R. Li et al., A PEPTIDE FROM ICAM-2 BINDS TO THE LEUKOCYTE INTEGRIN CD11A CD18 AND INHIBITS ENDOTHELIAL-CELL ADHESION/, The Journal of biological chemistry, 268(23), 1993, pp. 17513-17518
Numerous leukocyte functions depend on adhesive intercellular interact
ions. The leukocyte-specific integrins CD11a/CD18 (lymphocyte function
-associated antigen-1 (LFA-1)) and CD11b/CD18 (complement type 3 recep
tor (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 b
inding in molecular detail. We have now defined a peptide region from
the first immunoglobulin domain of ICAM-2 that is specifically involve
d in binding to CD11a/CD18. A synthetic peptide from this part of ICAM
-2, covering residues 21-42, bound to purified CD11a/CD18 and inhibite
d the adhesion of endothelial cells to this integrin. It also inhibite
d the binding of B lymphoblastoid cells to endothelial cells. Leukocyt
es bound to the peptide coated on plastic. Several shorter peptides fr
om the same region showed less or no activity.