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Post by lilsissy on Mar 1, 2010 4:04:41 GMT -5
About three years ago Karen had a biopsy done at University of Michigan on her thyroid . They said she had Thyroid Cancer from the results of that biopsy. She underwent complete removal of her thyroid and the thyroid was sent to pathology. She contacted her doctor on numerous occasions to get the results of the Path report. After weeks of being put off she saw her doctor who explained to her that her thyroid path report showed no Cancer but abnormal fiber growth. The doctor had requested a few rechecks to the Pathologist during the times she kept putting Karen off but he finally told her it was not cancer. As you all know she is now being told she has Pancreatic Cancer. www.medicinenet.com/script/main/art.asp?articlekey=104759Karen's husband has Alzheimer's . He was also in the tree business like Sue's husband Tom. I have myself seen fibers dark waxy looking fibers coming forth from the skin over Karen's knees after she applied Triple antibiotic ointment on them for 20 minutes followed by Caspian liquid 20 minutes. If you try this experiment do not touch the applicator to the skin but touch the applicator so the liquid leaks onto the skin. Be sure there is no fiber on the skin by running water over the skin and allow to air dry . You must wait the time or you will see nothing.
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Post by lilsissy on Mar 1, 2010 4:06:35 GMT -5
This next atrticle is very interesting to me . Do you guys remember the video of Baccilus fiber balls moving? Well if we have a prions we would have a happy colony of Baccilus . Bactracin cream is the only relief I get from the swollen ozzing scalp cysts I get. It works overnight sometimes you must repeat this twice. pubs.acs.org/doi/abs/10.1021/jf803072r
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Post by lilsissy on Mar 1, 2010 4:08:23 GMT -5
Here is the article about the mutation benefit of prions. outlook.wustl.edu/spring2005/prions.htmlFOR RESEARCHERS LIKE David A. Harris, MD, PhD, the long, slow exit from the twilight zone is all but over. Harris has been studying prions, a new kind of infectious agent thought to be at the heart of several rare neurodegenerative disorders that devastate the brains of humans, cows and sheep. The switch to prion-prone Sup35, which occurs spontaneously about once in every million generations of yeast, often has harmful effects. But in about 20 percent of test cases, the disruptions gave the yeast a survival advantage in an environment in which temperature, the availability of food or other factors had changed. Our world is changing rapidly . We are being bathed in wireless energy , energy that sets phosphorus aglow. We are part phosphorus. What does not merge through mutation will die off. Whatever this is, it does form fibers that very well could be cables, wires, prions , whatever one may call it . The end result is a network of fibers possibly optics.
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Post by lilsissy on Mar 1, 2010 4:10:04 GMT -5
Sound familar, proteinaceous infectious particle ? These were discovered in 1982 . All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. So it causes polymerization in the body , that would fit the fiber optic theroy. www.hepatitis-central.com/hcv/whatis/prion.htmlsingle infectious agent consisting only of protein and with no associated nucleic acid (RNA or DNA). Sound familar? The protein PrP can exists in two forms: a normal, harmless form (found in white blood cells and on the surface of brain nerve cells and believed to be involved in the trafficking of copper ions) and an abnormal, disease-causing form. The latter is very stable and has been found to be resistant to temperatures as high as 350°C/660°F, ultraviolet radiation, and strong enzymes. It causes infection by setting up a chain reaction that induces the normal protein to fold into the abnormal form. As the prions accumulate in the nervous system, they aggregate to form long filaments that damage the tissues, creating holes in the brain and giving it a characteristic spongy appearance. Because the immune system does not recognize the prions as foreign, no immune reaction develops. In 1992 German researchers showed that mice that lack the PrP gene are not susceptible to scrapie, a finding that strongly supports the theory that normal PrP proteins are necessary for the progression of the disease. Prion diseases have been found to arise both by transmission from other individuals (through, for example, diet or medical procedures) and by the inheritance of a mutation in the PrP gene. Different mutations give rise to slightly different prions, which accumulate in specific regions of the brain and cause particular symptoms and diseases. About 10% of human prion diseases are hereditary, including CJD and Gerstmann–Sträussler–Scheinker disease (a rare form of dementia). It has been suggested that prions consisting of other, non-PrP proteins might be responsible for other degenerative diseases in humans, including Alzheimer's disease. The infectivity of prions violates the central dogma of molecular biology inasmuch as it implies the transfer of genetic information (how to form infectious particles) directly from protein to protein, without the usual detour via nucleic acids. This aspect is even clearer in a group of proteins known as yeast prions. While these do not cause any disease, their alternative folded states can lead to different phenotypes, which can be passed on to the next generation without the involvement of nucleic acids. The protein that prions are made of (PrP) is found throughout the body, even in healthy people and animals. However, PrP found in infectious material has a different structure and is resistant to proteases, the enzymes in the body that can normally break down proteins. The normal form of the protein is called PrPC, while the infectious form is called PrPSc — the C refers to 'cellular' or 'common' PrP, while the Sc refers to 'scrapie', a prion disease occurring in sheep. [16] While PrPC is structurally well-defined, PrPSc is certainly polydisperse and defined at a relatively poor level. PrP can be induced to fold into other more-or-less well-defined isoforms in vitro, and their relationship to the form(s) that are pathogenic in vivo is not yet clear.
