A Peptide Derived from the Intercellular Adhesion Molecule-2 Regulates the Avidity of the Leukocyte Integrins CD11b/CD18 and CDllc/CD18

~2 integrin (CDlla,b,c/CD18)-mediated cell adhesion is required for many leukocyte functions. Under normal circumstances, the integrins are nonadhesive, and become adhesive for their cell surface ligands, the intercellular adhesion molecules (ICAMs), or soluble ligands such as fibrinogen and iC3b, when leukocytes are activated. Recently, we defined a peptide derived from ICAM-2, which specifically binds to purified CDlla/CD18. Furthermore, this peptide strongly induces T cell aggregation mainly mediated by CDlla/CD18-ICAM-1 interaction, and natural killer cell cytotoxicity. In the present study, we show that the same ICAM-2 peptide also avidly binds to purified CDllb/CD18, but not to CDllc/CD18. This binding can be blocked by the CD1 lb antibody OKM10. The peptide strongly stimulates CDllb/CD18-ICAM-l-mediated cell aggregations of the monocytic cell lines THP-1 and U937. The aggregations are energy and divalent cation-dependent. The ICAM-2 peptide also induces CDllb/CD18 and CDllc/CD18-mediated binding of THP-1 cells to fibrinogen and iC3b coated on plastic. These findings indicate that in addition to induction of CDlla/CD18mediated cell adhesion, the ICAM-2 peptide may also serve as a "trigger" for high avidity ligand binding of