Integrins in platelet activation

Authors

  • B. NIESWANDT,

    1. Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine, University of Würzburg
    2. Experimental Biomedicine, University Clinic, University of Würzburg, Würzburg, Germany
    Search for more papers by this author
  • D. VARGA-SZABO,

    1. Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine, University of Würzburg
    Search for more papers by this author
  • M. ELVERS

    1. Rudolf Virchow Center, DFG Research Center for Experimental Biomedicine, University of Würzburg
    2. Experimental Biomedicine, University Clinic, University of Würzburg, Würzburg, Germany
    Search for more papers by this author

Bernhard Nieswandt, Chair of Experimental Biomedicine, Rudolf Virchow Center, University of Würzburg, Zinklesweg 10, 97078 Würzburg, Germany.
Tel.: +49 931 201 44060; fax: +49 931 201 44068.
E-mail: bernhard.nieswandt@virchow.uni-wuerzburg.de

Abstract

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 Ca2+-dependent and -independent signaling events and essential functions of talin-1 and kindlin-3 in the terminal activation step.

Ancillary