调节活化正常T细胞表达和分泌的趋化因子可诱导人T细胞中稳定复合的粘着斑激酶p125和ζ链相关蛋白激酶70的酪氨酸激酶活性。
RANTES induces tyrosine kinase activity of stably complexed p125FAK and ZAP-70 in human T cells.
作者信息
Bacon K B, Szabo M C, Yssel H, Bolen J B, Schall T J
机构信息
DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, California 94304, USA.
出版信息
J Exp Med. 1996 Sep 1;184(3):873-82. doi: 10.1084/jem.184.3.873.
Abstract
The chemokine RANTES is a chemoattractant and activating factor for T lymphocytes. Investigation of the signal transduction mechanisms induced by RANTES in T cells revealed tyrosine phosphorylation of multiple protein species with prominent bands at 70-85 and 120-130 kD. Immunoprecipitation and Western analyses revealed that a protein of 125 kD was identical to the focal adhesion kinase (FAK) pp125FAK. RANTES stimulated phosphorylation of FAK as early as 30 seconds and immunoblots using antiphosphotyrosine monoclonal antibodies revealed that there was consistent phosphorylation of a 68-70 kD species in the pp125FAK immunoprecipitates. Immunoblotting and kinase assays showed this to be two separate proteins, the tyrosine kinase zeta-associated protein (ZAP) 70, and the focal adhesion protein paxillin. These results indicate a potentially important role for RANTES in the generation of T cell focal adhesions and subsequent cell activation via a molecular complex containing FAK, ZAP-70, and paxillin.
摘要
趋化因子RANTES是一种T淋巴细胞趋化剂和激活因子。对RANTES在T细胞中诱导的信号转导机制的研究揭示了多种蛋白质的酪氨酸磷酸化，在70 - 85kD和120 - 130kD处有明显条带。免疫沉淀和Western分析表明，125kD的一种蛋白质与粘着斑激酶（FAK）pp125FAK相同。RANTES最早在30秒时就刺激了FAK的磷酸化，使用抗磷酸酪氨酸单克隆抗体的免疫印迹显示，在pp125FAK免疫沉淀物中，一种68 - 70kD的蛋白质存在持续的磷酸化。免疫印迹和激酶分析表明这是两种不同的蛋白质，即酪氨酸激酶ζ相关蛋白（ZAP）70和粘着斑蛋白桩蛋白。这些结果表明，RANTES在通过包含FAK、ZAP - 70和桩蛋白的分子复合物产生T细胞粘着斑以及随后的细胞激活过程中可能发挥重要作用。
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