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- W3176549168 abstract "The plasma membrane Ca2+-ATPase (PMCA) plays an essential role in maintaining low cytosolic Ca2+ in resting human platelets by extruding Ca2+ from the cytoplasm across the plasma membrane. Since PMCA is the main agent of Ca2+ removal in platelets, it is a key point for regulation of platelet Ca2+ metabolism. The Ca2+-activated cysteine protease calpain, a major platelet protein, has been shown to excise the auto-inhibitory C-terminus of PMCA resulting in a 124 kDa calmodulin-independent species. To determine the kinetics PMCA degradation during platelet activation, the cleavage of PMCA into smaller forms (124 kDa and 100 kDa) was analyzed using SDS PAGE and immunoblotting. Platelet activation mediated by both collagen and thrombin resulted in proteolysis of PMCA (20 and 40% of total PMCA, respectively), leading to the formation of the active 124 kDa PMCA species and a 100 kDa inactive fragment. Calpeptin and ALLN, calpain inhibitors, blocked PMCA degradation and formation of the 124 kDa product. Proteolysis of PMCA to the 100 kDa species was also inhibited by calpain inhibitors but to a lesser extent indicating the participation of other proteases. Thus, calpain-mediated degradation of PMCA during platelet activation likely contributes significantly to Ca2+ regulation and, therefore, to platelet function." @default.
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- W3176549168 date "2006-03-01" @default.
- W3176549168 modified "2023-09-27" @default.
- W3176549168 title "Regulation of Plasma Membrane Ca2+‐ATPase in Human Platelets by Calpain" @default.
- W3176549168 doi "https://doi.org/10.1096/fasebj.20.4.a116-d" @default.
- W3176549168 hasPublicationYear "2006" @default.
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