Hostname: page-component-cd9895bd7-7cvxr Total loading time: 0 Render date: 2024-12-26T04:42:05.349Z Has data issue: false hasContentIssue false
  • English
  • Français

Okadaic acid-sensitive phosphatase is related to MII/G1 transition in mouse oocytes

Published online by Cambridge University Press:  10 February 2011

Naoko Moride ,
Akira Kuwahara ,
Ayako Sutoh ,
Yu Tanaka ,
Yukari Mukai ,
Mizuho Yamashita ,
Toshiya Matsuzaki ,
Toshiyuki Yasui  and
Minoru Irahara
Naoko Moride
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Akira Kuwahara*
Affiliation:
Department of Obstetrics & Gynecology, University of Tokushima Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Ayako Sutoh
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Yu Tanaka
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Yukari Mukai
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Mizuho Yamashita
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Toshiya Matsuzaki
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Toshiyuki Yasui
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
Minoru Irahara
Affiliation:
Department of Obstetrics and Gynecology, University of Tokushima, Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan.
*
All correspondence to: Akira Kuwahara. Department of Obstetrics & Gynecology, University of Tokushima Institute for Health Biosciences, 3–18–15 Kuramoto Tokushima 770–8503, Japan. Tel: +81 88 633 7177. Fax: +81 88 631 2630. e-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Summary

It is reported that okadaic acid (OA)-sensitive phosphatase is related to mitogen-activated protein kinase (MAPK)/p90rsk activation in mammalian oocytes. OA is also involved in the positive feedback loop between M phase-promoting factor (MPF) and cdc25c in Xenopus oocytes during meiotic maturation. However, the effect of phosphatase inhibition by OA on MPF and MAPK activities at the MII/G1 in oocytes remains unknown. The aim of this study is to clarify the relationship between OA-sensitive phosphatase and mitosis MII/G1 transition in mouse oocytes. MII-arrested oocytes were, isolated from mice, inseminated and cultured in TYH medium (control group) or TYH medium supplemented with 2.5 μM of OA (OA group). Histone H1 kinase and myelin basic protein (MBP) kinase activities were measured as indicators of MPF and p42 MAPK activities after insemination. Phosphorylation of cdc25c after insemination was analized in OA and control group by western blotting. Seven hours after insemination a pronucleus (PN) was formed in 84.1% (69/85) of oocytes in the control group. However, no PN was formed in oocytes of the OA group (p < 0.001). Although MPF and MAPK activities in the control group significantly decreased at 3, 4, 5, and 7 h after insemination, these decreases were significantly inhibited by OA addition (p < 0.05). Furthermore, OA addition prevented cdc25c dephosphorylation 7 h after insemination. In conclusion, OA-sensitive phosphatase correlates with inactivation of MPF and MAPK, and with the dephosphorylation of cdc25c at the MII/G1 transition in mouse oocytes.

Keywords

Cdc25cMAPKMouse oocyteMPFOkadaic acid
Type
Research Article
Information
Zygote , Volume 20 , Issue 2 , May 2012 , pp. 193 - 198
Copyright
Copyright © Cambridge University Press 2011

