Changes in histone modifications during in vitro maturation of porcine oocytes
Changes in histone modifications during in vitro maturation of porcine oocytes
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DOI：
10.1002/mrd.20288
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发表时间：
2005-05-01
影响因子：
2.5
通讯作者：
Tojo, H
中科院分区：
文献类型：
--
作者：
Endo, T;Naito, K;Tojo, H
核核心组蛋白修饰影响染色体结构和功能。最近，在小鼠卵母细胞成熟过程中，组蛋白乙酰化参与了基因表达的细胞记忆。目前，关于哺乳动物卵母细胞成熟过程中组蛋白修饰的可用数据很少。在本研究中，我们检测了猪卵母细胞体外成熟过程中组蛋白 H3 赖氨酸 9 (H3K9) 和 14 (H3K14) 以及组蛋白 H4 赖氨酸 5 (H4K5)、8 (H4K8) 和 12 (H4K12) 的乙酰化以及 H3K9 三甲基化的变化。免疫细胞化学分析表明，所有检测的赖氨酸在生发囊泡阶段均高度乙酰化，并且这种乙酰化水平一直维持到第一个前期。在第一个中期，靠近 N 末端的赖氨酸 H3K9 和 H4K5 完全脱乙酰化。远离 N 末端的赖氨酸 H2K14、H4K8 和 H4K12 的乙酰化明显减少，但仍然存在。乙酰化在第一个后期和末期短暂增加，然后在第二个中期再次降低至与第一个中期相同的水平。由于不同赖氨酸残基中抑制脱乙酰化的曲古抑菌素 A (TSA) 的有效浓度不同，因此表明多种组蛋白脱乙酰酶 (HDAC) 在减数分裂成熟过程中发挥作用。 H3K9 的三甲基化在整个成熟过程中保持在高水平。这些结果表明猪卵母细胞成熟过程中的组蛋白乙酰化受到细胞周期的精确控制。 (c) 2005 年 Wiley-Liss, Inc.
Nuclear core histone modifications influence chromosome structures and functions. Recently, the involvement of histone acetylations in the cell memory of gene expression has been suggested in mouse oocyte maturation. At present, there is little available data on histone modifications in mammalian oocyte maturation. In the present study, we examined changes in the acetylation of histone H3 lysines 9 (H3K9) and 14 (H3K14), and histone H4 lysines 5 (H4K5), 8 (H4K8) and 12 (H4K12), and trimethylation of H3K9 during in vitro maturation of porcine oocytes. Immunocytochernical analyses revealed that the all of the lysines examined were highly acetylated in the germinal vesicle stage, and this level of acetylation was maintained until the first prometaphase. In the first metaphase, the lysines near the N-terminal end, H3K9 and H4K5, were completely deacetylated. The acetylation of the lysines far from the N-terminal end, H2K14, H4K8, and H4K12, was markedly decreased but still present. The acetylations were increased transiently at the first anaphase and telophase, and then decreased again at the second metaphase to the same level as the first metaphase. Since effective concentrations of trichostatin A (TSA) to inhibit the deacetylation were different in various lysine residues, multiple histone deacetylases (HDACs) were suggested to function during meiotic maturation. The trimethylation of H3K9 was maintained in a high level throughout maturation. These results suggest that the histone acetylation during porcine oocyte maturation is precisely controlled by the cell cycle. (c) 2005 Wiley-Liss, Inc.