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首页> 外文期刊>Cellular Signalling >FSH-induced p38-MAPK-mediated dephosphorylation at serine 727 of the signal transducer and activator of transcription 1 decreases Cyp1b1 expression in mouse granulosa cells
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FSH-induced p38-MAPK-mediated dephosphorylation at serine 727 of the signal transducer and activator of transcription 1 decreases Cyp1b1 expression in mouse granulosa cells

机译：FSH诱导的p38-MAPK介导的信号转导和转录激活因子1的丝氨酸727的去磷酸化降低了小鼠颗粒细胞中Cyp1b1的表达

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Most mammalian follicles undergo atresia at various stages before ovulation, and granulosa cell apoptosis is a major cause of antral follicular atresia. Estradiol is an essential mitogen for granulosa cell proliferation in vivo and inhibition of apoptosis. The estradiol-producing capacity and metabolism levels are important for follicle health, and sufficient estradiol is necessary for follicle development and ovulation. Cyp1b1, a member of the cytochrome P450 1 subfamily, is responsible for the metabolism of a wide variety of halogenated and polycyclic aromatic hydrocarbons in diverse tissues. In mouse follicles, Cyp1b1 converts estradiol to 4-hydroxyestradiol. We investigated mouse granulosa cells (MGCs) in vivo and in vitro and found that Cyp1b1 played a crucial role in estradiol metabolism in dominant follicles. Follicle-stimulating hormone (FSH) decreased estrogen metabolism by reducing Cyp1b1 mRNA and protein levels in MGCs. Furthermore, FSH regulated signal transducer and activator of transcription 1 (STAT1), a significant transcription factor of Cyp1b1, by mediating the dephosphorylation of STAT1 on serine 727 (Ser(727)) in MGCs. p38 mitogen-activated protein kinase (MAPK) may be involved in the FSH-induced dephosphorylation of STAT1 on Ser(727) in MGCs. These results suggested that FSH functions via p38 MAPK-induced dephosphorylation at Ser(727) of STAT1 to downregulate Cyp1b1 expression and maintain the estradiol levels in mouse dominant follicles. (C) 2014 Elsevier Inc. All rights reserved.
机译：大多数哺乳动物卵泡在排卵前的各个阶段都会发生闭锁，而颗粒细胞凋亡是导致窦性卵泡闭锁的主要原因。雌二醇是体内颗粒细胞增殖和凋亡抑制的必需促分裂原。雌二醇的产生能力和代谢水平对于卵泡的健康很重要，而充足的雌二醇对于卵泡的发育和排卵是必需的。 Cyp1b1是细胞色素P450 1亚家族的成员，负责在各种组织中代谢各种卤代和多环芳烃。在小鼠卵泡中，Cyp1b1将雌二醇转化为4-羟基雌二醇。我们在体内和体外研究了小鼠颗粒细胞（MGCs），发现Cyp1b1在占主导地位的卵泡中的雌二醇代谢中起着至关重要的作用。促卵泡激素（FSH）通过降低MGC中的Cyp1b1 mRNA和蛋白水平来降低雌激素代谢。此外，FSH通过介导MGC丝氨酸727（Ser（727））上STAT1的去磷酸化作用来调节信号转导和转录激活因子1（STAT1），Cyp1b1的重要转录因子。 p38丝裂原激活的蛋白激酶（MAPK）可能参与了MSH中FSH诱导的Ser（727）STAT1的去磷酸化。这些结果表明FSH通过p38 MAPK诱导STAT1的Ser（727）处的去磷酸化来下调Cyp1b1的表达并维持小鼠优势卵泡中的雌二醇水平。 （C）2014 Elsevier Inc.保留所有权利。

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