Peptide LSARLAF induces integrin β3 dependent outside-in signaling in platelets.

ABSTRACT:

Introduction

Peptide LSARLAF (LSA) can bind and activate integrin αIIbβ3 in the absence of 'inside-out' signal. The active αIIbβ3 mediates 'outside-in' signaling that elicits platelet aggregation, granule secretion and TxA2 production. Here we identify the membrane glycoproteins which mediate LSA-induced platelet activation other than αIIbβ3, and determine the roles of Src, PLCγ2, FcRγ-chain, and SLP-76 in LSA-induced platelet activation.

Method

Ligand-receptor binding assay was performed to study the effect of peptide LSA or its control peptide FRALASL (FRA) on integrins binding to their ligands. Spreading of CHO cells expressing αIIbβ3 or αVβ3 on immobilized fibrinogen was measured in the presence of LSA or FRA. Washed β3, Src, FcRγ-chain, LAT and SLP-76 deficient platelet

SUBMITTER: Niu H 

PROVIDER: S-EPMC3393848 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature