Also, see the dark green & brown box near the top left of this page. The 3rd link is to state support groups.
Locals can help the best.
Posts: 1672 | From AL/WV/OH | Registered: Jun 2006
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Melanie Reber
Frequent Contributor (5K+ posts)
Member # 3707
posted
I am so sorry to know your friend is suffering with this. Here is some added information to help others understand.
...
History
The disease was first described by German neurologist Hans Gerhard Creutzfeldt in 1920 and shortly afterwards by Alfons Maria Jakob. In 1922 it was named Creutzfeldt-Jakob disease.
Some of the clinical findings described in their first papers do not match current criteria for Creutzfeldt-Jakob disease, and it is considered highly likely that at least two of the patients in initial studies were suffering from a different ailment.[citation needed]
Pathophysiology
Transmissible spongiform encephalopathy diseases are caused by prions. The diseases are thus sometimes called prion diseases. Other prion diseases include Gerstmann-Str�ussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI) and kuru in humans, as well as bovine spongiform encephalopathy (BSE, commonly known as mad cow disease) in cattle, chronic wasting disease (CWD) in elk and deer, and scrapie in sheep. Alpers' syndrome in infants is also thought to be a transmissible spongiform encephalopathy caused by a prion.[2][3]
The prion that is believed to cause Creutzfeldt-Jakob exhibits at least two stable conformations. One, the native state, is water-soluble and present in healthy cells. As of 2007[update], its biological function is presumably in transmembrane transport or signaling. The other conformational state is very poorly water-soluble and readily forms protein aggregates.
People can also acquire CJD genetically through a mutation of the gene that codes for the prion protein (PRNP). This only occurs in 5-10% of all CJD cases.
The CJD prion is dangerous because it promotes refolding of native proteins into the diseased state (Step 1: UNFOLDING of alpha-helices; Step 2: REFOLDING to beta-pleated sheets.). The number of misfolded protein molecules will increase exponentially,[citation needed] and the process leads to a large quantity of insoluble prions in affected cells.
This mass of misfolded proteins disrupts cell function and causes cell death. Mutations in the gene for the prion protein can cause a misfolding of the dominantly alpha helical regions into beta pleated sheets. This change in conformation disables the ability of the protein to undergo digestion. Once the prion is transmitted, the defective proteins invade the brain and are produced in a self-sustaining feedback loop, causing exponential spread of the prion, leading to death within a few months, although a few patients have lived as long as two years.
Stanley B. Prusiner of University of California, San Francisco (UCSF) was awarded the Nobel Prize in physiology or medicine in 1997 for his discovery of prions. For more than a decade, Yale University neuropathologist Laura Manuelidis has been challenging this explanation for the disease. In January 2007 she and her colleagues published an article in the Proceedings of the National Academy of Science and reported that they have found a virus-like particle (but without finding nucleic acids so far) in less than 10% of the cells a scrapie-infected cell line and in a mouse cell line infected by a human CJD agent.[4]
Is it tickborne? Here are three abstracts that seem to confirm that notion.
Spiroplasma spp. from transmissible spongiform encephalopathy brains or ticks induce spongiform encephalopathy in ruminants. Bastian FO, Sanders DE, Forbes WA, et al. J Med Microbiol 2007 Sep; 56(Pt 9):1235-42.
Spiroplasmas: infectious agents of plants, arthropods and vertebrates. Bov� JM Wien Klin Wochenschr 1997 Aug 8; 109(14-15):604-12.
[Spiroplasmas and hematophagous arthropods; prospects in tropical pathology] Chastel C, Abalain-Colloc ML, Gilot B, et al. Bull Soc Pathol Exot Filiales 1985; 78(5 Pt 2):769-79.
Posts: 7052 | From Colorado | Registered: Mar 2003
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bettyg
Unregistered
posted
breaking this up more for neuros to comprehend.
quote:Originally posted by Melanie Reber:
I am so sorry to know your friend is suffering with this. Here is some added information to help others understand. ...
History
The disease was first described by German neurologist Hans Gerhard Creutzfeldt in 1920 and shortly afterwards by Alfons Maria Jakob.
In 1922 it was named Creutzfeldt-Jakob disease.
Some of the clinical findings described in their first papers do not match current criteria for Creutzfeldt-Jakob disease, and it is considered highly likely that at least two of the patients in initial studies were suffering from a different ailment.[citation needed]
Pathophysiology
Transmissible spongiform encephalopathy diseases are caused by prions. The diseases are thus sometimes called prion diseases.
Other prion diseases include
Gerstmann-Str�ussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI) and kuru in humans, as well as bovine spongiform encephalopathy (BSE, commonly known as mad cow disease) in cattle,
chronic wasting disease (CWD) in elk and deer, and scrapie in sheep.
