I heard there is a disease where you don't sleep

[Curl]

Does anyone know what I'm talking about? I heard some people have a disorder where they can never go to sleep even if they try. I think I heard it can happen after some trauma.

My question is, how do I catch this disease?

 

[caffenta]

You mean insomnia? The disease transmission mechanism is not really known, but I read in J. Sarcast. Med. that it involves some kind of dark brownish powder that has a very pleasing smell. I forget what it's called. "Co-something."

Why do you want to catch this disease? Sleep is like the best thing in life. I get all giddy when it's time to go to bed. I start running around going "bed bed bed! sleep sleep sleep!"

 

[Pythagorean]

http://en.wikipedia.org/wiki/Fatal_familial_insomnia

 

[pergradus]

You realize you need sleep in order to be healthy? Lack of sleep is terrible for both your mind and your body.

 

[nismaratwork]

http://en.wikipedia.org/wiki/Fatal_familial_insomnia

I'm guessing this is what he meant... and it has to be one of the truly lousy ways to go... no treatment, no hope... :yuck:

One of those times where the case for suicide actually works.

 

[Lievo]

I think I heard it can happen after some trauma.

TBIs are more and more recognized as http://journals.lww.com/headtraumarehab/Abstract/2006/05000/Insomnia_in_Patients_With_Traumatic_Brain_Injury_.1.aspx" , but to my knowledge never to the extent of fatal insomnias. Maybe a tumor in the thalamus or some part of the brain stem could mimic that, but I have no example in mind.

 

[nismaratwork]

TBIs are more and more recognized as http://journals.lww.com/headtraumarehab/Abstract/2006/05000/Insomnia_in_Patients_With_Traumatic_Brain_Injury_.1.aspx" , but to my knowledge never to the extent of fatal insomnias. Maybe a tumor in the thalamus or some part of the brain stem could mimic that, but I have no example in mind.

AFAIK there is no such thing as aqquired Familial Fatal Insomnia, but even without TBI trauma alone can horribly disturb sleep.

It's not disease however, nor is it FFI.

 

[Lievo]

By definition Familial Fatal Insomnia is not acquired, or we call that Sporadic Fatal Insomnia. As it's a prion disease, it's likely that it can be acquired. And of course, it's a disease.

 

[nismaratwork]

By definition Familial Fatal Insomnia is not acquired, or we call that Sporadic Fatal Insomnia. As it's a prion disease, it's likely that it can be acquired. And of course, it's a disease.

No... TBI's are not a disease... missed that point, and both FFI and SFI are an issue of mutations in protein folding.

PrPSc is the issue for SFI, and there is no known vector or cause... it appears to be a spontneous mutation (which it probalby isn't), but who knows if it can be aqquired. True, Kuru, CJD, and others are transmissible, but what's the mechanism here? It seems to be a mutation in either case that causes the improper expression of a given protein... you make your own prions.

 

[Lievo]

No... TBI's are not a disease... missed that point, and both FFI and SFI are an issue of mutations in protein folding.

You say 'no' to something I did not wrote. Either it's red herring, or I was unclear. Let me be clearer: you are right to say TBIs are not diseases. You are wrong to say FFI and SFI are not.

 

[nismaratwork]

You say 'no' to something I did not wrote. Either it's red herring, or I was unclear. Let me be clearer: you are right to say TBIs are not diseases. You are wrong to say FFI and SFI are not.

I am saying that TBI's are not diseases, FFI and SFI ARE. I'm not trying to be coy, I may have misunderstood or miscommunicated.

 

[Lievo]

Maybe it's my Danishian English: when you say

It's not disease however, nor is it FFI.

does that means that FFI is a disease (what I understood) or does that means it is not?

 

[nismaratwork]

Maybe it's my Danishian English: when you say

does that means that FFI is a disease (what I understood) or does that means it is not?

Hmmm, that's me making an error, not you. I could go back and edit it, but that would be kind of cheating, and would make your comments seem out of context. Your English is fine, my brain aparrantly is becoming spongiform with age.

 

[tot]

Does anyone know what I'm talking about? I heard some people have a disorder where they can never go to sleep even if they try. I think I heard it can happen after some trauma.

My question is, how do I catch this disease?

