JAM-1 is a ligand of the β2 integrin LFA-1 involved in transendothelial migration of leukocytes
JAM-1 is a ligand of the β2 integrin LFA-1 involved in transendothelial migration of leukocytes
复制标题
DOI：
10.1038/ni755
复制
发表时间：
2002-02-01
影响因子：
30.5
通讯作者：
Weber, C
中科院分区：
文献类型：
--
作者：
Ostermann, G;Weber, KSC;Weber, C
白细胞的炎性募集受整合素和内皮免疫球蛋白超家族（IgSF）蛋白之间的动态相互作用控制。我们已经确定IgSF成员连接粘附分子1（JAM-1）作为2整合素淋巴细胞功能相关抗原1（LFA-1）的配体。在静态和生理流动条件下，JAM-1有助于T细胞和中性粒细胞的LFA-1依赖性跨内皮迁移以及LFA-1介导的T细胞停滞。后者是由内皮细胞上的趋化因子触发的，内皮细胞上的趋化因子被细胞因子刺激以重新分配来自紧密连接的JAM-1。表达JAM-1的转染子支持LFA-1介导的白细胞粘附，这需要JAM-1的近膜Ig样结构域2。因此，JAM-1是LFA-1的反受体，其理想地位于白细胞募集期间引导和控制迁移。
Inflammatory recruitment of leukocytes is governed by dynamic interactions between integrins and endothelial immunoglobulin superfamily (IgSF) proteins. We have identified the IgSF member junctional adhesion molecule 1 (JAM-1) as a ligand of the 2 integrin lymphocyte function-associated antigen 1 (LFA-1). Under static and physiological flow conditions, JAM-1 contributed to LFA-1-dependent transendothelial migration of T cells and neutrophils as well as LFA-1-mediated arrest of T cells. The latter was triggered by chemokines on endothelium that was stimulated with cytokines to redistribute JAM-1 from the tight junctions. Transfectants expressing JAM-1 supported LFA-1-mediated adhesion of leukocytes, which required the membrane-proximal Ig-like domain 2 of JAM-1. Thus, JAM-1 is a counter-receptor for LFA-1 that is ideally situated to guide and control transmigration during leukocyte recruitment.