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

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.

SUBMITTER: Derrick JM 

PROVIDER: S-EPMC1218561 | biostudies-other | 1997 Jul

REPOSITORIES: biostudies-other