:) Physics is a disorder where you don't sleep? or I mean order. it's orderly.

 

[fluidistic]

Another guess: http://en.wikipedia.org/wiki/African_trypanosomiasis. You catch it by the tse tse fly who lives in Africa.
EDIT: I got it all wrong. I'm not sure if it makes you sleep more or less actually. Sorry about that.

 

[nismaratwork]

:) Physics is a disorder where you don't sleep? or I mean order. it's orderly.

:rofl:

Along with reading, gaming, chatting, and... other things.

@Fluidistic: Oooohh... that is high on my list of, "ways not to die".

 

[bobze]

All prion diseases work as "trap" for the protein in question's equilibrium. That equilibrium;

PrP↔PrP^SC

The PrP^SC "form" of the protein is not soluble and easily polymerizes. So introduction of any PrP^SC, causes PrP^SC to "come out of solution" and pull the equilibrium to the right. Starting a chain reaction so to say, that keeps trapping more and more PrP as the PrP^SC form.

To my knowledge there isn't any other mechanisms for prion diseases.

Introducing prion protein would elicit this kind of "thermodynamic trap" response; how much? I don't think anyone knows at this point. That maybe something unique to each prion 'species'.

 

[nismaratwork]

All prion diseases work as "trap" for the protein in question's equilibrium. That equilibrium;

PrP↔PrP^SC

The PrP^SC "form" of the protein is not soluble and easily polymerizes. So introduction of any PrP^SC, causes PrP^SC to "come out of solution" and pull the equilibrium to the right. Starting a chain reaction so to say, that keeps trapping more and more PrP as the PrP^SC form.

To my knowledge there isn't any other mechanisms for prion diseases.

Introducing prion protein would elicit this kind of "thermodynamic trap" response; how much? I don't think anyone knows at this point. That maybe something unique to each prion 'species'.

Can the introduction be endogenous, or does it have to be a result of exposure?

 

[bobze]

Can the introduction be endogenous, or does it have to be a result of exposure?

The mutation can either come from the germ line, or during somatic cell division (you'd be one pretty unlucky person for that to happen!).

AFAIK, it would be transmissible if the prion protein were introduced into a non-infected individual (all prion diseases are transmissible in this way). I don't believe though there are recorded cases of this happening yet--But, I suspect this is to do with the rarity of this specific prion disease (as if not all prion disease were rare ).

To my knowledge, the familia form has only been found in around 20-50 families (depending on who you read) and only few 100 or so people (at most) have been diagnosed with the disease.

However, had those epileptic patients who had probes inserted in their heads had FFI/SFI instead of CJD, then I'm willing to bet FFI would have been what was transferred to the poor patients who got to follow them.

The neat, and terrible thing about prion diseases is they are so, extremely resistant to protein degradation--Not just chemical and thermal degradation, but to proteases as well. Which is why you can acquire the disease through food. That in itself is still a mystery of how those little guys are able to cross the GI epithelium whole and make it to the brain.

It is interesting to note though, that sufficiently higher doses of the prion protein are required for orally ingested transmission, than direct introduction to neural tissues. Which seems to suggest, that your GI system is able to fend off some of the little bastards!

 

[nismaratwork]

The mutation can either come from the germ line, or during somatic cell division (you'd be one pretty unlucky person for that to happen!).

AFAIK, it would be transmissible if the prion protein were introduced into a non-infected individual (all prion diseases are transmissible in this way). I don't believe though there are recorded cases of this happening yet--But, I suspect this is to do with the rarity of this specific prion disease (as if not all prion disease were rare ).

Heh, point taken, and of course you have the rather long period between exposure and frank symptoms. As for the unlucky fellow, I wonder if some of these prion diseases didn't originate with human lines... no way to tell though is there? It's not as though we can check the mitochondrial line of a protein... :grumpy: . Kuru... maybe that could have been the result of first, failed division, then exposure through post-mortem cannibalism?

To my knowledge, the familia form has only been found in around 20-50 families (depending on who you read) and only few 100 or so people (at most) have been diagnosed with the disease.

However, had those epileptic patients who had probes inserted in their heads had FFI/SFI instead of CJD, then I'm willing to bet FFI would have been what was transferred to the poor patients who got to follow them.

