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Intracellular adhesion molecule-2 (ICAM-2), one of the ligands
of CD11a/CD18 (LFA-1), is mainly expressed on endothelial and
hematopoietic cells. The biological significance of ICAM-2 has remained
unclear. Previous findings have shown that a peptide from ICAM-2,
spanning residues 21-42 from the first immunoglobulin domain,
enhances natural killer (NK) cell cytotoxicity and induces T cell
aggregation. We have now studied the effect of the same ICAM-2 peptide
on NK cell migration in the Boyden chamber assay. The peptide
significantly increased NK cell migration up to 215 ± 21%, as
compared to migration of control cells (100%), and the induction was
inhibited by anti-CD11a monoclonal antibodies. The ICAM-2 peptide also
induced polymerization of F-actin at the leading edge of migratory NK
cells. Cross-linking of CD11a/CD18 receptors with anti-CD11a or
anti-CD18 monoclonal antibodies and secondary antibodies resulted in
receptor recycling, increased migration, and actin polymerization, but
led to slight inhibition of cytotoxicity. The ICAM-2 peptide did not
induce such a receptor recycling. Phosphotyrosine immunoblotting
experiments showed that the ICAM-2 peptide increased the
phosphorylation of 150- and 35-kDa proteins. During cross-linking with
antibodies, only the 150-kDa protein showed increased phosphorylation.
The results show that depending on the type of CD11a/CD18 receptor
ligation different kinds of signals are transduced in NK cells. These
signals may either trigger only locomotion, or both locomotion and
cytotoxicity. Based on these findings, a major function for ICAM-2 on
endothelium may be triggering of migration of adhering leukocytes.
Volume 270,
Number 15,
Issue of April 14, pp. 8629-8636, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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