SCI/TECH: "Mad Cow" Disease Uses Immune System to Spread in Body, page 1
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Topic started on 30-1-2005 @ 05:20 PM by soficrow
Supposedly, some meat is safe from animals infected with prion diseases like "Mad Cow." This and other assumptions have been disproved one by one, most recently in a study led by Adriano Aguzzi at Zurich University Hospital, Switzerland. The study proves that if an animal infected with a prion disease "has an additional infection in the body, (then) the prions are no longer confined to the areas where they normally are." Super-imposed infections "somehow help the prions to replicate, and to spread to the parts of the body being targeted by the immune reaction."




www.nature.com
One assumption lies at the root of efforts to keep the meat we eat safe from mad cow disease: that tissues beyond an animal's brain, spinal cord and immune system are free of the prions that cause the disease.

(Now) Researchers have found that if an animal falls ill with another infection, its immune response can carry large numbers of prions to organs throughout its body. ..."The rules no longer apply," warns pathologist Adriano Aguzzi at Zurich University Hospital, Switzerland, who led the research.

(Aguzzi and his team) took mice with the equivalent of BSE and induced an 'inflammatory response' in them. This is the type of immune response that the body mounts in the face of a wide range of injuries and illnesses, including cuts, the common cold and type I diabetes.

There was an explosion of prions in the animals' pancreases, kidneys and livers, the researchers report in this week's issue of Science1. The amount of prions in these organs was just as high as is generally found in diseased spleens.

"If the animal has an additional infection in the body, the prions are no longer confined to the areas where they normally are," explains Surachai Supattapone, an expert in infectious diseases at the Dartmouth Medical School in Hanover, New Hampshire. ...The researchers believe that the cells involved in the inflammatory response somehow help the prions to replicate, and to spread to the parts of the body being targeted by the immune reaction.



Please visit the link provided for the complete story.


The implications of this information clearly are far reaching, and difficult to grasp all at once. Off the top, it seems to explain the appearance of new diseases, and growing epidemics in the USA and around the world of diseases like cancer, heart disease, stroke and probably, AIDS.

While the situation may look grim on the surface, there are new diagnostic tests, treatments, vaccines and preventive measures. Many have been collecting dust in the US Patent Office for the past four years.

Patent review of prion-related applications should be given priority. Also, Environmental Protection Agency (EPA), water treatment and food industry standards regulations should be up-graded, rather than ignored.


Related News Links:
www.bioedonline.org
www.bioedonline.org
cmbi.bjmu.edu.cn
www.teckis.com

Related AboveTopSecret.com Discussion Threads:
NEWS: Mad Cow Disease Is Found In Goat
ATS: Merck and Vioxx: A Twisted Tale of Cover-ups, Pork and Profits
Bioweapons - Types and Uses
NEWS: Threat Analysis: Genetically Engineered Stealth Bio-weapons


reply posted on 31-1-2005 @ 09:38 AM by DrHoracid
Prion Research

ARMY POSITION: The US Army Medical Research and Materiel Command (USAMRMC) manages biomedical research programs that are part of the Department of Defense (DOD) and Army budget submission. In addition, as directed by Congress, the USAMRMC manages congressionally targeted biomedical research programs.

One of the congressional research programs managed by the USAMRMC Office of the Congressionally Directed Medical Research Programs (CDMRP) is the National Prion Research Program (NPRP). The primary goals of the NPRP are to support the development of diagnostic tests and means to prevent and manage transmissible spongiform encephalopathies (TSE).

KEY FACTS:

