放线菌素D对豚鼠子宫前列腺素合成和分泌的影响

N.L. Poyser, S.C. Riley
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引用次数: 10

摘要

放线菌素D在第10天子宫内给予放线菌素D,可使体外培养第15天的豚鼠子宫分泌的前列腺素F2α(主要的PG释放物)减少80% ~ 85%。PGE2输出减少50%,而6-酮- pgf1 α输出不受影响。第15天,由于子宫PGF2α分泌减少,血浆孕酮水平升高(3 ~ 15 ng/ml)。放线菌素D处理使子宫内膜PGF2α合成能力降低50%,而子宫内膜PGE2和6-酮- pgf1 α合成能力未受影响。体内雌二醇处理不能逆转放线菌素D对子宫PG生成的抑制作用。A23187增加子宫PGF2α, 6-酮- pgf1 α和PGE2的输出,与处理无关,表明底物供应总是速率限制。放线菌素D抑制雌二醇的子宫营养作用,表明其抑制了新鲜蛋白的合成。总的来说,这项研究表明,增加的蛋白质合成参与刺激子宫内膜PGF2α的合成和释放。先前的研究表明,雌二醇诱导的酶活性增加只是刺激子宫内膜PGF2α生成的次要事件。我们提出雌二醇诱导一种蛋白质(“脂促素”)的合成,这种蛋白质作用于孕激素引发的子宫,通过引起子宫内膜磷脂酶A2的激活,“打开”子宫内膜PGF2α的合成和释放。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Effect of actinomycin D on prostaglandin synthesis by and output from the guinea-pig uterus

The intra-uterine administration of actinomycin D on Day 10 reduced the output of prostaglandin (PG) F (the major PG released) from the Day 15 guinea-pig uterus in vitro by 80 to 85%. PGE2 output was reduced by 50%, while 6-keto-PGF output was unaffected. Plasma progesterone levels were high (3 to 15 ng/ml) on Day 15 due to the reduction in uterine PGF output. Endometrial PGF synthesizing capacity was reduced by 50% by actinomycin D treatment, while endometrial PGE2 and 6-keto-PGF synthesizing capacities were unaffected. Oestradiol treatment in vivo did not reverse the inhibitory effects of actinomycin D on uterine PG production.A23187 increased uterine PGF, 6-keto-PGF and PGE2 outputs irrespective of treatment, indicating that substrate supply was always rate limiting. Actinomycin D inhibited the uterotrophic action of oestradiol indicating that fresh protein synthesis had been inhibited. Overall, this study suggests that increased protein synthesis is involved in stimulating endometrial PGF synthesis and release.Previous studies have shown that increases in enzyme activities induced by oestradiol are only secondary events in the stimulation of endometrial PGF production. We propose that oestradiol induces the synthesis of a protein (‘lipostimulin’) which, acting on a progesterone-primed uterus, “switches on” endometrial PGF synthesis and release by causing the activation of endometrial phospholipase A2.

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