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Originally posted by superdude
BSE is able to travel through the body by means of it's own immune system?
Originally posted by soficrow
Originally posted by DrHoracid
Although a Nobel Prize was awarded for the work underlying this proposed mechanism (Prusiner, 1997), it remains controversial because disease transmission traditionally is associated with an agent capable of replication.
The Strain Game:
Environmental Changes Induce Prions to Change and Create New Strains
Note: In this context, 'environmental change' has a broad meaning: it includes mechanical change like high blood pressure, exposure to toxins or super-imposed infections, temperature changes, the shape of the target cell and more.
“UCSF scientists have demonstrated for the first time that a change in the folded shape of a prion protein changes its infectious properties – including the prion’s ability to jump ‘species barriers.’ The research, based on studies of prion infectivity in yeast, solves one of the great puzzles about prions:
...If they are infectious proteins with no genetic material of their own and no ability to mutate genetically, how can a single prion exist in different strains that can cause different diseases? The puzzle has led some to doubt that a protein alone causes mad cow and related diseases.
…Studies of the melting temperatures of the prions and their resistance to breakdown by enzymes indicated that the conditions generated prions with different physical properties.”
“Prion shape affects nature of infection”
www.medicalnewstoday.com...
Background Highlights
New infectious prion strain called vacuolar protease B (PrB) identified by the US National Institute of Diabetes, National Institutes of Health (NIH) in Bethesda, Maryland. NIH officially acknowledges that:
a. Infectious prions can be enzymes;
b. Fibrous prion protein deposits are not necessarily amyloid proteins (Note: Previous research shows that 90% of type 2 diabetes patients have amyloid plaques in their pancreas); and
c. Infectious prions cause disease in other parts of the body besides the brain and central nervous system.
* Source: “A new kind of prion: a modified protein necessary for its own modification.” Cell Cycle. 2004 Mar-Apr;3(2):100-3. Roberts BT, Wickner RB. National Institute of Diabetes, National Institutes of Health, Bethesda, Maryland USA. PMID: 14712063
www.landesbioscience.com...
Also see: “Role of islet amyloid in type 2 diabetes mellitus: consequence or cause?” Mol Cell Endocrinol. 2002 Nov 29;197(1-2):205-12. Hoppener JW, Nieuwenhuis MG, Vroom TM, Ahren B, Lips CJ. Department of Clinical Endocrinology, University Medical Center Utrecht, Location University Hospital, G02.228, P.O. Box 85500, 3508 GA Utrecht, The Netherlands. PMID: 12431814
“...prions may overcome natural transmissibility barriers between two species of mammals. This may happen if prion proteins from one of these two species have been exposed to abnormal prions from a third species.”
* “Researchers Make Major Gain In Understanding How Prions Jump Species” Source: Case Western Reserve University
www.sciencedaily.com...
“Cross-species infection with transmissible spongiform encephalopathy agents may lead to subclinical infection and to adaptation of the infection to new species.”
* “Subclinical scrapie infection in a resistant species: persistence, replication, and adaptation of infectivity during four passages.” Race R, Meade-White K, Raines A, Raymond GJ, Caughey B, Chesebro B. Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, 903 S. Fourth Street, Hamilton, MT 59840, USA. J Infect Dis. 2002 Dec 1;186 Suppl 2:S166-70. PMID: 12424693
“Conformational variations in an infectious protein determine prion strain differences.” Nature. 2004 Mar 18;428(6980):323-8. Tanaka M, Chien P, Naber N, Cooke R, Weissman JS. Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94143, USA. PMID: 15029196
“...the biochemical isoform of PrP(Sc) found is influenced by the cell type in which it accumulates.”
* “Peripheral Tissue Involvement in Sporadic, Iatrogenic, and Variant Creutzfeldt-Jakob Disease: An Immunohistochemical, Quantitative, and Biochemical Study.” Am J Pathol. 2004 Jan;164(1):143-153. Head MW, Ritchie D, Smith N, McLoughlin V, Nailon W, Samad S, Masson S, Bishop M, McCardle L, Ironside JW. National Creutzfeldt-Jakob Disease Surveillance Unit and Division of Pathology, School of Molecular and Clinical Medicine, University of Edinburgh, Western General Hospital, Edinburgh, United Kingdom. PMID: 14695328
“Diverse human disorders …arise from misfolding and aggregation of an underlying protein.”
“Protein misfolding and disease: the case of prion disorders.” Cell Mol Life Sci. 2003 Jan;60(1):133-43. Hetz C, Soto C. Serono Pharmaceutical Research Institute, 14 Chemin des Aulx, 1228 Plan les Ouates, Switzerland. PMID: 12613663
“Prions, once dismissed as an impossibility, have now gained wide recognition as extraordinary agents that cause a number of infectious, genetic and spontaneous disorders”
www.cyber-dyne.com...
“…this hypothesis would shed some light on other diseases not presently classified as prion diseases and in the process of ageing.”
