Prostaglandin F2 alpha initiates polyphosphatidylinositol hydrolysis and membrane translocation of protein kinase C in swine ovarian cells.
Prostaglandin F2 alpha initiates polyphosphatidylinositol hydrolysis and membrane translocation of protein kinase C in swine ovarian cells.
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前列腺素 F2 α 启动猪卵巢细胞中的多磷脂酰肌醇水解和蛋白激酶 C 的膜易位。
DOI：
10.1016/0006-291x(87)91611-1
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发表时间：
1987
影响因子：
3.1
通讯作者：
Veldhuis,JD
中科院分区：
文献类型：
--
作者：
Veldhuis,JD
前列腺素F2α对卵巢细胞抑制作用的生化机制尚不清楚。由于蛋白激酶C途径在猪颗粒细胞中以抑制方式与类固醇生成偶联，因此我们验证了前列腺素F2α激活这种磷脂依赖性、钙刺激效应子途径的假设。使用单层培养的猪颗粒细胞，我们现在报道前列腺素F2α能够激活蛋白激酶C途径的关键组分，包括水溶性磷酸肌醇的产生、游离花生四烯酸的释放、内源性甘油二酯的释放以及胞质蛋白激酶C向富含磷脂的膜微环境的移位。
The biochemical mechanisms subserving the inhibitory actions of prostaglandin F2αon ovarian cells are not known. Since the protein kinase C pathway is coupled to steroidogenesis in an inhibitory fashion in pig granulosa cells, we have tested the hypothesis that prostaglandin F2αactivates this phospholipid-dependent, calcium-stimulated effector pathway. Using monolayer cultures of swine granulosa cells, we now report that prostaglandin F2αis capable of activating critical components of the protein kinase C pathway, including the production of water-soluble inositol phosphates, liberation of free arachidonic acid, release of endogenous diacylglycerol, and translocation of cytosolic protein kinase C to the phospholipid-enriched membrane microenvironment.