with Zn2+, Cu2+, and Fe3+. There is a high correlation between the amount of soluble Aß and the severity of the neurological dysfunction in AD. In transgenic AD models, severe neurological deficits occur in absence of amyloid deposits in tissue.
TAU.
Neurofibrillary degeneration is characterized by the deposition in the neuronal body and processes of insoluble polymers of over-phosphorylated microtubule associated protein tau. Tau aggregates as pairs of filaments that are twisted around one another (paired helical filaments). ... the spread of the pathology to anatomically linked areas occurs by passage of abnormal tau across synapses.
... There are two main lesions in AD, senile plaques (SPs) (also called Alzheimer's plaques) and neurofibrillary tangles (NFTs). SPs are spherical lesions in the cerebral cortex. ... NFTs are deposits of tau filaments in the neuronal body. Similar deposits are present in the dystrophic processes of NPs and in dendrites (neuropil threads-NTs). In advanced AD, the hippocampus often contains extracellular NFTs embedded in the neuropil, like fossilized skeletons of neurons (ghost tangles). The mechanism of accumulation of tau in NFTs is unclear.
... Each SP represents a focus of damage of the neuropil that includes axon terminals and dendrites of several neurons and probably thousands of synapses. Thus, SPs cause severe disconnection. The distribution of the lesions correlates with the clinical picture. Damage of the hippocampus explains the impairment of memory, and involvement of association cortex correlates with the loss of higher intellectual functions. SPs and NFTs are associated with loss of neurons and synapses, brain atrophy, and dilatation of the lateral ventricles due to loss of brain tissue (hydrocephalus ex vacuo). ...
High cholesterol levels during mid-life increase the risk of AD and lipid-lowering drugs lower this risk.
... Other than Aß and tau, neuroinflammation is the most important factor involved in the pathogenesis of AD. ...
Amyloid Precursor Protein (APP) is an acute phase protein which is released in brain tissue following trauma and other insults.
... Oxidative stress, compounding with advancing age, causes mitochondrial DNA mutations, mitochondrial dysfunction and more oxidative stress. This process is accelerated in AD by the action of Aß (a mitochondrial poison and free radical generator) and activated microglia, also a source of free radicals.
Type 2 diabetes is a risk factor for AD.
AD patients have low levels of insulin and insulin resistance in the brain.
These changes impair energy metabolism in neurons and adversely effect signaling pathways dependent on insulin and its receptors. ... aggravate oxidative damage. ... Increased levels of homocysteine (also a risk factor for stroke) and decreased dietary folate potentiate these neurotoxic effects. Homocysteine increases with advancing age and .... Elevated homocysteine and decreased folate are associated with increased free radicals,
Neuronal plasticity (the ability to make new synapses) is enhanced by trophic factors (neurotrophins).
The best known neurotrophin, nerve growth factor, is important for growth and maintenance of cholinergic neurons that are depleted in AD. Neuronal activity also enhances plasticity. (Using your brain functions creates new synapses ... which can compensate for the usual loss of neurons and synapses as we age.) ,,,
Middle age hypertension is also a risk for AD.
(So, release Energy Blocks and learn how to meditate-pray, cope with loss by acknowledging reality, and, increase your spiritual awareness and appreciation.) ,,, Autopsy studies show that the brains of most people over 65, even without clinical dementia, contain a few SPs and NFTs in the hippocampus and entorrhinal cortex. ... The brains of demented people contain more SPs and NFTs, not only in the limbic cortex but also in the neocortex and other regions. The more numerous and widespread the SPs and NFTs, the more severe the dementia. ... 90% of people over 65 have no clinical dementia. (according to research findings and interpretations up to 2016).
Factors contributing to AD.
- DNA mutations,
- High cholesterol levels,
- trauma and other insults,
- Increased levels of homocysteine,
- Middle age hypertension.
Possible protections against AD.
- release Energy Blocks,
- learn how to meditate-pray,
- cope with loss by acknowledging reality,
- increase your spiritual awareness and appreciation,
- Using your brain functions.
Diagnosing Alzheimer's Disease or a Prion Disease.
This note has been left until last because in my experience and opinion it is least relevant.
In my 74+ years of experience, across 3 provinces in the Canadian approach to medical healthcare, diagnosis is routinely avoided in place of spurious rationalizations and superstition-like associations projected from singular symptoms to elicit pharmaceutical prescriptions. Particularly in Canada (in my opinion) and throughout the USA, the use of imaging tests (CT scans and MRIs) is highly sabotaged by the economic penchant to assess the results in a 5 minute glance contrary to the 40+ minute study conducted by doctors who have been in the field for over 25 years. REAL significant findings, such as a stage 4 case of prostate cancer that was specifically the possibility for having the MRI, can be and are missed.
Academically limited articles and reports, commonly regurgitated on the Internet, present Possibilities as if they were definitive, professionally conducted, politically sanctioned, and administratively encouraged procedures. The REALITY, in my experience, research, and opinion are that they are NOT and that their presentation with the technical distance of aloofness and written authority to the public is a deception that encourages despair, depression, and denial in the public.
Prions: Names, Persistence, Neuroinvasion
INDEX
https://en.wikipedia.org/w/index.php?title=Prion/Archive_1&action=edit&redlink=1
This is an archive of past discussions.
Prions aren't affected much by proteolysis or anything else.
Otherwise the animal would be able to break them down when it's alive.
You can put prions in formaldehyde, boil them, in fact boil them in formaldehyde if you like, whatever - they survive a lot of stuff (their structure is very stable)
-- Purple 03:42, 10 March 2006 (UTC)
... prions have been heated to thousands of degrees, directly immolated with plasma torches, bombarded with high-energy gamma rays... no dice.
Methods such as those tend to destroy a significant percentage of prions in any particular sample, but, as far as I am aware, there is no known way to destroy them all, at least not in a living organism. They really are nasty little things. They undergo self-replication, but exhibit no free will, and so fall below the threshold separating life from nonlife. This means that, unlike biological reproduction, the propagation of prions consists of completely deterministic chemical interactions, which makes the prevention of their replicative process much, much more difficult than stopping a living, infectious organism.
Alexis Brooke M 04:06, 5 November 2007 (UTC)
... it has been found that the prion protein excreted by scrapie infected sheep can remain in the soil for extended periods of time and infect flocks that are later allowed to graze on the same pasture. It is thought that animal carcases may also release the disease into the soil contaminating it for years to come! Britain is the place to watch after the massive outbreak that occurred in the 90's!
(A.guinness (talk) 00:49, 27 May 2008 (UTC))
... There are other proteins than PrP that can form prions (i.e. that are truly infectious), but the only ones we know of are in yeast/fungi. You also need to bear in mind that 'amyloid' itself (beta-sheet protein fibrils) is not necessary for prion disease - it seems to build up as a kind of by-product. No-one knows what the actual infectious form looks like, or why other amyloid-forming proteins don't have this infectious form. ...
(Purple 13:03, 3 January 2007 (UTC)
... the nomenclature of the various forms of PrP is still debated amongst prion researchers.
For clarification, I've listed below just a few of the different names for some of the isoforms of PrP as outlined by Prof Charles Weissmann in his excellent review, The State of the Prion (Nature Reviews Microbiology 2, 861-871 (2004)).
PrPC
The physiologically occurring, mainly GPI-linked form of PrP, or prion protein, that can be glycosylated on one or both of two asparagine residues with a variety of glycans. As shown by NMR and X-ray crystallography, it is rich in alpha-helical structure and contains only a little beta-sheet structure.
PrPSc
An isoform of PrPC that is almost invariably detected in TSE-infected tissues and cells.
It comprises a carboxy-proximal segment of about 140 residues that is resistant to defined conditions of PK treatment.
The term PrPSc is used by some interchangeably with prion, a usage that should be avoided. PrPSc designates a structure, prion is a functional concept. The implication that a particular form of PrP is the only essential constituent of the prion remains to be proven.
PrP27-30
The PrP fragment remaining after controlled PK digestion of PrPSc. -
Contrary to popular belief PrPsc is not entirely resistant to protease digestion, but instead has a protease-resistant core. (Pikzee)
PrP*
A hypothetical isoform of PrP that is the essential component of the TSE agent or prion.
Prnp
The gene encoding PrP
rPrP
Denotes recombinant PrP.
When produced in Escherichia coli it lacks the GPI anchor and the glycan residues.
Pikzee 17:57, 21 March 2007 (UTC)
...
The prions replicate in the spleen and are carried by the Follicular Dendritic Cells (FDCs).
FDCs accumulate high levels of prions (PrPSc) during the infection and essentially "pass them" to the splenic nerves.
It's not known exactly how this happens but it has been shown that neuroinvasion is dependant on this process and occurs more quickly the closer the FDCs and the nerves are to each other. PrPc is present on the cell membrane of the nerves and it recycles between the membrane and internal compartments of the cell. Once it comes into contact with PrPsc from the FDCs, the conversion reaction may occur - whether this happens in the cell membrane or internal compartments is still unclear. The newly formed PrPSc can then go on to recruit and convert more PrPc within the cell into the abnormal infectious form. Through this continuing process, the prions may propagate or "travel" through the cell and pass from one cell to the next mediating the neuroinvasion.
Pikzee (talk) 14:54, 21 December 2009 (UTC)
The cellular basis for prion transmigration from the gut through the GALT into the lymphoid system is still poorly understood. Membranous epithelial cells (M cells) are believed to be the key sites of antigen sampling for the mucosa-associated lymphoid tissue (MALT), and function as major ports of entry for pathogens from the gut by transport across the epithelium.
Immune cells are crucially involved in the process of neuroinvasion following oral administration: mature follicular dendritic cells (FDCs), located in Peyer's patch, could be crucial for the transmission of prions from the gastrointestinal tract. FDCs, being mobile, could function as a bridge between the gut lumen and the lymphoid organs, where the prions can replicate. FDCs could transport prions from their sites of replication to peripheral nerves in lymphoid organs, thereby enabling the process of neuroinvasion.
Prions: How ... Prions Hitch A Ride Into Intestine.
INDEX
https://www.sciencedaily.com/releases/2004/12/041220002446.htm
New Study Shows How Mad Cow Prions Hitch A Ride Into Intestine.
Department of Pathology at Case Western Reserve University School of Medicine
Dec. 15 issue of the Journal of Neuroscience.
senior author Neena Singh, M.D., Ph.D.
December 30, 2004
... the main culprits behind the human form of mad cow disease or variant Creutzfeldt-Jakob Disease (vCJD), are not destroyed by digestive enzymes found in the stomach. ... prions, cross the normally stringent intestinal barrier by riding piggyback on ferritin, a protein normally absorbed by the intestine and abundantly present in a typical meat dish.
... Variant CJD results from eating contaminated beef products from cattle infected with mad cow disease.
To date (2004), 155 cases of confirmed and probable vCJD in the world have been reported, and it is unclear how many others are carrying the infection.
... in the case of humans where the infectious prions survive through stages of cooking and digestion.
... The prions were linked with ferritin, a cellular protein that normally binds excess cellular iron to store it in a soluble, non-toxic form within the cell.
"Since ferritin shares considerable similarity between species,
it may facilitate the uptake of prions from distant species by the human intestine,"said Singh.
...
Prions: Gut M cell influence on Prion Infection.
INDEX
https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1006075
Increased Abundance of M Cells in the Gut Epithelium
Dramatically Enhances Oral Prion Disease Susceptibility
Authors: David S. Donaldson, Anuj Sehgal, Daniel Rios, Ifor R. Williams, Neil A. Mabbott
Published: December 14, 2016
... After oral (ingestion and) infection TSE's (transmissible spongiform encephalopathies) -- prions first accumulate within the lymphoid tissues that line the intestine (known as Peyer’s patches) before they spread to the brain where they cause neurodegeneration. To do this, the prions must first cross the intestinal epithelium, a single layer of cells that separates the body from the gut contents. M cells are found within the epithelium that covers the Peyer’s patches and are specialised to transport large particles and whole bacteria across the gut epithelium. ... In the specific absence of M cells in these mice, the accumulation of prions within Peyer’s patches and the spread of disease to the brain was blocked, demonstrating a critical role for M cells in the initial transfer of prions across the gut epithelium in order to establish host infection.
Since pathogens, inflammatory stimuli and aging can modify M cell-density in the gut, these factors may also influence oral prion disease susceptibility. ... We show that prion uptake from the gut lumen was enhanced ... resulting in shortened survival times and increased disease susceptibility, equivalent to a 10-fold higher infectious titre of prions. Together these data demonstrate that M cells are the critical gatekeepers of oral prion infection, whose density in the gut epithelium directly limits or enhances disease susceptibility.
Following oral exposure the early accumulation and replication of prions upon follicular dendritic cells (FDC) within the gut associated lymphoid tissues (GALT), such as Peyer’s patches of the small intestine, is essential for efficient neuroinvasion (spread into nerves). FDC are a unique subset of stromal cells resident within the primary B cell follicles and germinal centres of lymphoid tissues. After amplification upon the surface of FDC, the prions then infect neighbouring enteric nerves and spread along these to the (Central Nervous System) CNS (a process termed neuroinvasion) where they ultimately cause neurodegeneration and death of the host.
The follicle-associated epithelia (FAE) which covers the lumenal surfaces of the Peyer’s patches contains a unique population of epithelial cells, termed M cells. These highly phagocytic epithelial cells are specialized for the trans-epithelial transfer of particulate antigens and microorganisms from the gut lumen (termed transcytosis), an important initial step in the induction of efficient mucosal immune responses against certain pathogenic bacteria and the commensal bacterial flora.
