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Platelet receptor recognition and cross‐talk in collagen‐induced activation of platelets
Author(s) -
FARNDALE R. W.,
SLATTER D. A.,
SILJANDER P. R.M.,
JARVIS G. E.
Publication year - 2007
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/j.1538-7836.2007.02521.x
Subject(s) - gpvi , collagen receptor , integrin , platelet , platelet activation , chemistry , receptor , microbiology and biotechnology , platelet membrane glycoprotein , biophysics , syk , biochemistry , immunology , biology , tyrosine kinase
Summary. Comprehensive mapping of protein‐binding sites within human collagen III has allowed the recognition motifs for integrin α 2 β 1 and VWF A3 domain to be identified. Glycoprotein VI‐binding sites are understood, although less well defined. This information, together with recent developments in understanding collagen fiber architecture, and crystal structures of the receptor collagen‐binding domains, allows a coherent model for the interaction of collagen with the platelet surface to be developed. This complements our understanding of the orchestration of receptor presentation by membrane microdomains, such that the polyvalent collagen surface may stabilize signaling complexes within the heterogeneous receptor composition of the lipid raft. The ensuing interactions lead to the convergence of signals from each of the adhesive receptors, mediated by FcR γ‐chain and/or FcγRIIa, leading to concerted and co‐operative platelet activation. Each receptor has a shear‐dependent role, VWF/GpIb essential at high shear, and α 2 β 1 at low and intermediate shear, whilst GpVI provides core signals that contribute to enhanced integrin affinity, tighter binding to collagen and consequent platelet activation.