Good Afternoon List Friends,
These are 3 snips from the Food Safety Network clipping service from the
University of Guelph. They are press releases or abstracts which tell
of some recent developments in the study of prion related diseases.
For those with access to libraries, the full papers are available in
volume 302, No 5646 of the Journal Science.
Regards
Ross Gould, P.Ag.
Calgary, Alberta
1. Mice recover for first time from madcow-related illness
October 30, 2003
Agence France Presse English
PARIS - A team of British scientists was cited as reporting today in the
journal Sceince that lab animals have for the first time recovered from
a brain disorder related to mad cow disease and its human version
Creutzfeldt-Jakob disease (vCJD) by producing mice whose nerve cells
were stripped of normal prions, a form of protein that can become
infected. Previously, researchers looking for a solution to the vexing
problem has focused their work on already infected prions, rather than
healthy ones.The scientists from a London neurology institute found that
"the depletion of neuronal (prions) in animals...prevented progression
to clinical prion disease and resulted in the long-term survival of
infected animals."
2. Depleting neuronal PrP in prion infection prevents disease and
reverses spongiosis
October 31, 2003
Science Vol 302, No 5646: 871-874
Giovanna Mallucci, Andrew Dickinson, Jacqueline Linehan, Peter-Christian
Kl�hn, Sebastian Brandner, John
Collinge*
The mechanisms involved in prion neurotoxicity are unclear, and
therapies preventing accumulation of PrPSc, the disease-associated form
of prion protein (PrP), do not significantly prolong survival in mice
with central nervous system prion infection. We found that depleting
endogenous neuronal PrPc in mice with established neuroinvasive prion
infection reversed early spongiform change and prevented neuronal loss
and progression to clinical disease. This occurred despite the
accumulation of extraneuronal PrPSc to levels seen in terminally ill
wild-type animals. Thus, the propagation of nonneuronal PrPSc is not
pathogenic, but arresting the continued conversion of PrPc to PrPSc
within neurons during scrapie infection prevents prion neurotoxicity.
Medical Research Council Prion Unit and Department of Neurodegenerative
Disease, Institute of Neurology, Queen
Square, London WC1, UK.
To whom correspondence should be addressed. E-mail:
j.collinge@prion.ucl.ac.uk
3. Games played by rogue proteins in prion disorders and Alzheimer's
disease
October 31, 2003
Science Vol 302, No 5646: 814-818
Adriano Aguzzi1* and Christian Haass2*
The incidence of Alzheimer's disease (AD) and that of prion disorders
(PrD) could not be more different. One-third of octogenarians succumb to
AD, whereas Creutzfeldt-Jakob disease typically affects one individual
in a million each year. However, these diseases have many common
features impinging on the metabolism of neuronal membrane proteins: the
amyloid precursor protein APP in the case of AD, and the cellular prion
protein PrPC in PrD. APP begets the A� peptide, whereas PrPC begets the
malignant prion protein PrPSc. Both A� and PrPSc are associated with
disease, but we do not know what triggers their accumulation and
neurotoxicity. A great deal has been learned, however, about protein
folding, misfolding, and aggregation; an entirely new class of
intramembrane proteases has been identified; and unsuspected roles for
the immune system have been uncovered. There is reason to expect that
prion research will profit from advances in the understanding of AD, and
vice versa.
1 Institute of Neuropathology, University Hospital of Zurich,
Schmelzbergstrasse 12, CH-8091 Zurich, Switzerland.
2 Department of Biochemistry, Adolf-Butenandt-Institute, Laboratory for
Alzheimer's and Parkinson's Disease
Research, Ludwig-Maximilians-University, Schillerstrasse 44, Munich,
Germany.
To whom correspondence should be addressed. E-mail:
adriano@pathol.unizh.ch (A.A.);
chaass@pbm.med.uni-muenchen.de (C.H.)
