Glycoprotein Ib Can Mediate Endothelial Cell Attachment to a von Willebrand Factor Substratum

Dorothy A Beacham; Miguel A Cruz; Robert I Handin

doi:10.1055/s-0038-1653770

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1995; 73(02): 309-317
DOI: 10.1055/s-0038-1653770

Original Article

Von Willebrand Factor

Schattauer GmbH Stuttgart

Glycoprotein Ib Can Mediate Endothelial Cell Attachment to a von Willebrand Factor Substratum

Authors

Dorothy A Beacham

²The Cardeza Foundation for Hematologic Research, Department of Medicine, Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA, USA
Miguel A Cruz

¹The Hematology/Oncology Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA
Robert I Handin

¹The Hematology/Oncology Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA, USA

Abstract

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Summary

Introduction of single amino acid substitutions into the C-terminal Arg-Gly-Asp-Ser (RGDS) site of von Willebrand Factor, referred to as RGD mutant vWF, selectively abrogated vWF binding to platelet glycoprotein IIb/IIIa (GpIIb/IIIa, α_IIbβ₃ and abolished human umbilical vein endothelial cell (HUVEC) spreading, but not attachment, to RGD mutant vWF (Beacham, D. A., Wise, R. J., Turci, S. M. and Handin, R. I. 1992. J. Biol. Chem. 167, 3409-3415). These results suggested that in addition to the vitronectin receptor (VNR, α_vβ₃), a second endothelial membrane glycoprotein can mediate HUVEC adhesion to vWF. HUVEC attachment to wild-type (WT) and RGD-mutant vWF was reduced by two proteins known to block the vWF-platelet glycoprotein Ib/IX (GpIb/IX) interaction, the monoclonal antibody AS-7 and the recombinant polypeptide, vWF-A1. The addition of cytochalasin B or DNase I to disrupt potential GPIbα-cytoskeletal interactions enhanced the immunoprecipitation of endothelial GPIbα, caused HUVEC to round up, and increased HUVEC adhesion to RGD mutant vWF. These results indicate that while the VNR is the primary adhesion receptor for vWF, endothelial GPIbα can mediate HUVEC attachment to vWF. GpIb-dependent attachment could contribute to HUVEC adhesion under conditions when cell surface expression of the VNR is downregulated, and VNR-dependent adhesion is reduced.

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References

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