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Vascular cell adhesion molecule-1 mediates lymphocyte adherence to
cytokine-activated cultured human endothelial cells [published erratum
appears in Blood 1990 Dec 1;76(11):2420]
TM Carlos, BR Schwartz, NL Kovach, E Yee, M Rosa, L Osborn, G Chi-Rosso, B Newman, R Lobb and M] Rosso M$[corrected to Rosa
Department of Medicine, University of Washington, Seattle.
The expression and function of a new cytokine-induced endothelial cell
adhesion protein, vascular cell adhesion molecule-1 (VCAM-1), was
characterized in vitro by using a monoclonal antibody, MoAb 4B9, which
recognizes a functional epitope on this protein. As determined by
enzyme-linked immunosorbent assay and radioimmunoprecipitation of
metabolically labeled cells, VCAM-1 was minimally expressed on unstimulated
human umbilical vein endothelium (HUVE), but was rapidly induced by
recombinant human tumor necrosis factor-alpha (rhTNF-alpha), rh
interleukin-1, and lipopolysaccharide. In contrast to intercellular
adhesion molecule-1, VCAM-1 was not induced on dermal fibroblasts or
arterial smooth muscle cells after stimulation with rhTNF, or on
keratinocytes after stimulation with rh interferon-gamma. MoAb 4B9
significantly inhibited the adherence of peripheral blood lymphocytes (PBL)
and lymphocytic cell lines, but not neutrophils, to rhTNF- activated HUVE.
The inhibitory effect of MoAb 4B9 on PBL adherence to HUVE was additive to
that produced by the CD18 MoAb 60.3. These results show that VCAM-1
mediates a CD18-independent pathway of peripheral blood lymphocyte
adherence to cytokine-stimulated HUVE. We propose that lymphocyte binding
to VCAM-1, induced on endothelium by cytokines, may be an important
component of lymphocyte emigration at sites of inflammation or immune
reaction.
Volume 76,
Issue 5,
pp. 965-970,
09/01/1990
Copyright © 1990 by The American Society of Hematology
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