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J. Cell Biol.,
Volume 145, Number 2, April 19, 1999 413-420
9
1 Mediates Adhesion to Activated Endothelial Cells and
Transendothelial Neutrophil Migration through Interaction with Vascular
Cell Adhesion Molecule-1
* Lung Biology Center, Center for Occupational and Environmental Health, Cardiovascular Research Institute and the
Department of Medicine, University of California, San Francisco, California 94143; and The integrin Elan Pharmaceuticals, South San
Francisco, California 94080
9
1 has been shown to be
widely expressed on smooth muscle and epithelial cells,
and to mediate adhesion to the extracellular matrix
proteins osteopontin and tenascin-C. We have found
that the peptide sequence this integrin recognizes in
tenascin-C is highly homologous to the sequence recognized by the closely related integrin 41, in the inducible endothelial ligand, vascular cell adhesion mole-cule-1 (VCAM-1). We therefore sought to determine
whether 91 also recognizes VCAM-1, and whether any such interaction would be biologically significant.
In this report, we demonstrate that 91 mediates stable cell adhesion to recombinant VCAM-1 and to
VCAM-1 induced on human umbilical vein endothelial
cells by tumor necrosis factor-. Furthermore, we show
that 91 is highly and selectively expressed on neutrophils and is critical for neutrophil migration on VCAM-1
and tenascin-C. Finally, 91 and 4 integrins contribute to neutrophil chemotaxis across activated endothelial monolayers. These observations suggest a possible
role for 91/VCAM-1 interactions in extravasation of
neutrophils at sites of acute inflammation.
91;
4;
neutrophil migration;
vascular cell adhesion molecule-1
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