Receptor-coupled activation of phosphoinositide-specific phospholipase C by an N protein.
Receptor-coupled activation of phosphoinositide-specific phospholipase C by an N protein.
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N 蛋白对磷酸肌醇特异性磷脂酶 C 的受体偶联激活。
DOI：
10.1126/science.3006254
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Snyderman,R
中科院分区：
文献类型：
--
作者：
Smith,CD;Cox,CC;Snyderman,R
磷脂酶C切割磷脂酰肌醇4，5-二磷酸导致产生两个重要的第二信使：肌醇-1，4，5-三磷酸和1，2-二酰基甘油。虽然有几种受体促进这种裂解，磷脂酶C激活的分子细节仍然没有得到解决。在这项研究中，发现人多形核白细胞质膜上的寡肽趋化因子受体（Ca 2+动员受体）的占据导致鸟苷5′-三磷酸激活鸟嘌呤核苷酸调节（N）蛋白。活化的N蛋白，然后刺激一个聚磷酸肌醇特异性磷脂酶C通过减少钙离子的要求，表达这种活性从超生理到正常的细胞内浓度。因此，N蛋白介导的磷脂酶C激活可能是化学引诱物和某些其他激素激活细胞途径中的关键步骤。
Cleavage of phosphatidylinositol 4,5-bisphosphate by phospholipase C results in the production of two important second messengers: inositol-1,4,5-trisphosphate and 1,2-diacylglycerol. Although several receptors promote this cleavage, the molecular details of phospholipase C activation have remained unresolved. In this study, occupancy of a Ca2+-mobilizing receptor, the oligopeptide chemoattractant receptor on human polymorphonuclear leukocyte plasma membranes, was found to lead to the activation of a guanine nucleotide regulatory (N) protein by guanosine 5′-triphosphate. The activated N protein then stimulated a polyphosphoinositide-specific phospholipase C by reducing the Ca2+requirement for expression of this activity from superphysiological to normal intracellular concentrations. Therefore, the N protein-mediated activation of phospholipase C may be a key step in the pathway of cellular activation by chemoattractants and certain other hormones.