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Related Experiment Videos

Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated T cells

B A Lollo1, K W Chan, E M Hanson

  • 1Department of Chemistry, University of California at San Diego, La Jolla 92093-0063.

The Journal of Biological Chemistry
|October 15, 1993
PubMed
Summary

Activated T cells show avid adhesion to ICAM-1 via LFA-1. This study reveals that T cell activation converts a fraction of LFA-1 molecules to a high-affinity state, explaining enhanced binding.

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Lymphocytes exhibit avid adhesion to ICAM-1 through LFA-1 upon activation.
  • The mechanisms driving this enhanced adhesion, whether increased binding affinity or post-receptor events, remain unclear.

Purpose of the Study:

  • To quantify the binding affinity of LFA-1 to ICAM-1 on unstimulated and stimulated T cells.
  • To elucidate the contribution of LFA-1 affinity modulation to lymphocyte adhesion.

Main Methods:

  • Utilized a recombinant soluble ICAM-1 to measure binding affinity to LFA-1 on T cells.
  • Employed competition assays with radiolabeled antibody Fab to determine binding equilibrium and kinetics.
  • Analyzed binding affinity on unstimulated and phorbol ester-stimulated T cells.

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Main Results:

  • The binding affinity of LFA-1 to ICAM-1 on unstimulated T cells is very low (approximately 100 microM).
  • T cell activation by phorbol esters resulted in a modest increase in average binding affinity.
  • Further analysis indicated that a subpopulation of LFA-1 molecules shifted to a state with 200-fold higher affinity.

Conclusions:

  • T cell activation significantly enhances LFA-1 binding affinity to ICAM-1.
  • This affinity modulation, driven by a fraction of LFA-1 molecules entering a high-affinity state, underlies the avid adhesion of stimulated lymphocytes.