T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1

Nature. 1989 Oct 19;341(6243):619-24. doi: 10.1038/341619a0.

Abstract

Effective interaction between T cells and their targets requires that recognition of specific antigen be coordinated with increased cell-cell adhesion. We show that antigen-receptor cross-linking increases the strength of the adhesion mechanism between lymphocyte function-associated molecule-1 (LFA-1) and intercellular adhesion molecules (ICAMs), with intracellular signals transmitted from the T-cell antigen receptor to the LFA-1 adhesion molecule. The increase in avidity is rapid and transient, providing a dynamic mechanism for antigen-specific regulation of lymphocyte adhesion and de-adhesion.

Publication types

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

MeSH terms

  • 1-Methyl-3-isobutylxanthine / pharmacology
  • Alkaloids / pharmacology
  • Antigens, Differentiation / physiology*
  • Bucladesine / pharmacology
  • Cell Adhesion Molecules / physiology*
  • Cell Adhesion*
  • Colforsin / pharmacology
  • Humans
  • In Vitro Techniques
  • Lymphocyte Activation
  • Lymphocyte Function-Associated Antigen-1
  • Micelles
  • Phorbol Esters / pharmacology
  • Receptors, Antigen, T-Cell / physiology*
  • Receptors, Leukocyte-Adhesion / physiology*
  • Staurosporine
  • T-Lymphocytes / physiology*
  • Temperature

Substances

  • Alkaloids
  • Antigens, Differentiation
  • Cell Adhesion Molecules
  • Lymphocyte Function-Associated Antigen-1
  • Micelles
  • Phorbol Esters
  • Receptors, Antigen, T-Cell
  • Receptors, Leukocyte-Adhesion
  • Colforsin
  • Bucladesine
  • Staurosporine
  • 1-Methyl-3-isobutylxanthine