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  • Title: Membrane binding and autolytic activation of calpain-I in human platelets.
    Author: Ariyoshi H, Shiba E, Sakon M, Kambayashi J, Kawasaki T, Kang J, Kawashima S, Mori T.
    Journal: Biochem Int; 1992 Jul; 27(2):335-41. PubMed ID: 1503568.
    Abstract:
    The binding of calpain-I (Ca2+ activated neutral protease with high Ca2+ sensitivity) to the membranes of human platelets and the subsequent autolytic activation of calpain-I were analyzed by an immunoblot technique. In A23187 stimulated platelets, cytosolic calpain-I translocated to the membranes with autolysis in a Ca2+ dependent manner and simultaneously underwent autolysis. Although calpeptin, a cell permeable calpain inhibitor, inhibited autolysis of calpain-I, it was unable to prevent the translocation of calpain-I. In a cell re-constituted system, the membrane binding of calpain-I was also Ca2+ dependent and was significantly inhibited by a substrate of calpain. It was suggested that the binding of calpain-I to the membranes required the substrate binding site of this enzyme.
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