A variety of bacterial and viral pathogens including Brucella abortus, Salmonella Typhimurium, Yersinia enterocolitica, norovirus and reovirus appear to exploit the transcytotic activity of M cells to cross the gut epithelium and infect the host. The food-borne botulinum neurotoxin has also been suggested to exert its toxicity after transcytosis by M cells. Independent studies suggest orally administered prions may similarly be transported by M cells into host tissues and that this transport may be important to establish host infection. ...
The differentiation of M cells from uncommitted precursors in the intestinal crypts is critically dependent on stimulation from the cytokine known as RANKL (receptor activator of nuclear factor-?B ligand). This cytokine is expressed by subepithelial stromal cells beneath the FAE in Peyer’s patches, and signals via its receptor RANK (receptor activator of nuclear factor-?B) which is expressed by epithelial cells throughout the intestine. Accordingly, M cell-differentiation is blocked in RANKL-deficient mice or following in vivo RANKL-neutralization with anti-RANKL antibody. ...
Certain pathogenic bacteria or exposure to inflammatory stimuli such as cholera toxin can significantly increase the density of M cells in the intestine. Inflammation or pathogen infection can also influence prion disease pathogenesis by enhancing the uptake, or expanding the distribution, of prions within the host. ...
These data show that an increased density of M cells in the intestinal epithelium at the time of oral exposure enhanced the uptake of prions from the gut lumen, as the RANKL-treated mice accumulated prions within their lymphoid tissues significantly earlier than control mice. ...
In the specific absence of M cells, the accumulation of prions in Peyer’s patches and subsequent neuroinvasion was blocked. ...
the density of functionally mature M cells in the Peyer’s patches of aged mice is substantially reduced, suggesting that the reduced susceptibility of aged mice to oral prion infection is at least in part due to the inefficient uptake of prions from the gut lumen by M cells. ... in the UK most clinical vCJD cases have predominantly occurred in young adults (median age at death, ~28 years). ... this age-related susceptibility
Furthermore, the accumulation of prions in the Peyer’s patches, MLN and spleens of orally-exposed M cell-deficient RANK?IEC mice was undetectable up to at least 440 d after exposure. As abundant prion accumulation is typically evident in these tissues in conventional (WT) mice by 105 d after exposure, this implies that in the absence of M cells, any prions that do enter the Peyer’s patches via alternative routes may be of insufficient magnitude to establish infection. Indeed PrPSc was also undetectable in the lymphoid tissues and CNS of these mice up to at least 440 dpi.
Instead the prions that are acquired from the gut lumen by these M cell-independent routes are most likely sequestered and destroyed by cells such as macrophages, which are considered to degrade prions, rather than being efficiently transported to FDC where they undergo amplification before neuroinvasion. RANK?IEC mice show reduced IgA production and delayed germinal centre responses in their Peyer’s patches. This suggests that antigens that are transcytosed by M cells are preferentially targeted to the FDC-containing B-cell follicles to initiate antibody responses. Therefore, M cells, in contrast to FAE enterocytes with large LAMP1+ endosomes, may be considered to facilitate the efficient transfer of prions from the gut lumen to FDC in the B-cell follicles of Peyer’s patches. ...
The GALT in the small intestine such as the Peyer’s patches, not those in the large intestine, are the major early sites of prion uptake, replication and neuroinvasion after oral exposure. ...
In my personal experience of 74 years in the Canadian provincial healthcare service delivery format, small intestine investigation, endoscopic review, and direct testing with a motive to diagnostic determination of the REALITY behind an intestinal disease presence, as indicated by symptoms, is avoided to the extreme of "almost never." If we never look in the area of first and usual prion generation, how would we ever become aware of the degree of its infective spread, what factors may be enhancements to its treatment, how we could better understand and prevent it, and, the conditions under which they begin.
Prions: Prion Diseases as Transmissible Zoonotic Diseases.
INDEX
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747681/
Osong Public Health Res Perspect. 2013 Feb; 4(1): 57–66.
Jeongmin Lee, Su Yeon Kim, Kyu Jam Hwang, Young Ran Ju, and Hee-Jong Wooa
2013 Feb 4
World Organization for Animal Health (Office International des Epizooties; OIE)
specific risk material (SRM)
4. Concluding Remarks
All emerging zoonotic diseases are NOT simple diseases and involve sociocultural issues because of their threatening and fearful characteristics. In that respect, BSE and vCJD are typical emerging epidemics along with AIDS; these diseases are still progressive and being studied. ...
Although OIE regulations are expected to be relaxed in time to keep up with the free-trade era, managing SRM is the most important aspect in controlling this disease. In one case, it took 5 years to change the age regulation of the EU on SRM (up to 6 months). The different regulations of the OIE and the EU regarding SRM standards cause confusion among people. SRM standards set by the OIE are “conditions or guidelines for trade” that can prevent the disease from spreading from one country to another. Based on these criteria, countries are supposed to establish their own trade regulations in which their industry structures, conditions for controlling the disease, and dietary habits should be considered. In other words, OIE regulations are the necessary conditions for all countries to follow to prevent the spread of the disease. However, SRM standards set by the EU are “scientifically sufficient conditions” that participating countries with different cultural and industrial backgrounds can utilize.
In Korea, it is critical to implement a traceability system or active total inspection to prevent prion diseases as soon as possible. In fact, the possibility of BSE and vCJD occurring naturally in Korea is extremely low. The major reason for this is that there are not enough preconditions for such diseases to occur. Korea has historically had few sheep farms. A British national institution reports that one of the main causes of the BSE outbreak in the UK was feeding cows with sheep intestines. However, Korea has not developed sheep farming, so the precondition of the BSE and vCJD pandemic does not exist there.
The second reason is that Koreans used to consume cow intestines.
For the epidemic to spread, there should be at least some infected entities; after the tipping point (threshold), it becomes an epidemic. Prion diseases have species barriers; within one species, the diseases spread more easily and quickly. However, a step for the multiplication of prions within a species is blocked since Koreans consume cow intestines themselves rather than feeding them to cows. In that respect, it is almost impossible for BSE or vCJD to occur naturally in Korea. If a BSE outbreak is reported in Korea, the cause would likely be from outside the country.
Disease: Creutzfeldt–Jakob disease (CJD)
INDEX
https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/
Fact-Sheets/Creutzfeldt-Jakob-Disease-Fact-Sheet
Date last modified: Tue, 2019-05-14
Prepared by:
Office of Communications and Public Liaison
National Institute of Neurological Disorders and Stroke
National Institutes of Health
Bethesda, MD 20892
LINK 2: https://www.alz.org/alzheimers-dementia/
what-is-dementia/types-of-dementia/creutzfeldt-jakob-disease
LINK 3: https://cjdfoundation.org/
LINK 4: https://medical-dictionary.thefreedictionary.com/Creutzfeldt-Jakob+disease
Creutzfeldt-Jakob (pronounced CROYZ-felt YAH-cob) disease (CJD) is a rare, degenerative, fatal brain disorder.
It (diagnosed in) about one person in every one million per year worldwide; in the United States there are about 350 cases per year. CJD usually appears in later life and runs a rapid course. Typical onset of symptoms occurs at about age 60, and about 70 percent of individuals die within one year.
Before 1995, Creutzfeldt-Jakob disease was not well known outside the medical profession.
Even within it, many practitioners did not know much about it. Most doctors had never seen a case.
With the recognition of a so-called "new variant" form of CJD and the strong possibility that those with it became infected simply by eating contaminated beef, CJD has become one of the most talked-about diseases in the world. Additionally, the radical theory that the infectious agent is a normal protein that has been changed in its form also has sparked much interest.
SYMPTOMS:
- failing memory,
- behavioral changes,
- lack of coordination,
- visual disturbances,
- mental deterioration,
- involuntary movements,
- blindness,
- weakness of extremities,
- coma,
- death.
There are three major categories of CJD.
-
In sporadic CJD, the disease appears even though the person has no known risk factors for the disease.
This is by far the most common type of CJD and accounts for at least 85 percent of cases.
In the sporadic form, the infectious prions are believed to be made by an error of the cell machinery that makes proteins and controls their quality. These errors are more likely to occur with aging, which explains the general advanced age at onset of CJD and other prion diseases. Once they are formed, abnormal prion proteins aggregate, or clump together. Investigators think these protein aggregates lead to the nerve cell loss and other brain damage seen in CJD. However, they do not know exactly how this damage occurs.
- In hereditary CJD, the person may have a family history of the disease and test positive for a genetic mutation associated with CJD. About 10 to 15 percent of cases of CJD in the United States are hereditary. In the hereditary form, infectious prions can arise when a mutation occurs in the gene for the body’s normal prion protein. As the mutated PrPC replicates itself, it spontaneously changes shape into the infectious form. (Prions themselves do not contain genetic information and do not require genes to reproduce themselves.) If the prion protein gene is altered in a person’s sperm or egg cells, the mutation can be transmitted to the person’s offspring. Several different mutations in the prion gene have been identified. The particular mutation found in each family affects how frequently the disease appears and what symptoms are most noticeable. However, not all people with mutations in the prion protein gene develop CJD.
- In acquired CJD, the disease is transmitted by exposure to brain or nervous system tissue, usually through certain medical procedures.
There is no evidence that CJD is contagious through casual contact with someone who has CJD.
Since CJD was first described in 1920, fewer than one percent of cases have been acquired CJD. ...
CJD cannot be transmitted through the air or through touching or most other forms of casual contact.
Spouses and other household members of people with sporadic CJD have no higher risk of contracting the disease than the general population. However, exposure to brain tissue and spinal cord fluid from infected persons should be avoided to prevent transmission of the disease through these materials.
In some cases, CJD has spread to other people from grafts of dura mater (a tissue that covers the brain), transplanted corneas, implantation of inadequately sterilized electrodes in the brain, and injections of contaminated pituitary growth hormone derived from human pituitary glands taken from cadavers. Doctors call these cases that are linked to medical procedures iatrogenic cases. Since 1985, all human growth hormone used in the United States has been synthesized by recombinant DNA procedures, which eliminates the risk of transmitting CJD by this route.
Many people are concerned that it may be possible to transmit CJD through blood and related blood products such as plasma. Some animal studies suggest that contaminated blood and related products may transmit the disease, although this has never been shown in humans. Recent studies suggest that while there may be prions in the blood of individuals with vCJD, this is not the case in individuals with sporadic CJD. Scientists do not know how many abnormal prions a person must receive before he or she develops CJD, so they do not know whether these fluids are potentially infectious or not. They do know that, even though millions of people receive blood transfusions each year, there are no reported cases of someone contracting sporadic CJD from a transfusion. Even among people with hemophilia (a rare bleeding disorder in which the blood does not clot normally), who sometimes receive blood plasma concentrated from thousands of donors, there are no reported cases of CJD.
While there is no evidence that blood from people with sporadic CJD is infectious, studies have found that infectious prions from BSE and vCJD accumulate in the lymph nodes (which produce white blood cells), the spleen, and the tonsils. At present, four cases of vCJD infection have been identified following transfusion of red blood cells from asymptomatic donors who subsequently died from vCJD. Recently, one case of likely transmission of vCJD infection by concentrates of blood-clotting protein has been reported in an elderly individual with hemophilia in the United Kingdom. The possibility that blood from people with vCJD may be infectious has led to a policy preventing individuals in the United States from donating blood if they have resided for more than three months in a country or countries where BSE is common.
Both brain biopsy and autopsy pose a small, but definite, risk that the surgeon or others who handle the brain tissue may become accidentally infected by self-inoculation.
Disease: Creutzfeldt–Jakob variant (vCJD)
INDEX
Prion Diseases as Transmissible Zoonotic Diseases.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747681/
Osong Public Health Res Perspect. 2013 Feb; 4(1): 57–66.
Jeongmin Lee, Su Yeon Kim, Kyu Jam Hwang, Young Ran Ju, and Hee-Jong Wooa
2013 Feb 4
Transmissible spongiform encephalopathy (TSE) is a general term for misfolded proteins, also called prions-related diseases, which had been discussed only among a few scientists until bovine spongiform encephalopathy (BSE), better known to the public as mad cow disease, became a public concern. It became widely known in the 1980s due to a sudden increase in the incidence of BSE in Europe; in the 1990s, it drew people’s attention as variant Creutzfeldt–Jakob disease (vCJD), which is also known as mad cow disease for humans.
Clinical symptoms similar to those of CJD that were reported in the 1920s were displayed in a patient who consumed contaminated beef (affected with BSE); the disease was called vCJD, which was first described in 1996. There are four types of CJDs: two nontransmittable CJDs, including sporadic CJD (sCJD) and familial or genetic CJD (implying a genetic cause), and two transmittable CJDs, including iatrogenic CJD and vCJD.
An endemic disease similar to CJD was found in cannibal tribes (such as the Fore, Gimi, and Yate in Papua New Guinea) who used to eat the dead bodies of their relatives as part of their rituals. This endemic disease, called kuru (meaning “shiver” in Uruna or Guzigli, among other tribes), was first reported in 1957. At that time, the cause could not be identified, so people assumed that the disease was caused by an unknown virus. However, ever since cannibalism was banned, the incidence of kuru decreased sharply.
Meanwhile, many studies have sought to identify the association between specific genotypes and the occurrence of the disease; a correlation between vCJD and methionine homozygote (MM type) at codon 129 in the human prion suggests that the MM type is highly related and susceptible to prion infection, and is clearly documented as a significant genetic risk factor.