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Post by lilsissy on Mar 1, 2010 4:11:28 GMT -5
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Post by skyship on Mar 2, 2010 4:40:50 GMT -5
some links here gotta look at the sup35p forms ure2 amyloids etc. Sup35p From Wikipedia, the free encyclopedia Jump to: navigation, search Sup35p is the Saccharomyces cerevisiae (a yeast) eukaryotic translation release factor. More specifically, it is the yeast eukaryotic release factor 3 (eRF3), which forms the translation termination complex with eRF1 (Sup45p in yeast). This complex recognizes and catalyzes the release of the nascent polypeptide chain when the ribosome encounters a stop codon. While eRF1 recognizes stop codons, eRF3 facilitates the release of the polypeptide chain through GTP hydrolysis. Partial loss of function results in nonsense suppression, in which stop codons are ignored and proteins are abnormally synthesized with carboxyl terminal extensions. Complete loss of function is fatal. History Sup35p was shown to propagate in a prion form in 1994 by Reed Wickner. For this reason it is an intensely studied protein. When yeast cells harbor Sup35p in the prion state the resulting phenotype is known as [PSI+]. In [PSI+] cells Sup35p exists in an amyloid state that can be propagated and passed to daughter cells. This results in less soluble and functional protein and thus an in increased rate of nonsense suppression (translational read-through of stop codons). Several recent journal articles have suggested that the ability to interconvert between [PSI+] and [psi-](prion-free) states provides an evolutionary advantage, but this remains an area of much debate. Susan Lindquist has shown that isogenic populations of yeast can express different phenotypes based on whether they had the prion form of Sup35p or the non-prion form. She did an experiment where seven strains of yeast with different genetic backgrounds were grown on many different plates, all with a single food source, each strain having a prion positive and a prion negative form. In some cases, the prion conformation was advantageous to the non-prion conformation, and vice versa. When the strains were grown on fermentable carbon sources, only 5/35 cases showed a significant difference between prion positive and prion negative. The overexpression of the gene has been shown to induce the [Psi+] conformation. en.wikipedia.org/wiki/Sup35pPsi+ conformation from Sup35p: Enter in HSP104...............................heat shock protein 104........has archaea in it! Abstract The yeast non-Mendelian factor [ETA+] is lethal in the presence of certain mutations in the SUP35 and SUP45 genes, which code for the translational release factors eRF3 and eRF1, respectively. One such mutation, sup35-2, is now shown to contain a UAG stop codon prior to the essential region of the gene. The non-Mendelian inheritance of [ETA+] is reminiscent of the yeast [PSI+] element, which is due to a self-propagating conformation of Sup35p. Here we show that [ETA+] and [PSI+] share many characteristics. Indeed, like [PSI+], the maintenance of [ETA+] requires the N-terminal region of Sup35p and depends on an appropriate level of the chaperone protein Hsp104. Moreover, [ETA+] can be induced de novo by excess Sup35p, and [ETA+] cells have a weak nonsense suppressor phenotype characteristic of weak [PSI+]. We conclude that [ETA+] is actually a weak, unstable variant of [PSI+]. We find that although some Sup35p aggregates in [ETA+] cells, more Sup35p remains soluble in [ETA+] cells than in isogenic strong [PSI+] cells. Our data suggest that the amount of soluble Sup35p determines the strength of translational nonsense suppression associated with different [PSI+] variants. www.citeulike.org/group/336/article/925781skyship
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Post by skyship on Mar 2, 2010 4:45:00 GMT -5
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Post by skyship on Mar 3, 2010 1:28:40 GMT -5
lil sissy,
This is hard to explain, but, they are finding prions where no cjd or tse is present.
