NR AMWK
AU Yoo,B.C.; Krapfenbauer,K.; Cairns,N.J.; Belay,G.; Bajo,M.; Lubec,G.
TI Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease
QU Neuroscience Letters 2002 Dec 16; 334(3): 196-200
PT journal article
AB Earlier studies have failed to detect covalent modifications in beta-sheet-rich scrapie isoform prion protein (PrPsc) and have concluded that the conversion of alpha-helix-rich cellular form prion protein (PrPc) to PrPsc represents purely conformational transition not involving chemical reactions. However, recent studies have shown that the intradisulfide bond of PrPc can play an important role for instability and conformational change to PrPsc. Interestingly, we found overexpressed protein disufide isomerase (PDI) in brains of sporadic Creutzfeldt-Jakob disease (sCJD, human prion disease) patients using two dimensional electrophoresis and Western blot analysis but not in other neurodegenerative disorders as Down Syndrome and Alzheimer's disease. However, proteinase K digestion and plasminogen binding assay of brain homogenates incubated with PDI suggest that PDI has no effect on either proteinase resistance or conformational change of PrP. Overexpression of PDI protein in sCJD brain may simply reflect a cellular defense response against the altered prion protein.
AD Byong Chul Yoo, Kurt Krapfenbauer, Michal Bajo, Gert Lubec, Department of Pediatrics, University of Vienna, Waehringer Guertel 18, A-1090, Vienna, Austria; Kurt Krapfenbauer, F. Hoffmann-La Roche Ltd, Pharmaceuticals Division, Basel, Switzerland; Nigel J. Cairns, Brain Bank, Department of Neuropathology, Institute of Psychiatry, King's College, London, UK; Girma Belay, Institute of Preventive and Clinical Medicine, Bratislava, Slovakia
SP englisch
PO Irland