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- W2141905650 endingPage "1520" @default.
- W2141905650 startingPage "1511" @default.
- W2141905650 abstract "The platelet plasma membrane is literally at the cutting-edge of recent research into proteolytic regulation of the function and surface expression of platelet receptors, revealing new mechanisms for how the thrombotic propensity of platelets is controlled in health and disease. Extracellular proteolysis of receptors irreversibly inactivates receptor-mediated adhesion and signaling, as well as releasing soluble fragments into the plasma where they act as potential markers or modulators. Platelet-surface sheddases, particularly of the metalloproteinase-disintegrin (ADAM) family, can be regulated by many of the same mechanisms that control receptor function, such as calmodulin association or activation of signaling pathways. This provides layers of regulation (proteinase and receptor), and a higher order of control of cellular function. Activation of pathways leading to extracellular shedding is concomitant with activation of intracellular proteinases such as calpain, which may also irreversibly deactivate receptors. In this review, platelet receptor shedding will be discussed in terms of (1) the identity of proteinases involved in receptor proteolysis, (2) key platelet receptors regulated by proteolytic pathways, and (3) how shedding might be regulated in normal physiology or future therapeutics. In particular, a focus on proteolytic regulation of the platelet collagen receptor, glycoprotein (GP)VI, illustrates many of the key biochemical, cellular, and clinical implications of current research in this area." @default.
- W2141905650 created "2016-06-24" @default.
- W2141905650 creator A5039148455 @default.
- W2141905650 creator A5055483790 @default.
- W2141905650 creator A5065834493 @default.
- W2141905650 creator A5072400072 @default.
- W2141905650 date "2007-07-01" @default.
- W2141905650 modified "2023-09-27" @default.
- W2141905650 title "Platelet Receptor Proteolysis" @default.
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