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The VLA-2 (alpha 2 beta 1) I domain functions as a ligand-specific
recognition sequence for endothelial cell attachment and spreading:
molecular and functional characterization
WF Bahou, CL Potter and H Mirza
Department of Medicine, State University of New York at Stony Brook
11794-8151.
The integrin VLA-2 (alpha 2 beta 1), generally considered to represent the
specific collagen receptor on human endothelial cells, contains an alpha
2-subunit inserted I domain with structural similarity to the type A
domains found within the recently described superfamily of receptor-ligand
recognition proteins. This region of the cDNA has now been isolated and
used for molecular and functional characterization of this heterodimeric
receptor complex. Comparative sequence analysis with the porcine homologue
revealed 93% amino acid sequence identity, suggestive of a developmentally
conserved function. To complete structure/function studies, this region of
the human cDNA was expressed as a chimeric protein in Escherichia coli, and
a rabbit polyclonal antibody (anti-I domain) was used to study determinants
of endothelial cell attachment and spreading in vitro. Quantifiable and
visual disruption of endothelial cell attachment to gelatin, type I
collagen, and laminin was evident using the specific anti-I domain
antibody, with minimal inhibitory effects demonstrable using fibronectin or
fibrinogen matrices. Therefore, these data would suggest that the alpha 2
beta 1 I domain confers ligand-binding specificity for both known alpha 2
beta 1 substrates (laminin and collagen), and that this region subserves a
regulatory function in the molecular processes controlling endothelial cell
attachment and spreading in vitro.
Volume 84,
Issue 11,
pp. 3734-3741,
12/01/1994
Copyright © 1994 by The American Society of Hematology
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