A PEPTIDE FROM ICAM-2 BINDS TO THE LEUKOCYTE INTEGRIN CD11A/CD18 AND INHIBITS ENDOTHELIAL-CELL ADHESION

被引：0
作者：
LI, R [1 ]
NORTAMO, P [1 ]
VALMU, L [1 ]
TOLVANEN, M [1 ]
HUUSKONEN, J [1 ]
KANTOR, C [1 ]
GAHMBERG, CG [1 ]
机构：
[1] UNIV HELSINKI, DEPT BIOCHEM, UNIONINKATU 35, SF-00170 HELSINKI 17, FINLAND
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 1993年 / 268卷 / 23期
关键词：
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页码：17513 / 17518
页数：6
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