Li R, Nortamo P, Valmu L, Tolvanen M, Huuskonen J, Kantor C, Gahmberg C G
Department of Biochemistry, University of Helsinki, Finland.
J Biol Chem. 1993 Aug 15;268(23):17513-8.
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.
众多白细胞功能依赖于细胞间的黏附相互作用。白细胞特异性整合素CD11a/CD18（淋巴细胞功能相关抗原-1（LFA-1））和CD11b/CD18（补体3型受体（Mac-1））可与细胞间黏附分子ICAM-1和ICAM-2结合，在黏附中起关键作用。目前对其分子层面的结合情况了解甚少。我们现已确定ICAM-2第一个免疫球蛋白结构域中有一个肽段区域，该区域特别参与与CD11a/CD18的结合。ICAM-2这一部分的一个合成肽，覆盖第21至42位残基，可与纯化的CD11a/CD18结合，并抑制内皮细胞与该整合素的黏附。它还抑制B淋巴母细胞与内皮细胞的结合。白细胞可与包被在塑料上的该肽结合。来自同一区域的几个较短肽段活性较低或无活性。
