| Literature DB >> 9230107 |
J M Derrick1, D B Taylor, R G Loudon, T K Gartner.
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.Entities:
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Year: 1997 PMID: 9230107 PMCID: PMC1218561 DOI: 10.1042/bj3250309
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857