Post by crystalriver on Nov 18, 2009 17:41:51 GMT -5
The Prion As The Vector For Morgellons--By Skyship
Posted By: CrystalRiver <Send E-Mail>
Date: Wednesday, 18-Nov-2009 17:31:27 Not a bug, not a worm, not a plant, but a vector.
The Original filament of life and its cohort, The Prion.
The Amyloid filament and the Prion got together and decided
to create new life, new life birthed in a lab, so that proteins
could unfold, fold in, switch channels, take away, add in,
promote, report, integrate with natural native genes on
its molecular journey toward artificial life.
Well, it does appear that in the process many more
amyloid-type, prion-type diseases are unfolding as well.
================================
www.medicinenet.com/amyloidosis/article.htm
users.rcn.com/jkimball.ma.ultranet/BiologyPages/P/Prions.html
MORGELLONS
==============================
I shall present my case here:
=========================
...."But the idea that a protein could transmit information did not disappear. Carleton Gajdusek had already proposed that proteins could be infectious, based on his discovery that kuru disease was possibly caused by a protein from the brain (Gajdusek, 1977). It took a long time before this idea was accepted. Only after an extended uphill battle did the biomedical community finally accept Prusiner's theory that proteins are the only pathogen to cause scrapie in sheep, bovine spongiform encephalopathy in cattle and Creutzfeldt–Jakob disease in humans (Prusiner, 1982). Prusiner's work, which earned him the Nobel Prize, was a minor revolution against an established dogma as the biomedical research community believed that only viruses and bacteria—organisms that carry nucleic acids—could be infectious. I will not discuss the enormous scientific work that followed the establishment of prions as pathogens, but will instead concentrate on the more recent discovery of prions as genetic elements that store and transmit information in various organisms, mainly yeast, the fungi Podospora and the sea hare Aplysia (Fig 1Figure 1; Shorter & Lindquist, 2005).
Figure 1
The sea hare Aplysia.
.......In science, the introduction of a new technical tool commonly opens new avenues of knowledge. Yeast quickly became a model organism for molecular biologists because it is a very simple eukaryote with a growth cycle of 80 minutes, which allows a large amount of material for biochemical analysis to be collected in a few hours. It was in yeast that researchers found the first evidence of non-mendelian transmission of phenotypic traits (Cox, 1965; Lacroute, 1971). These phenomena baffled scientists for more than 40 years before they could be attributed to prions: [PS1+] suppresses nonsense codons in translation, and [URE3] inhibits nitrogen catabolite repression (Wickner, 1994). Both are caused by self-replicating conformational changes—to the translation suppressor sup35 in the case of [PS1+], and the Ure2 protein, an antagonist of the transcriptional activators Gln3 and Gat1, in the case of [URE3]. Another prion, [Hets] in Podospora anserina, was found to be involved in programmed cell death when two fungal strains with different genotypes fuse (Coustou et al, 1997; Maddelein et al, 2002). In addition, work by Kandel showed that a prion has an important role in the formation and maintenance of long-term memory (Si et al, 2003).".......................
www.ncbi.nlm.nih.gov/pmc/articles/PMC1369155/
===================================
Now lets just digest this for a minute......
skyship
Posted By: CrystalRiver <Send E-Mail>
Date: Wednesday, 18-Nov-2009 17:31:27 Not a bug, not a worm, not a plant, but a vector.
The Original filament of life and its cohort, The Prion.
The Amyloid filament and the Prion got together and decided
to create new life, new life birthed in a lab, so that proteins
could unfold, fold in, switch channels, take away, add in,
promote, report, integrate with natural native genes on
its molecular journey toward artificial life.
Well, it does appear that in the process many more
amyloid-type, prion-type diseases are unfolding as well.
================================
www.medicinenet.com/amyloidosis/article.htm
users.rcn.com/jkimball.ma.ultranet/BiologyPages/P/Prions.html
MORGELLONS
==============================
I shall present my case here:
=========================
...."But the idea that a protein could transmit information did not disappear. Carleton Gajdusek had already proposed that proteins could be infectious, based on his discovery that kuru disease was possibly caused by a protein from the brain (Gajdusek, 1977). It took a long time before this idea was accepted. Only after an extended uphill battle did the biomedical community finally accept Prusiner's theory that proteins are the only pathogen to cause scrapie in sheep, bovine spongiform encephalopathy in cattle and Creutzfeldt–Jakob disease in humans (Prusiner, 1982). Prusiner's work, which earned him the Nobel Prize, was a minor revolution against an established dogma as the biomedical research community believed that only viruses and bacteria—organisms that carry nucleic acids—could be infectious. I will not discuss the enormous scientific work that followed the establishment of prions as pathogens, but will instead concentrate on the more recent discovery of prions as genetic elements that store and transmit information in various organisms, mainly yeast, the fungi Podospora and the sea hare Aplysia (Fig 1Figure 1; Shorter & Lindquist, 2005).
Figure 1
The sea hare Aplysia.
.......In science, the introduction of a new technical tool commonly opens new avenues of knowledge. Yeast quickly became a model organism for molecular biologists because it is a very simple eukaryote with a growth cycle of 80 minutes, which allows a large amount of material for biochemical analysis to be collected in a few hours. It was in yeast that researchers found the first evidence of non-mendelian transmission of phenotypic traits (Cox, 1965; Lacroute, 1971). These phenomena baffled scientists for more than 40 years before they could be attributed to prions: [PS1+] suppresses nonsense codons in translation, and [URE3] inhibits nitrogen catabolite repression (Wickner, 1994). Both are caused by self-replicating conformational changes—to the translation suppressor sup35 in the case of [PS1+], and the Ure2 protein, an antagonist of the transcriptional activators Gln3 and Gat1, in the case of [URE3]. Another prion, [Hets] in Podospora anserina, was found to be involved in programmed cell death when two fungal strains with different genotypes fuse (Coustou et al, 1997; Maddelein et al, 2002). In addition, work by Kandel showed that a prion has an important role in the formation and maintenance of long-term memory (Si et al, 2003).".......................
www.ncbi.nlm.nih.gov/pmc/articles/PMC1369155/
===================================
Now lets just digest this for a minute......
skyship