I'm not betting against you... CSF contamination with prions strikes me as a rather nasty death sentence.

The neat, and terrible thing about prion diseases is they are so, extremely resistant to protein degradation--Not just chemical and thermal degradation, but to proteases as well. Which is why you can acquire the disease through food. That in itself is still a mystery of how those little guys are able to cross the GI epithelium whole and make it to the brain.

I wonder if they're actively carried through, or if it's a matter of causing precipitation in the brain without needing to REACH the brain. I'd imagine, although there is clearly no evidence, that it might be the very "misshapen" nature of these proteins that save them from proteases. I'd guess that a novel protease would be needed for any given prion disease.

It is interesting to note though, that sufficiently higher doses of the prion protein are required for orally ingested transmission, than direct introduction to neural tissues. Which seems to suggest, that your GI system is able to fend off some of the little bastards!

Hmmm... could it be that some proteins are denatured by HCl, and not the usual enzymes? A limit to that of course, but it would explain how they survive, but some end as... well... food and excreta.

Keep talking, I like reading your posts... VERY informative!

 

[bobze]

Heh, point taken, and of course you have the rather long period between exposure and frank symptoms. As for the unlucky fellow, I wonder if some of these prion diseases didn't originate with human lines... no way to tell though is there? It's not as though we can check the mitochondrial line of a protein... :grumpy: . Kuru... maybe that could have been the result of first, failed division, then exposure through post-mortem cannibalism?

I think some of them are likely to be extra-human in origin--Only because of the incredibly high amount of conservation between coding regions from species to species. And since prion proteins are coded proteins (though, we're not sure what they do yet), then it seems likely that at least some of the species of prion proteins may have origins that predate humans.

For the evidence available that would seem to make sense. Bovine Spongiform Encephalopathy (BSE) is transmissible to humans, though you don't actually get BSE. You get a variant of CJD (vCJD I believe those creative researchers named it), from a protein almost identical to the CJD one. Which suggests then, that BSE protein responsible for BSE in cows, is also coded for and produced in people.

I think though, not all prion diseases have homologues in other species--Which may mean there has been unique gene duplication events and subsequent protein family radiations which produce unique prion proteins in species as well.


Really a lot more work needs done on prions, but I think because of their rarity in causing human morbidity, the funding (unfortunately) just isn't there. Sad to say, but that happens to a lot of rare diseases.

I'm not betting against you... CSF contamination with prions strikes me as a rather nasty death sentence.

Certainly, any 'death by prion' would probably be up there with my top "least ways I would want to die". Especially considering there is literally no treatments for the cause of the disease. We can really only target symptoms and try to make a person comfortable as they lapse into dementia, insanity, neurodegeneration or in the case FFI--death from insomnia.

I wonder if they're actively carried through, or if it's a matter of causing precipitation in the brain without needing to REACH the brain.

I don't know, that would be a pretty amazing feat of biology. But with all the new stuff we've learned about prions, I wouldn't put it past them.

I'd imagine, although there is clearly no evidence, that it might be the very "misshapen" nature of these proteins that save them from proteases. I'd guess that a novel protease would be needed for any given prion disease.

I know some naturally occurring prions have been shown to have sensitivity to proteases, but I'm not sure if these are endogenous to the organism or if researchers are digesting them with exogenous (to the species) proteases.

Many of the synthetic model prion systems created in bacteria also show sensitivity to proteases, specifically eukaryotic ones. We're still working out what exactly creates that high protease resistance in disease causing prions.

You would think, from a functional and steric standpoint, that prions would be resistant to either exoproteases or endoproteases, not both. But, it seems if they are one of those protein flukes of nature that get to have their cake and eat it too.

I'd agree, a species would probably need to evolve a new novel protease to deal with the disease. I suspect though, that historically (evolutionary speaking), prion mortality has "flown under the radar" so to say and not exerted enough selective pressure on a population for such a thing to occur. Who knows though? Maybe some proteases, yet to be discovered actually do protect us from prion diseases and we are just unawares, as of yet.

