Title : Shear-induced disulfide bond formation regulates adhesion activity of von Willebrand factor.

Pub. Date : 2007 Dec 7

PMID : 17925407






4 Functional Relationships(s)
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1 In this study, we demonstrate that some of the plasma VWF multimers contain surface-exposed free thiols. Sulfhydryl Compounds von Willebrand factor Homo sapiens
2 The shear-induced thiol-disulfide exchange increases VWF binding to platelets. Sulfhydryl Compounds von Willebrand factor Homo sapiens
3 The thiol-disulfide exchange involves some or all of nine cysteine residues (Cys(889), Cys(898), Cys(2448), Cys(2451), Cys(2490), Cys(2491), Cys(2453), Cys(2528), and Cys(2533)) in the D3 and C domains as determined by mass spectrometry of the tryptic VWF peptides. Sulfhydryl Compounds von Willebrand factor Homo sapiens
4 These results suggest that the thiol-disulfide state may serve as an important structural determinant of VWF adhesion activity and can be modified by fluid shear stress. Sulfhydryl Compounds von Willebrand factor Homo sapiens