Alpers' syndrome in infants is also thought to be a transmissible spongiform encephalopathy caused by a prion.[2][3]
The prion that is believed to cause Creutzfeldt-Jakob exhibits at least two stable conformations.
One, the native state, is water-soluble and present in healthy cells. As of 2007[update], its biological function is presumably in transmembrane transport or signaling.
The other conformational state is very poorly water-soluble and readily forms protein aggregates.
People can also acquire CJD genetically through a mutation of the gene that codes for the prion protein (PRNP). This only occurs in 5-10% of all CJD cases.
The CJD prion is dangerous because it promotes refolding of native proteins into the diseased state
(Step 1: UNFOLDING of alpha-helices;
Step 2: REFOLDING to beta-pleated sheets.).
The number of misfolded protein molecules will increase exponentially,[citation needed] and the process leads to a large quantity of insoluble prions in affected cells.
This mass of misfolded proteins disrupts cell function and causes cell death.
Mutations in the gene for the prion protein can cause a misfolding of the dominantly alpha helical regions into beta pleated sheets.
This change in conformation disables the ability of the protein to undergo digestion.
Once the prion is transmitted, the defective proteins invade the brain and are produced in a self-sustaining feedback loop, causing exponential spread of the prion, leading to death within a few months, although a few patients have lived as long as two years.
Stanley B. Prusiner of University of California, San Francisco (UCSF) was awarded the Nobel Prize in physiology or medicine in 1997 for his discovery of prions.
For more than a decade, Yale University neuropathologist Laura Manuelidis has been challenging this explanation for the disease.
In January 2007 she and her colleagues published an article in the Proceedings of the National Academy of Science and reported that they have found a virus-like particle (but without finding nucleic acids so far) in less than 10% of the cells a scrapie-infected cell line and in a mouse cell line infected by a human CJD agent.[4]
posted
Not related to LD. We were living in Europe during the mad cow scare in 2001ish. My understanding is that the cows got it from eating infected feed. People get the CJD variant from eating infected beef.
Posts: 41 | From SC | Registered: Jan 2009
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sparkle7
Frequent Contributor (5K+ posts)
Member # 10397
1. Able to kill spirochetes as well as ANY other pathogenic microbe - virus, bacterial, yeast, mycoplasma, parasite, prion, etc., contacted. In fact, is ATTRACTED to them by polarity.
Posts: 7772 | From Northeast, again... | Registered: Oct 2006
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In the rogues' gallery of microscopic infectious agents, the prion is the toughest hombre in town.
Warped pathogens that lack both DNA and RNA, prions are believed to cause such fatal brain ailments as chronic wasting disease (CWD) in deer and moose, mad cow disease in cattle, scrapie in sheep and Creutzfeldt-Jakob disease in humans. In addition to being perhaps the weirdest infectious agent know to science, the prion is also the most durable. It resists almost every method of destruction from fire and ionizing radiation to chemical disinfectants and autoclaving, which reduce prion infectivity but fail to completely eliminate it.
Now, however, a team of Wisconsin researchers has found that a common soil mineral, an oxidized from of manganese known as birnessite, can penetrate the prion's armor and degrade the protein.
The new finding, which was reported earlier this month (Jan. 2) in the Journal of General Virology, is important because it may yield ways to decontaminate soil and other environments where prions reside.
"Prions are resistant to many of the conventional means of inactivating pathogens," says Joel Pedersen, a University of Wisconsin-Madison environmental chemist and the senior author of the new study. For example, autoclaving, a standard method for sterilization in the laboratory, will reduce the concentration of prions in solution, but fails to eliminate them altogether, as it does for virtually all other types of pathogens.
Because prions infect both wild and domesticated animals, the agent can contaminate barnyards and other areas where infected livestock are kept, as well as persist in natural environments where deer, elk and other animals can become infected by contact with contaminated soil.
Other studies have shown that prions can survive in the soil for at least three years, and that soil is a plausible route of transmission for some animals, Pedersen says. "We know that environmental contamination occurs in deer and sheep at least," he notes.
Prion reservoirs in the soil, Pedersen explains, are likely critical links in the chain of infection because the agent does not appear to depend on vectors - intermediate organisms like mosquitoes or ticks - to spread from animal to animal.
That the birnessite family of minerals possessed the capacity to degrade prions was a surprise, Pedersen says. Manganese oxides like birnessite are commonly used in such things as batteries and are among the most potent oxidants occurring naturally in soils, capable of chemically transforming a substance by adding oxygen atoms and stripping away electrons. The mineral is most abundant in soils that are seasonally waterlogged or poorly drained.