The scary thing, is how many different proteins we've discovered (and thinking of those yet to be discovered) which belong to the prion family. Maybe it will turn out, this has been an ongoing evolutionary battle for a long time and many of the prion "traps" are kept in check by such novel protreases. I'd suspect though, if that were the case, we'd see prion diseases more often when the genes for these proteases get's wrecked.

I'd counter that though (I'm debating myself here, must be my prion disease :)!) with, there maybe diseases which are prion diseases and we just don't know it. Alzheimer's and a few others (especially many of the "unknown cause dementias") spring to mind--As we still don't really know what causes them, and many of the symptoms (especially the plaque findings) ring suspiciously of prion disease to me.


EDIT: Ohhhhhhh, very excited now! I'd never looked into this link before and just did a quick Google for Alzheimer's and prions and am pleasantly surprised by the results.

"[URL
'Harmless' prion protein linked to Alzheimer's disease[/URL]

Prions, it could turn out, maybe the smoking gun on a lot of these multifactorial diseases of the brain. Maybe the breast cancer people should share some money with the prion guys! They might turn out to a play a much larger role in human morbidity than anyone suspected.

Hmmm... could it be that some proteins are denatured by HCl, and not the usual enzymes? A limit to that of course, but it would explain how they survive, but some end as... well... food and excreta.

I suspect you are right. Modern genetics has certainly taught us (polymorphisms and whatnot) the amount of variability between individuals at the molecular level. It would have been a very interesting study to look at the onset of disease, exposure amount and acidity of the GI tract in individuals who acquired Kuru before the practices which lead to transmission stopped.

Certainly, its something that could investigated in an animal model. Now if I can just find an unsuspecting herd of sheep, a pile of scrapie and someone to fund the research :tongue2:

Keep talking, I like reading your posts... VERY informative!

Thanks

 

[nismaratwork]

I think some of them are likely to be extra-human in origin--Only because of the incredibly high amount of conservation between coding regions from species to species. And since prion proteins are coded proteins (though, we're not sure what they do yet), then it seems likely that at least some of the species of prion proteins may have origins that predate humans.

For the evidence available that would seem to make sense. Bovine Spongiform Encephalopathy (BSE) is transmissible to humans, though you don't actually get BSE. You get a variant of CJD (vCJD I believe those creative researchers named it), from a protein almost identical to the CJD one. Which suggests then, that BSE protein responsible for BSE in cows, is also coded for and produced in people.

I think though, not all prion diseases have homologues in other species--Which may mean there has been unique gene duplication events and subsequent protein family radiations which produce unique prion proteins in species as well.


Really a lot more work needs done on prions, but I think because of their rarity in causing human morbidity, the funding (unfortunately) just isn't there. Sad to say, but that happens to a lot of rare diseases.



Certainly, any 'death by prion' would probably be up there with my top "least ways I would want to die". Especially considering there is literally no treatments for the cause of the disease. We can really only target symptoms and try to make a person comfortable as they lapse into dementia, insanity, neurodegeneration or in the case FFI--death from insomnia.




I don't know, that would be a pretty amazing feat of biology. But with all the new stuff we've learned about prions, I wouldn't put it past them.



I know some naturally occurring prions have been shown to have sensitivity to proteases, but I'm not sure if these are endogenous to the organism or if researchers are digesting them with exogenous (to the species) proteases.

Many of the synthetic model prion systems created in bacteria also show sensitivity to proteases, specifically eukaryotic ones. We're still working out what exactly creates that high protease resistance in disease causing prions.

You would think, from a functional and steric standpoint, that prions would be resistant to either exoproteases or endoproteases, not both. But, it seems if they are one of those protein flukes of nature that get to have their cake and eat it too.

I'd agree, a species would probably need to evolve a new novel protease to deal with the disease. I suspect though, that historically (evolutionary speaking), prion mortality has "flown under the radar" so to say and not exerted enough selective pressure on a population for such a thing to occur. Who knows though? Maybe some proteases, yet to be discovered actually do protect us from prion diseases and we are just unawares, as of yet.

The scary thing, is how many different proteins we've discovered (and thinking of those yet to be discovered) which belong to the prion family. Maybe it will turn out, this has been an ongoing evolutionary battle for a long time and many of the prion "traps" are kept in check by such novel protreases. I'd suspect though, if that were the case, we'd see prion diseases more often when the genes for these proteases get's wrecked.

