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reply posted on 31-1-2005 @ 07:20 AM by DrHoracid
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...





[edit on 31-1-2005 by DrHoracid]


reply posted on 31-1-2005 @ 07:26 AM by soficrow
Originally posted by DrHoracid
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...

If scientists who speak out end up in Guantanamo, we'll never know what's really going on, will we?


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Can you prove this? Where does the patriot act ban prion research?


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).

Grabbed a few links from my files:

* Bioterrorism Preparedness and Response Act of 2002
www.aphis.usda.gov...
* Executive Order 12958 [Prion Gag Order] www.whitehouse.gov...
* Interesting testimony before the Judiciary Committee:
commdocs.house.gov...
* Bill Summary and status:
www.congress.gov...:H.R.339
* Current text:
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...


Interesting note: biomedcentral's publication, 'the scientist,' used to be fully open access - now it's not. It was the one reliable source for analysis of US politics-science-medicine controversies and conflicts-of-interest.


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reply posted on 31-1-2005 @ 10:43 AM by soficrow
Originally posted by sardion2000
can you point me in the direction of any alternate theories of the root causes of this potential plauge.


FYI Sardion - Legitimate scientists no longer question prions' existence - attempts to discredit Prusiner's work shifted gears in 1997 when he won a Nobel Prize for his 1982 prion discovery. ...Certain economic interests continue blocking the public release of prion research results - 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

Also see: "Mad Cow" Disease Uses Immune System to Spread in Body
www.abovetopsecret.com...



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 31-1-2005 @ 04:48 PM by soficrow
Originally posted by DrHoracid
"If" one had the technology, and the "time", they could target specific individuals with specific disease, in particular cancerous tumors, all based on that individuals source "dna" sample........in theory of course.



Got that DrH. ...and that 'tailored' disease then could spread, mutate, create a brand new disease and get loose in the world - right?

[re: 'in theory of course' - if you insist, but I do know the science and technology exist - and am fairly certain the motive does too]

Leaving aside the potential for assassination, genocide and depopulation, interesting as it is -

I am most concerned about a) assessing the earth's current level of contamination with prions and prion diseases, b) treatments and vaccines, and c) clean up and prevention.

My sense is:

a) The little suckers are rampant - in soil, water, rivers, oceans, never mind tap water - and pretty much coat every surface in your average hospital and food processing plant;

b) Treatments and vaccines already exist - but require "personalized medicine" for diagnosis and individualized protein cocktails for treatment - and there's not an insurance company in the world that gonna touch that with a ten foot pole - not to mention it has to be done over again with every new infection;

c) Clean up is possible - with new enzymes, filters and methods;

d) It is possible to prevent further spread and work to prevent new disease mutations by getting rid of pollution, toxins in our food etc - but requires major investments and a complete sterilization of various facilities and "restructuring" of systems.

e) ...Someone opened Pandora's box - and broke a barrier - because the world is out of balance, said barrier can't 'heal' or close naturally. ...Theoretically, if we clean up, then the barrier may close again.


Comments? Crit?




[edit on 1-2-2005 by soficrow]


reply posted on 1-2-2005 @ 05:40 AM by DrHoracid
Sofi, prions have been with us always, perhaps since day one. Data indicate that the lack of a specific enzyme "allows" the PrP to "attack" the host cells. It is possible that the "outbreak" is realted to an enviromental cause that reduces the "guard" enzyme amount to allow PrP replication. Here is another link on the subject.

www.pbs.org...

"

An abnormal form of the PrP protein, (called PrPSc) is found when we try to purify the agent which causes the disease from infected brain. It was originally discovered by David Bolton and his colleagues. PrP is also a normal host protein, in other words it is found in uninfected brains and in other tissues. In TSE-infected brains PrP changes its biochemical properties which allows us to distinguish between the two forms. It becomes more difficult to destroy with enzymes that digest proteins (proteases) and it will sediment in an ultracentrifuge when spun very fast, although the normal protein continues to float in solution. This protein probably has something to do with the infective agent, but what and how is again disputed. "






[edit on 1-2-2005 by DrHoracid]



reply posted on 1-2-2005 @ 12:29 PM by soficrow
Originally posted by DrHoracid
Sofi, prions have been with us always, perhaps since day one.



No argument here - but these rampant infectious prion epidemics haven't always been around. ...and there is absolutely no doubt that fibromuscular dysplasia appeared for the very first time in the early 1900's.

Hence my suggestion, "..Someone opened Pandora's box - and broke a barrier - because the world is out of balance, said barrier can't 'heal' or close naturally. ...Theoretically, if we clean up, then the barrier may close again. "



Data indicate that the lack of a specific enzyme "allows" the PrP to "attack" the host cells. It is possible that the "outbreak" is realted to an enviromental cause that reduces the "guard" enzyme amount to allow PrP replication.


...An interesting point on the path to understanding prion disease mechanics - but arguably, PrP isn't impacted until late-stage progression. ...More significant work looks at 'actin' proteins - eg. the accumulation of "a-smooth muscle actin" in the earlier stages of the disease process.

Actin is the key to understanding prion disease epidemics because virtually every cell in every lifeform on the planet contains actin - it's the pathway - and that's why prion diseases are now out of control.

An interesting link:
nessie.bch.ed.ac.uk...


..."Environmental" factors are critical - but looking for straight 'cause-and-effect' relationships is really old science.

Early research on the Environmental Genome Project (EGP) between 1997 and 2001 was more promising, and research from the National Center for Toxicogenomics (NCT)...

iccvam.niehs.nih.gov...


.....DrH - you're begging the issues and avoiding the implications:




a) The little suckers are rampant - in soil, water, rivers, oceans, never mind tap water - and pretty much coat every surface in your average hospital and food processing plant;

b) Treatments and vaccines already exist - but require "personalized medicine" for diagnosis and individualized protein cocktails for treatment - and there's not an insurance company in the world that gonna touch that with a ten foot pole - not to mention it has to be done over again with every new infection;

c) Clean up is possible - with new enzymes, filters and methods;

d) It is possible to prevent further spread and work to prevent new disease mutations by getting rid of pollution, toxins in our food etc - but requires major investments and a complete sterilization of various facilities and "restructuring" of systems.




...Please, pick one or all, and address the issues directly...



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