Congress directed the DOD's involvement in the NPRP in fiscal year 2002 (FY02).
The USAMRMC was tasked by Congress to manage the $42.5 million (M) NPRP appropriation, which was received by the USAMRMC in February 2002.
TSE are of military relevance due to their potential threat to food and blood supplies, and the health threats posed by TSE put military beneficiaries in affected areas overseas at risk.
The NPRP is conducted according to the two-tier review model recommended in 1993 to the USAMRMC by the National Academy of Sciences Institute of Medicine (IOM); this model has received high praise from the scientific community, advocacy groups, and Congress.
The USAMRMC negotiated with the IOM to assess the field of TSE, focusing specifically on prion detection and disease diagnosis. A progress report was received in August 2002, an interim report was received in January 2003, and the final report was received in November 2003.
A meeting was held May 22-23, 2002 in which military, scientific, regulatory, and public health stakeholders provided input on the major issues in TSE research and received an overview of the USAMRMC science management processes. Based upon the stakeholders' recommendations, a smaller programmatic advisory group (Integration Panel), composed of TSE experts from the military, scientific, regulatory, industry, and public health communities, was selected.
The FY02 NPRP investment strategy was determined by the Integration Panel at a vision setting meeting held June 24-25, 2002. A request for proposals was released on August 2, 2002, and 136 proposals were received by the proposal submission due date of October 30, 2002. Peer review was conducted December 4-6, 2002, and programmatic review was conducted February 27-28, 2003. Programmatic review deliberations were supported by an IOM interim report on prion detection and diagnosis.
The Integration Panel submitted a recommended for funding list of 38 proposals to the Commanding General, USAMRMC for approval. The Commanding General, USAMRMC approved the award recommendations on March 10, 2003. Award negotiations have been completed.
Congress has not provided any follow-up appropriations for this research.
BACKGROUND:

Disease Background. TSE refers to several apparently related diseases including Creutzfeltd-Jacob disease (CJD) and its new variant (nvCJD), kuru, bovine spongiform encephalopathy ("mad cow disease"), and others. Except for nvCJD, the TSE appear to develop progressively over many years, lead to extensive central nervous system vacuole formation, and are invariably fatal. At present, definitive diagnosis can only be made at autopsy. The diseases are relatively rare in humans but have been documented most extensively in hoofed mammals. The current disease theory attributes TSE to "prions," normal cell membrane proteins with atypical three-dimensional configurations, transmitted by ingestion or blood transfer. 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.

cdmrp.army.mil...


reply posted on 31-1-2005 @ 09:52 AM 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.




Right - Legitimate scientists no longer question prions' existence - that argument shifted gears in 1997. ...Now, certain economic interests attack solid prion research differently - to prevent public awareness, block public education, and protect profits.

Currently, there are two important prion controversies:

1. Prion researchers say prions 'mutate' to cause a range of different diseases - opposition says no, impossible, asking, "If prions 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 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




2. Prion researchers say underlying "subclinical" prion infections cause disease well before the infection moves to the brain, that there is a progressive, degenerative disease process affecting various body parts and systems - opposition says prion diseases only affect the brain, and maybe the central nervous system. ... Prion researchers counter that it’s a political strategy to say prions only cause brain disease and just come from cattle – not sound science.



“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




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reply posted on 6-6-2009 @ 09:14 PM by Murky
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.....


Around 2002-2003, two avid elk hunters (who ate their kills all their lives) died of Creutzfeld-Jakob Disease in Colorado. CJD was the diagnosis of the first human mad-cow victims in Britain (in humans, the disease is still referred to as "new variant Creutzfeld-Jakob Disease," or nvCJD). And the older variants of CJD, which are sometimes familial and always sporadic in incidence, are probably also prion diseases - as evidenced by the spread of CJD in recipients of human growth hormone from human cadavers, some of whom were apparently neurology patients who had "donated their brains to medical science" and whose pituitaries were harvested for the manufacture of HGH.

So we have evidence in the medical literature already for a slow and sporadic mechanism for transmission of CJD within families - whether by vertical transmission (parent to child, genetically or during conception or gestation) or commensalism (where the family members may have ingested or otherwise been exposed to the same sources of prions).

The two unfortunate elk hunters in Colorado may have just given us a window on how a prion zoonosis like Chronic Wasting Disease, which is endemic in herds of cervids such as elk, deer and moose, can pass from animals to humans.

Prions are everywhere. As long as we consume other living things for food, as we must (unless we go over to a food production economy based on single-cell protein sources like yeasts and culture every morsel of food we eat industrially in steel or glass), we have to deal with the real possibility that prions will enter our food production process at some level - as they did when cattle dead of mad-cow disease were rendered and processed into animal feed in Britain, when the rendering process had changed to make it easier for prions to spread throughout the end-products of the rendering plant. Other misadventures involving prions in the food chain are almost guaranteed to happen and much more probable to impact huge communities where animal food production involves the gathering together of huge numbers of animals and the combining of their carcasses in the food production process.

Good analysis.

[edit on 6-6-2009 by Murky]
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