I'd counter that though (I'm debating myself here, must be my prion disease :)!) with, there maybe diseases which are prion diseases and we just don't know it. Alzheimer's and a few others (especially many of the "unknown cause dementias") spring to mind--As we still don't really know what causes them, and many of the symptoms (especially the plaque findings) ring suspiciously of prion disease to me.




I suspect you are right. Modern genetics has certainly taught us (polymorphisms and whatnot) the amount of variability between individuals at the molecular level. It would have been a very interesting study to look at the onset of disease, exposure amount and acidity of the GI tract in individuals who acquired Kuru before the practices which lead to transmission stopped.

Certainly, its something that could investigated in an animal model. Now if I can just find an unsuspecting herd of sheep, a pile of scrapie and someone to fund the research :tongue2:



Thanks

This is extremely informative! I think it might be the best angle for funding in a counter-terrorism role, now that inhaled prions have been shown to be potentially dangerous. It seems like an area of inquiry that could yield a deeper understanding of how genes code specific proteins... not exactly a bad area to fund.

Ah well... maybe someone else will fall to cannibalism again and we'll have a chance to do a bit of the old autopsy. Grim, but I can't help but think it would be an eye-opener.

 

[bobze]

This is extremely informative! I think it might be the best angle for funding in a counter-terrorism role, now that inhaled prions have been shown to be potentially dangerous. It seems like an area of inquiry that could yield a deeper understanding of how genes code specific proteins... not exactly a bad area to fund.

Ah well... maybe someone else will fall to cannibalism again and we'll have a chance to do a bit of the old autopsy. Grim, but I can't help but think it would be an eye-opener.

Don't miss the edit I just put in about prions and Alzheimer's !

 

[bobze]

Damn, all this end of block med school stuff to study--But now the wheels are turning and I just want to look further into what research links have been found between prions and these brain diseases which cause plaque formations!

You know, since the prions are sequenced I believe it would be an interesting little BLAST experiment to see how much homology you can find between them and other parts of the genome--Specifically stuff like tau-map genes. Once spring break hits, I'll look further into and report my BLAST findings back here :)

 

[nismaratwork]

Don't miss the edit I just put in about prions and Alzheimer's !

Very interesting... my grandmother died of Alzheimers, and I must say that it's a very strange ailment. Given amyloid plagues and the slooooow degenerative course, I'm hardly going to scoff at that. It would also explain why the damage is so easy to see, but the cause and treatment remain elusive. Sad, but a good point to make...

 

[nismaratwork]

Damn, all this end of block med school stuff to study--But now the wheels are turning and I just want to look further into what research links have been found between prions and these brain diseases which cause plaque formations!

You know, since the prions are sequenced I believe it would be an interesting little BLAST experiment to see how much homology you can find between them and other parts of the genome--Specifically stuff like tau-map genes. Once spring break hits, I'll look further into and report my BLAST findings back here :)

Excellent! It would be very intersting to find that one or more of these diseases classified molstly by autopsy and symptoms had a common cause. Frankly, it would make a lot of sense.

 

[hshields]

Recently scientists have said Alzheimer's and Parkinson Diseases in humans are transmissible prion/protein misfolding diseases:
spam link deleted

Human prion diseases such as Alzheimer's and Parkinson's, may be due to lack of USDA testing for mad cow disease (in 2010 only 34,386 cows were tested out of 37 million slaughtered)
http://www.aphis.usda.gov/newsroom/hot_issues/bse/surveillance/ongoing_surv_results.shtml

Prions in animal feeds are also a serious risk:

Livestock, sheep, goats, pigs, poultry, dogs, cats, etc. are being fed the MBM (meat and bone meal) rendered remains of potentially prion infected animals. The US Dept. of Agriculture has been covering up for years the fact that 1.9 million "downer cows" - the animals most likely to have Bovine Spongiform Encephalopathy (BSE) - Mad Cow Disease - are rendered into animal feeds and pet food.each year. Only about 5000 are tested for BSE. Rendering does not inactivate prions.

