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From: TSS (216-119-144-23.ipset24.wt.net)
Subject: Advances in the detection of prion protein in peripheral tissues of vCJD patients using paraffin-embedded tissue blotting
Date: August 16, 2004 at 9:27 am PST

-------- Original Message --------
Subject: Advances in the detection of prion protein in peripheral tissues of variant Creutzfeldt-Jakob disease patients using paraffin-embedded tissue blotting
Date: Mon, 16 Aug 2004 11:31:53 -0500
From: "Terry S. Singeltary Sr."
To: Bovine Spongiform Encephalopathy
CC: cjdvoice@yahoogroups.com


Neuropathology & Applied Neurobiology
Volume 30 Issue 4 Page 360 - August 2004
doi:10.1111/j.1365-2990.2003.00544.x

Advances in the detection of prion protein in peripheral tissues of
variant Creutzfeldt-Jakob disease patients using paraffin-embedded
tissue blotting
D. L. Ritchie, M. W. Head and J. W. Ironside

The accumulation of PrPSc, an abnormal and disease-associated form of
the normal prion protein (PrPc), within the central nervous system (CNS)
is a key pathological feature of Creutzfeldt-Jakob disease (CJD).
Following limited proteolytic digestion of PrPSc, the detection of
PrPres within lymphoid tissues is a unique characteristic of variant CJD
in comparison with other human prion diseases, raising fears of an
increased risk of iatrogenic spread. Because levels of PrPres in
lymphoid tissues are lower than those found in CNS tissue, there is
concern that other peripheral tissues may harbour infectivity at levels
that current detection systems cannot demonstrate PrPres. We have
modified the paraffin-embedded tissue blot (PET blot), a technique
combining immunohistochemistry (IHC), histoblot and Western blotting,
for the detection of PrPres in paraffin sections in peripheral tissues
in variant CJD. Five cases of variant CJD were examined, using a panel
of anti-PrP antibodies. In each of these five cases, spleen, tonsil,
lymph nodes and dorsal root ganglia showed an increase in the
sensitivity and specificity of labelling using the PET blot when
compared with optimized PrPres IHC methods. Control cases showed no
evidence of PrP accumulation in either peripheral or CNS tissues.
Autopsy and biopsy brain material from sporadic CJD cases also showed an
increased sensitivity of PrPres detection with the PET blot, confirming
its value as an important diagnostic and research tool in human prion
diseases.

http://www.blackwell-synergy.com/links/doi/10.1111/j.1365-2990.2003.00544.x/abs/

TSS






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