NR AJIU
AU Perera,W.S.S.; Hooper,N.M.
TI Proteolytic fragmentation of the murine prion protein: role of Tyr-128 and His-177.
QU FEBS Letters 1999 Dec 17; 463(3): 273-6
PT journal article
AB The prion protein (PrP) has been proposed to display sequence and structural similarities to membrane-anchored signal peptidases [Glockshuber et al. (1998) FEBS Lett. 426, 291-296]. We have investigated the role of Tyr-128 and His-177 in the proteolytic fragmentation of murine PrP by mutating these residues to Phe and Leu, respectively, and expressing the resultant mutants in the human neuroblastoma SH-SY5Y. Both PrP-Y128F and PrP-H177L were expressed at the cell surface as glycosyl-phosphatidylinositol-anchored forms and were localised in detergent-insoluble membrane domains similar to wild type PrP. Following deglycosylation, the 19 kDa proteolytic fragment PrP-II was present in cells expressing either mutant, indicating that Tyr-128 and His-177 are not involved in the proteolytic fragmentation of PrP.
MH Animal; Comparative Study; Endopeptidase K; Glycosylation; Glycosylphosphatidylinositols/biosynthesis/*chemistry; Histidine/*chemistry; Human; Leucine/chemistry; Membrane Proteins/biosynthesis/*chemistry; Mice; Mutation; Neuroblastoma; Phenylalanine/chemistry; Phospholipase C; Prions/biosynthesis/*chemistry; Serine Endopeptidases/chemistry; Support, Non-U.S. Gov't; Transfection; Tumor Cells, Cultured; Tyrosine/*chemistry
AD School of Biochemistry and Molecular Biology, University of Leeds, Leeds, UK
SP englisch
PO Niederlande