This formation of the yeast promoer I believe contains the prion forming amyloid, which is connected to the pancreas, downs syndrome and alzheimers.
Here is an article that might explain it better.========================== The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3.by: P. Zhou, I. L. Derkatch, S. M. Uptain, M. M. Patino, S. Lindquist, S. W. Liebman Abstract The yeast non-Mendelian factor [ETA+] is lethal in the presence of certain mutations in the SUP35 and SUP45 genes, which code for the translational release factors eRF3 and eRF1, respectively. One such mutation, sup35-2, is now shown to contain a UAG stop codon prior to the essential region of the gene. The non-Mendelian inheritance of [ETA+] is reminiscent of the yeast [PSI+] element, which is due to a self-propagating conformation of Sup35p. Here we show that [ETA+] and [PSI+] share many characteristics. Indeed, like [PSI+], the maintenance of [ETA+] requires the N-terminal region of Sup35p and depends on an appropriate level of the chaperone protein Hsp104. Moreover, [ETA+] can be induced de novo by excess Sup35p, and [ETA+] cells have a weak nonsense suppressor phenotype characteristic of weak [PSI+]. We conclude that [ETA+] is actually a weak, unstable variant of [PSI+]. We find that although some Sup35p aggregates in [ETA+] cells, more Sup35p remains soluble in [ETA+] cells than in isogenic strong [PSI+] cells. Our data suggest that the amount of soluble Sup35p determines the strength of translational nonsense suppression associated with different [PSI+] variants. www.citeulike.org/group/336/article/925781Wicker goes on again to say: "Prion Model for [PSI+] In 1994, Reed Wickner (10) presented evidence that [URE3] is a prion form of the Ure2 protein (see accompanying review by Wickner et al. (58)) and at the same time suggested that [PSI +] is a prion form of the Sup35 protein (Sup35p). This revolutionary hypothesis (Table I) explained much of the old [PSI +] data as well as two newer results that directly linked SUP35 to [PSI +] (16, 17). The idea was not that Sup35p (or Ure2p) had any functional similarity with the mammalian PrPSc prion but rather that all three had a similar novel mode of inheritance involving the self-propagation of alternate protein conformations. "www.jbc.org/content/274/3/1181.fullHere is an image (diagram):The Yeast [PSI+] Prion: Making Sense of Nonsensewww.jbc.org/content/274/3/1181/F1.expansion.htmlWicker is saying that the sup35p propogates prions as well as cjd and tse. so, i am thinking this is the same mechanism that causes Alz, pancreas etc problems. Involves other areas other than the brain. skyship
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Post by skyship on Mar 4, 2010 3:25:16 GMT -5
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Post by lilsissy on Mar 4, 2010 19:08:35 GMT -5
Casein ll found in yogurt changes normal Ppr protein into a scrape type PrPsc . It folds the normal into the abnormal, got milk?
Jen
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Post by skyship on Mar 5, 2010 3:40:52 GMT -5
yup.... I have been doing an experiment. The artificial milk or cream vanilla, amaretto, etc. has casein in it. I notice when I use that, I get the activity going in intestinal area.
If I use cream, I get a different reaction.
Seems this casein is not a good thing either, like the fructose, and I do know the calcium carbonate in sodas makes it worse, panceatitis type stuff and gastritis, seems the calcium pump doesn't work, calcium gets trapped and grows where it is trapped.
