Monday, February 24, 2014

UPDATE ON CREUTZFELDT–JAKOB DISEASE Masters et al Australia

UPDATE ON CREUTZFELDT–JAKOB DISEASE Masters et al Australia
 
 
UPDATE ON CREUTZFELDT–JAKOB DISEASE

 

Colin L. Masters

 

Mental Health Research Institute, Florey Institute of Neuroscience and Mental Health, the University of Melbourne, Vic, Australia

 

Creutzfeldt–Jakob disease (CJD) is a transmissible spongiform encephalopathy caused by the accumulation of an abnormal conformer of the prion protein (PrPCJD). The abnormally folded protein has the autocatalytic capacity for converting natural conformers of PrP, and this property underlies its infectivity/transmissibility. Closely related to the causal mechanism of bovine spongiform encephalopathy (BSE), the zoonotic spread of BSE to humans has proven to be a major threat to the public health system. Infection control guidelines have been updated. New sensitive and specific diagnostic assays based on protein-misfolding amplification are being developed which also have the capacity to screen for the safety of the blood supply.

 

The spectrum of prion-like diseases has emerged with the recognition that Ab, tau and a-synuclein also have the capacity to spread within the human brain to cause Alzheimer’s disease, frontotemporal dementia and Parkinson’s disease.

 

PDF

 

http://pdfs.journals.lww.com/pathologyrcpa/2014/02001/Update_on_Creutzfeldt_Jakob_Disease.92.pdf?token=method|ExpireAbsolute;source|Journals;ttl|1393261976602;payload|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;hash|vc6+RCn4HF2d0BFMF46X7A==

 

 

Aggregate-Depleted Brain Fails to Induce Aβ Deposition in a Mouse Model of Alzheimer's Disease

 

Claudia Duran-Aniotz, Affiliations: Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, Texas, United States of America, Universidad de los Andes, Facultad de Medicina, Santiago, Chile

 

X Rodrigo Morales, Affiliation: Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, Texas, United States of America

 

X Ines Moreno-Gonzalez, Affiliation: Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, Texas, United States of America

 

X Ping Ping Hu, Affiliations: Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, Texas, United States of America, Education Ministry Key Laboratory on Luminescence and Real-Time Analysis, College of Life Sciences, Southwest University, Chongqing, China

 

X Joseph Fedynyshyn, Affiliation: Novartis Vaccines and Diagnostics, Emeryville, California, United States of America

 

X Claudio Soto mail * E-mail: Claudio.Soto@uth.tmc.edu

 

Affiliation: Mitchell Center for Alzheimer's Disease and Related Brain Disorders, Department of Neurology, University of Texas Houston Medical School, Houston, Texas, United States of America

 

X Published: February 12, 2014 DOI: 10.1371/journal.pone.0089014

 

Abstract Recent studies in animal models of Alzheimer's disease (AD) show that amyloid-beta (Aβ) misfolding can be transmissible; however, the mechanisms by which this process occurs have not been fully explored. The goal of this study was to analyze whether depletion of aggregates from an AD brain suppresses its in vivo “seeding” capability. Removal of aggregates was performed by using the Aggregate Specific Reagent 1 (ASR1) compound which has been previously described to specifically bind misfolded species. Our results show that pre-treatment with ASR1-coupled magnetic beads reduces the in vivo misfolding inducing capability of an AD brain extract. These findings shed light respect to the active principle responsible for the prion-like spreading of Alzheimer's amyloid pathology and open the possibility of using seeds-capturing reagents as a promising target for AD treatment.

 


 

 

Wednesday, May 16, 2012

 

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ?

 

Proposal ID: 29403

 


 

 

Wednesday, September 21, 2011

 

PrioNet Canada researchers in Vancouver confirm prion-like properties in Amyotrophic Lateral Sclerosis (ALS)

 


 

 

Sunday, February 10, 2013

 

Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion-Like Disorder?

 


 

 

Ann N Y Acad Sci. 1982;396:131-43.

