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Prion Proteins Play Powerful Role in Survival, Evolution

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posted on Feb, 16 2012 @ 10:10 AM
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Prion proteins play powerful role in survival, evolution of wild yeast strains

Prions, the much-maligned proteins most commonly known for causing "mad cow" disease, are commonly used in yeast to produce beneficial traits in the wild. Moreover, such traits can be passed on to subsequent generations and eventually become "hard-wired" into the genome, contributing to evolutionary change.

...Lindquist speculates that these shape-shifting proteins may be "remnants of early life," from a time when inheritance was predominantly protein-based rather than nucleic-acid based. She also theorizes that prions may play such roles beyond yeast, and her lab intends to take similar approaches in the hunt for prion activity in other organisms.


Prion research has the ability to bring about a much-needed and major paradigm shift in our thinking about disease, life and everything.

Bottom line: We are all connected - microbes, proteins, molecules, complex organisms - and we share everything with one another. Time to wake up and quit mucking up the machinery.





Check out this thread too: The real midichlorians: A case for Pleomorphism





edit on 16/2/12 by soficrow because: (no reason given)




posted on Feb, 16 2012 @ 10:15 AM
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I've been fascinated with Prions ever since I read "Circumference of Darkness." You don't have to read the whole book. Just use Google Books to search for it, then skip to Section 22/Chapter 28/ Page 275. Heres a link:

books.google.com...= onepage&q=cow&f=false



posted on Feb, 16 2012 @ 12:14 PM
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reply to post by questforevidence
 


Thanks for the link - but the excerpt only goes to page 198, so your point is missed. ...Having read the review, the book sounds like yet another "OMG, the terrorists are coming" warning, which would completely miss the mark on prions as an evolutionary force and (again) misrepresent their primary role as an adaptive mechanism.



posted on Feb, 16 2012 @ 12:54 PM
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Let's just hope this doesn't lead some to conclude that Soylent Green is ready for roll out.

But, really, prions are pretty darn cool. A protein that can persist in the ground soil for decades after being eliminated from the organism of origin? A protein that behaves in mammals like a virus, and resists all kinds of disinfecting agents? Whoa.

Lots of different sorts, but the mammalian strains tend to be bad news. Friends don't let friends engage in cannibalism.
edit on 16-2-2012 by Eidolon23 because:




posted on Feb, 16 2012 @ 06:59 PM
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reply to post by Eidolon23
 


RE:



.....mammalian strains


Prions probably are responsible for cross-species, cross-kingdom and even cross-domain communication aka "infectivity." Evidence suggests protein strains don't respect biological boundaries...



posted on Feb, 16 2012 @ 09:09 PM
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reply to post by soficrow
 


Er, sort of..


I really enjoyed that article. Have you looked at fungal prions?

www.ncbi.nlm.nih.gov...

This article goes into that, as well as the differences between strains.



posted on Feb, 16 2012 @ 09:53 PM
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reply to post by soficrow
 


Here you go:

Page1


Page2


Page3


It's an interesting book. Kind of like a more extreme version of Live Free Or Die Hard.



posted on Feb, 16 2012 @ 10:45 PM
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reply to post by Eidolon23
 


Your article dates from 2008 - much has been discovered since then, although granted, much remains 'controversial.' For example, it's now commonly recognized that virtually any proteins can misfold (not just the brain's 'prion' protein). Fact is too, other molecules misfold as well. And regardless of source, the 'right' shape can be a key to access similar molecules across species and other barriers. Turns out the "species barrier" is a bit of a myth - there's even evidence of cross-domain infectivity.

Also, the article's intro refers to "uniformly fatal" mammalian strains, focusing exclusively on the brain's "prion protein." Just a linguistic game - as pointed out above, virtually any protein can misfold and cause disease. ...Mammalian prion strains now are defined as related to the brain protein now called 'prion protein' - other misfolded proteins are not officially called prions, and other diseases caused by misfolded proteins are called "conformational disorders" or "protein misfolding disorders."


PS. Good article though! Thanks. GREAT history of prion science.


PPS. I should probably delete this and rewrite, not just tinker and tweak. But won't. We should talk more though. ...My assessment is that prion science has been suppressed because acknowledging the truth would change the whole paradigm, and pretty much destroy Big Pharma, the medical industry and a whole lot more. ...It's also true I make a few leaps - but either way, this is world changing stuff.






edit on 16/2/12 by soficrow because: (no reason given)

edit on 16/2/12 by soficrow because: more tinkering, additions



posted on Feb, 16 2012 @ 10:55 PM
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reply to post by questforevidence
 



It's an interesting book. Kind of like a more extreme version of Live Free Or Die Hard.


I'll probably like it then.


Thanks for the text - I'm not happy with that very limited understanding of prions and prion diseases, but any press is good I guess.



posted on Feb, 16 2012 @ 11:32 PM
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reply to post by Eidolon23
 


Here's another interesting article for you.



Scientists Identify Most Lethal Known Species of Prion Protein

Scientists from the Florida campus of The Scripps Research Institute have identified a single prion protein that causes neuronal death similar to that seen in "mad cow" disease, but is at least 10 times more lethal than larger prion species. This toxic single molecule or "monomer" challenges the prevailing concept that neuronal damage is linked to the toxicity of prion protein aggregates called "oligomers."

….Lasmézas explains that prion diseases are similar to Alzheimer's and other protein misfolding diseases in that they are caused by the toxicity of a misfolded host protein. Recent work, as reported in The New York Times, also found that diseases such as Alzheimer's resemble prion diseases by spreading from cell to cell.

The new study adds another twist. "Until now, it was thought that oligomers of proteins are toxic in all these diseases," Lasmézas said. "Since we found for the first time that an abnormally folded monomer is highly toxic, it opens up the possibility that this might be true also for some other protein misfolding diseases as well."


Also see: Highly neurotoxic monomeric α-helical prion protein


Enjoy.



posted on Feb, 17 2012 @ 06:46 AM
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reply to post by soficrow
 


Whoa! Thank you so much!

I'm going to crack into those toot suite.

My favorite historical tidbit from the 2008 article:

The Chinese character for "disease" + the character for "sheep" = the character for "itchy".
Suggesting that the Chinese were familiar with scrapie.



posted on Feb, 18 2012 @ 07:57 AM
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reply to post by Eidolon23
 


...There's little doubt that prions have been around for a long, long time - they seem to be the key for understanding historical periods of accelerated evolution.

You might be interested in this thread too: Beyond DNA! Prions Point to a New Form of Evolution (VIDEO)




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