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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.
Previous Article | Next Article 
Submitted April 5, 2004
Accepted June 1, 2004
Integrins: Dynamic Scaffolds for Adhesion and Signaling in Platelets
Sanford J Shattil* and Peter J Newman
Cell Biology, The Scripps Research Institute, La Jolla, CA, USA
Blood Research Institute, Blood Center of Southeastern Wisconsin, Milwaukee, WI, USA
* Corresponding author; email: blood{at}scripps.edu.
The major platelet integrin, IIb 3, is required for platelet interactions with proteins in plasma and the extracellular matrix (ECM) that are essential for platelet adhesion and aggregation during hemostasis and arterial thrombosis. Ligand binding to IIb 3 is controlled by inside-out signals that modulate receptor conformation and clustering. In turn, ligand binding triggers outside-in signals through IIb 3 that, when disrupted, can cause a bleeding diathesis. In the past five years, there has been an explosion of knowledge about the structure and function of IIb 3 and the related integrin, V 3. These developments are discussed here and current models of bidirectional IIb 3 signaling are presented as frameworks for future investigations. An understanding that IIb 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.

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N. Mohandas
The sticking point
Blood,
April 15, 2005;
105(8):
3008 - 3009.
[Full Text]
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C. S. Buensuceso, A. Obergfell, A. Soriani, K. Eto, W. B. Kiosses, E. G. Arias-Salgado, T. Kawakami, and S. J. Shattil
Regulation of Outside-in Signaling in Platelets by Integrin-associated Protein Kinase C{beta}
J. Biol. Chem.,
January 7, 2005;
280(1):
644 - 653.
[Abstract]
[Full Text]
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