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• W1484853482 endingPage "11977" @default.
• W1484853482 startingPage "11970" @default.
• W1484853482 abstract "Platelets have previously been shown to contain a membrane skeleton that is composed of actin filaments, actin-binding protein, and three membrane glycoproteins (GP), GP Ib, GP Ia, and a minor glycoprotein of Mr = 250,000. The present study was designed to determine how the membrane glycoproteins were linked to actin filaments. Unstimulated platelets were lysed with Triton X-100, and the membrane skeleton was isolated on sucrose density gradients or by high-speed centrifugation. The association of the membrane glycoproteins with the actin filaments was disrupted when actin-binding protein was hydrolyzed by activity of the Ca2+-dependent protease, which was active in platelet lysates upon addition of Ca2+ in the absence of leupeptin. Similarly, activation of the Ca2+-dependent protease in intact platelets by the addition of a platelet agonist also caused the membrane glycoproteins to dissociate from the membrane skeleton. Affinity-purified actin-binding protein antibodies immunoprecipitated the membrane glycoproteins from platelet lysates in which actin filaments had been removed by DNase I-induced depolymerization and high-speed centrifugation. These results demonstrate that actin-binding protein links actin filaments of the platelet membrane skeleton to three plasma membrane glycoproteins and that filaments are released from their attachment site when actin-binding protein is hydrolyzed by the Ca2+-dependent protease within intact platelets during platelet activation." @default.
• W1484853482 created "2016-06-24" @default.
• W1484853482 creator A5020003804 @default.
• W1484853482 date "1985-10-01" @default.
• W1484853482 modified "2023-10-18" @default.
• W1484853482 title "Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membranes." @default.
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• W1484853482 doi "https://doi.org/10.1016/s0021-9258(17)38972-x" @default.
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