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J Biol Chem, Vol. 274, Issue 10, 6586-6593, March 5, 1999

Distinct Structural Attributes Regulating von Willebrand Factor A1 Domain Interaction with Platelet Glycoprotein Ib under Flow

From the Roon Research Center for Arteriosclerosis and Thrombosis, Division of Experimental Hemostasis and Thrombosis, Departments of Molecular and Experimental Medicine and of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037

We have used recombinant von Willebrand factor (vWF) fragments to investigate the properties regulating A1 domain interaction with platelet glycoprotein (GP) Ib. One fragment, rvWF^508-704, represented the main portion of domain A1 (mature subunit residues 497-716) within the Cys⁵⁰⁹-Cys⁶⁹⁵ disulfide loop. The other, rvWF^445-733, included the carboxyl-terminal region of domain D3, preceding A1, and corresponded to the proteolytic fragment originally identified as the GP Ib-binding site (residues 449-728). Conformational changes were induced by reduction and alkylation of the Cys⁵⁰⁹-Cys⁶⁹⁵ bond and/or exposure to acidic pH. The cyclic rvWF^445-733 fragment exhibited the function of native vWF A1 domain. When immobilized onto a surface, it tethered platelets at shear rates up to 6,300 s¹ mediating low velocity translocation but not stable attachment; in solution, it exhibited limited interaction with GP Ib. In contrast, fragments with perturbed conformation could not tether platelets at high shear rates but promoted stable adhesion at lower shear and bound tightly to GP Ib. Only in the presence of the exogenous modulator, botrocetin, did cyclic rvWF^445-733 mediate irreversible adhesion. Thus, conformational transitions in the vWF A1 domain may influence differentially the efficiency of bond formation with GP Ib and the stability of binding.

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