A study on kuru among cannibal tribes shows that the incubation period of prion diseases differs among individuals based on genotype.
The MM type at codon 129 of the prion is most common in Korean people and has the shortest incubation period, with death following shortly after disease development;
the methionine–valine heterozygote (MV type) appears to be most resistant to the disease, and a case with 40 years of incubation has also been reported.
At present, all vCJD patients in Europe (including patients affected through transfusion) have the MM type except for one case. Therefore, Aguzzi at University Hospital of Zurich in Switzerland warns that patients should be observed for at least 40 years since the number of patients with the MV type may increase in the future. The Spongiform Encephalopathy Advisory Committee appointed by ministers from the UK assumes that there may be 4000–10000 infected persons with no symptoms in the UK; however, valine homozygote- (VV type) or MV-type patients may die of different causes due to the long incubation period after they have been exposed to the pathogenic prion.
Since vCJD was first reported in 1996, a total of 224 patients with this disease from 12 countries have been identified worldwide, as shown in Table 3;
the main symptoms include
- unstable emotions;
- abnormal senses;
- paralysis in linguistic, visual, and other senses;
- the inability to move and
- cognitive disability before death.
While sCJD is common in older people, vCJD can occur in young people after a short incubation period.
There is much epidemiological and laboratory evidence of a strong correlation between variants of CJD and BSE; vCJD differs from other CJDs clinically and histopathologically, and the initial extended exposure of the population to potentially BSE-contaminated food (1984–1986) was geographically and chronologically consistent with the initial onset of vCJD cases (1994–1996), considering the incubation period.
The facts that sCJD occurs in old people at the ratio of one to two out of 1 million people and vCJD is frequent in people in their 20s and 30s have led the public to believe that the dietary habits of the younger generation (who tend to eat more fast food such as hamburgers) may be the cause of the disease. However, recent findings suggest that age-related body conditions are the causative factors of the disease. The EU has been establishing countermeasures against the transmission of vCJD via blood transfusion. Current studies are focusing on the possibility of transmission via dental treatment.
Disease: Gerstmann–Sträussler–Scheinker syndrome (GSS).
INDEX
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2851297/
A Case of Gerstmann-Sträussler-Scheinker Disease
Min Jeong Park, MD, Hee Young Jo, MD, Sang-Myung Cheon, MD,
Sun Seob Choi, MD, Yong-Sun Kim, MD, and Jae Woo Kim, MD
J Clin Neurol. 2010 Mar; 6(1): 46–50.
LINK 2: https://rarediseases.org/rare-diseases/gerstmann-syndrome/
2019-02
LINK 3: https://en.wikipedia.org/wiki/Gerstmann
%E2%80%93Str%C3%A4ussler%E2%80%93Scheinker_syndrome
last edited on 21 March 2019
LINK 4: https://rarediseases.info.nih.gov/diseases/
7690/gerstmann-straussler-scheinker-disease
Last updated: 7/11/2016
LINK 5: GTR - Genetic Testing Registry
https://www.ncbi.nlm.nih.gov/gtr/conditions/C0017495/
22 tests
GSS is a rare genetic form of TSE (transmissible spongiform encephalopathy) that was originally described in a large Austrian family.
The overall disease duration may last several months to several years (median 5 years). Onset may occur as early as 25 years.
The syndrome was first described in 1936 by the Austrian neurologists Josef Gerstmann (1887-1969), Ernst Sträussler (1872-1959), and I. Scheinker.
GSS (may) have many different gene mutation types, with some showing different symptoms first or having other symptoms worse than others. Doctors in different parts of the world are uncovering more generations and families that have the mutation. It is hard to discover GSS for two main reasons:
(1) the disease has been reported in only a few countries; and
(2) the disease may be underreported due to its clinical similarity to other diseases.
Symptoms.
- loss of memory,
- a P102L (proline-to-leucine) mutation in codon 102,
- awareness is diminished,
- involuntary movement of the eyes,
- cognitive decline,
- clumsiness,
- unsteadiness,
- difficulty in walking,
- uncooperative,
- speech disturbance,
- a slowly progressive ataxic gait,
- Lack of coordination in swallowing,
- weakness in the legs,
- poor reflexes,
- abnormal sensations,
- mimicking chewing,
- fidgeting,
- severe dementia,
- confused states,
- blindness,
- deafness,
- coma,
- death.
In a Korean patient, 2 sisters out of 7 siblings developed similar symptoms in their 4th and 5th decades, respectively, and both expired approximately 5 years after the onset of symptoms. A gene study revealed that two of her three children carried the same mutation.
PRNP analysis revealed a proline-to-leucine (P102L) mutation in codon 102.
The EUROCJD collaborative surveillance project found that nearly 50% of GSS cases were positive for the 14-3-3 protein in CSF.
Previous studies found that the usual neuro-imaging findings for GSS may be normal or show non-specific atrophy affecting the cerebral hemispheres and/or cerebellum and, rarely, decreased T2-weighted signal changes in the basal ganglia. Only a few studies have found abnormally high signal intensities in DWI of the cerebral cortex in GSS.
... although it is a very rare human prion disease, GSS should be considered in the differential diagnosis when hereditary cerebellar ataxia and progressive cognitive decline develops. Unlike CJD, GSS is characterized by long periods of illness, and dementia develops late in the course of the illness.
Gerstmann syndrome is a rare neurological disorder that can occur as the result of a brain injury or as a developmental disorder. The syndrome is characterized by the loss or absence of four cognitive abilities-
- the loss of the ability to express thoughts in writing (agraphia, dysgraphia),
- to perform simple arithmetic problems (acalculia),
- to recognize or indicate one's own or another's fingers (finger agnosia), and
- to distinguish between the right and left sides of one's body.
Additional cognitive defects may occur in some cases.
The disorder has not been found to run in families.
In extremely rare cases, children who are bright and functioning intellectually at a high level may be affected by the disorder as well as those who suffer brain damage.
Gerstmann syndrome is different from Gerstmann-Sträussler-Scheinker syndrome, a rare genetic degenerative brain disorder.
A few cases have been reported in children and called developmental Gerstmann syndrome.
These cases usually become apparent when children begin school. Affected children may demonstrate poor handwriting, spelling and math skills (e.g., difficulty adding, subtracting, dividing and multiplying). Some children have difficulty reading or understanding written words (alexia) and difficulty copying or tracing simple objects (constructional apraxia).
The disorder was first described by Dr. Josef Gerstmann, a Viennese neurologist, in 1924.
In adults, the syndrome can arise in adults as a result of impaired blood flow to the brain (cerebrovascular disease) such as a stroke or other damage to the brain. The parietal lobes (upper side lobes) of the brain are affected in Gerstmann syndrome. The parietal lobes are involved with sensation and perception as well as understanding sensory input.
In rare cases, traumatic brain injury or a brain tumor in the same region of the brain can cause the various symptoms associated with Gerstmann syndrome.
Disease: Fatal familial insomnia (FFI).
INDEX
https://rarediseases.info.nih.gov/diseases/6429/fatal-familial-insomnia
Last updated: 6/1/2019
LINK 2: https://en.wikipedia.org/wiki/Fatal_insomnia
Last updated: June 03, 2019 --- by various contributors
LINK 3: http://www.bbc.com/future/story/
20160118-the-tragic-fate-of-the-people-who-stop-sleeping
By David Robson --- 19 January 2016
FFI (most often) begins as a sudden and unexplained sleeplessness sometime during middle age.
As this is after the childrearing years, most sufferers have already passed on the (prion) to their children.
Because Fatal Familial Insomnia is genetic, there is a 50% chance of a parent passing it on to their offspring.
Like all prion diseases, FFI is a progressive neurodegenerative disease, which means over time there are fewer neurons.
... recent studies have found a direct correlation between Alzheimer's, sleep loss, and the formation of amyloid plaques in the brain.
In FFI, prions (disintegrate) the thalamus region of the brain, responsible for regulating sleep and various sensory and motor systems, replacing it with amyloid plaques. The thalamus manages our sleep/wake cycle; the flow of visual, auditory, and motor information; our sense of balance; how we experience pain; aspects of learning, memory, speech and understanding language; and even emotional experiences, expression, and our personalities.
This increasingly prevents the sufferer from losing consciousness - although their EEG readings show signs associated with REM sleep during waking hours. They are so sleep deprived, they are dreaming while awake.
Fatal insomnia has two forms:
Familial: This form, called fatal familial insomnia, is inherited.
It is due to a specific mutation in the gene for a normal protein called cellular prion protein (PrPC).
Sporadic: This form occurs spontaneously, without a genetic mutation.
In fatal familial insomnia, symptoms may begin in a person's late 20s to the early 70s (average is 40 years).
Death usually occurs 7 to 73 months after symptoms begin.
The sporadic form begins slightly later, and life expectancy is slightly longer.
The first symptoms of fatal familial insomnia (FFI) usually begin between the ages of 32 and 62 (mean average 51 years), but have been reported to begin as early as 18 to as late as 72.
Symptoms.
(Beginning with)
- sweating ...
- pupils (that) shrunk to two tiny black pinpricks ...
- a glassy-eyed stare ... followed by ...
- difficulty speaking,
- Tremors, muscle twitches,
- impotence and
- constipation ...
- disappearance of sleep – almost total insomnia for months;
- loss of appetite,
- Sphincter disturbances,
- Hallucinations,
- fever,
- anxiety,
- confused states,
- a kind of waking coma that ultimately would end in
- death.
One of the most tragic aspects of FFI is that though the sufferer shows signs of dementia, they have a clear understanding of what is happening to them, while enduring the physical agony of total sleeplessness.
(He) drew me his genealogical tree from the 18th Century, all by heart.” In each generation, Silvano could name family members who had succumbed to the same fate. (related to) a misshapen protein in the brain called a prion, caused by a tiny genetic mutation. For some reason it is only at middle age that the prions begin to proliferate wildly, collecting in pockets that poison the neurons. (It) seems to target parts of the thalamus, at the very centre of the skull. Normally the size and shape of a walnut, the thalamus in Silvano’s brain appeared to have been riddled with boring worms.
(The thalamus) this hub orchestrates all our “autonomic” responses to the environment – things like temperature control, blood pressure, heart rate, and the release of hormones to keep the body ticking over comfortably. When it breaks down, it is as if your central heating is going haywire, your water pipes have sprung a leak, your windows are wide open and your loudspeakers are blaring at full volume – everything is in chaos. Hence the profuse sweating and shrunken pupils, the impotence and the constipation. This erratic autonomic control could also contribute to the patients’ insomnia: their bodies can’t prepare for a night’s sleep. Where blood pressure typically drops before sleep, theirs would be abnormally high, for instance, giving the sensation that their body is still on high alert. “If the sympathetic nervous system is unbalanced, of course you’ve got insomnia,” says Pietro Cortelli, a doctor.
Disease: Kuru
INDEX
Prion Diseases as Transmissible Zoonotic Diseases.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747681/
Osong Public Health Res Perspect. 2013 Feb; 4(1): 57–66.
Jeongmin Lee, Su Yeon Kim, Kyu Jam Hwang, Young Ran Ju, and Hee-Jong Wooa
2013 Feb 4
LINK 2: https://www.rightdiagnosis.com/k/kuru/basics.htm
LINK 3: https://www.ninds.nih.gov/Disorders/All-Disorders/Kuru-Information-Page
An endemic disease similar to CJD was found in cannibal tribes (such as the Fore, Gimi, and Yate in Papua New Guinea) who used to eat the dead bodies of their relatives as part of their rituals. This endemic disease, called kuru (meaning “shiver” in Uruna or Guzigli, among other tribes), was first reported in 1957. At that time, the cause could not be identified, so people assumed that the disease was caused by an unknown virus. However, ever since cannibalism was banned, the incidence of kuru decreased sharply.
Kuru is a prion disease found exclusively among the Fore linguistic group natives of the highlands of NEW GUINEA.
The illness is primarily restricted to adult females and children of both sexes. It is marked by the subacute onset of tremor and ataxia followed by motor weakness and incontinence. Death occurs within 3-6 months of disease onset. The condition is associated with ritual cannibalism, and has become rare since this practice has been discontinued. Pathologic features include a noninflammatory loss of neurons that is most prominent in the cerebellum, glial proliferation, and amyloid plaques. (From Adams et al., Principles of Neurology, 6th ed, p 773)
Symptoms.
- Joint pain
- Headaches
- Fevers
- Shivers
- Slurred speech,
- Mood changes,
- Incontinence,
- Loss of coordination
- Paralysis,
- Coma,
- Death.
Brain tissue from individuals with kuru was highly infectious.
Similar to other the TSEs, kuru had a long incubation period; it was years or even decades before an infected person showed symptoms. Because kuru mainly affected the cerebellum, which is responsible for coordination, the usual first symptoms were an unsteady gait, tremors, and slurred speech. (Kuru is the Fore word for shiver.) Unlike most of the other TSEs, dementia was either minimal or absent. Mood changes were often present. Eventually, individuals became unable to stand or eat, and they died in a comatose state from 6 to 12 months after the first appearance of symptoms.
Disease: Scrapie in sheep
INDEX
Prion Diseases as Transmissible Zoonotic Diseases.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747681/
Osong Public Health Res Perspect. 2013 Feb; 4(1): 57–66.
Jeongmin Lee, Su Yeon Kim, Kyu Jam Hwang, Young Ran Ju, and Hee-Jong Wooa
2013 Feb 4
In 1732, scrapie -- a disease among sheep -- was first reported in the UK, affecting the wool industry.
