on August 28, 2003
Published online before print August 28, 2003, doi: 10.1161/01.ATV.0000093470.51580.0F
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Submitted on August 7, 2003
Accepted on August 20, 2003
Effects of Thrombin on Interactions Between 
3-Integrins and Extracellular Matrix in Platelets and Vascular Cells
G. A. Stouffer * and S. S. Smyth
From the Division of Cardiology and Carolina Cardiovascular Biology Center, University of North Carolina, Chapel Hill.
* To whom correspondence should be addressed. E-mail: rstouff{at}med.unc.edu.
Abstract--The 
3-integrin family consists of 
IIb3 (also known as glycoprotein IIb/IIIa) and v3. IIb3 is found on platelets and megakaryocytes and has an essential role in hemostasis. v3 has a broader distribution, and it functions in angiogenesis, neointimal formation after vascular injury, and leukocyte trafficking. There are important interactions between thrombin and 3-integrins relative to both "inside-out" (integrin activation) and "outside-in" (modification of cellular events by ligand binding to integrins) signaling. Thrombin, by binding to G protein-coupled, protease-activated receptors, is a potent activator of IIb3. Conversely, outside-in signaling through IIb3 amplifies events initiated by thrombin and is necessary for full platelet spreading, platelet aggregation, granule secretion, and the formation of a stable platelet thrombus. In smooth muscle cells, v3-integrins influence various responses to thrombin, including proliferation, c-Jun NH2-terminal kinase-1 activation, and focal adhesion formation. Other interactions between 3-integrins and thrombin include 3-integrin promotion of the generation of thrombin by localizing prothrombin to cellular surfaces and/or enhancing the formation of procoagulant microparticles and the requirement of 3-integrin function for platelet-dependent clot retraction. In summary, there is increasing evidence that interactions between 3-integrins and thrombin play important roles in the regulation of hemostatic and vascular functions.
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