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. 1997 Jul 15;325(Pt 2):309–313. doi: 10.1042/bj3250309

The peptide LSARLAF causes platelet secretion and aggregation by directly activating the integrin alphaIIbbeta3.

J M Derrick 1, D B Taylor 1, R G Loudon 1, T K Gartner 1
PMCID: PMC1218561  PMID: 9230107

Abstract

A novel peptide (designed to bind to alphaIIbbeta3) caused platelet aggregation and aggregation-independent secretion of the contents of alpha-granules in an alphaIIbbeta3-dependent fashion. The agonist peptide induced secretion in the presence of prostaglandin E1. In cell-free assays, alphaIIbbeta3 bound specifically to immobilized agonist peptide and the peptide enhanced the binding of fibrinogen to immobilized alphaIIbbeta3. The agonist peptide apparently activates alphaIIbbeta3 by directly inducing a conformational change in the receptor. This change activates the platelets and causes secretion in a manner independent of fibrinogen binding.

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Selected References

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