VCAM-1 on activated endothelium interacts with the leukocyte integrin VLA-4 at a site distinct from the VLA-4/Fibronectin binding site

Mariano J. Elices, Laurelee Osborn, Yoshikazu Takada, Carol Crouse, Stefan Luhowskyj, Martin E. Hemler, Roy R. Lobb

Research output: Contribution to journalArticle

1406 Scopus citations


Cytokine-activated human endothelial cells express vascular cell adhesion molecule-1 (VCAM-1), which binds lymphocytes. We now identify the integrin VLA-4 as a receptor for VCAM-1 because VLA-4 surface expression on K-562 cells (following transfection of the VLA α4 subunit cDNA) resulted in specific cell adhesion to VCAM-1, and anti VLM4 antibodies completely inhibited VCAM-1-dependent cell-cell attachment. In addition, VLA-4 expression allowed K562 cells to attach to the heparin 11 binding region (FN-40) of fibronectin. However, VLA-41VCAM-1 and VLA-4/FN-40 interactions are readily distinguishable: only the former was inhibited by the anti VLA-4 monoclonal antibody HP1/3, and only the latter was inhibited by soluble FN40. The VCAM-1/VLA-4 ligand-receptor pair may play a major role in the recruitment of mononuclear leukocytes to inflammatory sites in vivo.

Original languageEnglish (US)
Pages (from-to)577-584
Number of pages8
Issue number4
StatePublished - Feb 23 1990
Externally publishedYes


ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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