Activation-independent binding of human memory T cells to adhesion molecule ELAM-1

Nature. 1991 Feb 28;349(6312):799-802. doi: 10.1038/349799a0.


The induction of an ensemble of adhesion molecules on endothelial cells by inflammatory cytokines is likely to be crucial to the differential migration of T-lymphocyte subsets into inflammatory sites. Two molecular pathways involving the VLA-4 and LFA-1 integrins are known to mediate T-cell adhesion to activated endothelium. Here we show that a third pathway involving the rapidly inducible endothelial cell-surface adhesion molecule ELAM-1 contributes to the binding of resting CD4+ T cells to IL-1-induced human endothelial cells. All three pathways contribute to the greater adhesion to endothelium of memory T cells than naive T cells. There are two unique features of T-cell adhesion to purified ELAM-1: first, ELAM-1 exclusively mediates adhesion of memory T cells; second, memory T-cell binding to ELAM-1 is independent of acute activation events that regulate integrin-mediated adhesion. Thus, ELAM-1 may be of primary importance in the initial attachment of memory T cells to inflamed endothelium in vivo and to the preferential migration of memory T cells into tissue and inflammatory sites.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • CD4 Antigens / immunology
  • Cell Adhesion Molecules / immunology*
  • Cell Adhesion Molecules / isolation & purification
  • Cell Adhesion*
  • E-Selectin
  • Fibronectins / physiology
  • Humans
  • Immunologic Memory*
  • In Vitro Techniques
  • Lymphocyte Activation
  • T-Lymphocytes / immunology*


  • CD4 Antigens
  • Cell Adhesion Molecules
  • E-Selectin
  • Fibronectins