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From: TSS (216-119-143-153.ipset23.wt.net)
Subject: Biochemical fingerprints of prion diseases:
Date: December 23, 2004 at 2:32 pm PST

-------- Original Message --------
Subject: Biochemical fingerprints of prion diseases:
Date: Thu, 23 Dec 2004 09:15:36 -0600
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy
To: BSE-L@LISTSERV.KALIV.UNI-KARLSRUHE.DE


##################### Bovine Spongiform Encephalopathy #####################

J Neurochem. 2005 Jan;92(1):132-42.

Biochemical fingerprints of prion diseases: scrapie prion protein in
human prion diseases that share prion genotype and type.

Pan T, Li R, Kang SC, Pastore M, Wong BS, Ironside J, Gambetti P, Sy MS.

Division of Neuropathology, Case Western Reserve University,
Cleveland, Ohio, USA.

Abstract The phenotype of human prion diseases is influenced by the
prion protein (PrP) genotype as determined by the methionine
(M)/valine (V) polymorphism at codon 129, the scrapie PrP (PrP(Sc))
type and the etiology. To gain further insight into the mechanisms
of phenotype determination, we compared two-dimensional immunoblot
profiles of detergent insoluble and proteinase K-resistant PrP
species in a type of sporadic Creutzfeldt-Jakob disease (sCJDMM2),
variant CJD (vCJD) and sporadic fatal insomnia (sFI). Full-length
and truncated PrP forms present in the insoluble fractions were also
separately analyzed. These three diseases were selected because they
have the same M/M PrP genotype at codon 129 and the same type 2
PrP(Sc), but different etiologies, also sCJDMM2 and sFI are
sporadic, whereas vCJD is acquired by infection. We observed minor
differences in the PrP detergent-insoluble fractions between sCJDMM2
and vCJD, although both differ in the corresponding fractions from
sFI. We detected more substantial heterogeneity between sCJDMM2 and
vCJD in the two-dimensional blots of the proteinase K-resistant PrP
fraction suggesting that different PrP species are selected for
conversion to proteinase K-resistant PrP in sCJDMM2 and vCJD. These
differences are mostly, but not exclusively, due to variations in
the type of the N-linked glycans. We also show that the
over-representation of the highly glycosylated forms distinctive of
the proteinase K-resistant PrP(Sc) of vCJD in one-dimensional blots
is due to differences in both the amount and the natures of the
glycans. Overall, these findings underline the complexity of
phenotypic determination in human prion diseases.


http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15606903

1: J Virol. 2005 Jan;79(2):934-43.

Biochemical Fingerprints of Prion Infection: Accumulations of
Aberrant Full-Length and N-Terminally Truncated PrP Species Are
Common Features in Mouse Prion Disease.

Pan T, Wong P, Chang B, Li C, Li R, Kang SC, Wisniewski T, Sy MS.

Room 933, BRB, School of Medicine, Case Western Reserve University,
10900 Euclid Ave., Cleveland, OH 44107-1712. mxs92@po.cwru.edu.

Infection with any one of three strains of mouse scrapie prion
(PrP(Sc)), 139A, ME7, or 22L, results in the accumulation of two
underglycosylated, full-length PrP species and an N-terminally
truncated PrP species that are not detectable in uninfected animals.
The levels of the N-terminally truncated PrP species vary depending
on PrP(Sc) strain. Furthermore, 22L-infected brains consistently
have the highest levels of proteinase K (PK)-resistant PrP species,
followed by ME7- and 139A-infected brains. The three strains of
PrP(Sc) are equally susceptible to PK and proteases papain and
chymotrypsin. Their protease resistance patterns are also similar.
In sucrose gradient velocity sedimentation, the aberrant PrP species
partition with PrP(Sc) aggregates, indicating that they are
physically associated with PrP(Sc). In ME7-infected animals, one of
the underglycosylated, full-length PrP species is detected much
earlier than the other, before both the onset of clinical disease
and the detection of PK-resistant PrP species. In contrast, the
appearance of the N-terminally truncated PrP species coincides with
the presence of PK-resistant species and the manifestation of
clinical symptoms. Therefore, accumulation of the underglycosylated,
full-length PrP species is an early biochemical fingerprint of
PrP(Sc) infection. Accumulation of the underglycosylated,
full-length PrP species and the aberrant N-terminally truncated PrP
species may be important in the pathogenesis of prion disease.


http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15613322

TSS

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