spam link deleted

Bovine Spongiform Encephalopathy (BSE) (mad cow) has been circulating and amplifying in the US food chain since the mid 1980s when Dr. Richard Marsh proved that farmed mink were dying from Transmissible Mink Encephalopathy (TME) after being fed downer cattle.
http://www.organicconsumers.org/madcow/andrew1804.cfm

"Could Alzheimer's be infectious? " http://neurophilosophy.wordpress.com/2006/11/24/could-alzheimers-be-infectious/

SEE reply posted by:
Dr. Murray Waldman, coroner for the city of Toronto, Canada:
"In answer to the question how would Alzheimer’s (AD) be transmitted, I have written a book “Dying For A Hamburger” that hypothesizes that AD is spread by how we in North America and Europe feed and process meat, mainly beef.
If you study the rates of AD and its geographical distribution, you will find that rates start to soar when a country becomes meat eating (i.e. Japan and Korea in the 1960s) and rises even faster when it adopts a fast food culture (the US and Western Europe in the 50s and 60s) and remains low in vegetarian countries (India) and those without a processed meat industry or fast foods (equatorial Africa)…Murray "

See VIDEO Interview –Mad Cow and Misdiagnosed Alzheimer’s Disease

http://www.healthydepartment.com/alzheimers-disease/interview-mad-cow-and-misdiagnosed-alzheimers-disease-4541.html

Interview with Dr. Colm Kelleher author of “Brain Trust:The Hidden Connection Between Mad Cow and Misdiagnosed Alzheimer’s Disease” recorded November 16, 2004. video about 1 hour long – well worth the time

Prion diseases may also be caused by modern meat packing practices where by "a typical burger patty is packed with the meat and fat of 50 to 100 cattle from multiple states and two to four countries.

Eat two hanburgers a week — as the average American does — and in a year's time the consumer samples a stampede: 5,200 to 10,400 cattle."

http://www.think-aboutit.com/health/CattleDrive.htm

Human and animal prions in sewage sludge "biosolids" being topdressed as "fertilizer" on America's cropland, including grazing land, hay fields and dairy pastures, are putting livestock and wildlife at risk:

spam links deleted

 

[Proton Soup]

^ I'm sorry, but all this parkinson's/alzheimer's prion stuff above is plain quackery. and likely just more vegan PeTArded propaganda that you don't actually even believe.

 

[hshields]

^ I'm sorry, but all this parkinson's/alzheimer's prion stuff above is plain quackery. and likely just more vegan PeTArded propaganda that you don't actually even believe.

Alzheimer's is a prion disease: [COLOR="Blue"]spam link deleted [/C...Disease_a_Prion_Like_Disease__Experts.12.aspx

January 21, 2010 -
<



Is Parkinson Disease a Prion-Like Disease? Experts Say Yes (Maybe)
ROBINSON, RICHARD

Free Access
Back to Top | Article Outline
ARTICLE IN BRIEF
A theory gaining traction among some Parkinson disease (PD) experts is that PD may be a prion-like disorder, based on evidence that alpha-synuclein can be transmitted from neuron to neuron, leading to the development of Lewy body-like inclusions in the receiving cell, and other findings from neuroanatomy, fetal transplantation surgery, and basic science.

Is Parkinson disease (PD) a prion-like disorder, with alpha-synuclein playing the role of infectious protein? The answer to that provocative question may be “yes,” according to a growing number of PD experts, as they consider findings from neuroanatomy, fetal transplantation surgery, and basic science.

Dr. Prusiner won the Nobel Prize in 1997 for his discovery of the prion.

http://cshperspectives.cshlp.org/content/3/1/a006833.full.pdf+html David Colby & Stanley Prusiner - Released January 2011

ENLARGING SPECTRUM OF PRION-LIKE DISEASES

The discovery that prions form amyloid prompted one of us to suggest that the common neurodegenerative diseases are also caused by prions (Prusiner 1984; Prusiner 2001) despite the inability to transmit such illnesses to monkeys and apes (Goudsmit et al. 1980).

