TAILIEUCHUNG - Báo cáo khoa học: The leech product saratin is a potent inhibitor of platelet integrin a2b1 and von Willebrand factor binding to collagen

Subendothelial collagen plays an important role, via both direct and indir-ect mechanisms, in the initiation of thrombus formation at sites of vascular injury. Collagen binds plasma von Willebrand factor, which mediates plate-let recruitment to collagen under high shear. | ỊFEBS Journal The leech product saratin is a potent inhibitor of platelet integrin a2Pi and von Willebrand factor binding to collagen Tara C. White1 Michelle A. Berny1 David K. Robinson1 Hang Yin2 William F. DeGrado2 3 Stephen R. Hanson1 and Owen J. T. McCarty1 4 1 Department of BiomedicalEngineering Oregon Health Science University Portland OR USA 2 Department of Biochemistry and Biophysics Schoolof Medicine University of Pennsylvania Philadelphia PA USA 3 Department of Chemistry University of Pennsylvania Philadelphia PA USA 4 Celland DevelopmentalBiology Oregon Health Science University Portland OR USA Keywords a2p1 collagen platelet saratin von Willebrand factor Correspondence O. J. T. McCarty Department of Biomedical Engineering Oregon Health Science University 13B-CHH 3303 SW Bond Ave Portland OR 97239 USA Fax 1 503 418 9311 Tel 1 503 418 9307 E-mail mccartyo@ Received 22 October 2006 revised 20 December 2006 accepted 11 January 2007 doi Subendothelial collagen plays an important role via both direct and indirect mechanisms in the initiation of thrombus formation at sites of vascular injury. Collagen binds plasma von Willebrand factor which mediates platelet recruitment to collagen under high shear. Subsequently the direct binding of the platelet receptors glycoprotein VI and a2p1 to collagen is critical for platelet activation and stable adhesion. Leeches have evolved a number of inhibitors directed towards platelet-collagen interactions so as to prevent hemostasis in the host during hematophagy. In this article we describe the molecular mechanisms underlying the ability of the leech product saratin to inhibit platelet binding to collagen. In the presence of inhibitors of ADP and thromboxane A2 both saratin and 6F1 a blocking a2p1 mAb abrogated platelet adhesion to fibrillar and soluble collagen. Additionally sara-tin eliminated a2p1-dependent platelet adhesion to soluble collagen in the presence of an Src kinase .

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