Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
Role of Rho in chemoattractant-activated leukocyte adhesion through integrins
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DOI：
10.1126/science.271.5251.981
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发表时间：
1996-02-16
期刊：
影响因子：
56.9
通讯作者：
Butcher, EC
中科院分区：
文献类型：
--
作者：
Laudanna, C;Campbell, JJ;Butcher, EC
化学引诱物亚家族的异源三聚体鸟嘌呤核苷酸结合蛋白（G蛋白）连接的受体可以通过白细胞整联蛋白触发粘附，并且在此作用中，它们被认为调节免疫细胞-细胞相互作用和运输。在用甲酰肽或白细胞介素-8受体转染的淋巴细胞中，激动剂刺激在几秒钟内激活了小的三磷酸鸟苷结合蛋白RhoA上的核苷酸交换。通过C3转移酶外切酶灭活Rho阻断激动剂诱导的淋巴细胞α 4 β 1与血管细胞粘附分子1的粘附和中性粒细胞β 2整合素与纤维蛋白原的粘附。这些发现表明，Rho参与从趋化因子受体的信号传导，以触发白细胞中的快速粘附。
Heterotrimeric guanine nucleotide binding protein (G protein)-linked receptors of the chemoattractant subfamily can trigger adhesion through leukocyte integrins, and in this role they are thought to regulate immune cell-cell interactions and trafficking. In lymphoid cells transfected with formyl peptide or interleukin-8 receptors, agonist stimulation activated nucleotide exchange on the small guanosine triphosphate-binding protein RhoA in seconds. Inactivation of Rho by C3 transferase exoenzyme blocked agonist-induced lymphocyte alpha 4 beta 1 adhesion to vascular cell adhesion molecule-1 and neutrophil beta 2 integrin adhesion to fibrinogen. These findings suggest that Rho participates in signaling from chemoattractant receptors to trigger rapid adhesion in leukocytes.