The official name for the disease (scrapie) was used from 1853 onward. The name scrapie is derived from one of the clinical signs of the condition, wherein the affected flock will compulsively scrape off their fleece against rocks, trees, or fences. The disease apparently causes an itching sensation in the animals. Other clinical signs include excessive lip smacking, altered gaits, and convulsive collapse. Fortunately, other livestock did not have such symptoms; therefore, it was only a concern among sheep-farming communities, and not among other people or other animal farmers.
In the 1900s, farmers in the UK started to feed cows with internal organs or bones of sheep to benefit economically from the increase in milk and meat production. By the 1930s, other European countries and the United States (USA) had adopted this practice. Based on the findings of epidemiological studies on the origin of BSE, this later became the main cause of prion disease transmission from sheep to cows across the species barrier.
As the PrPSc-inducing disease in sheep and cows is also found in other animals, TSE can be considered an inclusive term for the disease. TSE is subdivided into BSE for bovines, vCJD for humans, scrapie for sheep, chronic wasting disease (CWD) for deer, and transmissible mink encephalopathy for mink (Table 1); TSE is found in 26 species, including goats, cats, and wild ruminants. It is noteworthy that prion diseases among sheep and deer can be transmitted horizontally by saliva, unlike BSE or vCJD; CWD can even be transmitted via aerosols, according to a recent animal experiment report.
Disease: Chronic Wasting Disease (CWD) in deer
INDEX
http://cwd-info.org/faq/ ---
LINK 2: https://www.usnews.com/news/healthiest-communities/articles/
2019-02-25/chronic-wasting-disease-risk-very-high-of-transmission-to-humans
By Joseph P. Williams Staff Writer
Feb 26, 2019
LINK 3: https://facty.com/ailments/body/
frequently-asked-questions-about-chronic-wasting-disease/....
By Sarika, Faculty Staff ---- Updated: May 24, 2018
LINK 4: https://en.wikipedia.org/wiki/Chronic_wasting_disease
by various contributors --- May 23, 2019
Chronic wasting disease (CWD) is a prion disease affecting cervids, the deer family, and ...
In the US, CWD affects mule deer, white-tailed deer, elk (or "wapiti"), moose, caribou, and reindeer.
CWD can affect animals of all ages and some infected animals may die without ever developing the disease.
Experimental transmission of CWD to other species, such as squirrel, monkeys and genetically modified mice has been shown.
In 1967, CWD was first identified in mule deer at a wildlife research facility in northern Colorado, United States. It was initially recognized as a clinical "wasting" syndrome and then in 1978, it was identified more specifically as a TSE disease. Since then, CWD has been found in free-ranging and captive animal populations in 26 US states and three Canadian provinces. In addition, CWD has been found in one wild reindeer herd in Norway (March 2016) as well as sporadic cases in wild moose and one red deer. Single cases of CWD in moose have been found in Finland (March 2018) and in Sweden (March and May 2019). CWD was found in South Korea in some deer imported from Canada. CWD is typified by chronic weight and clinical signs compatible with brain lesions, aggravated over time, always leading to death.
As of March 6, 2019, there were 270 counties in 24 states with reported CWD in free-ranging cervids.
The clinical signs and symptoms of the disease alone aren't conclusive.
Also, there's currently no live animal test. Right now, the only definite diagnosis would involve the examination of the tonsils, lymph nodes or brain of the infected animal and it's done after death.
Most cases of CWD occur in adult animals; the youngest animal to exhibit clinical symptoms of the disease was 15 months.
The disease is progressive and always fatal. The first signs are difficulties in movement. The most obvious and consistent clinical sign of CWD is weight loss over time. Behavioral changes also occur in the majority of cases, including decreased interactions with other animals, listlessness, lowering of the head, tremors, repetitive walking in set patterns, and nervousness. Excessive salivation and grinding of the teeth also are observed. Most deer show increased drinking and urination; the increased drinking and salivation may contribute to the spread of the disease.
The origin of CWD is unknown, and it may never be possible to definitively determine how or when CWD arose.
It was first recognized as a syndrome in captive mule deer held in wildlife research facilities in Colorado in the late 1960s, but it was not identified as a TSE until the 1970s. Computer modeling suggests the disease may have been present in free-ranging populations of mule deer for more than 40 years.
Environmental transmission has been linked to contact with infected bodily fluids and tissues, as well as contact with contaminated environments. Once in the environment, CWD prions may remain infectious for many years. Thus, decomposition of diseased carcasses, infected "gut piles" from hunters who field dress their cervid harvests, and the urine, saliva, feces, and antler velvet of infected individuals that are deposited in the environment, all have the potential to create infectious environmental reservoirs of CWD.
One avian scavenger, the American crow, was recently evaluated as a potential vector for CWD. As CWD prions remain viable after passing through the bird's digestive tract, crows represent a possible mechanism for the creation of environmental reservoirs of CWD. Additionally, the crows' extensive geographic range presents ample opportunities for them to come in contact with CWD. This, coupled with the population density and longevity of communal roosting sites in both urban and rural locations, suggests that the fecal deposits at roosting sites may represent a CWD environmental reservoir. Conservative estimates for crows' fecal deposits at one winter roosting site for one winter season ranged from 391,552 to 599,032 kg.
CWD prions adhere so tightly to soil surface particles that the ground becomes a source of infection and may be a major route of transmission due to frequent ground contact when cervids graze.
Cattle and other domestic livestock appear to be resistant to natural infection.
There are no reported cases of natural transmission of CWD from infected elk or deer to domestic livestock.
However, the disease has been experimentally reproduced in cattle by the direct injection of the infectious agent into their brains.
It's highly recommended not to consume any meat from animals which might have a chronic wasting disease.
So hunters in CWD areas should bone out the meat and not consume any of the animal's parts where the prions typically accumulate. Since there isn't enough information regarding the risk to humans, it's best to stay away from any infected animals. This is especially important since there are similarities between the human and the animals TSEs. So the hunters who harvest elk and deer in areas known to have CWD infections should take extra precautions to avoid exposure.
In the 1980s, Michael Osterholm was among a vanguard of public health scientists warning of a new, potentially deadly disease known as AIDS, and how gay men were at high risk. The next decade, he sounded the alarm about a mysterious neurological ailment showing up in cattle in the United Kingdom – nicknamed mad cow disease – and how scientific evidence indicated it could infect humans.
"I think the risk is very high" that CWD could emerge in humans exposed by eating infected deer meat,
says Osterholm, an epidemiologist, professor and director of the Center for Infectious Disease Research and Policy at the University of Minnesota. ...
it's "probable that human cases of CWD associated with the consumption of contaminated meat will be documented in the years ahead. It is possible that number of human cases will be substantial and will not be isolated events.”
I recall getting booed off the stage multiple times talking about the early days of HIV/AIDS in social and business groups, gay men's groups. They thought I was scaring the hell out of them needlessly, back in '83 and '84. I wrote a book in 2000 about bioterror, why it was going to become a huge problem. I think I bought eight of the 12 copies that were sold in 2000. After 9/11, it became a New York Times best-seller. I've been here before.
My job as an epidemiologist is not to be a historian and record history.
My job as an epidemiologist is to be an interventionist and change the future.
Disease: Bovine Spongiform Encephalopathy (BSE) in cattle
(commonly known as "mad cow disease")
INDEX
Prion Diseases as Transmissible Zoonotic Diseases.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3747681/
Osong Public Health Res Perspect. 2013 Feb; 4(1): 57–66.
Jeongmin Lee, Su Yeon Kim, Kyu Jam Hwang, Young Ran Ju, and Hee-Jong Wooa
2013 Feb 4
There are several theories regarding the cause of the first reported case of BSE in the mid-1980s; some insist that the BSE pathogen (PrPSc) formed naturally and others claim that the disease was caused by the cow feed made from sheep infected with scrapie. By an extensive epidemiologic investigation, the main cause for BSE turned out to be a meat and bone meal (MBM) made from the discarded bones and intestines of slaughtered cows and sheep. In the UK, in particular, cow intestines have been used in MBM as a protein supplement since 1972, which accelerated the increase of the occurrence of BSE.
BSE has occurred in European countries that import MBM from the UK; according to statistics from the World Organization for Animal Health (Office International des Epizooties; OIE), there have been 190,628 BSE cases in 25 countries worldwide as of August 30, 2012 (http://www.oie.int). Most reported cases are from the UK, peaking in 1992, and in other countries the epidemic peaked in 2002 or 2003; from then the number started to decrease sharply.
BSE is a chronic degenerative neurological disease in cows; part of the brain becomes sponge like, and exhibits many different kinds of neurotic symptoms and paralysis, eventually leading to death. In BSE, nerve cells and central nerve tissues take on a sponge-like form. After approximately 2–5 years of incubation, the animal dies within approximately 2 weeks to 6 months of development of the disease. Clinical symptoms include extreme sensitivity to external stimuli such as light and sound, neurotic changes (depression and nervousness), positional imbalance, inability to stand straight or move, paralysis in the hind legs, and paralysis of the whole body before death.
At present, BSE is under surveillance by the OIE; in Korea, it is classified as a second category of animal epidemics along with scrapie and CWD. BSE has no effect on the cattle younger than 7 months old; by the time cows reach 24 months of age, there are many variant prions in the body. Most occurrences of BSE are in cows older than 36 months. Therefore, the OIE examines the occurrence of BSE in 24-month-old cows.
In the UK, more than 184,000 cases of BSE have been reported and more than 3 million cows were destroyed to stop the spread of the disease; hence, the UK strictly banned MBM. Owing to their efforts, the occurrence of BSE was dramatically reduced. However, since the 2000s, the disease has been spreading worldwide, including in the USA, Japan, Israel, and various African countries. Determining the precise number of occurrences is challenging, as some infected animals do not exhibit any particular symptoms. Without total inspection and surveillance, it is difficult to research the actual status of the disease.
However, some BSE cases have been reported even after stricter surveillance was put in place, which means that the disease is not controllable by monitoring animal feed alone. Some scientific evidence is given regarding this: pathogenic prions from the feces of TSE-infected
animal can be
absorbed into the soil,
can combine with minerals in the soil, and
can become stable.
... the possibility of transmission via a contaminated environment.
BSE-infected cows show the possibility of self-mutation of the BSE prion, since the prion gene that causes vCJD in humans, which had some mutations, was found in the brains of affected cows. This implies that a wide range of monitoring systems in DNA and/or protein levels is necessary in addition to a strict animal feed policy. Considering the transmission of BSE to humans, control SRM is the most important step to take. Based on recent findings on the relationship between SRM and the occurrence of the disease, the EU developed some guidelines in April 2008 for its member countries to follow regarding SRM. According to these guidelines, the tonsils, whole intestine, and mesenterium are all vulnerable to prions across all ages; the brains, eyes, spinal cords, and skulls of cows that are older than 12 months are considered to be SRM.
Some older cows have an atypical form of BSE (BASE), which differs from typical BSE with respect to its molecular and biochemical properties; it appears to be a sporadic BSE, although more precise etiological studies need to be performed for confirmation. Recently, attention has been given to BASE because of its infectivity and relation to vCJD.
Personal: Developmental and Pausing possibilities.
INDEX
As of June, 2019, we know a few details about each form of Transmissible Spongiform Encephalopathies [TSEs] and everything is theoretical (best guess - rational projection - spurious reasoning) about the factors which promote the development of this toxic substance, how to ameliorate its influence, and, possibly how to avoid it or recover from it. Even more basic, we humans have no easy and quick means of testing for its presence either in ourselves or in the environment around us.
As of June, 2019, I am over the age of 74.
I have experienced a fairly wide range of accidental injuries, ailments, high internal toxin rates, medical misjudgements, errors, and abandonments. I have worked at between 1 and 5 concurrent jobs since I was 8 years old. I was born with a high level of Energy Blocks (addiction-like patterns of reactive behavior and attitude) which I was fortunate to found a therapy to release and assist others in likewise changing their lives. I have seldom been unemployed and I found it necessary, for financial reasons, to retire earlier than desired because I had not earned enough income while ill with CFS-ME to qualify for disability insurance. I was medically diagnosed as having CFS-ME, but that was inadequate to qualify me for disability benefits!
Like most other challenges I have encountered, I found ways for myself to fully recover and that could assist others. Educationally, I was trained to be an engineer, customer service professional, sociologist, commercial salesperson, contractor, private investigator. Those built upon experiences of working in agriculture, mini-computer servicing, computer programming, and, conflict resolution. Hobbies additionally exposed me intensively to religions, organic gardening, housing design, carpentry, electrical wiring, plumbing design and installation, SCUBA and snorkeling, forensics, careers in health, and car repair. Professional guidance counselling in my late-20's affirmed that I had the skills, aptitude, and interests to fit perfectly in the additional fields of surgery, and police detective.
As of late May, 2019, after doing my best to cope with and recover from a multi-faceted medical disaster that began in 2016 or earlier, I found that I had a "prion" complication. I confirmed this by Spiritual Guidance (prayer-meditation) which with my developed skill has never been incorrect and has contributed to ALL of my recoveries, coping, and ability to assist hundreds of others. Prions had been glimpsed in my awareness earlier. This was the best time for me to research and build a monograph in accord with more recently publicly available research.
Speech Disturbance had gradually developed over a period of 12 months from late 2018.
I spoke with contacts on the phone on a daily basis, often for as long as 45 to 90 minutes.
