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Prepublished online as a Blood First Edition Paper on January 9, 2003; DOI 10.1182/blood-2002-06-1847.
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Blood, 1 May 2003, Vol. 101, No. 9, pp. 3477-3484
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Role of the intracellular domains of GPIb in controlling the
adhesive properties of the platelet GPIb/V/IX complex
Christelle Perrault,
Pierre Mangin,
Martine Santer,
Marie-Jeanne Baas,
Sylvie Moog,
Susan L. Cranmer,
Inna Pikovski,
David Williamson,
Shaun P. Jackson,
Jean-Pierre Cazenave, and
François Lanza
From INSERM U311, Etablissement Français du Sang,
Alsace, Strasbourg, France; and the Australian Centre for
Blood Diseases, Department of Medicine, Monash Medical School,
Australia.
Glycoprotein (GP) Ib/V/IX complex-dependent platelet adhesion to
von Willebrand factor (VWF) is supported by the 45-kd N-terminal extracellular domain of the GPIb subunit. Recent results with an
adhesion blocking antibody (RAM.1) against GPIb , which is disulfide
linked to GPIb, have suggested a novel function of this subunit in
regulating VWF-mediated platelet adhesion, possibly involving its
intracellular face. A putative cooperation between the GPIb and
GPIb cytoplasmic domains was investigated by measuring the adhesion
under flow to immobilized VWF of K562 and Chinese hamster ovary
(CHO) cells transfected with GPIb/(V)/IX containing mutations in this region. Adhesion of cells carrying a glycine substitution of the GPIb Ser166 phosphorylation site was 50% lower
than normal and became insensitive to inhibition by RAM.1. In contrast,
forskolin or PGE1 treatment increased both the
phosphorylation of GPIb and adhesion of control cells, both effects
being reversed by RAM.1, but had no influence on cells expressing the
Ser166Gly mutation. A role of the GPIb intracellular domain
was also apparent as the VWF-dependent adhesion of cells containing
deletions of the entire ( 518-610) or portions (535-568,
569-610) of the GPIb cytoplasmic tail was insensitive to RAM.1
inhibition. Cells carrying progressive 11 amino acid deletions spanning
the GPIb 535-590 region were equally unresponsive to RAM.1, with the
exception of those containing GPIb 569-579, which behaved like
control cells. These findings support a role of the GPIb
intracellular domain in controlling the adhesive properties of the
GPIb/V/IX complex through phosphorylation of GPIb Ser166 and point
to the existence of cross-talk between the GPIb and GPIb
intracellular domains.
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