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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A peptide from ICAM-2 binds to the leukocyte integrin CD11a/ CD18 and inhibits endothelial cell adhesion.

Numerous leukocyte functions depend on adhesive intercellular interactions. The leukocyte-specific integrins CD11a/ CD18 (lymphocyte function-associated antigen-1 (LFA-1)) and CD11b/ CD18 (complement type 3 receptor (Mac-1)), which bind to the intercellular adhesion molecules ICAM-1 and ICAM-2, play a key role in adhesion. Little is known about the binding in molecular detail. We have now defined a peptide region from the first immunoglobulin domain of ICAM-2 that is specifically involved in binding to CD11a/ CD18. A synthetic peptide from this part of ICAM-2, covering residues 21-42, bound to purified CD11a/ CD18 and inhibited the adhesion of endothelial cells to this integrin. It also inhibited the binding of B lymphoblastoid cells to endothelial cells. Leukocytes bound to the peptide coated on plastic. Several shorter peptides from the same region showed less or no activity.[1]

References

  1. A peptide from ICAM-2 binds to the leukocyte integrin CD11a/CD18 and inhibits endothelial cell adhesion. Li, R., Nortamo, P., Valmu, L., Tolvanen, M., Huuskonen, J., Kantor, C., Gahmberg, C.G. J. Biol. Chem. (1993) [Pubmed]
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