 

Alzheimer's disease and transmissible virus dementia (Creutzfeldt-Jakob disease).

 

Brown P, Salazar AM, Gibbs CJ Jr, Gajdusek DC.

 

Abstract

 

Ample justification exists on clinical, pathologic, and biologic grounds for considering a similar pathogenesis for AD and the spongiform virus encephalopathies. However, the crux of the comparison rests squarely on results of attempts to transmit AD to experimental animals, and these results have not as yet validated a common etiology. Investigations of the biologic similarities between AD and the spongiform virus encephalopathies proceed in several laboratories, and our own observation of inoculated animals will be continued in the hope that incubation periods for AD may be even longer than those of CJD.

 


 

 

CJD1/9 0185 Ref: 1M51A

 

IN STRICT CONFIDENCE

 

Dr McGovern From: Dr A Wight Date: 5 January 1993 Copies: Dr Metters Dr Skinner Dr Pickles Dr Morris Mr Murray

 

TRANSMISSION OF ALZHEIMER-TYPE PLAQUES TO PRIMATES

 

1. CMO will wish to be aware that a meeting was held at DH yesterday, 4 January, to discuss the above findings. It was chaired by Professor Murray (Chairman of the MRC Co-ordinating Committee on Research in the Spongiform Encephalopathies in Man), and attended by relevant experts in the fields of Neurology, Neuropathology, molecular biology, amyloid biochemistry, and the spongiform encephalopathies, and by representatives of the MRC and AFRC. 2. Briefly, the meeting agreed that:

 

i) Dr Ridley et als findings of experimental induction of p amyloid in primates were valid, interesting and a significant advance in the understanding of neurodegenerative disorders;

 

ii) there were no immediate implications for the public health, and no further safeguards were thought to be necessary at present; and

 

iii) additional research was desirable, both epidemiological and at the molecular level. Possible avenues are being followed up by DH and the MRC, but the details will require further discussion. 93/01.05/4.1

 


 

 

BSE101/1 0136

 

IN CONFIDENCE

 

5 NOV 1992 CMO From: Dr J S Metters DCMO 4 November 1992

 

TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES

 

1. Thank you for showing me Diana Dunstan's letter. I am glad that MRC have recognized the public sensitivity of these findings and intend to report them in their proper context. This hopefully will avoid misunderstanding and possible distortion by the media to portray the results as having more greater significance than the findings so far justify.

 

2. Using a highly unusual route of transmission (intra-cerebral injection) the researchers have demonstrated the transmission of a pathological process from two cases one of severe Alzheimer's disease the other of Gerstmann-Straussler disease to marmosets. However they have not demonstrated the transmission of either clinical condition as the "animals were behaving normally when killed'. As the report emphasizes the unanswered question is whether the disease condition would have revealed itself if the marmosets had lived longer. They are planning further research to see if the conditions, as opposed to the partial pathological process, is transmissible. What are the implications for public health?

 

3. The route of transmission is very specific and in the natural state of things highly unusual. However it could be argued that the results reveal a potential risk, in that brain tissue from these two patients has been shown to transmit a pathological process. Should therefore brain tissue from such cases be regarded as potentially infective? Pathologists, morticians, neuro surgeons and those assisting at neuro surgical procedures and others coming into contact with "raw" human brain tissue could in theory be at risk. However, on a priori grounds given the highly specific route of transmission in these experiments that risk must be negligible if the usual precautions for handling brain tissue are observed.

 

92/11.4/1-1 BSE101/1 0137

 

4. The other dimension to consider is the public reaction. To some extent the GSS case demonstrates little more than the transmission of BSE to a pig by intra-cerebral injection. If other prion diseases can be transmitted in this way it is little surprise that some pathological findings observed in GSS were also transmissible to a marmoset. But the transmission of features of Alzheimer's pathology is a different matter, given the much greater frequency of this disease and raises the unanswered question whether some cases are the result of a transmissible prion. The only tenable public line will be that "more research is required" before that hypothesis could be evaluated. The possibility on a transmissible prion remains open. In the meantime MRC needs carefully to consider the range and sequence of studies needed to follow through from the preliminary observations in these two cases. Not a particularly comfortable message, but until we know more about the causation of Alzheimer's disease the total reassurance is not practical.

