Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes.

Contributions of UBE2C and UBE2S to meiotic progression of porcine oocytes.
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DOI:
10.1262/jrd.2018-006
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发表时间:
2018-06-22
期刊:
The Journal of reproduction and development
影响因子:
--
通讯作者:
Naito K
Naito K
中科院分区:
其他
文献类型:
--
作者:
Fujioka YA;Onuma A;Fujii W;Sugiura K;Naito K

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脊椎动物卵母细胞在第一次减数分裂前期停滞,在受精前必须进入第二次减数分裂中期(MII)。这种减数分裂过程需要精确控制蛋白质降解。卵母细胞中的部分蛋白质降解由泛素缀合酶家族的成员UBE 2C和UBE 2S控制,已知它们分别参与单泛素化和多泛素化。虽然UBE 2酶在有丝分裂中已经得到了很好的研究,但它们对哺乳动物卵母细胞减数分裂的贡献相对未知,并且仅在小鼠中进行了研究。在这里,我们调查的贡献UBE 2C和UBE 2S猪卵母细胞成熟使用RNA注射方法。UBE 2S的过表达阻止了卵母细胞的MII停滞,并导致在培养48 h时形成原核(PN)。这种效果也观察到长期培养的UBE 2C-过表达的卵母细胞,表明多聚泛素化的有效性,在猪卵母细胞的M期快速逃逸。尽管注射反义RNA(asRNA)抑制UBE 2C或UBE 2S对卵母细胞成熟没有影响,但注射asRNA的卵母细胞在孤雌激活后显示出抑制PN形成。这些结果表明,UBE 2S和UBE 2C对某些因子的遍在化在猪卵母细胞逃避MII停滞中发挥作用。进一步的研究,以确定的因素,以及如何单和/或多聚泛素化有助于蛋白质降解,可以提供一个更好的理解UBE 2在卵母细胞成熟的作用。
Vertebrate oocytes arrested at the first meiotic prophase must proceed to the second meiotic metaphase (MII) before fertilization. This meiotic process requires the precise control of protein degradation. Part of the protein degradation in oocytes is controlled by members of the ubiquitin-conjugating enzyme family, UBE2C and UBE2S, which are known to participate in mono-ubiquitination and poly-ubiquitination, respectively. Although UBE2 enzymes have been well studied in mitosis, their contribution to mammalian oocyte meiosis is relatively unknown and has been studied only in mice. Here, we investigated the contribution of UBE2C and UBE2S to porcine oocyte maturation using an RNA injection method. Overexpression of UBE2S prevented MII arrest of oocytes and led to the formation of a pronucleus (PN) at 48 h of culture. This effect was also observed for prolonged cultures of UBE2C-overexpressing oocytes, suggesting the effectiveness of poly-ubiquitination in the rapid escape from M-phase in porcine oocytes. Although the inhibition of either UBE2C or UBE2S by antisense RNA (asRNA) injection had no effect on oocyte maturation, asRNA-injected oocytes showed inhibited PN formation after parthenogenetic activation. These results indicated that ubiquitination of certain factors by UBE2S and UBE2C plays a role in the escape from MII arrest in porcine oocytes. Further investigations to identify the factors and how mono- and/or poly-ubiquitination contributes to protein degradation could provide a better understanding of UBE2 roles in oocyte maturation.
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