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Integrins in platelet activation
Author(s) -
NIESWANDT B.,
VARGASZABO D.,
ELVERS M.
Publication year - 2009
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.1538-7836.2009.03370.x
Subject(s) - integrin , platelet activation , microbiology and biotechnology , platelet , hemostasis , platelet adhesiveness , cell adhesion , receptor , chemistry , adhesion , biology , platelet aggregation , immunology , biochemistry , medicine , organic chemistry
Summary. Heterodimeric receptors of the β1 and β3 integrin families mediate platelet adhesion and aggregation in hemostasis and thrombosis. In resting platelets, integrins are expressed in a low‐affinity state but they shift to a high‐affinity state and efficiently bind their ligands in response to cellular activation. This review summarizes recent advances in understanding the functional regulation and (patho‐) physiological significance of individual platelet integrins with a special focus on studies in genetically modified mice. It is now recognized that β1 and β3 integrins have partially redundant roles in the adhesion process and that their activation is regulated by similar mechanisms, involving Ca 2+ ‐dependent and ‐independent signaling events and essential functions of talin‐1 and kindlin‐3 in the terminal activation step.