REGULATION OF ADHESION TO ICAM-1 BY THE CYTOPLASMIC DOMAIN OF LFA-1 INTEGRIN BETA-SUBUNIT
REGULATION OF ADHESION TO ICAM-1 BY THE CYTOPLASMIC DOMAIN OF LFA-1 INTEGRIN BETA-SUBUNIT
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DOI：
10.1126/science.1672776
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发表时间：
1991-03-29
期刊：
影响因子：
56.9
通讯作者：
SPRINGER, TA
中科院分区：
文献类型：
--
作者：
HIBBS, ML;XU, H;SPRINGER, TA
细胞毒性淋巴细胞与其靶点之间的相互作用需要T细胞抗原受体（TCR）和整合素淋巴细胞功能相关分子-1（LFA-1，CD 11 a/CD 18）。LFA-1不是组成性地对其反受体细胞间粘附分子（ICAM）-1和-2具有亲和力。TCR的交联将LFA-1瞬时转化为高亲合力状态，从而提供了以抗原特异性方式调节细胞粘附和去粘附的机制。截断LFA-1的β亚基而非α亚基的胞质结构域消除了与ICAM-1的结合和对佛波酯的敏感性。因此，发现LFA-1与ICAM-1的结合受LFA-1的β亚基的胞质结构域调节。
Interactions between cytotoxic lymphocytes and their targets require the T cell antigen receptor (TCR) and the integrin lymphocyte function-associated molecule-1 (LFA-1, CD11a/CD18). LFA-1 is not constitutively avid for its counterreceptors, intercellular adhesion molecules (ICAMs)-1 and -2. Cross-linking of the TCR transiently converts LFA-1 to a high avidity state and thus provides a mechanism for regulating cellular adhesion and de-adhesion in an antigen-specific manner. Truncation of the cytoplasmic domain of the beta, but not the alpha, subunit of LFA-1 eliminated binding to ICAM-1 and sensitivity to phorbol esters. Thus, LFA-1 binding to ICAM-1 was found to be regulated by the cytoplasmic domain of the beta-subunit of LFA-1.