Brain extracts from either Alzheimer’s patients or aged Tg mice expressing mutant APP injected into the brains of Tg mice expressing the amyloid precursor protein (APP) carrying the Swedish point mutation (Haass et al. 1995) accelerated the formation of Ab amyloid plaques (Meyer-Luehmann et al. 2006; Eisele et al. 2009). Brain extracts from Tg mice expressing mutant tau injected into the brains of Tg mice expressing human wt tau produced aggregates of human tau (Clavaguera et al. 2009). Similar results were found for aggregated tau protein added to cultured cells, which induced the aggregation of nascent tau (Frost et al. 2009).

These findings suggest that the tauopathies result from a prion-like process that induces hyperphosphorylation of tau followed by polymerization into filamentous aggregates. The production of hyperphosphorylated tau also appears to be stimulated by oligomers of the Ab peptide, whereas amyloid fibrils comprised of Ab are a much less efficient stimulus (Lambert et al. 1998). An expanded 44-mer polyglutamine repeat of a truncated huntingtin protein was found to stimulate aggregation of a “normal” 25 mer; this aggregated state could be maintained in cell culture over many generations, arguing for prion-like propagation of huntingtin aggregates (Ren et al. 2009).

Patients suffering from Parkinson’s disease who received fetal grafts of substantia nigral cells later showed aberrantly folded a-synuclein in Lewy bodies within the transplanted grafts, arguing that a-synuclein acted like a prion (Kordower et al. 2008; Li et al. 2008; Olanow and Prusiner 2009). Taken together, these findings argue that prion-like, self-propagating states feature in many different, if not all, neurodegenerative diseases.

A general model of propagation of mammalian prion-like conformational states should include the following considerations (Table 2): First, when the precursor protein is converted to a prion, it undergoes posttranslational modification. Such changes generally result in the acquisition of a high b-sheet content. Proteolytic cleavage features in Alzheimer’s disease (AD) (Glenner and Wong 1984; Masters et al. 1985) and hyperphosphorylation occurs in both AD and the tauopathies (Grundke-Iqbal et al. 1986; Lee et al. 1991).

 

[Proton Soup]

Alzheimer's is a prion disease:
Nobel Laureate Stanley Prusiner and Dr. Warren Olanow:


http://journals.lww.com/neurotodayo...Disease_a_Prion_Like_Disease__Experts.12.aspx

the problem for you is that alpha-synuclein is encoded on the human genome.

http://en.wikipedia.org/wiki/Alpha-synuclein

so your speculation about beef is unsupported. we make the protein ourselves. you could just as easily speculate that eating a vegetable causes the disease cascade to occur.

 

[bobze]

Time-Out!

Hshields, some of your stuff does seem to be a little "fringe". The possible link to Alzheimer's and prions exists, but whether it is causative is certainly speculative. And certainly saying that it is the cause is incorrect. Alzheimer's is mutlifactorial, I suspect that prion proteins or some of their homologous coding regions play a role, but other things (like tau-MAPs) are certainly involved.

Proton-While I agree that some of the linked stuff is "fringy", the link certainly exists between protein folding disorders (like Alzheimer's and Parkinson's) and prion proteins.

All prion proteins are encoded for by the organisms genome. There is more than one (probably from gene duplication events or amino acid homology which can lead to aggregate and precipitate formation) in our genomes.

I explained above, prion proteins (where not really sure what exactly they do yet--At least most of them, but probably all play integral roles in neural functions) exist in a balance between a structural isoforms. One favors alpha helices, the other beta sheets.

When the beta sheet isoform dominates, it precipitates out of solution which drives the reaction to the right and pulls more protein out of solution. This leads to plaque and fibrillary tangle formation--Which is what causes destruction of neurons.

The general equilibrium for prions looks something like;

PrP↔PrP^sc**→PrP^sc aggregates.

**SC was the prion protein species initially discovered in the prion disease scrapie (sheep) but "PrP^sc" is now used when discussing any general form of prion protein.

Introducing PrP^sc, rather than just driving the equilibrium back to the left, causes the aggregate formation--Which forces more prion protein in the equilibrium to the prion form. For reasons unknown, aggregate deposition fuels more and more aggregate deposition and ultimately leads to a prion disease.

 

[bobze]

the problem for you is that alpha-synuclein is encoded on the human genome.

http://en.wikipedia.org/wiki/Alpha-synuclein

so your speculation about beef is unsupported. we make the protein ourselves. you could just as easily speculate that eating a vegetable causes the disease cascade to occur.

