A leukocyte integrin binding peptide from intercellular adhesion molecule-2 stimulates T cell adhesion and natural killer cell activity

• Published in: The Journal of biological chemistry 1993-10, Vol.268 (29), p.21474-21477
• Main Authors: RUI LI, NORTAMO, P, KANTOR, C, KOVANEN, P, TIMONEN, T, GAHMBERG, C. G
• Format: Article
• Language: English
• Subjects: Alkaloids - pharmacology; Amino Acid Sequence; Analysis of the immune response. Humoral and cellular immunity; Antigens, CD - metabolism; Biological and medical sciences; CD18 Antigens; Cell Adhesion - drug effects; Cell Adhesion Molecules - metabolism; Cell interactions; Cytotoxicity, Immunologic; Ethers, Cyclic - pharmacology; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Humans; Immunobiology; Integrins - metabolism; Killer Cells, Natural - immunology; Lymphocyte Function-Associated Antigen-1 - metabolism; Molecular Sequence Data; Okadaic Acid; Peptide Fragments - metabolism; Protein Binding; Protein Kinase C - antagonists & inhibitors; Receptors, Leukocyte-Adhesion - metabolism; Staurosporine; T-Lymphocytes - cytology; T-Lymphocytes - immunology; Tumor Cells, Cultured
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(20)80561-4

Adhesion is of pivotal importance for a number of leukocyte functions. Little is known about the binding between leukocyte integrins and the intercellular adhesion molecules (ICAMs). Normally integrins are nonadhesive, and require a stimulus to become active. We have now identified a peptide from ICAM-2, which binds to leukocyte integrins and activates adhesion. Furthermore, the peptide strongly increased the binding and cytotoxicity of natural killer cells. These findings show that adhesion-dependent leukocyte functions can be activated by ligand-derived peptides, and therefore provide evidence that the avidity of leukocyte integrins is up-regulated by integrin-ligand interactions.