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Human vascular endothelial cells express a membrane protein complex
immunochemically indistinguishable from the platelet VLA-2 (glycoprotein
Ia-IIa) complex
JC Giltay, HJ Brinkman, PW Modderman, AE von dem Borne and JA van Mourik
Central Laboratory of the Netherlands Red Cross Blood Transfusion Service,
Amsterdam.
Endothelial cells express surface molecules that are involved in cell-
matrix interaction, including the vitronectin receptor and the fibronectin
receptor, both members of a family of cell adhesion receptors (integrins).
Here we provide evidence that endothelial cells express a membrane
molecule, indistinguishable from the platelet VLA-2 complex, which is a
collagen receptor and a member of the integrin family. To identify this
endothelial molecule, we have used a monoclonal antibody, CLB-10G11, which
recognizes the VLA-2 complex from platelets. The molecule recognized by
CLB-10G11 from endothelial cells was characterized as follows. (1) The
monoclonal antibody precipitated two proteins from surface-labeled
endothelial cells that corresponded to the platelet VLA-2 subunits
(glycoprotein Ia and IIa) as judged by one-dimensional sodium dodecyl
sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional
nonreduced/reduced SDS- PAGE. (2) Preclearing of endothelial cells with
monoclonal antibody A- 1A5, an antibody that is directed against the common
VLA beta subunit, removed all the CLB-10G11-binding material. (3) Crossed
immunoelectrophoresis revealed that CLB-10G11 recognizes a single
precipitation arc from either platelets or endothelial cells. Analysis of
these two cell types in one gel again revealed one precipitation arc. The
antigen of either cell type, recognized by CLB-10G11 could be precipitated
by either polyclonal antiplatelet or polyclonal antiendothelial cell
antiserum. Hence, it appears that endothelial cells express at least three
different surface molecules (the vitronectin receptor, the fibronectin
receptor and a collagen receptor), which may play an important role in
controlling the anchorage of endothelial cells to the extracellular matrix.
Volume 73,
Issue 5,
pp. 1235-1241,
04/01/1989
Copyright © 1989 by The American Society of Hematology
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