Gradually, the duration that I could continue in the conversation diminished. I would SUDDENLY begin to find it difficult to recall words to finish sentences or phrases. Cognition of what I was hearing was unaffected. Cognition of what I was going to say to reply, acknowledge, or provide feedback on remained CLEAR. I KNEW what I was going to say, but, the words became LOST between my Consciousness and my speech. This active duration time slide down from almost unlimited to 10 minutes. It became necessary for me to mention to and remind frequent contacts that I would only be able to be on the phone for 10 minutes maximum per call. This INTERRUPTION of Speech was neither longer lasting, or, gradual. In most instances, 30 minutes off out of the conversation and everything was back to normal. The INTERRUPTION came suddenly and seemed to almost leave as suddenly. Activation of some neural sequences or brain areas triggered the Interruption. Unlike a stroke, blood clot, or something of that nature ... the Interruptions were CONSISTENT in expression, SUDDEN in activation and exit, and near TOTAL in functional break.
Writing-Typing neural losses appeared SUDDENLY in early April, 2022.
Changes appeared within a 24 hour period and have remained constant since April 01.
Particularly during the past 3 decades I have used a computer to type HTML code and content into hundreds of contact Profiles (which require updating), Health oriented and other Reports, and for e-mails and social media. While I sometimes find it necessary to correct the rare spelling mistake or grammatical error ... THIS was entirely unlike anything I had personally experienced, or, heard of anyone else encountering as a health neural aberration. While typing I would miss a SPACE between words and miss a character in the spelling of a word .. in almost every sentence. This has remained constant with no indication of it becoming more frequent or less. Neither do the BREAKAGES have any consistency in terms of words, phrases, position on the page, or how long I have been working. They begin when I begin; they end when I end. The dynamic is NOT associated with any of the other diseases I note above in any medical literature. They are associated, by way of Spiritual Guidance, with Prion sourced neural damage.
I will note a number of factors which have contributed to my own development of this prion reality.
These factors may be considered as possibilities for future research, as possible options for others with prion illnesses, and, as caution choices and decisions for those not yet so encumbered. Fortunately, I was divinely Gifted (as we all are) with Basic Personality strength. Mine are in learning, spirituality, interacting with others, truth, and action. Dealing directly with the subjects of interest, and often facing disability or death as a consequence of failure to resolve ... I was motivated. I did the research which doctors had no enthusiasm or encouragement to do, and, which technician scientists lacked any personal connection to. Persistence was elementary and refreshed by my Choice to work with God and continually be directed to sources and options which were always RELEVANT and often led to new realizations and appreciations.
-
Heavy metal toxicities.
Throughout the 1990s I encountered several instances of Mercury toxicity from dental amalgams which were almost fatal. Each time I detoxed and fully recovered. In 2012, unknown to me at the time, I acquired another presence of Mercury toxicity. This time, I would confirm in 2017 that it was accompanied by multiple HIGH levels of other metal toxins including aluminum, copper, lead, gadolininium, uranium. ALL heavy metals have the side effect of cellular and genetic MUTATION. No one recovers from a mutation. They cannot be reversed. Further mutations may lead to better or worse results. Best, is to remove the source, detox the presence, and cope with any mutations that have occurred. Prion development is connected with heavy metal presence. Heavy metal environment pollution (air, water, soil, food, medicine) is endemic in any industrialized region and many commercialized economies.
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Significant Virus exposures.
I have been exposed to 6 severe viral exposures including one in 2012.
Like all of my peers, I acquired, in early public school (1950s) measles, mumps, chickenpox (all in the same Spring) , many colds, several bouts of tonsilitis, and a few flu -- which don't enter the realm of severe here. Severe means that I had symptoms which forced me to stay in bed by symptoms of weakness, disorientation, headache, fever, etc. I never went to a doctor for assistance with these once I had experienced their consistent lack of diagnostic and treatment options, and found that there were no drugs recognized as effective against viruses. Several times I had been prescribed antibiotics ... which we all learned later were ineffective against viruses and often encouraged a disruption of healthy internal bacteria colonies. A VIRUS is a known factor in the catalyzing of GMO and heavy metal mutations into cells and tissues.
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Systemic fungal infections.
During my earlier hypersensitivities experiences in the early 1990s, I had developed a systemic presence of Candida Albicans. I learned how to eliminate it and the hypersensitivities ... both of which healthcare professionals of the time informed me was permanent. The incidences of mercury poisoning were not helpful in this regard as it also encourages pathogenic bacteria and fungi, including Candida Albicans. By 2015, I had not had any presence of Candida Albicans in 12 years. Now, I acquired something greatly different, Aspergillosis. I was already experiencing colon problems from a minor anal surgery gone bad. A significant change in lifestyle led to my working an average of 80 hours per week at a largely sedentary voluntary job involving internet-based research, international voice communication, and political conflict awareness and resolution. ALL of these resulted in minimal exercise and minimal flexing of my intestines. Suddenly, by the Fall of 2016, it became necessary for me to DAILY cleanse my colon with enemas when my intestinal peristalsis stopped. The alternative, almost reached a number of times, would be auto-toxicity from retention of stool, resulting in decreasing consciousness to eventual coma. If that were allowed, death would follow.
The lack of intestinal peristalsis, not even influenced by TWO pharmaceutical Fleet intestinal flush kits used together, provided a perfect environment for fungal development. Aspergillosis overgrowth followed. An inability to raise any medical interest in resolving the situation, and, my own ignorance and distraction with other issues led to it becoming systemic. That usually only happens when one has cancer and the aspergillosis blocks the intestines and the patient dies from auto-toxicity, not cancer. The only way that I have found to release an aspergillosis block that has cemented shut an intestinal valve or sphincter (to allow stool to flow) is a drug named Manerix which enhances serotonin. A MEDICAL research report I found and kept while researching Candida noted that Manerix, specifically was anti-aspergillosis. From early 2016 through to the Spring of 2019, Manerix in Spiritually Guided doses would result in the release of an aspergillosis blockage in anywhere from 1 to 4 hours. I had for a long time tested as having a High level of magnesium, so, I never considered that I might benefit from a supplement. Early in 2019, I also found that HIGH doses of Magnesium would also assist in my releasing of Aspergillosis blockages.
If one's intestines are working normally, one has periodic peristaltic action daily to transfer digestive fluids and nutrients from one section of the small intestine to the next one. There are FEW causes for an almost immediate loss of intestinal peristalsis. One, is a blockage. This is a temporary and largely non-repetitive experience. A bolus of parasites is a potentially more continual one. I had experienced several different intestinal parasite infestations in the past. None had developed to a bolus blockage stage and they had been totally eradicated. None could be found now either by the tests available to me or by following intensive anti-parasitic protocols.
Genetic modification of intestinal tissues by exposure to GMO foods had become a known and well reported problem in India where water buffalo, fed GMO feed could die within 24 hours from sudden intestinal blockage. Their intestinal tissues and function were being modified on an immediate exposure basis. It is becoming difficult for anyone living in an urban area, purchasing imported foods, not to eat GMO foodstuffs. Not every meal of a GMO food will result in a genetic modification. And, combinations of GMO foods may further encourage such mutations. It only takes ONE mutation out of 1000s of exposures to change tissue performance, forever. Prions are also known to take their first hold on the body from the small intestine. They may modify the tissue and function there and yet not progress to neuroinvasion for decades. We cannot test efficiently for prions in us, in foods, on foods. It may be that Genetically Modified Foods can sponsor a prion creation as a mutation once the mutated food mutates tissues in the intestine.
-
Slime mold -- Biofilm -- Rope Worms.
Slime molds are nature's way of reintegrating the nutrients in dead plant and animal tissues back into the soil for uptake by lifeforms. Their home environment is darkness, moisture, a static physical base, and undigested or predigested (by bacteria and fungi and enzymes) foods and tissues. Within body systems, slime molds develop into biofilms which tend to coat parts of the walls of the intestines. They engulf parts of digestive material, bacteria, viruses ... and protect them from further attention from either the immune system or digestive juices and intestinal dynamics. When these formations are excreted, which is seldom even when they are present in mass, they present as rope-like or worm-like structures in one's toilet bowl. They further contribute to a lack of intestinal motility and are highly encouraged by the host having a largely sedentary lifestyle, eating processed foods, having a diet with a grain biased carbohydrate base, having significantly compromised intestinal function by the significant influence of heavy metals, and not having a regular input of herbs or nutritionals which have a strong BITTER flavor. Many North Americans fit this profile, especially the 60% who are retired, underemployed or otherwise economically restricted, disabled, addicted, depressed, and/or socially obsessed.
After 1977, my previously very physically ACTIVE lifestyle continually declined into increasing sedentariness.
I went to university after working for 12 years. I followed that with careers in sales which involved much interpersonal contact, continual study, and minimal physical activity. Then came 25 years of increasingly intensive development of and provision of Balancing Therapy with demanding and long sessions of preparation followed by long, calm, interactions with clients. A 5-year stint with CFS-ME diminished minimal physical activity to near nothing activity. That was followed by about 4 years of re-integrating my life and delving intensively into a sedentary lifestyle of spiritually focused intellectual and research urgency for an average of 80 hours weekly to influence a decrease in global political conflict. During this later endeavor, my intestinal peristaltic activity ceased. It would be a further several years before I became aware of my having a HIGH level of multiple heavy metals and toxins and the mutational realities of those and some GMO foods on my intestinal tissues. Following an intensive detoxing period of over a year, I then began to excrete rope worm biofilms.
The ropeworm biofilms had likely been present for an extended period.
Present research and considerations on them suggest that people may harbor them for 40 or 50 years without even excreting any and becoming aware of them consciously. Other individuals have noted that they became obvious only after a detoxing of heavy metals and other toxins. Certainly, the intestinal dynamics including limited peristaltic activity, high levels of mutation enhancing heavy metals, occasional presence of potentially significant mutation enhancing genetically modified foods (GMOs), the experience of viruses capable of catalyzing the stability of a genetic transfer and modification, and, the mutational capability of overgrowth destructive fungal organisms presented an optimum environment for a prion tanglement.
-
Protozoa infection.
Through my more recent study of protozoan infections, it has become straightforward to consider that I have had several protozoan diseases which were elevated to systemic presence in early to mid-2017. They had been acquired at earlier times and left untreated, largely because the doctors available to me either minimized my definitive symptoms (denial, ignorance), and/or avoided running any diagnostic tests (laboratory, endoscopic, or other), resulting in them becoming systemic, and, promoting the further influence of the above factors. These diseases include
Giardiasis, Trichomoniasis, and Endolimax Nana.
As known, symptoms possible for any disease represent a spectrum of possibilities.
Some protozoa infected persons show NO symptoms, A few present a full range of symptoms. Most have symptoms that are highly personalized and restricted to those which are relevant to the disease, and, to the immune experience of the person. Combine this with a presence of multiple protozoan diseases and one may demonstrate a FEW symptoms suggestive of each illness together with compositional symptoms which are not usually indicative of any of the diseases present. Combine this reality with the presence of other pathogens and other mutational factors (see above) and we have an INTERNAL environment which is highly prone to cell and tissue mutation. Prions develop from mutations of cells or tissues in the intestine.
You may benefit from the knowledge in this monograph, from some of these Personal options, from some, or, you may deny and ignore all. It is your life and your health. It is also your choice and responsibility as to how many other persons have meaning for you and who you may assist.
Personal: Misinformed and Overlooked.
INDEX
It is late June, 2019 as I write this.
I have not yet fully recovered from the multiple health challenges that became disabling in mid-2016, but I have defined a number of them, eliminated some, significantly reduced others, and remained able to look after myself independently throughout the process. Here is a reflective BRIEF of how such a health disaster developed and how it has been diminished. As a REAL example of what can be, perhaps you can avoid something similar, cope with something less complex, and/or have the confidence that a partial or full recovery may be possible for something others will be confident to tell you that you will NEVER recover, or, respond to your requests for assistance (as they have MANY more resources) with blank questioning stares and suggestions that you are somehow weird because they don't have a simple explanation beyond a reactive prescription for what they have not made any scientific effort to diagnose.
The possibility of a Protozoan infection came late.
The main symptoms I had suggested the presence of something more "major", bigger, and more common.
The reality is that a protozoan infection can be major ... they kill people; it can be silent, chronic, or acute; it is considered by those familiar with protozoan diseases that EVERY person has one or two such infections ... which may remain with them for a lifetime (depending on how long you live). I may have been fortunate in not finding out about mine until more recently AFTER ridding myself with multiple other significant illnesses. Attempting to rid myself of a protozoan infection BEFORE lessening the influence of the other factors could have been terminal --- just too much of a challenge for anyone.
This life challenge of significant health distress began suddenly (within hours) in mid-2015.
During the early 1970s, I had an at work severe back injury, later fully recovered from.
After that, I was treated for "missing time" with a botched lumbar puncture leading to 30 hours of severe pain.
Beginning in mid-1970 and repeated in the early 1990s and early 2000s, I had been exposed to SEVERE whiplash injuries.
During the early 1980s I was earning a Combined Honors at university and studying neurophysiology & communications.
During the mid-1980s, I had acquired 36 hypersensitivities of which 4 were life threatening. I fully recovered.
During the 1990s and early 2000s I had experienced and recovered from 3 very HIGH levels of Mercury toxicity.
During the early 2000s, I suddenly acquired CFS-ME which took me 5 years to understand and recover fully from.
In late 2018, I had another severe lower back injury and this added a few more months of patience demanding delays.
In early 2019, I confirmed, by herbal use, that I had a long present enlarged prostate, adding to the blockage problems.
By early summer, I confirmed that I had at least one Prion illness infection and I could cope with it.