 

JS METTERS Room 509 Richmond House Pager No: 081-884 3344 Callsign: DOH 832 121/YdeS 92/11.4/1.2

 


 

 

BSE101/1 0136

 

IN CONFIDENCE

 

CMO

 

From: Dr J S Metters DCMO

 

4 November 1992

 

TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES

 


 

 

CJD1/9 0185

 

Ref: 1M51A

 

IN STRICT CONFIDENCE

 

From: Dr. A Wight Date: 5 January 1993

 

Copies:

 

Dr Metters Dr Skinner Dr Pickles Dr Morris Mr Murray

 

TRANSMISSION OF ALZHEIMER-TYPE PLAQUES TO PRIMATES

 


 

 

Wednesday, January 5, 2011

 

ENLARGING SPECTRUM OF PRION-LIKE DISEASES Prusiner Colby et al 2011 Prions

 

David W. Colby1,* and Stanley B. Prusiner1,2

 


 


 

Friday, September 3, 2010

 

Alzheimer's, Autism, Amyotrophic Lateral Sclerosis, Parkinson's, Prionoids, Prionpathy, Prionopathy, TSE

 


 


 

 

SCENARIO 3: ‘THE THIN STEMMED GLASS’

 

... a TSE is found that is linked to Alzheimer’s disease.

 


 

 

Tuesday, November 26, 2013

 

Transmission of multiple system atrophy prions to transgenic mice

 


 

Transmission of Prions and Alzheimer’s disease Abeta Amyloid

 

Claudio Soto, PhD

 

Mitchell Center for Alzheimer’s disease and Related Brain Disorders, Dept of Neurology

 

University of Texas Medical School at Houston

 


 

 

Tuesday, October 4, 2011

 

Molecular Psychiatry

 

advance online publication 4 October 2011; doi: 10.1038/mp.2011.120

 

De novo induction of amyloid-ß deposition in vivo

 

Our results suggest that some of the typical brain abnormalities associated with AD can be induced by a prion-like mechanism of disease transmission through propagation of protein misfolding. These findings may have broad implications for understanding the molecular mechanisms responsible for the initiation of AD, and may contribute to the development of new strategies for disease prevention and intervention. Keywords: amyloid; prion; protein misfolding; disease transmission

 


 

 

see more here ;

 


 


 

 

Friday, January 31, 2014

 

***Confidentiality in preclinical Alzheimer disease studies

 


 

Tuesday, February 11, 2014

 

Novant Health Forsyth Medical Center Information on potential CJD exposure

 


 

I suppose one of the most disturbing studies I have ever read, was the one of Gibbs et al, way back, with electrodes that caused CJD, again, and again.

 

I am not posting this to scare folks, so be it if it does, but I am posting this for you to see what you are dealing with. ...this study still amazes me. read it more than once.

 

please see ;

 

1: J Neurol Neurosurg Psychiatry 1994 Jun;57(6):757-8

 

*** Transmission of Creutzfeldt-Jakob disease to a chimpanzee by electrodes contaminated during neurosurgery.

 

Gibbs CJ Jr, Asher DM, Kobrine A, Amyx HL, Sulima MP, Gajdusek DC.

 

Laboratory of Central Nervous System Studies, National Institute of

 

Neurological Disorders and Stroke, National Institutes of Health,

 

Bethesda, MD 20892.

 

*** Stereotactic multicontact electrodes used to probe the cerebral cortex of a middle aged woman with progressive dementia were previously implicated in the accidental transmission of Creutzfeldt-Jakob disease (CJD) to two younger patients. The diagnoses of CJD have been confirmed for all three cases. More than two years after their last use in humans, after three cleanings and repeated sterilisation in ethanol and formaldehyde vapour, the electrodes were implanted in the cortex of a chimpanzee. Eighteen months later the animal became ill with CJD. This finding serves to re-emphasise the potential danger posed by reuse of instruments contaminated with the agents of spongiform encephalopathies, even after scrupulous attempts to clean them.

