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首页> 外文期刊>Molecular and Cellular Biology >Phosphatidylinositol 3-kinase activity is important for progesterone-induced Xenopus oocyte maturation.
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Phosphatidylinositol 3-kinase activity is important for progesterone-induced Xenopus oocyte maturation.

机译：磷脂酰肌醇3-激酶活性对于孕激素诱导的爪蟾卵母细胞成熟很重要。

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摘要

In somatic cells, phosphatidylinositol 3-kinase (PI3 kinase) is a critical intermediary in growth factor-induced mitogenesis. We have examined the role of this enzyme in meiotic maturation of Xenopus laevis oocytes. PI3 kinase activity was present in immunoprecipitates of the p85 subunit of PI3 kinase from immature oocytes and markedly increased following progesterone stimulation. Injection of bacterially expressed protein corresponding to the C-terminal SH2 domain of p85 (SH2-C) inhibited progesterone-induced PI3 kinase activation and meiotic maturation. Injection of protein corresponding to the N-terminal SH2 domain or the SH3 domain of p85 did not inhibit PI3 kinase activation or maturation. SH2-C did not inhibit oocyte maturation induced by c-mos RNA injection. In addition, radiolabelled SH2-C was used to probe oocyte lysates, revealing that a novel 200-kDa protein bound to SH2-C. This protein may be an important mediator of progesterone-induced lipid metabolism in oocytes.
机译：在体细胞中，磷脂酰肌醇3-激酶（PI3激酶）是生长因子诱导的有丝分裂的关键中介。我们已经检查了该酶在非洲爪蟾卵母细胞减数分裂成熟中的作用。 PI3激酶活性存在于来自未成熟卵母细胞的PI3激酶p85亚基的免疫沉淀物中，并在孕激素刺激后显着增加。注射对应于p85 C-末端SH2结构域的细菌表达蛋白（SH2-C）可抑制孕激素诱导的PI3激酶激活和减数分裂成熟。注射对应于p85 N末端SH2结构域或SH3结构域的蛋白质不会抑制PI3激酶的激活或成熟。 SH2-C不抑制c-mos RNA注射诱导的卵母细胞成熟。此外，放射性标记的SH2-C被用于探测卵母细胞裂解物，揭示了一种新型的200 kDa蛋白与SH2-C结合。该蛋白可能是卵母细胞中孕酮诱导的脂质代谢的重要介质。

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