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 Blood, 15 September 2004, Vol. 104, No. 6, pp. 1606-1615.
Prepublished online as a Blood First Edition Paper on June 17, 2004; DOI 10.1182/blood-2004-04-1257.

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REVIEW ARTICLES

Integrins: dynamic scaffolds for adhesion and signaling in platelets

Sanford J. Shattil, and Peter J. Newman

From the Departments of Cell Biology and Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA; and the Blood Research Institute, the Blood Center of Southeastern Wisconsin, Milwaukee, WI.

The major platelet integrin, {alpha}IIb{beta}3, is required for platelet interactions with proteins in plasma and the extracellular matrices (ECMs) that are essential for platelet adhesion and aggregation during hemo stasis and arterial thrombosis. Lig and binding to {alpha}IIb{beta}3 is controlled by inside-out signals that modulate receptor conformation and clustering. In turn, ligand binding triggers outside-in signals through {alpha}IIb{beta}3 that, when disrupted, can cause a bleeding diathesis. In the past 5 years there has been an explosion of knowledge about the structure and function of{alpha}IIb{beta}3 and the related integrin, {alpha}V{beta}3. These developments are discussed here, and current models of bidirectional {alpha}IIb{beta}3 signaling are presented as frameworks for future investigations. An understanding that {alpha}IIb{beta}3 functions as a dynamic molecular scaffold for extracellular and intracellular proteins has translated into diagnostic and therapeutic insights relevant to hematology and cardiovascular medicine, and further advances can be anticipated. (Blood. 2004;104:1606-1615)


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