This, 2016 to mid-2019+ episode involved NO intestinal peristaltic action and a suddenly ballooning belly.
The mid-2016 symptoms put an end to the political conflict resolution volunteer work that had occupied me for an average of 80 hours per week, after a year and a half of intensive involvement. For the next year, I made preparation to die, move, or recover. Local medical and other affordable health resources proved unhelpful and discouraging. Options for diagnosis existed but those with the resources were restricted in their application by ignorance, educational inertia, institutional restraint and control, and my own financial resources preventing me from going to another country for more relevant assistance. In mid-2017, I moved to the southern part of the Canadian province of Alberta. A new start with the customary medical tests went nowhere. Exposure to both privately funded tests and their availability enabled me to research further and define several significant health challenging realities: HIGH levels of (toxic) heavy metals and HIGH toxic levels of other minerals. ANY of these are known to depress physiological functions (like peristalsis), encourage cell & tissue mutations (including cysts, tumors, cancers), and result in fatigue and lead to death.
I embarked on detoxing as fast as personally safely possible.
This process had to be interrupted a number of times to enable me to cope with and get past several SEVERE viral infections, an episode of Bartonella, a challenge of Hansen's Disease (leprosy), local infestations of cockroaches and bedbugs, and, an increasing presence of Aspergillosis which grew to become systemic. NONE of these were considered worth diagnosing nor medical problems by my doctor. Other doctors, if available, were restricted within the same bureaucratic attitudes, training, and denial --- not THEIR problem. Once these were out of the way, or severely reduced ... I discovered a ropeworm/biofilm infection which might have been present long-term. I also confirmed that PART of my belly sudden growth was likely due to an acute Potassium deficiency ... which usually is usually fatal, so had not been researched since the early 1950's! Once these were significantly reduced ... I got to Prions and Protozoan infections.
Following my Spiritually Guided (always found by me to be super scientific) daily best supplement, health device usage, and food choices, I passed a thick layer of FOAM onto the top of the toilet water in mid-June, 2019. I had begun to have periods of NORMAL passage of NORMAL pooh earlier in June. From this event, I have had NORMAL excretion activities ... even more often than I would prefer, since. The culprit was GIARDIA. With the physical weaknesses imposed on me by the earlier and other factors, the Giardia had taken an expanding residence of its own in my Small Intestine. It had contributed to the lack of peristaltic action ... which encouraged the aspergillosis and biofilm problems. I am not finished yet, but getting close to reacquiring the best health I can have, given my lifetime experiences, exposures, choices, and resources. I have (mid-2019) another protozoan infection to recover from, and, a Prion reality which can only be coped with. Together with those, I have the legacy of 22 Physical mutations that I have adjusted to over the years and presently, largely with dietary changes.
Balancing one's Reality.
During the Summer of 2022, it became clear to me that as long as I could continue to be INTELLECTUALLY Active on a daily basis and that such activity was challenging ... the further generation, spread, and neural disabling of prion presence and action was PAUSED. Eating more than a minimum of meat protein also encouraged further prion activity. Brain neurally challenging activity would encourage the replacement growth of new neural tissue. This was VERY difficult to sustain as the other disease symptoms I experienced almost all the time produced Fatigue and muscle weakness symptoms. Taking action to minimize these debilitating symptoms was RISKY for me, as what I could do to LESSEN the Pulmonary obstructions would also encourage the health, multiplication, and spread of the Echinococcus multilocularis .. which would destroy more organ tissues ... including eventually, brain tissue. Further REDUCTION of the previously HIGH levels of Heavy Metal toxins would also ease the WEAKENING influence they exerted on the Echinococcus multilocularis while possibly affording more Energy and Alertness. It thus became a BEST option to consciously PUSH brain activity, sometimes, when such felt impossible due to fatigue and weakness from the oxygen deprivation imposed by the Pulmonary blockages.
Wishing YOU a much easier and less costly health maintenance and recovery set of experiences.
Most often, it is our ignorance, lack of responsibility, denial, cultural imprinting, Energy Blocks, distorted medical institutions, and resources that bring us to disability, chronic illness, dependencies on others, and a premature death. You can remain part of that systemic reality of Failure, or, you can choose to be humble and revere God and work with God who wants the best available for you.
The current REALITY of Prions can be Horrifying, or, simply Informative.
"Horrifying" suggests that it will be imposed on you and that you can do nothing about it.
"Informative" conveys that it is a Danger which with knowledge can be minimized and coped with, to some degree.
YES, it is likely that 65% (as of mid-2019) of Americans, Canadians, Indians, Chileans, Pakistanis, Britons, French, Irish, Mexicans, and others in nations who import much food, sponsor companies who develop and promote GMO products, have medical systems which encourage the use of dental mercury amalgams, and have large nationally sanctioned armaments industries ... are infected with at least ONE Prion infection and one or more Protozoa infection.
We know also that these illnesses will NOT graduate into their ACUTE and largely debilitating stage (like diagnosed Alzheimer's) of presentation until they are triggered. Other substances and some experiences will be capable of Encouraging a Prion to be increasingly susceptible to a Trigger. And, those triggers may be nearly universal for a specific FORM of Prion, or, they may range anywhere in uniqueness to being triggered only by something universal, or, to something specific to the infected person. As Prions can transfer from almost any food, body fluid, water, air ... and are receptive to infection of any Earth living lifeform that is alive. It is not so much a case of IF you are infected, but WHEN. We also know that there is no known way of diagnosing dependably the presence of a prion presence in a LIVING entity, and, that there is NO likelihood of determining what could healthfully and effectively treat ANY of them beyond a notion of palliative care. Of course we do suspect that they could be eradicated by exposure to the heat of a Hydrogen Bomb solar plus heat burst ... which we have built more than enough to destroy most life on the Earth, excepting some insects.
So, how might we actually LIVE LIFE?
I provide you with an option which I have learned over the years.
Your SOUL is the memory impression which others have of you AFTER you die.
Support any and all efforts to hold others and the media responsible for making dramatic lies.
Do your best to treat others with Respect and provide them with Encouragement when Relevant.
Seek to establish a PERSONAL connection with God that enables you to receive ACCURATE Advice.
Do your Best every day with what resources are available to you to maintain and recover your health.
Do your Best to understand your enemies, seek to lessen their Pain, and be open to their possible Change.
Learn to Revere the Love of God who is always ready to Assist you and reflect that Love towards others.
Stop holding God responsible for mistakes YOU Chose to make without ever considering what God would have advised.
|
Comment: Prions as a result of human environmental contamination.
INDEX
Within human knowledge, prions did not exist until humans chose to adapt, in desperation to human overpopulation and high social densities, by an industrialization of herding, metallurgy, chemistry, agriculture, transportation, and food supply. This unnatural and unhealthy concentration of these resources included the introduction of life challenging components (pesticides, fungicides, bactericides, etc.) intended to preserve foodstuffs both during the growth, collection, packaging, transportation, preservation, storage, and preparation stages of their usage. Heavy metals and chemical toxins were a basic addition to this dynamic.
Heavy metals and chemical toxins have long been known in the healthcare field to mutate tissues and lifeforms.
Industry has been spurred on in its indiscriminate application and use by desperate competition within an economic structure which has rewarded symbolic entities (corporations, their shareholders, and their owners) for monopolization of various forms of production and marketing of foodstuffs and other products. This intra-market war dynamic has encouraged practices which focus on lower cost, high production practices with NO sincere concern for human or other lifeform health.
Pride and imprinted indoctrination of human authority structures together with a well intentioned yet God-less mutation of the human genome have driven human population expansion, and, wholesale destruction of the environment for the past 20,000 years ... variously referred to as human "history." The transition from normal periodic sexual lust (shared by all other animal life) to a constant form of lust (Aggression, Activity, Never Enough, Greed, theft, conflict, murder) has formed the growth and death of many "civilizations" throughout this period of more recent human presence. Most of these mass organizations of humans have created their own form of apocalyptic extinction by way of a compulsive utilization of technologies to provide concentration of resources without which they could not survive, or, with which they would self-destruct.
Authority dominated large human aggregations have built their power, wealth and presence on irrigation used in arid regions only to destroy the fertility of the soils by leaching the deep laden Salt to the surface. When a specific threshold of contamination was reached, surface soils became infertile. In other regions, irrigation was used to depress groundwater sources until the ever deepening water levels either became contaminated with arsenic or uranium, or, dried up. Herds-keepers travelling over vast distances to circulate their cattle from one lush resource to another came into conflict with colonizing agricultural settlers who raised fences, allotted ownership to land plots and eradicated the foraging itinerant freedom on which herding depended. Fishing villages and cultures experienced the death of their industry when overfishing and the lustful introduction of foreign species and GMO species devastated much of their fishing resources into extinction. The intensive and non-crop-rotating practice of agriculture has seen topsoil depths diminish from over 30 feet to less than a foot in a space of 300 years rather than the growth base being conserved. Industry has been transferred from origin locations to foreign countries with lower wages and standards of living to thus leave the industry pioneers destitute and unemployed. A constant inability to appreciate and respect ecological balance in favor of short term wealth continually results in environmental collapse.
Prions are an extension of the heavy metal mutation of biological structures (bacteria, fungus, virus, tissue cells) into incomplete and twisted structures. These broken structures, no longer possessing a gene-based pattern of replication towards a determined and finite structure, simply replicate incessantly toward a completion form ... which doesn't exist. They have no mature, adult lifeform target. Yet, most often, their initial replicating form is restrained by a missing catalyst - a trigger which completes their "invasive" abilities. Once this missing key arrives within the infected organism, the prion expands its presence into that of a disease. Once exposed, there is NO recovery. This interim PAUSE duration is now known to be capable of lasting anywhere from days to decades and may be considered as possibly ranging between 7 days and 7 decades, depending upon what the individual is exposed to, or chooses to be exposed to.
Prions are known to originate in industrialized food production dynamics as well as in lifeforms exposed to polluted environments. At present (2019-07) prions are present in potential food products including beef, sheep, pork, chicken, fish, deer, some tuber vegetables, and, many mass produced grains. As there is no means of detecting the presence of prions in foodstuffs and on other lifeforms before the disease stage, the likelihood of a present endemic spread and contamination of humans by prions is HIGH. With no known consistent means of treatment and no dependable means of diagnosis most of commerce exposed humanity will be infected by one or more prions by the year 2030. The expression of these prions into neurodegenerative diseases will possibly present, anytime from Now to the year 2100, if, humans do not become extinct from other means in the interim. Like the dead and dying civilizations before us, we have forced into existence a means for our extinction through our proud irreverent actions which betray a belief that we are more powerful than the God of creation.
Disease: Finding Assistance; Recovery Efforts.
INDEX
https://rarediseases.info.nih.gov/diseases/6429/fatal-familial-insomnia
Last updated: 6/1/2019
1-888-205-2311 --- Information Specialist
LINK 2: NIND, NIH Factsheet.
https://www.ninds.nih.gov/Disorders/Patient-Caregiver-Education/
Fact-Sheets/Creutzfeldt-Jakob-Disease-Fact-Sheet
Date last modified: Tue, 2019-05-14
Prepared by:
Office of Communications and Public Liaison
National Institute of Neurological Disorders and Stroke
National Institutes of Health
Bethesda, MD 20892
If you can’t find a specialist in your local area, try contacting national or international specialists.
They may be able to refer you to someone they know through conferences or research efforts.
Some specialists may be willing to consult with you or your local doctors over the phone or by email if you can't travel to them for care.
You can find more tips in our guide, How to Find a Disease Specialist.
To find a medical professional who specializes in genetics, you can ask your doctor for a referral or you can search for one yourself.
Many disease advocacy organizations have medical advisory boards, physician locator services, or patient networks, all of which may help you find a healthcare professional who is familiar with a particular condition. You can search for a condition on this website to find related disease advocacy organizations. These would be located in the "Organizations" section. If you don’t find a specific group, search the Genetic Alliance and the National Organization for Rare Disorders (NORD) websites.
Published resources provide another way to find a specialist for a particular condition.
Experts are often called upon to contribute to online publications such as GeneReviews, NORD, and Medscape Reference.
Many of these resources list the author’s name and institution and may provide an e-mail address or phone number.
You can also search the medical literature to find healthcare professionals or researchers who have published recent articles or case reports on a particular condition. You can find relevant articles through PubMed, a searchable database of biomedical journal articles. Although not all of the articles are available online for free, most articles listed in PubMed have a summary/abstract available. In addition, contact information for one of the authors may be listed. On the Results page, select "Abstract" under Display Settings to view information about the authors.
Online directories.
LINK: American College of Medical Genetics
http://www.acmg.net/ACMG/Genetic_Services_Directory_Search.aspx
LINK: Clinical Trials
http://www.clinicaltrials.gov/
LINK: Creutzfeldt-Jakob Disease Foundation
3634 W. Market Street, Suite 110
Akron, OH 44333
HelpLine: 1-800-659-1991
help@cjdfoundation.org
LINK: Genetic Alliance
http://geneticalliance.org/diseaseinfosearch
LINK: GeneReviews, https://www.ncbi.nlm.nih.gov/books/NBK1116/
LINK: Genetics Testing Registry (of laboratories)
http://www.ncbi.nlm.nih.gov/gtr/
LINK: MedlinePlus
http://www.nlm.nih.gov/medlineplus/directories.html
LINK: NORD - National Organization for Rare Diseases.
http://rarediseases.org/for-patients-and-families/
connect-others/find-patient-organization/
LINK: National Society of Genetic Counselors.
https://www.findageneticcounselor.com/
LINK: PubMed, http://www.ncbi.nlm.nih.gov/pubmed
LINK: American Society for Human Genetics
http://www.ashg.org/pages/member_search.shtml
You may want to consider contacting a doctor at a university health center in your area, since university health centers tend to have the latest technology and treatments. University health centers have doctors who are involved in clinical trials and who may work together with others to diagnose and treat patients.
