REGULATION OF HUMAN-LEUKOCYTE P21-ACTIVATED KINASES THROUGH G-PROTEIN-COUPLED RECEPTORS
REGULATION OF HUMAN-LEUKOCYTE P21-ACTIVATED KINASES THROUGH G-PROTEIN-COUPLED RECEPTORS
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DOI：
10.1126/science.7618083
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发表时间：
1995-07-14
期刊：
影响因子：
56.9
通讯作者：
BOKOCH, GM
中科院分区：
文献类型：
--
作者：
KNAUS, UG;MORRIS, S;BOKOCH, GM
Rac鸟苷5‘-三磷酸(GTP)结合蛋白调节吞噬细胞产生氧化剂。两个与Ste20相关的p21激活的蛋白激酶(PAK)被确定为人中性粒细胞中RAC的靶点。通过百日咳毒素敏感的异源三聚体GTP结合蛋白(G蛋白)作用于趋化剂，可迅速刺激类似于65和68千道尔顿PAK的活性。天然和重组PAKS磷酸以RAC-GTP依赖的方式磷酸化P47(Phox)还原的烟酰胺腺嘌呤二核苷酸磷酸(NADPH)氧化酶组分。PAKs通过G蛋白偶联途径激活吞噬细胞过程中的作用可能有助于调节NADPH氧化酶活性。
The Rac guanosine 5'-triphosphate (GTP)-binding proteins regulate oxidant production by phagocytic leukocytes. Two Ste20-related p21-activated kinases (PAKs) were identified as targets of Rac in human neutrophils. Activity of the similar to 65- and similar to 68-kilodalton PAKs was rapidly stimulated by chemoattractants acting through pertussis toxin-sensitive heterotrimeric GTP-binding proteins (G proteins). Native and recombinant PAKs phos phorylated the p47(phox) reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase component in a Rac-GTP-dependent manner. The action of PAKs during phagocyte activation by G protein-coupled pathways may contribute to regulation of NADPH oxidase activity.