人红细胞ICAM-4配体的整合素受体特异性。α iibeta3结合的关键残基。

Patricia Hermand, Pierre Gane, Isabelle Callebaut, Nelly Kieffer, Jean-Pierre Cartron, Pascal Bailly
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引用次数: 37

摘要

红细胞细胞间粘附分子-4 (ICAM-4)与整合素受体家族的不同成员结合。为了更好地确定ICAM-4整合素受体的特异性,使用单独表达各种整合素的细胞转染物来证明alphaLbeta2、alphabeta2和alphaIIbbeta3(活化)特异性地和剂量依赖性地结合重组ICAM-4- fc蛋白。我们还发现细胞表面ICAM-4与细胞表面alphaVbeta3整合素相互作用。此外,利用转染的alpha4beta1细胞和缺乏bet2整合素的LAD细胞,我们发现ICAM-4无法与alpha4beta1相互作用,即使在alpha4beta1被phorbol酯或单克隆抗体TS2/16 (+ Mn2+)激活后。通过结构域缺失分析、定点诱变和合成肽抑制,确定了对alphaIIbbeta3和alphaVbeta3相互作用至关重要的ICAM-4氨基酸。我们的结果提供了证据,证明β a3整合素结合位点包含ICAM-4的第一和第二ig样结构域。然而,alphaIIbbeta3接触位点包括D1结构域的ABED面,并在D2结构域的C'-E环中有一个延伸,而alphaVbeta3接触位点包括D1的两个面和D2的C'-E环中的残基。这些数据与我们之前的结果一起表明,不同的整合素结合到ICAM-4上不同但部分重叠的位点,并且ICAM-4可能容纳存在于白细胞、血小板和内皮细胞上的多种整合素受体。
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Integrin receptor specificity for human red cell ICAM-4 ligand. Critical residues for alphaIIbeta3 binding.

The red cell intercellular adhesion molecule-4 (ICAM-4) binds to different members of the integrin receptor families. To better define the ICAM-4 integrin receptor specificity, cell transfectants individually expressing various integrins were used to demonstrate that alphaLbeta2, alphaMbeta2, and alphaIIbbeta3 (activated) bind specifically and dose dependently to the recombinant ICAM-4-Fc protein. We also show that cell surface ICAM-4 interacts with the cell surface alphaVbeta3 integrin. In addition, using a alpha4beta1 cell transfectant and beta2 integrin-deficient LAD cells, we show here that ICAM-4 failed to interact with alpha4beta1 even after alpha4beta1 activation by phorbol ester or with the monoclonal antibody TS2/16 (+ Mn2+). ICAM-4 amino acids that are critical for alphaIIbbeta3 and alphaVbeta3 interaction were identified by domain deletion analysis, site-directed mutagenesis and synthetic peptide inhibition. Our results provide evidence that the beta3 integrin binding sites encompass the first and second Ig-like domains of ICAM-4. However, while the alphaIIbbeta3 contact site comprises the ABED face of domain D1 with an extension in the C'-E loop of domain D2, the alphaVbeta3 contact site comprises residues on both faces of D1 and in the C'-E loop of D2. These data, together with our previous results, demonstrate that different integrins bind to different but partly overlapping sites on ICAM-4, and that ICAM-4 may accommodate multiple integrin receptors present on leukocytes, platelets and endothelial cells.

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