AS is found in association with amyloid plaques (it has been found with them in prion diseases like vCJD) but is not strictly colocalized. Since it thought to be a molecular chaperone it would make sense that is found there and may play a central part in the role in neurodegenerative protein folding disorders.

That we code for it doesn't really mean anything. As I pointed out earlier in the topic, because of homology, some prion species can cross species boundaries (though I am not saying that AS is a prion).

 

[EntropicLove]

Didn't lab mice die after 2 weeks of not sleeping? I believe it was related to immune system shut-down.

 

[nismaratwork]

Didn't lab mice die after 2 weeks of not sleeping? I believe it was related to immune system shut-down.

I'm not sure about the timing, but they have a much faster metabolism... it's part of why they're used for testing. In essence, they die faster from any metabolic syndrome, which is usually a part of death from true sleep deprivation.

 

[nismaratwork]

Recently scientists have said Alzheimer's and Parkinson Diseases in humans are transmissible prion/protein misfolding diseases:

Human prion diseases such as Alzheimer's and Parkinson's, may be due to lack of USDA testing for mad cow disease (in 2010 only 34,386 cows were tested out of 37 million slaughtered)
http://www.aphis.usda.gov/newsroom/hot_issues/bse/surveillance/ongoing_surv_results.shtml

Prions in animal feeds are also a serious risk:

Livestock, sheep, goats, pigs, poultry, dogs, cats, etc. are being fed the MBM (meat and bone meal) rendered remains of potentially prion infected animals. The US Dept. of Agriculture has been covering up for years the fact that 1.9 million "downer cows" - the animals most likely to have Bovine Spongiform Encephalopathy (BSE) - Mad Cow Disease - are rendered into animal feeds and pet food.each year. Only about 5000 are tested for BSE. Rendering does not inactivate prions.



Bovine Spongiform Encephalopathy (BSE) (mad cow) has been circulating and amplifying in the US food chain since the mid 1980s when Dr. Richard Marsh proved that farmed mink were dying from Transmissible Mink Encephalopathy (TME) after being fed downer cattle.
http://www.organicconsumers.org/madcow/andrew1804.cfm

"Could Alzheimer's be infectious? " http://neurophilosophy.wordpress.com/2006/11/24/could-alzheimers-be-infectious/

SEE reply posted by:
Dr. Murray Waldman, coroner for the city of Toronto, Canada:
"In answer to the question how would Alzheimer’s (AD) be transmitted, I have written a book “Dying For A Hamburger” that hypothesizes that AD is spread by how we in North America and Europe feed and process meat, mainly beef.
If you study the rates of AD and its geographical distribution, you will find that rates start to soar when a country becomes meat eating (i.e. Japan and Korea in the 1960s) and rises even faster when it adopts a fast food culture (the US and Western Europe in the 50s and 60s) and remains low in vegetarian countries (India) and those without a processed meat industry or fast foods (equatorial Africa)…Murray "

See VIDEO Interview –Mad Cow and Misdiagnosed Alzheimer’s Disease

http://www.healthydepartment.com/alzheimers-disease/interview-mad-cow-and-misdiagnosed-alzheimers-disease-4541.html

Interview with Dr. Colm Kelleher author of “Brain Trust:The Hidden Connection Between Mad Cow and Misdiagnosed Alzheimer’s Disease” recorded November 16, 2004. video about 1 hour long – well worth the time

Prion diseases may also be caused by modern meat packing practices where by "a typical burger patty is packed with the meat and fat of 50 to 100 cattle from multiple states and two to four countries.

Eat two hanburgers a week — as the average American does — and in a year's time the consumer samples a stampede: 5,200 to 10,400 cattle."

http://www.think-aboutit.com/health/CattleDrive.htm

Human and animal prions in sewage sludge "biosolids" being topdressed as "fertilizer" on America's cropland, including grazing land, hay fields and dairy pastures, are putting livestock and wildlife at risk:

Don't take this the wrong way, but you've presented (valid) speculation as fact, and used highly questionable sources with clear agendas. If you expect to be anything other than dismissed a crackpot here, you need to back your statements of FACT with more than exists right now.

Beyond that, what Bobze said.