Activation of ribosomal S6 kinase (RSK) during porcine oocyte maturation

K. Sugiura, K. Naito, N. Iwamori, H. Kagii, S. Goto, S. Ohashi, H. Naruoka, E. Yada, K. Yamanouchi, H. Tojo

研究成果: ジャーナルへの寄稿学術誌査読

16 被引用数 (Scopus)


The normal kinetics of ribosomal S6 kinase (RSK) during the meiotic maturation of porcine oocytes were examined. The phosphorylation states of RSK and extracellular signal-regulated kinase (ERK), major mitogen-activated protein (MAP) kinases in maturating porcine oocytes, were detected by Western blotting analysis. The S6 protein kinase activity was assayed using a specific substrate peptide which contained the major phosphorylation sites of S6 kinase. Full phosphorylation of RSK was correlated with ERK phosphorylation and was observed before germinal vesicle breakdown. S6 kinase activity was low in both freshly isolated and 20 h cultured oocytes. S6 kinase activity was significantly elevated in matured oocytes to a level about 6 times higher than that in freshly isolated oocytes. Furthermore, full phosphorylation of RSK was inhibited when oocytes were treated with U0126, a specific MAP kinase kinase inhibitor, in dose-dependent manner, indicating that RSK is one of the substrates of MAP kinase. These results suggest that the activation of RSK is involved in the regulation of meiotic maturation of porcine oocytes.

出版ステータス出版済み - 2月 1 2002

!!!All Science Journal Classification (ASJC) codes

  • 発生生物学
  • 細胞生物学


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