Editorials |
From the Department of Medicine, University of Wisconsin, Madison.
Correspondence to Deane F. Mosher, Department of Medicine, University of Wisconsin, 1300 University Ave, Madison, WI 53706. E-mail dfmosher@wisc.edu
An extract of the first 250 words of the full text is provided, because this article has no abstract. |
Accumulation and cohesion of platelets at sites of vascular injury are essential for the formation of the hemostatic plug but also result in thrombosis.1,2 Platelet plug or thrombus formation is initiated by interaction of platelet receptors with components of extracellular matrix (ECM) of injured vessels. Fibronectin is both an ECM component and moderately abundant 460-kDa glycoprotein in blood, present at 300 to 400 µg/mL (0.6 to 0.9 µmol/L) in plasma and 0.5 µg per 3x108 platelets in platelet
-granules.35 Plasma fibronectin is a dimer of nearly identical 230-kDa subunits (Figure) that can multimerize to the insoluble form found in ECM.6 Because it is a ligand of platelet surface receptors and an ECM component, fibronectin has long been suspected of playing a role in platelet biology.4,5 Interestingly, fibronectin and its type I module, of which there are 12 in fibronectin (Figure), are well characterized to date only in vertebrates.7,8 Therefore, fibronectin seems to be a recent addition to the armamentarium of proteins that function in the vertebrate vasculature.
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Related Article:
Arterioscler Thromb Vasc Biol 2006 26: 1391-1396.
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A. Reheman, H. Yang, G. Zhu, W. Jin, F. He, C. M. Spring, X. Bai, P. L. Gross, J. Freedman, and H. Ni Plasma fibronectin depletion enhances platelet aggregation and thrombus formation in mice lacking fibrinogen and von Willebrand factor Blood, February 19, 2009; 113(8): 1809 - 1817. [Abstract] [Full Text] [PDF] |
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