NR AFLW
AU Holada,K.; Mondoro,T.H.; Muller,J.; Vostal,J.G.
TI Increased expression of phosphatidylinositol-specific phospholipase C resistant prion proteins on the surface of activated platelets
QU British Journal of Haematology 1998 Oct; 103(1): 276-82
KI British Journal of Haematology 2000 Sep;110(3):745-8. PMID: 10997991 British Journal of Haematology 2000 Sep;110(3):748-50. PMID: 10997993
PT journal article
AB The surface expression of prion protein (PrPc) on human platelets, as detected by flow cytometry with the monoclonal antibody 3F4, increased more than two-fold (4300 v 1800 molecules/platelet) after full activation. Maximal surface expression of PrPc occurred within 3 min of platelet activation and declined to approximately half of maximal levels by 2 h at 37 degrees C. In comparison, PrPc on the surface of platelets, activated at 22 degrees C took 10 min to reach maximum but then remained constant for 2 h. In sonicated resting platelets, PrPc and P-selectin remained in intact granules after subcellular fractionation. Both glycoproteins were found in the ruptured membranes of activated platelets, suggesting that the PrPc was translocated from internal granules to the plasma membrane during activation, as is P-selectin. Platelet PrPc was not removed from the surface of platelets by phosphatidylinositol-specific phospholipase C (PIPLC) treatment but was degraded by proteinase K. Platelets may serve as a useful model for following the cellular processing of PrPc.
MH Blood Platelets/*enzymology; Blotting, Western; Human; Phosphatidylcholines/*metabolism; Phospholipase C/*metabolism; Platelet Activation; PrPc Proteins/*metabolism; RNA, Messenger/metabolism
AD Division of Hematology, Center for Biologics Evaluation and Research, FDA, Bethesda, Maryland 20892, USA
SP englisch
PO England