Caution: Gelatin production & Use and Prions.
INDEX
https://amazinghealth.com/AH-health-pork-gelatin-protein-prion
Getting the Pork Out
by Christine Peck --- Jun 22, 2009
LINK 2: https://www.
http://www.mad-cow.org/~tom/gel_Roland.html
By Roland Heynke, Germany --- 14 October 1996
LINK 3: https://www.chop.edu/centers-programs/vaccine-education-center/
vaccines-and-other-conditions/vaccines-mad-cow-disease
Children's Hospital of Philadelphia, (CHOP)
The Vaccine Education Center --- 1-800-879-2467
3401 Civic Center Blvd., Philadelphia, PA 19104
Reviewed by Paul A. Offit, MD, Lori Handy, MD, MSCE on February 08, 2018
LINK 4: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3330701/
Prion Protein Misfolding.
Curr Mol Med. 2009 Sep; 9(7): 826–835.
by L Kupfer, W Hinrichs, and M.H Groschup
Where does (Gelatin) come from?
Gelatin is manufactured from collagen derived from animal carcasses.
Leiner Davis Gelatin in Davenport, Iowa claims to have the largest gelatin manufacturing plant in the northern hemisphere. Their website states that they use the skin of pork and beef to make gelatin. The Gelatine Manufacturers of Europe website claims that they also use the bones of these animals.
The raw material in gelatin production.
About 65 % of the world-wide produced gelatin comes from hidesplits, connective tissue and the bones of cattle.
Otherwise pigs serve for source material. Only in Australia, South Africa and New Zealand also sheep are used. The quality of the gelatin is influenced by the source of supply, which in Europe traditionally is mainly from pigs in the case of gelatin for food and medicaments.
There is such a huge demand of raw material, that a limitation to very young or especially natural living animals is not possible. But at least in Germany only slaughter wastes from animals, which are released for human consumption, are used for the production of gelatin for food and medicaments. Because however, up to now BSE can only be diagnosed very lately, most of the infected animals are not identified. Thus the veterinarian's check-up before slaughtering does not provide a remarkable protection against BSE and scrapie.
It is (a direct expectation), that hidesplits, connective tissues and bones of BSE-infected animals are far less infectious than the central nervous system. But as long as the agents are not definitely identified and not detectable by any sensitive test, not any tissue and body liquid can seriously be declared free of infectivity. Skin and bones from infected animals must also be supposed to be infectious, because they are well supplied with blood and nerves. The infectivity of blood has been demonstrated as early as 1962 with a goat and among others in 1992 with human beings. That this did not work with cattle until now, is due to the very low sensitivity of the common functional test and absolutely insufficient efforts made in this concern.
The 10-15 kg raw material from one cow (becomes a part of) production batches of 20,000 to 100,000 kg.
(The batch of gelatin) is then (further) diluted with other gelatin about (a) factor 10-100 to achieve the final products. Thus the agent is certainly diluted to a great extent, but at the same time it is distributed to a very large number of end products. (This makes testing for Prion Presence almost ridiculously impossible.)
What is it used in?
Gelatin is used in a variety of ways by the food industries.
According to Leiner Davis Gelatin, it can be used as a gelling agent, thickener, film former, adhesive agent, stabilizer, or whipping agent. Another website states that gelatin is used in hard capsules, soft gels, plasma expanders, tablet binders and coatings, and vaccine stabilizers as well as numerous consumer food applications. The Gelatine Manufacturers of Europe website also indicates the major food uses for gelatin are jelly, bakery, meat products, fish products, confectionery, ice cream, alcoholic and soft drinks, dairy products, and yellow fats and spreads.
So, general(ly) speaking, gelatin may be an ingredient in any processed food product on the market today, especially those with a chewy consistency or requiring thickeners and gravies. They are often listed as mono- and diglycerides on nutrition labels. ...
Gelatin also has other food application such as gelling of canned seafood products; micro-encapsulation of flavors, colors, and vitamins; stabilizing of cream fillings for frozen baked products; protein enrichment of foods such as beverages and dietetic products; film forming in panned chewing gum varieties; coating of fruits meats and delicatessen items; thickening and emulsifying soups, sauces, and gravies; and thickening and stabilizing low fat mayonnaise and salad dressing. ...
Viral vaccines are weakened forms of natural viruses.
Some viral vaccines are made by "growing" viruses in specialized cells in the laboratory.
Many growth factors are needed for cells to grow. An excellent source of these growth factors is serum obtained from the fetuses of cows (known as fetal bovine serum). Fetal bovine serum is a naturally filtered source of growth factors. The natural filter is the bovine placenta. Whereas the human placenta contains one-and-a-half layers that separate the mother's blood from fetal blood, the bovine placenta contains six layers. Many proteins are excluded from the bovine fetal circulation by these six layers (for example, bovine fetal blood contains 1/500th of the antibodies found in bovine maternal blood).
Another product from animals that may be used in vaccines is gelatin.
Gelatin is a protein formed by boiling skin or connective tissue. Gelatin is used to stabilize vaccines so that they remain effective after manufacture.
Prions in Gelatin
Prions are infectious substances made of protein.
They carry fatal diseases such as mad cow disease and Creutzfeldt-Jakob disease (CJD).
The American Food and Drug Administration has recently (2009?) raised concerns about the safety of gelatin as a food product in light of the spread of mad cow disease. Gelatin is manufactured at temperatures lower than 200°F, while it takes a temperature of 800°F (if temperature is a factor at all) to destroy the prion that causes mad cow disease.
Quality-tested wines, cider, apple juice and in some countries also beer, are freed from blurrings, tannin agent and bitter constituents with the help of gelatin. From fizzy drinks it is not removed at all. In milk-shakes with fruit or vegetable additives gelatin prevents the milk from curdling. Vegetable juices are thickened with gelatin and enriched with vitamins and minerals. In tinned meat gelatin binds the meat juice. In some cases salami and pepper sausage are protected from drying up by gelatin.
The pharmaceutical industries use gelatin in soft and hard medicament capsules, for binding in tablets and dragees, in form of sponges for treating wounds and as a colloid to expand the plasma after severe losses of blood. They are also included in vitamin compounds and cosmetics. People having problems with their nail growth or with their joints and cartilage are treated with gelatin. Animal food industries sometimes use gelatin in substitute milk products for calves.
As gelatin is so omnipresent, nobody in the industrial nations can avoid its assimilation.
Therefore even vegetarians have to doubt whether the production of gelatin from slaughter wastes of pigs and cattle totally removes BSE infectivity.
The mad cow disease prion is found most commonly in the central nervous system and bones of animals.
Nerve tissue reaches all parts of the body, including the skin. As well, there is no safety in being selective about the parts you eat because the butchering process slices the bone and smears its contents across the face of the cut produced.
It only takes one prion to start trouble.
Scientists have observed that a prion placed next to a normal protein will change the normal protein to a prion.
CJD cases from Britain show that it only takes 18 months for symptoms of mad cow disease to show up in humans who (have) eaten infected beef.
The Bottom Line
If you want to avoid pork in your food, don’t eat commercially manufactured foods.
Make your prepared dishes yourself. Make them from whole grains you cook yourself, legumes you prepare yourself, fresh and frozen vegetables, fresh fruits, and raw nuts and seeds you roast yourself.
Obtain your sweeteners from dates, raisins, honey, apples, and jams, jellies, and apple “butters” made from 100% fruit without additives (pectin and citric acid are okay; they come from fruits). If you must add gravies or thickeners, make your own from flours, water or nut milks, olive oil, and herbs. Nut creams, nut milks, and tofu work well as replacements for milk and milk products in gravies and sauces. Many dishes can be prepared ahead of time and placed in the freezer for quick use.
If you feel it’s too hard to make your favorite dishes from scratch, try changing your menu plan.
Train your palate to enjoy simple foods from natural sources, and your body will be healthier for it.
(Some) Nutritionists today advocate eating a diet of whole grains, vegetables, fruits, and nuts.
Eliminate sugary desserts, most commercially prepared cookies, and candy from your diet.
Replace them with (some) fresh fruit, but avoid eating fruits and vegetables in the same meal
(See The Health Message, Vol.1 no.7). Eat healthy and stay healthy!
Prion Safety in Food Production.
... Compared with the conditions during gelatin production, in experiments (Prions) withstood an acidity, which was 10 times as high, an alkaline concentration 20 times as high and a drying temperature that was about 220°C higher. ...
Apart from prion diseases, there are a number of other protein misfolding diseases:
Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, spinocerebellar ataxias, type II diabetes, amyotrophic lateral sclerosis, as well as diffuse Lewy body dementia and the fronto-temporal dementias. Studying the key molecular mechanisms involved in prion diseases may also help to understand these other amyloidoses. Inducible proteinopathies, such as amyloid A amyloidosis or apolipoprotein A II amyloidosis, show remarkable similarities to prion diseases. Most recently Meyer-Luehmann reported that in Alzheimer's disease the exogenous induction of cerebral ß-amyloidogenesis is governed by agent and host factors. The striking parallels of infectious prion disorders to the above-mentioned putatively non-infectious protein misfolding and assembly diseases make it more and more difficult to delimitate their pathological mechanisms from each other.
Device: The SOTA Magnetic Pulser.
INDEX
https://www.sota.com/magnetic-pulser.html
USA $350.00 --- 2018-07-10
LINK 2: https://www.chrisbeatcancer.com/bobbeck/
LINK3: https://www.sota.com/files/pdf/sota_brochure_legal.pdf
LINK 4: https://www.sota.com/default.aspx?page=Silver-Pulser
LINK 5: User Guide, 8 pages, pdf
This is a device that creates a PEMF (Pulsed Electromagnetic Field).
This is a moving magnetic field which causes 50-100 micro-amperes to be generated deep within tissues to neutralize the parasites, viruses, and pathogens that are latent in tissues and not circulating in the blood. The magnetic pulser is designed for specifically targeting lymph nodes, organs, and tumor sites, and should be used in conjunction with the Silver Pulser blood electrification device.
The SOTA Magnetic Pulser offers the benefits of a pulsed magnetic field to help balance the body’s natural electricity for health.
- Automatic Timer
- Bio-North Pole identified
- Fast and Slow Modes
- Output greater than 6,000 Gauss
- Magnetic Field penetrates up to 9 inches
- Two-year limited Warranty
The Magnetic Pulser generates pulsed magnetic fields which are known to create microcurrents.
For most applications, it is best to use the Bio North (-) polarity side of the Hand Paddle — the polarity is clearly marked on the Hand Paddle. The Bio North (-) polarity of the Hand Paddle can be applied to any area of the body. The Magnetic Pulser can be applied over clothing as the magnetic field penetrates clothing. Keep the Hand Paddle on one area or move to different locations during a session.
Basic Wellness Program:
Begin slowly, 10 minutes per day, and then gradually increase the length of each session until you are applying at least 20 minutes per day.
Daily use varies from 20-30 minutes to two hours or more.
Continue use for 8 to 12 weeks minimum.
When used as part of a wellness program, consistent daily use for many weeks is more important for results than using occasionally.
Longer and more frequent sessions may be more beneficial.
Focused Wellness Program:
Increase the amount of time used daily by increasing the number of sessions.
Use beyond the 8 to 12 week minimum. When following a more intense program, it may be necessary to continue for many months or even years.
Device: Microbe Electrifier/ DC combo.
INDEX
http://www.dragonfly75.com/eng/MEDC.html
USA $189.00 --- 2018-07-10 --- Plus shipping.
LINK 2: http://www.dragonfly75.com/eng/video.html (10 min)
1. Current Indicator
2. Frequency Selector: 4 Hz, 10 Hz, ..
3. Electrode Selection: electrodes on both wrists, both ankles, separate wrists.
4. Damped Wave Option: spiked or square wave.
LINK 3: http://www.dragonfly75.com/eng/2wrist.html
LINK 4: http://www.dragonfly75.com/eng/order61.html (Price List Page)
by Michael Forrest, BioElectric
1636 NW 82nd Avenue
Doral, FL 33126 USA
19jaguar75@gmail.com
USA phone: 305-572-5327 (limit 10 minutes)
Skype: bioelectric7
Online FORM: http://www.123formbuilder....
Payment is by PayPal or Western Union (or Money Gram).
--- One can pay by credit card or from a bank account on PayPal.
This is a Microbe Electrifier Plus with the extra option of either allowing an AC blood electrification frequency (4, 10, or 40 Hz) or the selection of DC (direct current) output instead in order to have a good treatment method for localized infections (an infection in one part of the body). You should use the 3" square electrodes when using this feature. As an example DC works great on dental infections. People with root canals should treat them with DC to kill the residual bacteria left there which create the toxins which disable cancer immunity. [more info] It works good against things like gastritis, appendicitis, bladder infections, toenail fungus, and sore throats.
If you are interested in any of my Microbe Electrifiers then first you need to see my YouTube video (above) explaining why I think they are the best and worth every penny. Otherwise just go to the price list page (above). You need to understand that all the other blood electrifiers are made to have both electrodes on one wrist which is more comfortable but very ineffective, and what is the purpose of buying an electromedicine device but to have something effective? A full explanation of why this ineffective method is the most popular (is below). I want to help people get well and guiding them away from the ineffective devices and to BioElectric devices is how to do it. ...
