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J. Biol. Chem., Vol. 276, Issue 20, 16952-16959, May 18, 2001
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From the The platelet receptor for von Willebrand factor
(vWF), glycoprotein Ib-IX (GPIb-IX), mediates initial platelet adhesion
and activation. We show here that the receptor function of GPIb-IX is
regulated intracellularly via its link to the filamin-associated membrane skeleton. Deletion of the filamin binding site in GPIb
Regulation of von Willebrand Factor Binding to the Platelet
Glycoprotein Ib-IX by a Membrane Skeleton-dependent
Inside-out Signal*
§,§,,
Department of Pharmacology, University of
Illinois, College of Medicine, Chicago, Illinois 60612 and the
¶ Departments of Molecular and Experimental Medicine and of
Vascular Biology, The Scripps Research Institute,
La Jolla, California 92037
markedly enhances ristocetin- (or botrocetin)-induced vWF binding and
allows GPIb-IX-expressing cells to adhere to immobilized vWF under both
static and flow conditions. Cytochalasin D (CD) that depolymerizes
actin also enhances vWF binding to wild type GPIb-IX. Thus, vWF binding
to GPIb-IX is negatively regulated by the filamin-associated membrane
skeleton. In contrast to native vWF, binding of the isolated recombinant vWF A1 domain to wild type and filamin binding-deficient mutants of GPIb-IX is comparable, suggesting that the membrane skeleton-associated GPIb-IX is in a state that prevents access to the
A1 domain in macromolecular vWF. In platelets, there is a balance of
membrane skeleton-associated and free forms of GPIb-IX. Treatment of
platelets with CD increases the free form and enhances vWF binding. CD
also reverses the inhibitory effects of prostaglandin E1 on vWF binding
to GPIb-IX. Thus, GPIb-IX-dependent platelet adhesion is doubly
controlled by vWF conformation and a membrane skeleton-dependent inside-out signal.
*
This work was supported in part by National Institutes of
Health Grants HL52547 and HL62350 (to X. D.) and HL31950, HL42846, and
HL48728 (to Z. M. R.) and by a grant-in-aid from the American Heart
Association.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.
An Established Investigator of the American Heart Association.
To whom correspondence should be addressed: Dept. of Pharmacology, University of Illinois, College of Medicine, 835 S. Wolcott Ave., Chicago, IL 60612. Tel.: 312-355-0237; Fax: 312-996-1225; E-mail: xdu@uic.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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