 

PMID: 8006664 [PubMed - indexed for MEDLINE]

 


 

New studies on the heat resistance of hamster-adapted scrapie agent: Threshold survival after ashing at 600°C suggests an inorganic template of replication

 


 

Prion Infected Meat-and-Bone Meal Is Still Infectious after Biodiesel Production

 


 

Detection of protease-resistant cervid prion protein in water from a CWD-endemic area

 


 

A Quantitative Assessment of the Amount of Prion Diverted to Category 1 Materials and Wastewater During Processing

 


 

 Rapid assessment of bovine spongiform encephalopathy prion inactivation by heat treatment in yellow grease produced in the industrial manufacturing process of meat and bone meals

 


 

PPo4-4:

 

Survival and Limited Spread of TSE Infectivity after Burial

 


 

*** The potential impact of prion diseases on human health was greatly magnified by the recognition that interspecies transfer of BSE to humans by beef ingestion resulted in vCJD. While changes in animal feed constituents and slaughter practices appear to have curtailed vCJD, there is concern that CWD of free-ranging deer and elk in the U.S. might also cross the species barrier. Thus, consuming venison could be a source of human prion disease. Whether BSE and CWD represent interspecies scrapie transfer or are newly arisen prion diseases is unknown. Therefore, the possibility of transmission of prion disease through other food animals cannot be ruled out. There is evidence that vCJD can be transmitted through blood transfusion. There is likely a pool of unknown size of asymptomatic individuals infected with vCJD, and there may be asymptomatic individuals infected with the CWD equivalent. These circumstances represent a potential threat to blood, blood products, and plasma supplies.

 


 

Wednesday, April 24, 2013

 

Chimpanzees Released After 30 Years Of Testing, Brace Yourself For Smiles

 


 

see full text ;

 

Saturday, November 16, 2013

 

Management of neurosurgical instruments and patients exposed to creutzfeldt-jakob disease 2013 December

 

Infect Control Hosp Epidemiol.

 


 

Thursday, February 06, 2014

 

*** Commons Science and Technology Committee announce new inquiry on blood, tissue and organ screening Parliament exposure vcjd and blood risk while still ignoring recent risks factors of sporadic CJD

 


 

Wednesday, February 12, 2014

 

USDA/APHIS NOTICE: Final Rule Regarding Imports and BSE Effective March 4, 2014

 

LOL !!! Laughing out loud

 


 

Sunday, January 19, 2014

 

National Prion Disease Pathology Surveillance Center Cases Examined1 as of January 8, 2014

 


 

Wednesday, January 15, 2014

 

*** INFECTION PREVENTION AND CONTROL OF CJD, VCJD AND OTHER HUMAN PRION DISEASES IN HEALTHCARE AND COMMUNITY SETTINGS Variably Protease-Sensitive Prionopathy (VPSPr) January 15, 2014

 


 

Monday, January 13, 2014

 

Prions in Variably Protease-Sensitive Prionopathy: An Update Pathogens 2013

 

Pathogens 2013, 2, 457-471; doi:10.3390/pathogens2030457

 


 

Friday, January 10, 2014

 

*** vpspr, sgss, sffi, TSE, an iatrogenic by-product of gss, ffi, familial type prion disease, what it ???

 


 

Friday, January 10, 2014

 

*** vpspr, sgss, sffi, TSE, an iatrogenic by-product of gss, ffi, familial type prion disease, what it ???

 


 

 

Monday, February 24, 2014

 

Sporadic Fatal Insomnia in an Adolescent

 


 

 

 

CJD QUESTIONNAIRE USA

 


 


 

CJD VOICE

 


 


 


 


 


 


 


 


 


 


 

 

 layperson

 

Terry S. Singeltary Sr. P.O. Box 42 Bacliff, Texas USA 77518 flounder9@verizon.net

 

 

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