* “Prion plaques: molecular tumors. A hypothesis on the etiopathogenesis of prion diseases.” Ossa JE, Machado G, Giraldo MA, McEwen JG. Facultad de Medicina, Universidad de Antioquia, Medellin, Colombia. Med Hypotheses. 1995 Feb;44(2):124-6. PMID: 7596306
* “Cyclic amplification of protein misfolding: application to prion-related disorders and beyond.” Trends Neurosci. 2002 Aug;25(8):390-4. Soto C, Saborio GP, Anderes L. Serono International SA, Geneva, Switzerland. PMID: 12127750
* “Chronic Subclinical Prion Disease Induced by Low-Dose Inoculum” Received September 24, 2001; J Virol. 2002 March; 76 (5): 2510–2517 Alana M. Thackray,1 Michael A. Klein,2 Adriano Aguzzi,3 and Raymond Bujdoso www.pubmedcentral.nih.gov...
For example, research shows prion infections cause diverse muscle disorders in skeletal, heart and smooth muscles - the three kinds of muscle in the human body:
“...mutant PrP in the brain and spinal cord, intermediate levels in skeletal muscle, heart, and testis and low levels in kidney, lung, spleen, intestine, and stomach. Up to 70% of the PG14 PrP expressed in peripheral tissues”
* “Primary myopathy and accumulation of PrPSc-like molecules in peripheral tissues...” Neurobiol Dis. 2001 Apr;8(2):279-88. Chiesa R, Pestronk A, Schmidt RE, Tourtellotte WG, Ghetti B, Piccardo P, Harris DA. Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA. PMID: 11300723
* “Prions in skeletal muscle.” Brazier MW, Cappai R, Collins SJ. Aust Vet J. 2002 Aug;80(8):484-5. PMID: 12224617
* “Deposition of disease-associated prion protein involves the peripheral nervous system in experimental scrapie.” Acta Neuropathol (Berl). 1999 Nov;98(5):453-7. Groschup MH, Beekes M, McBride PA, Hardt M, Hainfellner JA, Budka H. Bundesforschungsanstalt fur Viruskrankheiten der Tiere, Institut fur Impfstoffe, Tubingen, Germany. PMID: 10541866
“...diseased individuals forming lesions, vacuoles and ... New marker for human prion protein (CD230 ... reported on neurons, astrocytes, smooth muscle cells and...”
* “New marker for human prion protein (CD230)”
www.serotec.co.uk/supplement%20pdfs/June2001.pdf
“... effect of A[beta] peptides on vascular smooth muscle cells and ...”
* “Anchor-dependent and -independent Prion Protein Association” JBC -- Abstracts: Mahfoud et al. 277 (13): 11292 www.jbc.org/cgi/content/abstract/277/13/11292
NOTE: “Cholesterol is necessary both for the toxic effect of A[beta] peptides on vascular smooth muscle cells and for A[beta] binding to vascular smooth muscle cell membranes” J. Neurochem., February 1, 2003; 84(3): 471 - 479. S. Subasinghe, S. Unabia, C. J. Barrow, S. S. Mok, M.-I. Aguilar, and D. H. Small
“Subclinical prion infection in humans and animals.” Br Med Bull. 2003;66:161-70. Hill AF, Collinge J. MRC Prion Unit, Department of Neurodegenerative Disease, Institute of Neurology, London, UK. PMID: 14522857
Originally posted by accountability
so is prion gag order still in effect?
Do you have to have a blood culture done in order to find out what kind of infection you have?
I am so sick of being sick and tired.
I just though this article deserved a bump with all the scarey stuff going on. ...and give me an update before I croak- PLEASe
Originally posted by magickalworld
Well, this explains why the "Men in Black" have been tracking the cattle herds in the U.S......I hadn't heard about the goats having it.....I know that a similar disease called "Chronic Wasting Disease" has been an epidemic in the Western states in deer and elk.....
Originally posted by Murky
Good analysis.
Originally posted by soficrow
Looks like it already is - the real kicker is, there are new diagnostic tests, treatments, vaccines - plus new effective ways to prevent the spread - but they're all being blocked.
.
Originally posted by HunkaHunka
Originally posted by soficrow
Looks like it already is - the real kicker is, there are new diagnostic tests, treatments, vaccines - plus new effective ways to prevent the spread - but they're all being blocked.
.
surprise surprise... a crazy statement with nothing backing it up.
How about some examples of what you mean maybe?
Where is the "blocking" occuring?
[edit on 11-6-2009 by HunkaHunka]
Originally posted by soficrow
Bush made prion research illegal under anti-terrorism legislation and also made it illegal for US scientists to talk publicly about prions and prion diseases...
...the Bioterrorism Preparedness and Response Act of 2002 terminated infectious prion research in the USA in all but two laboratories; Prion Gag Order 12958 (amendment to Executive Order) gags US scientists and prevents them from speaking publicly about prions, under threat of military arrest and incarceration.
In this study, UK researchers looked at immune cells called follicular dendritic cells (FDCs) in mice infected with a version of the prion disease scrapie. FDCs are found in tissues such as the spleen, lymph nodes and tonsils.
When the disease prions first enter the body, the FDCs attract the prions and cause them to multiply.
Why vCJD is more common in young people