"A variety of manganese oxide minerals exist and one of the most common is birnessite. They are common in the sense that you find them in many soils, but in low concentrations," says Pedersen. "They are among the strongest oxidants in soil."
The new study, which was led by Fabio Russo of the University of Naples and Christopher J. Johnson of UW-Madison, was conducted on prions in solution in the laboratory. The group's working hypothesis, according to Pedersen, is that the mineral oxidizes the prion, a chemical process that can be seen in things like iron oxidizing to form rust or how cut pears and apples turn brown when exposed to oxygen.
The next step, Pedersen says, is to mix the mineral with contaminated soil to see if it has the same effect. If it does, birnessite may become a useful tool for cleaning up contaminated farmyards and other places where the prion may be concentrated in the soil.
"I expect that its efficacy would be somewhat diminished in soil," says Pedersen. "It's something we'll explore."
Posts: 789 | From CT, | Registered: Jun 2006
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posted
Study Type: Interventional Study Design: Treatment, Randomized, Double-Blind, Placebo Control, Parallel Assignment, Efficacy Study Official Title: Novel Therapeutics For Prion Diseases: A Randomized, Double-Blinded, Placebo-Controlled Study of the Efficacy of Quinacrine in the Treatment of Sporadic Creutzfeldt-Jakob Disease
Further study details as provided by National Institute on Aging (NIA):
Primary Outcome Measures: Survival from the time of randomization
Secondary Outcome Measures: Scores on functional scales, neurological exam and functional testing
Estimated Enrollment: 60 Study Start Date: April 2005 Detailed Description: Creutzfeldt-Jakob disease (CJD)is a rapidly progressive, invariably fatal and untreatable neurodegenerative disease with a mean duration of about eight months. Beyond the debilitating cognitive and motor deficits that accompany CJD, the difficulty in treating behavioral and mood disturbances and the rapidity of its course compound its tragedy. Recent results from experiments show that, at physiological concentrations, the anti-malarial drug quinacrine permanently clears abnormal prion proteins from cell culture. The demonstrated efficacy of quinacrine in cell culture, its relative safety and well known side-effects in the clinical setting, and the universal fatality of CJD justify quinacrine as an immediate candidate for the treatment of CJD.
The purpose of this clinical trial is to determine the efficacy of the medication quinacrine on survival in sporadic CJD (sCJD). This will be accomplished by bringing approximately 60 patients with probable or definite sCJD over approximately three years to UCSF for evaluation and initiation of a randomized, double-blinded, placebo-controlled (delayed treatment start) treatment study of quinacrine. Each patient will have a 50:50 chance of being placed on quinacrine or placebo upon study enrollment; however, all patients will be offered quinacrine after two months. Prior to study enrollment, patients will have a comprehensive clinical assessment to confirm the diagnosis of sCJD. Participants will come to UCSF for initial evaluation, potential study enrollment and, if possible, return to UCSF for follow-up at two and twelve months. Patients will receive telephone follow-up (every 2 weeks for the first two months and monthly thereafter) and local blood and testing to monitor for possible medication toxicity.
NanaDubo
Frequent Contributor (1K+ posts)
Member # 14794
posted
Thanks everyone. I wish my friend had told me sooner about the condition of her friend with CJD.
They don't expect her to live through the weekend.
To answer - female in her fifties, living in Maine.
Posts: 1129 | From Maine | Registered: Feb 2008
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Pinelady
Frequent Contributor (5K+ posts)
Member # 18524
posted
Whilst I believe the testing procedures are as aloof as the ones for Lyme it would not be confirmed until autopsy.
For which I don't believe will happen if they suspect CJD.
In Europe, if suspect there is no autopsy performed unless it is by a research facility.
The main cause of transmission here in the states they believe was and still could be caused by HGH from unknown sources.
Sorry for your friends illness. Prayers to you and yours.
-------------------- Suspected Lyme 07 Test neg One band migrating in IgG region unable to identify.Igenex Jan.09IFA titer 1:40 IND IgM neg pos 31 +++ 34 IND 39 IND 41 IND 83-93 + DX:Neuroborreliosis Posts: 5850 | From Kentucky | Registered: Dec 2008
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posted
Prion Discovery Gives Clue To Control Of Mass Gene Expression 16 Mar 2009
The discovery in common brewer's yeast of a new, infectious, misfolded protein -- or prion -- by University of Illinois at Chicago molecular biologists raises new questions about the roles played by these curious molecules, often associated with degenerative brain diseases like "mad cow" and its human counterpart, Creutzfeldt-Jakob.
Susan Liebman, distinguished university professor of biological sciences, and postdoctoral research associate Basant Patel propagated the new prion from a normal yeast protein called Cyc8. They note that like the Cyc8 protein, the prion of Cyc8 can affect the expression of a large number of yeast genes.
