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The Journal of Immunology, Vol 155, Issue 7 3619-3628, Copyright © 1995 by American Association of Immunologists
ARTICLES |
J Xie, R Li, P Kotovuori, C Vermot-Desroches, J Wijdenes, MA Arnaout, P Nortamo and CG Gahmberg
Department of Biosciences, University of Helsinki, Finland.
The interactions between the leukocyte-specific beta 2-integrins cluster of differentiation (CD) Ag CD11/CD18 and their ligands, the intercellular adhesion molecules (ICAMs), play important roles in many adhesion-dependent leukocyte functions. ICAM-1 is known to be a ligand for both CD11a/CD18 and CD11b/CD18. ICAM-2, whose two extracellular Ig domains show the highest homology to the two NH2-terminal domains of ICAM-1, has been previously shown to be a ligand for CD11a/CD18. We recently found that a 22-amino acid CD11a/CD18-binding peptide, P1, derived from the first domain of ICAM-2, also binds to purified CD11b/CD18. In the present study, we demonstrate that the ICAM-2 protein interacts with CD11b/CD18, and the binding is through the CD11b A domain.
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