Activities of maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are not required for the global histone deacetylation observed after germinal vesicle breakdown (GVBD) in porcine oocytes
Activities of maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are not required for the global histone deacetylation observed after germinal vesicle breakdown (GVBD) in porcine oocytes
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DOI：
10.1530/rep.1.00924
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发表时间：
2006-03-01
期刊：
影响因子：
3.8
通讯作者：
Tojo, H
中科院分区：
文献类型：
--
作者：
Endo, T;Naito, K;Tojo, H
核核心组蛋白的乙酰化被认为可以作为将基因表达模式传递给子细胞的表观遗传标记。尽管组蛋白脱乙酰化的调节机制尚未得到很好的研究，但在小鼠和猪卵母细胞减数分裂成熟过程中，在生发囊泡破裂（GVBD）后以细胞周期依赖性方式观察到了全局组蛋白脱乙酰化，可能与基因表达的重编程有关。在本研究中，我们研究了关键的细胞周期调节因子成熟促进因子（MPF）和减数分裂相关激酶丝裂原激活蛋白激酶（MAPK）在猪卵母细胞成熟过程中整体组蛋白去乙酰化中的参与情况。为了了解GVBD后观察到的整体组蛋白脱乙酰化是否需要MPF和MAPK的活性，或者GV膜的破坏是否足够，我们人为破坏了猪未成熟卵母细胞的GV膜。人工 GV 破坏 (AGVD) 诱导组蛋白脱乙酰化，但不激活 MPF 和 MAPK。 AGVD 后的这种脱乙酰化不受 MPF 抑制剂 roscovitine 或蛋白质合成抑制剂放线菌酮的影响，但被组蛋白脱乙酰酶 (HDAC) 抑制剂曲古抑菌素 A 完全阻止。HDAC1 存在于未成熟卵母细胞的 GV 中，并在 GVBD 和 AGVD 后定位于染色体上。这些结果表明 MPF 和 MAPK 活性是可有可无的，GV 膜的分解足以进行由 HDAC 活性催化的整体组蛋白脱乙酰化
The acetylation of nuclear core histone has been suggested to work as an epigenetic mark for transmitting gene expression patterns to daughter cells. Global histone deacetylations, presumably involved in the reprogramming of the gene expression, have been observed after germinal vesicle breakdown (GVBD) in a cell cycle-dependent manner during meiotic maturation of mouse and porcine oocytes, although the regulation mechanism of histone deacetylation has not been studied well. In the present study, we examined the involvement of a crucial cell-cycle-regulator, maturation-promoting factor (MPF), and a meiosis-related kinase, mitogen-activated protein kinase (MAPK), in the global histone deacetylation during porcine oocyte maturation. In order to know whether the activities of MPF and MAPK were required, or the breakdown of GV membrane was sufficient, for the global histone deacetylation observed after GVBD, we artificially destroyed the GV membrane of the porcine immature oocytes. The artificial GV destruction (AGVD) induced histone deacetylation without the activation of MPF and MAPK. This deacetylation after AGVD was not affected by an MPF inhibitor, roscovitine, or an inhibitor of protein synthesis, cycloheximide, but was completely prevented by an inhibitor of histone deactylases (HDACs), trichostatine A. HDAC1 was present in the GV of the immature oocytes and localized on chromosomes after GVBD and AGVD. These results suggest that the MPF and MAPK activities were dispensable and the breakdown of the GV membrane was sufficient for the global histone deacetylation, which was catalyzed by HDAC activity