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
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]
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8006664&dopt=Abstract
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
posted by Terry S. Singeltary Sr. at
12:15 PM
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