NR ARCV
AU Korth,C.; Lingappa,V.
TI Bioconformatics: Detection, interactions, and manipulation of prion protein isoforms
QU TSE-Forum, 4. Kongress - Nationale TSE-Forschungsplattform, Düsseldorf 28.10.-29.10.2004, Vortrag V-12
PT Konferenz-Vortrag
AB
Prion diseases are unique since replication as well as neurotoxicity involves generation of different stable conformations of one polypeptide chain. Methods to distinguish the normal from the infectious conformational isoform of PrP, PrPc and PrPsc, respectively, currently rely on rather crude procedures like hot (37° for 1 h) protease digestion. A neurodegeneration-causing non-infectious isoform of PrP, CTMPrP has previously been characterized to mediate the neurotoxic effects of PrP-associated diseases. CTMPrP, as well as NTMPrP, are topological and conformational isoforms of PrP that initially were described in the in vitro translation system.
We have started to produce specific ligands to better characterize the biology of the conformational and biological isoforms of normal PrPc, in particular CTMPrP and NTMPrP. We report about a monoclonal antibody, 19B10, that recognizes an isoform of PrPc corresponding to NTMPrP in the in vitro translation system that has unique apoptosis-inducing effects in several cell types, whereas a universal PrP-recognizing antibody 6H4 does not. We conclude that biological functions are differentially regulated by isoforms of the normal prion protein.
AD Carsten Korth, Institute for Neuropathology, Heinrich Heine University of Duesseldorf; Vishwanath Lingappa, Department of Medicine and Physiology, University of California San Francisco
SP englisch
PO Deutschland
OR Tagungsband