FUNCTIONAL CLONING OF ICAM-2, A CELL-ADHESION LIGAND FOR LFA-1 HOMOLOGOUS TO ICAM-1
FUNCTIONAL CLONING OF ICAM-2, A CELL-ADHESION LIGAND FOR LFA-1 HOMOLOGOUS TO ICAM-1
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DOI：
10.1038/339061a0
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发表时间：
1989-05-04
期刊：
影响因子：
64.8
通讯作者：
SPRINGER, TA
中科院分区：
文献类型：
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作者：
STAUNTON, DE;DUSTIN, ML;SPRINGER, TA
白细胞粘附分子LFA-1介导广泛的淋巴细胞、单核细胞、自然杀伤细胞和粒细胞与免疫和炎症中的其他细胞的相互作用1，2。LFA-1（CD 11 a/CD 18）是细胞间粘附分子1（ICAM-1，CD 54）的受体，细胞间粘附分子1是一种表面分子，在炎症中在一些组织上组成型表达并在其他组织上诱导3 -5。上皮细胞、内皮细胞和成纤维细胞上ICAM-1的诱导介导淋巴细胞的LFA-1依赖性粘附4，6，7。几条证据表明存在第二种LFA-1配体：一种细胞系的同型粘附被LFA-1的单克隆抗体抑制，但不被ICAM-18的单克隆抗体抑制;存在LFA-1依赖的、ICAM-1非依赖的粘附内皮细胞的途径6;而且，存在某些类型的靶细胞，其中LFA-1依赖性T淋巴细胞粘附和溶解不依赖于ICAM-19。我们已经克隆了这第二个配体，命名为ICAM-2，使用一种新的方法来识别粘附分子的配体。ICAM-2是具有两个免疫球蛋白样结构域的完整膜蛋白，而ICAM-1具有五个免疫球蛋白样结构域10，11。值得注意的是，与ICAM-1或ICAM-2与免疫球蛋白超家族的其他成员相比，ICAM-2与ICAM-1的两个最N-末端结构域的关系更密切（34%同一性），这表明存在结合相同整联蛋白受体的免疫球蛋白样配体亚家族。
THE leukocyte adhesion molecule LFA-1 mediates a wide range of lymphocyte, monocyte, natural killer cell, and granulocyte interactions with other cells in immunity and inflammation1,2. LFA-1 (CD 1 la/CD 18) is a receptor for intercellular adhesion molecule 1 (ICAM-1, CD54), a surface molecule which is constitu-tively expressed on some tissues and induced on others in inflammation3–5. Induction of ICAM-1 on epithelial cells, endothelial cells and fibroblasts mediates LFA-1-dependent adhesion of lymphocytes4,6,7. Several lines of evidence have suggested the existence of a second LFA-1 ligand: homotypic adhesion of one cell line was inhibited by a monoclonal antibody to LFA-1, but not by one to ICAM-18; there exists an LFA-1-dependent, ICAM-1-indepen-dent pathway of adhesion to endothelial cells6; and also, there are some types of target cells in which LFA-1-dependent T-lymphocyte adhesion and lysis are independent of ICAM-19. We have cloned this second ligand, designated ICAM-2, using a novel method for identifying ligands of adhesion molecules. ICAM-2 is an integral membrane protein with two immunoglobulin-like domains, whereas ICAM-1 has five10,11. Remarkably, ICAM-2 is much more closely related to the two most N-terminal domains of ICAM-1 (34% identity) than either ICAM-1 or ICAM-2 is to other members of the immunoglobulin superfamily, demonstrating the existence of a subfamily of immunoglobulin-like ligands that bind the same integrin receptor.