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首页> 外文期刊>Journal of Molecular Biology >Critical role of Mac-1 sialyl Lewis x moieties in regulating neutrophil degranulation and transmigration
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Critical role of Mac-1 sialyl Lewis x moieties in regulating neutrophil degranulation and transmigration

机译：Mac-1唾液酸化的Lewis x部分在调节中性粒细胞脱粒和转运中的关键作用

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摘要

Leukocyte cell surface sialyl Lewis x (sLe(x)) and related epitopes play an important role in cell rolling and adhesion during diapedesis via interaction with E-selectin. Here, we present evidence that Mac-1 (CD11b/CD18, CR-3) is a major neutrophil glycoprotein decorated with sLe(x) and ligation of these carbohydrate moieties by anti-sLe(x) antibody significantly impairs neutrophil functions. First, Western blot analysis shows that both CD11b and CD18 subunit of purified Mac-1 are decorated with sLe(x) moieties. A significant co-localization of CD11b and sLe(x) moieties is observed at neutrophil secondary granules. With stimulation of formyl-Met-Leu-Phe (fMLP), neutrophil surface labeling with anti-sLe(x) antibody follows an identical up-regulation pattern of Mac-1. Second, protein-binding assays indicate that sLe(x) moieties on Mac-1 are critical for binding interaction of Mac-1 to E-selectin. Removal of sLe(x) moieties completely abolishes Mac-1-E-selectin binding. Finally, ligation of Mac-1 sLe(x) by anti-sLe(x) antibody induces a significant degranulation of neutrophil secondary granules at the absence of chemoattractant stimulation. This "dysregulated" degranulation induced by anti-sLe(x) antibody strongly inhibits neutrophil transmigration in response to fMLP. In summary, Mac-1 sLe(x) moieties play a critical role in regulating 1 2 integrin functions during neutrophil transmigration and degranulation. (c) 2007 Elsevier Ltd. All rights reserved.
机译：白细胞表面唾液酸化的路易斯x（sLe（x））和相关的表位通过与E-选择素的相互作用，在血透过程中在细胞滚动和粘附中起着重要作用。在这里，我们提供的证据表明Mac-1（CD11b / CD18，CR-3）是装饰有sLe（x）的主要嗜中性粒细胞糖蛋白，而抗sLe（x）抗体与这些碳水化合物部分的连接显着削弱了嗜中性粒细胞的功能。首先，蛋白质印迹分析表明，纯化的Mac-1的CD11b和CD18亚基都被sLe（x）部分修饰。在嗜中性粒细胞次级颗粒中观察到CD11b和sLe（x）部分的显着共定位。随着甲酰-Met-Leu-Phe（fMLP）的刺激，用抗-sLe（x）抗体进行的中性粒细胞表面标记遵循与Mac-1相同的上调模式。其次，蛋白质结合测定表明Mac-1上的sLe（x）部分对于Mac-1与E-选择素的结合相互作用至关重要。 sLe（x）部分的删除完全废除了Mac-1-E-选择素结合。最后，在没有趋化因子刺激的情况下，抗sLe（x）抗体连接Mac-1 sLe（x）会引起嗜中性粒细胞次级颗粒的明显脱粒。抗-sLe（x）抗体诱导的这种“失调”脱颗粒强烈响应fMLP抑制嗜中性粒细胞的迁移。总之，Mac-1 sLe（x）部分在嗜中性粒细胞迁移和脱粒过程中在调节1 2整合素功能中起关键作用。 （c）2007 Elsevier Ltd.保留所有权利。

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