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Increased expression of phosphatidylinositol‐specific phospholipase C resistant prion proteins on the surface of activated platelets
Author(s) -
Holada Karel,
Heath Mondoro Traci,
Muller Jacqueline,
Vostal Jaroslav G.
Publication year - 1998
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.1998.01032.x
Subject(s) - platelet , platelet activation , phospholipase c , flow cytometry , phosphatidylinositol , chemistry , microbiology and biotechnology , membrane glycoproteins , glycoprotein , p selectin , monoclonal antibody , whole blood , biochemistry , antibody , biology , immunology , signal transduction
The surface expression of prion protein (PrP C ) 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 PrP C occurred within 3 min of platelet activation and declined to approximately half of maximal levels by 2 h at 37°C. In comparison, PrP C on the surface of platelets, activated at 22°C took 10 min to reach maximum but then remained constant for 2 h. In sonicated resting platelets, PrP C and P‐selectin remained in intact granules after subcellular fractionation. Both glycoproteins were found in the ruptured membranes of activated platelets, suggesting that the PrP C was translocated from internal granules to the plasma membrane during activation, as is P‐selectin. Platelet PrP C 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 PrP C .