SAVE 10%
Send a "gift" via PayPal directly to 19jaguar75@gmail.com as to "friends and family" so PayPal won't take out 5%.
Multiply your total by .9 and send that amount. Don't mention what the money is for and then email me what it is you want and your mailing address and phone.
Don't forget the shipping/handling fee.
Usage: Microbe Electrifier Plus / DC Electrifier.
INDEX
http://www.dragonfly75.com/eng/MEPDC2-instr.html
LINK 2: http://www.dragonfly75.com/eng/usage.html
YouTube: https://www.youtube.com/watch?time_continue=4&v=SB4YNr2R5TU
(NOTE: Go to the above original online LINK to access the in-text ONLINE links)
Install batteries:
Remove the back cover using a small Phillips screwdriver.
Attach four 9 volt alkaline batteries to the battery clips.
Be sure not to pull on the battery wires since they are a small gauge wire and not made to be pulled on.
Click here to see correct battery placement.
--- LINK: http://www.dragonfly75.com/eng/batteries.html
Put the bubble wrap on top of them (to keep them from being able to move around) and screw on the lid.
To test for proper operation and strength of batteries:
Flip the power switch to the ON position and the frequency switch to 4 Hz.
Press the Test button down and look at the green test lights to see that they are
alternating on and off.
(At 10 Hz and 40 Hz the lights will mostly stay on).
If the four 9 volt batteries need replacement the Test lights will not light at all.
To replace the batteries just use a Phillips screwdriver to unscrew the cases bottom 4 screws, pull off the cover, and then pull off the snap clips from each battery so that they can be replaced with new alkaline ones. Reinstall the padding as it was so as to prevent the batteries from rattling when the box is jiggled.
Choosing electrode site:
Both electrodes on the inside of one wrist is the easiest site for convenient usage, but it affects the least amount of blood and the current has to be turned up to a painful level for enough to flow in the arteries since most of it will just cross over through the muscles. Beck proved that 3mA of current is necessary with this arrangement but no one except for nerve-damaged people can tolerate that high level. Using one electrode on one wrist and the second one on the other wrist is my favorite because plenty of blood is affected. This method causes people to worry about current affecting the heart but the current doesn't go thru it. [drawing] Using the electrodes on both ankles affects the most amount of blood, but will barely allow enough electrical current for some people (due to mineral deficiencies) and is hardest for initiating and maintaining correct electrode placement.
--- LINK: (offline) dragonfly/arterialsystem.png
Locating electrode placement sites for both wrists:
The locations are the inner side of the wrists about 1+1/2 inches below the wrist crease to the outside of the main tendon on the thumb side. Each wrist should have one electrode held in place by one wrist band.
(picture) (Offline: dragonfly/hands.jpg)
This is the most preferred electrode placement.
Locating electrode placement sites for ankles:
On the inner side of each foot locate the pulse of the unseen artery between the ankle and the heel.
If you can't feel it then go for a brisk walk for ten minutes and then feel for it without elevating your foot.
On top of these pulsating arteries are the sites.
(picture) (Offline: dragonfly/feet.jpg)
Connecting Electrodes:
Clean & dry the electrode sites. Soak each of the cloth electrodes thoroughly with tap water or saltwater.
Squeeze the middle of the insulation of the Microbe Electrifier's alligator clips (at the end of its wires) so that you open the jaws and then let them bite onto the electrodes ends with one jaw inside the electrode.
(picture) (Offline: dragonfly/caiman.jpg)
Place the electrode over the artery. Then put the elastic band around it and the wrist (or ankle).
Don't pull it tight. Just enough stretch to keep it in place is good.
If using electrodes on the ankles, then attach them there with 1" wide medical tape.
Re-wet the cloth electrode after 1 hour of use.
Making Saltwater:
Tap water (not distilled or de-ionized) is to be used to wet the cloth electrodes so that they'll be electrically conductive.
If you can turn the unit's current control fully clockwise and not get a zing from the electricity then it's probably because your tap water is deficient in minerals which makes it not very electrically conductive. To remedy that you can make some saltwater by putting a couple of shakes of salt from the saltshaker into a cup of water and stirring it. This is very electrically conductive but also corrosive to the alligator clips.
Using the device:
Clean your skin where you want to place the electrodes and then connect the wet electrodes to you.
Turn the current control dial fully counter-clockwise, set the unit to 10Hz, and flip the switch to the ON position.
Turn the current dial slowly clockwise until the red current light comes on fully.
Then switch the frequency switch to the frequency setting you want to use if it's not 10Hz.
The current light will indicate when you are getting at least .14mA (140uA) through your bloodstream.
If it won't light at maximum dial position then one of three conditions exist;
1) Your body's salt & mineral level is very low (read this), (Offline: dragonfly/salt.html)
2) Where you placed the electrodes is unsuitable,
3) You need to use saltwater on the electrodes instead of tap water.
If your body's salt level is low then start salting your food with sea salt (which doesn't cause high blood pressure).
If the electrodes 'sting' or 'bite' then
1) the current dial setting is too high,
2) your skin is dirty,
3) you need to relocate the electrodes.
Below is a video showing how to wet the electrodes, connect them to your wrists, and then how to turn up the current dial till the red light is fully on. (It is with the simple version of the Microbe Electrifier.)
--- LINK: https://www.youtube.com/watch...
Current Level:
The target .14mA is right at the beginning of the effective range of electrical current which is shown by the active red light.
More current is likely to damage the skin. Never turn the current up high enough to cause a stinging sensation which indicates skin being damaged. If .14mA causes stinging then set it to a lower level that is safe for your skin. Think of the .14mA level not as something essential but as a reference point from which you can find the perfect setting for yourself.
Comfort Suggestions:
If the elastic strap is too tight it will leave ridges on the skin when taken off.
You can also sew something soft onto the inside of the band (if a natural fiber then not where the electrodes will be because natural fibers will wick away the electrodes moisture). If your skin becomes irritated where the electrodes touch then maybe you're applying too much current or you should place the electrodes on the ankles instead of the wrists.
AC/DC Option:
The AC/DC switch allows you to select either Alternating Current for blood electrification with the small wrist electrodes or Direct Current for localized infection treatment with the large electrodes.
Transfection, or, electroporation:
When doing 4 hertz blood electrification, why do I have to limit taking herbs and medicine to the time right after finishing device usage? Because during electric current application (at low frequencies) blood cells more readily absorb chemicals that are in the bloodstream. (~20x more.) So it would be necessary to give the body plenty of time (22-23 hours) to expel the medicinal chemicals by only taking them after each session. (otherwise use 40 Hz which doesn't allow much of this effect). This high-absorption effect on blood cells exists only while the electric current is applied and is called 'transfection' or 'electroporation'.
Product: The Adjustable Oxygen Bar.
INDEX
https://www.hammacher.com/product/at-home-adjustable-oxygen-bar
?promo=search&query=va-96293 ---- --- Lifetime Guarantee
VA-96293 --- USA $449.95 --- Source Code: 214005 -- January 2021
Item 96293
LINK 2: https://www.themindrelaxer.com/
the-at-home-adjustable-oxygen-bar-a-personal-oxygen-bar-that-increases-
the-concentration-of-oxygen-inhaled-for-calm-relaxation/
USA $499.95 --- Lifetime Guarantee
LINK 3: https://zadroinc.com/aromatherapy-personal-oxygen-bar/
USA $449.95 ---
Features:
- Experience luxurious spa-like aromatherapy during your session
----- using essential oil of your choice or with the included lavender essential oil**
- 5 adjustable oxygen concentration settings from 30% oxygen up to 90% oxygen
- Quadruple air filtration system and French-imported molecular membrane
-------- produces highly purified oxygen of up to 90% concentration
- Auto shutoff timer with 8 timer settings from 15 minutes up to 2 hours
- Personalize your experience using the digital LCD screen display panel
... or easily change the settings during your session with the convenient remote control (CR2025 battery included)
- Enhance the oxygen purification with the optional negative ions booster function***
- .. in a dry climate, use the optional water reservoir which infuses the purified oxygen with humidity
- Enjoy less noise (<45 dB) from the machine >
- Internal overheat protection will automatically shut off the machine for safety
- Plugs into a standard electrical outlet
- Remote control, AC power adapter, headset, nasal tube attachment, and essential oil included
- Available in White with Blue Accents
- This ... should not be used as a replacement for prescribed medical treatments
- Product Dimensions: 14.1" x 9.1" x 12.64"
- Weight: 14.33 lbs.
- Imported
Modeled after oxygen bars found in resorts and spas, this is the personal oxygen bar that increases the concentration of oxygen inhaled from 35% to 90% for calm relaxation.
A compressor draws in ambient air and first passes it through four filters that remove larger dust particles and impurities. A membrane isolates oxygen, increasing its total concentration which is pumped through a tube to a headset where it gently exits near the mouth.
It has an adjustable oxygen flow rate, five concentration settings, and works with essential oils for aromatherapy.
AC plug. 14" L x 12 3/4" W x 9" H. (14 1/2 lbs.)
The Hammacher Schlemmer Lifetime Guarantee
Our merchandise is guaranteed for life.
Items that we sell are guaranteed for their normal life under standard non-commercial use.
Should any product fail to meet your expectations, we will replace it or refund the cost of the item less shipping and service fees. Returns older than one year will be credited in form of a gift certificate.
We know you have a choice, thank you for choosing Hammacher Schlemmer.
What are the symptoms of low oxygen?
When you aren’t getting enough oxygen, you’ll experience a host of symptoms, including:
- rapid breathing
- shortness of breath
- fast heart rate
- coughing or wheezing
- sweating
- confusion
- changes in the color of your skin
Oxygen therapy can also reduce symptoms such as:
- headaches
- irritability
- fatigue
- swollen ankles
Device : Tests for Prions.
INDEX
https://www.cdc.gov/prions/cjd/diagnostic-criteria.html
CDC’s Diagnostic Criteria for Creutzfeldt-Jakob Disease (CJD), 2018
LINK 2: Clinical and Pathologic Characteristics.
https://www.cdc.gov/prions/cjd/
clinical-pathologic-characteristics.html
Last_updated: October 18, 2021
LINK 3: Cerebrospinal Fluid Diagnostic Tests.
https://case.edu/medicine/pathology/divisions/national-prion-disease
-pathology-surveillance-center/human-prion-diseases/
cerebrospinal-fluid-diagnostic-tests
LINK 4: Testing Protocols.
https://case.edu/medicine/pathology/
divisions/national-prion-disease-pathology-surveillance
-center/resources-professionals/testing-protocols
Autopsy Coordinators at 216-368-0587
LINK 5: Contact and Shipping Information.
https://case.edu/medicine/pathology/divisions/
national-prion-disease-pathology-surveillance-center/
resources-professionals/contact-and-shipping-information
Instructions by Type of Sample.
Institute of Pathology
Case Western Reserve University
2085 Adelbert Road, Room 418
Cleveland, Ohio 44106-4907
Tel: 216.368.0587
Email: CJDsurveillance@uhhospitals.org
(There is an 8 week test result)
LINK 6: CJD Foundation
(A Patient / Family Support Organization)
http://www.cjdfoundation.org/
24 Hour Support Line: 1-(800)-659-1991
3634 W. Market Street, Suite 110
Akron, OH 44333
help@cjdfoundation.org
LINK 7: National Prion Disease Pathology Surveillance Center.
https://case.edu/medicine/pathology/divisions/prion-center/
Sponsored by the American Association of Neuropathologists.
School of Medicine, Case Western Reserve University
2103 Cornell Rd., Cleveland, Ohio 44106
Phone: 216.368.3611
Updated: 2020-01-10
AND
2085 Adelbert Rd Rm 419
Cleveland, Ohio 44106
Phone: 216-368-0587
Email: cjdsurveillance@uhhospitals.org
LINK 8: Information for Funeral & Crematory Practitioners.
https://www.cdc.gov/prions/cjd/funeral-directors.html
Last_updated: September 10, 2021
LINK to
INDEX page
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LINK to Empower,
Maintain, & Repair
YOUR Health
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Articles on the Internet are transitory.
The publishers may remove them, change sites, change URLs, or change titles.
For the purpose of maintaining an availability of these articles for myself and you, I have reprinted parts in the relevant monographs with authorship maintained, coding simplified for error-free loading and minimal file size, and a LINK to the original document. Identity trackers and advertising bots have been removed from the original bloated and manipulative coding. NOTHING in writing is absolute; don't treat human opinion, projection, and observation as an Idol. Doing so can kill you, or worse, have you impose abuse on others.
I gathered and researched this data, mediated with the Grace of God through prayer as a benefit in my integrating discovered available digital information which would acquaint me with the overall content related to the health issues. I have found that God is ALWAYS available when we are Reverent in our Asking, open-minded in our Listening, and, Assertive in our Choice of Action. Doctors did not expect me to survive birth. In the past 25 years, medical and health "experts" have cautioned or directed me, more than 14 times, that I had little time left to live, or would die ... because THEY did not understand my challenges, were not motivated to professionally diagnose, or, chose to superstitiously recall as absolute previously flawed training. I am still alive beyond age 70. With the assistance of God, my Personality, the research and a lack of dismissiveness of a number of persons ... I have found resolution to numerous health challenges. This has enabled me to assist many others who had been abandoned, brainwashed, or traumatized. May my experience and successes also empower you. This is one document which you may find helpful as a BASIC introduction to maintaining and improving YOUR health.
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