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Related Experiment Videos

Adhesion-promoting receptors on phagocytes.

S D Wright1, P A Detmers

  • 1Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York, NY 10021.

Journal of Cell Science. Supplement
|January 1, 1988
PubMed
Summary

Leukocyte adhesion receptors like LFA-1 and CR3, part of the integrin family, are regulated by clustering. This clustering enables their binding to various surfaces, crucial for immune cell function.

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Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Phagocytes utilize LFA-1, CR3, and p150,95 receptors for leukocyte adhesion.
  • These receptors mediate binding to diverse targets, including iC3b-coated surfaces, endothelial cells, and bacterial lipopolysaccharide.

Purpose of the Study:

  • To review the structure and function of LFA-1, CR3, and p150,95 receptors.
  • To present evidence linking these receptors to the integrin superfamily.
  • To emphasize the modulation of adhesion capacity by stimuli and its structural basis.

Main Methods:

  • Literature review focusing on receptor structure, function, and regulation.
  • Analysis of evidence for integrin superfamily classification.
  • Examination of studies on stimulus-dependent modulation of receptor binding activity.

Main Results:

  • LFA-1, CR3, and p150,95 are structurally related adhesion receptors belonging to the integrin family.
  • Adhesion capacity is reversibly modulated by soluble and surface-bound stimuli.
  • Receptor binding activity is regulated by changes in their 2D distribution within the cell membrane.

Conclusions:

  • Inactive integrin receptors are randomly distributed.
  • Ligand-independent movement into clusters enables binding to ligand-coated surfaces.
  • Membrane distribution changes are key to regulating integrin-mediated adhesion.

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