The study demonstrates a reciprocal interaction between the glycoprotein IIb-IIIa complex and the cytoskeleton in Con A-activated human platelets, suggesting cross-linking of a membrane-associated cytoskeletal complex.
No immediate clinical implications; leaves open glycoprotein-cytoskeleton targeting as a hypothesis for future platelet research.
Concanavalin A (Con A) has been used to activate platelets, inducing a specific interaction between the glycoprotein IIb-IIIa complex and the cytoskeleton of the activated platelet. In agreement with this, we have shown that Con A activates human platelets, initiating phosphorylation, secretion, and cytoskeletal formation. Con A and cytochalasin B were used to demonstrate a reciprocal interaction of the glycoprotein complex with the platelet cytoskeleton. Additionally, we have shown that a similar reciprocity is provided by the multivalent fibrin-fibrinogen platelet interaction found in the thrombin-induced clot. Con A differs from other activators in precipitating an apparent cytoskeletal core despite a complete inhibition of platelet activation by prostaglandin E1. We suggest, from this result, that Con A may be cross-linking a membrane-associated cytoskeletal complex present in the unactivated platelet.
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Wheeler et al. (1985) studied this question.
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