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Researchers confirm prion-like properties in ALS

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posted on Sep, 22 2011 @ 09:53 PM
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Researchers confirm prion-like properties in ALS


www.labcanada.com

A team of researchers …have found a key link between prions and the neurodegenerative disease amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig's disease.

…These findings provide a molecular explanation for the progressive spread of ALS through the nervous system, and highlight the central role of the propagation of misfolded proteins in the pathogenesis of neurodegenerative diseases, including ALS, Alzheimer's and Parkinson's.
(visit the link for the full news article)


Related News Links:
www.als.net
www.medicalnewstoday.com

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posted on Sep, 22 2011 @ 09:53 PM
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Let's call a spade a spade. ALS is yet another prion disease - along with Mad Cow, cancer, diabetes, atherosclerosis and practically every chronically debilitating, now-pandemic modern "disease of civilization."

Numerous proteins misfold, propagate and cause disease. However, it is politically incorrect to call every disease caused by a misfolded protein a "prion disease." Arguably though, that's exactly what they are. And there are a LOT of them. Worse, there have been "gag orders" on scientists since about 2003-4 preventing them from talking publicly about prions.

In ALS - amyotrophic lateral sclerosis, also known as Lou Gehrig's disease - a protein misfolds, spreads through the nervous system and causes progressive neurodegeneration. Infectious misfolded proteins infect similar proteins on contact, just by touch. It's called "template-directed misfolding," and refers to the "coercion of one protein by another protein to change shape and accumulate in large complexes in a fashion similar to the process underlying prion diseases." …Ergo, ALS is yet another prion disease.


Key Finding: "Intermolecular transmission of SOD-1 misfolding in living cells" - Published in the Proceedings of the National Academy of Sciences (PNAS), September 2011

* The paper shows that superoxide dismutase 1 (SOD1) participates in template-directed misfolding, in other words, the coercion of one protein by another protein to change shape and aggregate such as prion diseases do.
* The results will be significant to the ALS field because it connects prion mechanisms behind the biological progression of ALS, and provides a molecular explanation for the linear and temporal spread of ALS through the nervous system.
* Furthermore, the research has identified a specific molecular target, which when manipulated, halts the conversion of SOD1 to a misfolded, disease-causing form. This is a first-step towards the development of targeted treatments that may stop ALS, which PrioNet is further exploiting through newly-funded research.
* This research was supported by PrioNet Canada and in part by Amorfix Life Sciences and the Canadian Institutes of Health Research.



But - looks like the gag orders are loosening, if not dropping. Good news. Thank you Oprah and all the scientists and researchers who didn't give up.




Originally titled "Prion-like intermolecular transmission of SOD1 misfolding in living cells," the title was modified to "Intermolecular transmission of SOD-1 misfolding in living cells" in this week's Proceedings of the National Academy of Sciences (PNAS).


www.labcanada.com
(visit the link for the full news article)



posted on Sep, 23 2011 @ 01:13 AM
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Originally posted by soficrow
In ALS - amyotrophic lateral sclerosis, also known as Lou Gehrig's disease - a protein misfolds, spreads through the nervous system and causes progressive neurodegeneration.



And for more information on Lou Gehrig's disease, see this video, starting at 4:23...
www.youtube.com...



posted on Sep, 23 2011 @ 01:34 AM
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reply to post by alfa1
 


Stephen Hawking, an English theoretical physicist and cosmologist, also has ALS.




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