Same for kidney stones, pancreatic stones, gallbladder stones.
I was told once the pump wasn't working. mmmmmm
Flavinoids causing problems as well as the artificial colors.
what a mess!
yogurt probiotia, just might be e-coli? as well?
got milk? that is a good one.
Skyship
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Post by skyship on Mar 5, 2010 15:18:50 GMT -5
Proteins acting as genes: 17 Prions of yeast as epigenetic phenomena: High protein “copy number” inducing protein “silencing” Abstract Yeast infectious protein (prion) forms of the Ure2 and Sup35 proteins determine the nonchromosomal genes [URE3] and [PSI], and these are, therefore, the basis for a kind of epigenetic phenomena. In many systems, introduction of multiple copies of a DNA gene, or dsRNA copies of its sequence, results in the epigenetic silencing of that gene. In parallel with these homology effects, which act at the level of DNA or RNA, elevated copy number of the Ure2 and Sup35 proteins increases the frequency of their own “silencing” by prion formation. Both [ URE3] and [PSI] appear to be due to self-propagating amyloid formation of Ure2p and Sup35p, respectively. Another prion, [ Het-s] of the filamentous fungus, Podospora anserina, is necessary for a normal cellular function, heterokaryon incompatibility. Since these prions are nonchromosomal genes, they are proteins acting as genes, a parallel to the fact that nucleic acids can catalyze enzymatic reactions._ tiny.cc/i3vtl
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Post by lilsissy on Mar 8, 2010 0:01:52 GMT -5
A positive connection could be presenilin 2 ,which is a 1q42 mutation. here, www.ihop-net.org/UniPub/iHOP/pm/2120944.html?nr=4&pmid=10631141We conclude that because of the lack of specific antemortem diagnostic markers for FAD and hereditary prion disease, all four genes should be included in a molecular diagnostic program in patients with EOD who had PFH. here, www.ncbi.nlm.nih.gov/pubmed/9121700We need to check in to this some more. This article is very lengthy and involving but the last line does seem to be the question. How do we switch off Ppr? I know that mice bred to be be Ppr free will not show active Ppr infection after being subjected to infectious prions. If this is not possible then what can we do to reduce the effects of abnormal folding. I read that a few drops of D.M.S.O. in your drinking water will not kill prions but relaxes them and holds this disease at rest but that sounds dangerous. I don't know? www.biochemsoctrans.org/bst/036/1299/bst0361299.htmD.M.S.O. in your water? www.earthclinic.com/CURES/mad_cow.htmlD.M.S.O. effective , found in urine We need to see if our Urine contains prions. tinyurl.com/yeu2avb
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Post by lilsissy on Mar 8, 2010 0:04:39 GMT -5
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Post by lilsissy on Mar 8, 2010 0:09:52 GMT -5
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Post by lilsissy on Mar 8, 2010 0:17:00 GMT -5
wow check this out www.abovetopsecret.com/forum/thread182849/pg1President Bush was so concerned about prions that he made them "Select Agents" under the 2002 Bioterrorism Act. Now, it is an act of treason for US scientists to speak publicly about these agents. So you won't be getting any argument from the scientific community in the USA. Can you please point out the page on this copy of the Bioterroism Act of 2002 that details those claims? The constraints are established by the combination of Acts and Executive Orders - the main Gag Order is in the amendment to Executive Order 12958. I covered most of these issues long ago, here: U.S. Still Silencing Scientists More supporting info: * Interesting testimony before the Judiciary Committee: commdocs.house.gov... * Bill Summary and status: http://www.congress.gov...:H.R.339 * Current text: http://www.congress.gov...:4:./temp/~c108KV7HDS “Mad cow as bioterrorism? Scientists worry that US gov't classification of BSE prions as ‘select agents’ could hinder research” www.biomedcentral.com... “US blocking prion research” www.biomedcentral.com... “US amends ‘select agent’ regs,” The Scientist, November 10, 2003. J.M. Perkel, www.biomedcentral.com... * Bioterrorism Preparedness and Response Act of 2002 www.aphis.usda.gov...
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Post by skyship on Mar 9, 2010 9:59:27 GMT -5
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