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Chesnel, F. & Eppig, J.J. (1995). Induction of precocious germinal vesicle breakdown (GVB) by GVB-incompetent mouse oocytes: possible role of mitogen-activated protein kinase rather than p34cdc2 kinase. Biol. Reprod. 52, 895–902.Google Scholar
Chian, RC., Tan, S.L. & Sirard, M.A. (1999). Protein phosphorylation is essential for formation of male pronucleus in bovine oocytes. Mol. Reprod. Dev. 52, 43–9.3.0.CO;2-C>CrossRefGoogle Scholar
Colledge, W.H., Carlton, M.B., Udy, G.B. & Evans, M.J. (1994). Disruption of c-mos causes parthenogenetic development of unfertilized mouse eggs. Nature 370, 65–8.CrossRefGoogle ScholarPubMed
Cyert, M.S. & Kirschner, M.W. (1988). Regulation of MPF activity in vitro. Cell 53, 185–95.Google Scholar
Doree, M. & Hunt, T. (2002). From Cdc2 to Cdk1: when did the cycle kinase join its cyclin partner? J. Cell. Sci. 115, 2461–4.CrossRefGoogle ScholarPubMed
Dunphy, W.G. & Kumagai, A. (1991). The cdc25 protein contains an intrinsic phosphatase activity. Cell 67, 189–96.CrossRefGoogle ScholarPubMed
Fan, H.Y., Tong, C., Lian, L., Lim, S.W., Gao, W.S., Cheng, Y., Chen, D.Y., Schatten, H. & Sun, Q.Y. (2003). Characterization of ribosomal S6 protein kinase p90rsk during meiotic maturation and fertilization in pig oocytes, mitogen-activated protein kinase-associated activation and localization. Biol. Reprod. 68, 968–77.Google Scholar
Gautier, J. & Maller, J.L. (1991). Cyclin B in Xenopus oocytes: implications for the mechanism of pre-MPF activation. EMBO J. 10, 177–82.CrossRefGoogle ScholarPubMed
Gavin, A.C., Cavadore, J.C. & Schorderet-Slatkine, S. (1994). Histone H1 kinase activity, germinal vesicle breakdown and M phase entry in mouse oocytes. J. Cell Sci. 107, 275–83.Google Scholar
Hashimoto, N., Watanabe, N., Furuta, Y., Tamemoto, H., Sagata, N., Yokoyama, M. et al. (1994). Parthenogenetic activation of oocytes in c-mos-deficient mice. Nature 370, 68–71.CrossRefGoogle ScholarPubMed
Hoffmann, I., Clarke, P.R., Marcote, M.J., Karsenti, E. & Draetta, G. (1993). Phosphorylation and activation of human cdc25-C by cdc2-cyclin B and its involvement in the self-amplification of MPF at mitosis. EMBO J. 12, 53–63.CrossRefGoogle ScholarPubMed
Izumi, T. & Maller, J.L. (1993). Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase. Mol. Biol. Cell 4, 1337–50.CrossRefGoogle ScholarPubMed
Kobayashi, H., Minshull, J., Ford, C., Golsteyn, R., Poon, R. & Hunt, T. (1991). On the synthesis and destruction of A- and B-type cyclins during oogenesis and meiotic maturation in Xenopus laevis. J. Cell Biol. 114, 755–65.CrossRefGoogle ScholarPubMed
Kubiak, J.K., Weber, M., Géraud, G. & Maro, B. (1992). Cell cycle modification during the transitions between meiotic M-phase in mouse oocytes. J. Cell Sci. 102, 457–67.CrossRefGoogle ScholarPubMed
Kumagai, A. & Dunphy, W.G. (1992). Regulation of the cdc25c protein during the cell cycle in Xenopus extracts. Cell 70, 139–51.CrossRefGoogle ScholarPubMed
Millar, J.B. & Russell, P. (1992). The cdc25 M-phase inducer: an unconventional protein phosphatase. Cell 68, 407–10.Google Scholar
Moos, J., Visconti, P.E., Moore, G.D., Schultz, R.M. & Kopf, G.S. (1995). Potential role of mitogen-activated protein kinase in pronuclear envelope assembly and disassembly following fertilization of mouse eggs. Biol. Reprod. 53, 692–9.CrossRefGoogle ScholarPubMed
Naito, K. & Toyoda, Y. (1991). Fluctuation of histone H1 kinase activity during meiotic maturation in porcine oocytes. J. Reprod. Fertil. 93, 467–73.CrossRefGoogle ScholarPubMed
Palmer, A., Gavin, A.C. & Nebreda, A.R. (1998). A link between MAP kinase and p34(cdc2)/cyclin B during oocyte maturation:p90(rsk) phosphorylates and inactivates the p34(cdc2) inhibitory kinase Myt1. EMBO J. 17, 5037–47.CrossRefGoogle ScholarPubMed
Tan, X., Chen, D.Y., Yang, Z., Wang, Y.C., Li, M., Schatten, H. & Sun, Q.Y. (2001). Phosphorylation of p90rsk during meiotic maturation and parthenogenetic activation of rat oocytes: correlation with MAP kinases. Zygote 9, 269–76.Google Scholar