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Originally published In Press as doi:10.1074/jbc.M101035200 on February 23, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16690-16694, May 18, 2001
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Tyrosine Sulfation of Glycoprotein Ibalpha
ROLE OF ELECTROSTATIC INTERACTIONS IN VON WILLEBRAND FACTOR BINDING*

Jing-fei Dong, Pei Ye, Alicia J. Schade, Shan Gao, Gabriel M. Romo, Nancy T. Turner, Larry V. McIntire, and José A. LópezDagger

From the Division of Thrombosis Research, Department of Medicine, and Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030 and the Cox Laboratory for Bioengineering, Rice University, Houston, Texas 77005

Glycoprotein Ibalpha (GP Ibalpha ), the ligand binding subunit of the platelet glycoprotein Ib-IX-V complex, is sulfated on three tyrosine residues (Tyr-276, Tyr-278, and Tyr-279). This posttranslational modification is known to be critical for von Willebrand factor (vWF) binding; yet it remains unclear whether it provides a specific structure or merely contributes negative charges. To investigate this issue, we constructed cell lines expressing GP Ibalpha polypeptides with the three tyrosine residues converted to either Glu or Phe and studied the ability of these mutants to bind vWF in the presence of modulators or shear stress. The mutants were expressed normally on the cell surface as GP Ib-IX complexes, with the conformation of the ligand-binding domain preserved, as judged by the binding of conformation-sensitive monoclonal antibodies. In contrast to their normal expression, both mutants were functionally abnormal. Cells expressing the Phe mutant failed to bind vWF in the presence of either ristocetin or botrocetin. These cells adhered to and rolled on immobilized vWF only when their surface receptor density was increased to twice the level that supported adhesion of cells expressing the wild-type receptor and even then only 20% as many rolled and rolled significantly faster than wild-type cells. Cells expressing the Glu mutant, on the other hand, were normal with respect to ristocetin-induced vWF binding and adhesion to immobilized vWF but were markedly defective in botrocetin-induced vWF binding. These results indicate that GP Ibalpha tyrosine sulfation influences the interaction of this polypeptide with vWF primarily by contributing negative charges under physiological conditions and when the interaction is induced by ristocetin but contributes a specific structure to the botrocetin-induced interaction.

* This work was supported by National Institutes of Health Grants HL02463, HL46416, HL18673, and NS23327, Robert A. Welch Foundation Grant C938, a grant-in-aid from the American Heart Association-Texas Affiliate, and by the National Institutes of Health Medical Scientist Training Program at Baylor College of Medicine.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Thrombosis Research Section, Dept. of Medicine, BCM286, N1319, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030. Tel.: 713-798-3470; Fax: 713-798-3415; E-mail: josel@bcm.tmc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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