"We know this prion turns on the expression of genes but we don't know if the prion forms naturally," said Liebman. "If it were to form, it would have this effect. But whether it happens out in the wild all the time, we don't know."
Liebman and her coworkers discovered that Cyc8 was a prion candidate using a genetic screen that looks for proteins that when overproduced can spur formation of new prions. To date, scientists have discovered only seven prions, six of which are only in fungi, including yeast. The latest two discovered, Cyc8 and another, identified as Swi1, came from genes screened in Liebman's lab. The Cyc8 prion was characterized by the UIC scientists, while the Swi1 prion was found by Northwestern University researchers.
The normal Cyc8 protein shuts down expression of more than 300 genes in yeast, says Patel, including some genes that are involved in stress tolerance.
"Once Cyc8 is converted to a prion, it loses that function," he said. "This might provide some advantages under stressful conditions. Since the protein represses more than 300 genes, it's possible the prion form can activate the genes on a mass level." If an organism wanted to activate all the genes in a cell that the protein repressed, he said, "converting the protein into a prion would be an easy way to do it."
Patel and others in Liebman's lab are testing the protein to see if this molecular mechanism does in fact take place naturally. They're also studying the interaction of prions to determine if pre-existing prions facilitate or destabilize new prions.
Whether the actions of prions in yeast are analogous to mammalian models is not yet fully known, but the possibility certainly is on the minds of Liebman and her associates.
"There could be prions in humans that are not causing disease but have important effects on the cell or organism," said Liebman. "They may even be related to the ones we find in yeast. The more prions we learn about and study, the more information we learn from them -- how they arrive, what proteins are needed to maintain them. As we study other models, we have a better idea."
Notes:
Jackie Gavin-Smyth, a former research specialist in Liebman's lab now at the University of Chicago, was another co-author of the letter in the March issue of Nature Cell Biology describing the new prion.
The work was supported by a grant from the National Institutes of Health.
Source: Paul Francuch University of Illinois at Chicago --------------------------------------------------------------------------------
Posts: 789 | From CT, | Registered: Jun 2006
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D Bergy
Frequent Contributor (1K+ posts)
Member # 9984
posted
capable of chemically transforming a substance by adding oxygen atoms and stripping away electrons.
I copied this from one of the posts above. I noticed that the chemical transformation process is exactly the same as Miracle Mineral Supplement (MMS)aka Chlorine Dioxide.
Chlorine Dioxide is known as the most powerful disinfectant known to man. It may take something like this to even begin to slow down prions.
Dan
Posts: 2919 | From Minnesota | Registered: Aug 2006
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Iron is involved in prion disease-associated neuronal demise:
Imbalance of iron homeostasis is a common feature of prion disease-affected human, mouse, and hamster brains, according to a new study by Dr. Neena Singh and colleagues at Case Western Reserve University School of Medicine, alongside collaborators from Creighton University.
These findings, published March 13 in the open-access journal PLoS Pathogens, provide new insight into the mechanism of neurotoxicity in prion disorders, and novel avenues for the development of therapeutic strategies.
Unlike other neurodegenerative conditions, prion disorders are sporadic, inherited, and infectious, and affect both humans and animals; common examples are mad cow disease in cattle, scrapie in sheep, and Creutzfeldt-Jakob disease in humans.
The causative agent is a misfolded protein referred to as PrP-scrapie that replicates itself by changing the conformation of neighboring copies of the same protein, namely the prion protein.
Aggregates of PrP-scrapie are toxic to brain cells and cause a spongy-like appearance in diseased brains.
Research from the Singh laboratory suggests that accumulation of PrP-scrapie alters the metabolism of iron in diseased brains.
The imbalance of brain iron homeostasis worsens with disease progression, and is not an outcome of end-stage disease.
Since iron is highly toxic when mismanaged, this condition is likely to contribute significantly to prion-disease-associated neurotoxicity.
The likely cause of this condition is loss of normal function of the prion protein in cellular iron metabolism demonstrated recently by Singh and colleagues, combined with gain of toxic function by the redox-active PrP-scrapie complex as shown in this report.
Singh and her team were surprised to find that prion disease-affected brains are iron deficient despite a significant increase in their overall iron content.
The group concludes that ferritin, a major iron storage protein, co-aggregates with PrP-scrapie in diseased brains and sequesters bound iron in the complex, creating a state of apparent iron deficiency.
The brain cells respond to this condition by increasing their level of iron uptake, thus creating a vicious cycle of increased iron uptake in the presence of increased iron.
These observations contribute to our understanding of how the prion agent causes neurotoxicity, and may enable the development of novel therapeutic strategies targeted at restoring brain iron homeostasis in prion disorders.
Dr. Neena Singh Public Library of Science
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