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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Activation of natural killer cell migration by leukocyte integrin-binding peptide from intracellular adhesion

K Somersalo1, O Carpén, E Saksela

  • 1Department of Pathology, University of Helsinki, Finland.

The Journal of Biological Chemistry
|April 14, 1995
PubMed

Insights

A peptide from Intracellular Adhesion Molecule-2 (ICAM-2) significantly boosts natural killer (NK) cell migration by interacting with CD11a/CD18 receptors. This ICAM-2 peptide triggers distinct signaling pathways influencing NK cell locomotion and cytotoxicity.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Intracellular Adhesion Molecule-2 (ICAM-2) is expressed on endothelial and hematopoietic cells, but its function is largely unknown.
  • Previous studies indicated an ICAM-2 peptide enhances NK cell cytotoxicity and T cell aggregation.
  • The specific role of ICAM-2 in leukocyte migration requires further elucidation.

Purpose of the Study:

  • To investigate the effect of an ICAM-2 peptide (residues 21-42) on natural killer (NK) cell migration.
  • To explore the signaling pathways involved in ICAM-2 mediated NK cell activation.
  • To compare the effects of ICAM-2 peptide ligation versus antibody-mediated CD11a/CD18 receptor cross-linking.

Main Methods:

  • Boyden chamber assay to measure NK cell migration.
  • Treatment with ICAM-2 peptide and anti-CD11a monoclonal antibodies.
  • F-actin polymerization analysis.
  • Western blotting for phosphotyrosine.
  • Analysis of CD11a/CD18 receptor recycling and NK cell cytotoxicity.

Main Results:

  • The ICAM-2 peptide significantly increased NK cell migration by over 215%, an effect inhibited by anti-CD11a antibodies.
  • The peptide induced F-actin polymerization at the leading edge of migratory NK cells.
  • Antibody-mediated cross-linking of CD11a/CD18 receptors increased migration and actin polymerization but slightly inhibited cytotoxicity, unlike the peptide.
  • The ICAM-2 peptide specifically increased phosphorylation of 150- and 35-kDa proteins, while antibody cross-linking primarily affected the 150-kDa protein.

Conclusions:

  • Ligation of CD11a/CD18 receptors by the ICAM-2 peptide triggers distinct intracellular signals compared to antibody cross-linking.
  • These signals differentially regulate NK cell locomotion and cytotoxicity.
  • ICAM-2 on endothelium likely plays a key role in initiating leukocyte migration.

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