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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 903-910
Requirement of leucine-rich repeats of glycoprotein (GP) Ib
for shear-dependent and static binding of von Willebrand factor to
the platelet membrane GP Ib-IX-V complex
Yang Shen,
Gabriel M. Romo,
Jing-fei Dong,
Alicia Schade,
Larry V. McIntire,
Dermot Kenny,
James C. Whisstock,
Michael C. Berndt,
José A. López, and
Robert K. Andrews
From the Hazel and Pip Appel Vascular Biology Laboratory, Baker
Medical Research Institute, Melbourne, Australia; Departments of
Medicine and Molecular and Human Genetics, Baylor College of Medicine,
Houston, TX; Veterans Affairs Medical Center, Houston, TX; Cox
Laboratory for Biomedical Engineering, Rice University, Houston, TX;
The Blood Center of Southeast Wisconsin, Milwaukee, WI; and Department
of Biochemistry and Molecular Biology, Monash University, Clayton,
Australia.
The platelet glycoprotein (GP) Ib-IX-V complex mediates adhesion to
von Willebrand factor (vWf) in (patho)physiologic thrombus formation.
The vWf-binding site on GP Ib-IX-V is within the N-terminal 282 residues of GP Ib , which consist of an N-terminal flanking sequence
(His-1-Ile-35), 7 leucine-rich repeats (Leu-36-Ala-200), a C-terminal
flank (Phe-201-Gly-268), and a sulfated tyrosine sequence
(Asp-269-Glu-282). We have used mammalian cell expression of
canine-human chimeras of GP Ib, corresponding to precise structural boundaries, to demonstrate the first specific requirement for individual leucine-rich repeats for binding of vWf either induced by a
modulator, ristocetin, or under hydrodynamic flow. Implicit in this
approach was that the GP Ib chimeras retained a functional conformation, a supposition confirmed by analyzing restoration of
function to reversed human-canine chimeras and demonstrating that all
chimeras bound vWf activated by botrocetin, a modulator that is
indiscriminate between species. Leucine-rich repeats 2, 3, and 4 of GP
Ib were identified as being critical for vWf adhesion to GP
Ib-IX-V.
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