Progesterone-Induced Maturation and Down Regulation of Membrane Bound Na+, K+-ATPase

Mohanty Bk
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引用次数: 3

Abstract

Progesterone induces maturation by releasing oocyte from G2 of MI cell cycle arrest. This process is rate limiting as it produces fertilizable eggs. Therefore, it draws a lot of attention. Na+, K+-ATPase is a membrane bound enzyme molecule that has known to have various functions. One of these functions is to act as receptor for Progesterone. In oocyte maturation to egg entirely depends on progesterone, a hormone that is known to reduce risk of cancer. Using EM Histo-cytochemical novel technique, we have shown that membrane bound Na+, K+-ATPase are gradually down-regulated following Progesterone-induced maturation. By Germinal Vesicle Break down, Na+, K+-ATPase is completely down-regulated from oolemma and only present in the narrow region of Germinal Vesicle Break Down. This is an important phenonmena as this down-regulation coincides with cell entering M-phase. Here, I also briefly introduce you to a technique that only localizes phosphate cleaving membrane bound Na+, K+-ATPase.
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黄体酮诱导的膜结合Na+, K+- atp酶成熟及下调
黄体酮通过释放卵母细胞使其脱离心肌细胞周期阻滞诱导成熟。这个过程是速率限制,因为它产生受精卵。因此,它引起了很多关注。Na+, K+- atp酶是一种具有多种功能的膜结合酶分子。其中一个功能是充当孕激素的受体。卵母细胞成熟到卵细胞完全取决于黄体酮,一种已知可以降低癌症风险的激素。利用EM组织细胞化学新技术,我们发现细胞膜结合的Na+, K+- atp酶在黄体酮诱导成熟后逐渐下调。在生发囊泡分解过程中,Na+, K+- atp酶从胚轴上完全下调,仅存在于生发囊泡分解的狭窄区域。这是一个重要的现象,因为这种下调与细胞进入m期一致。在这里,我还简要介绍了一种仅定位磷酸切膜结合Na+, K+- atp酶的技术。
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