Function of the Mos/MAPK pathway during oocyte maturation in the Japanese brown frog Rana japonica
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Published on: September 27, 2015
N Yoshida1, K Mita, M Yamashita
1Laboratory of Molecular and Cellular Interactions, Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, Japan.
Abstract:
Fully grown immature oocytes acquire the ability to be fertilized with sperm after meiotic maturation, which is finally accomplished by the formation and activation of the maturation-promoting factor (MPF). MPF is the complex of Cdc2 and cyclin B, and its function in promoting metaphase is common among species. The Mos/mitogen-activated protein kinase (MAPK) pathway is also commonly activated during vertebrate oocyte maturation, but its function seems to be different among species. We investigated the function of the Mos/MAPK pathway during oocyte maturation of the frog Rana japonica. Although MAPK was activated in accordance with MPF activation during oocyte maturation, MPF activation and germinal vesicle breakdown (GVBD) was not initiated when the Mos/MAPK pathway was activated in immature oocytes by the injection of c-mos mRNA. Inhibition of Mos synthesis by c-mos antisense RNA and inactivation of MAPK by CL100 phosphatase did not prevent progesterone-induced MPF activation and GVBD. However, continuous MAPK activation and MAPK inhibition through oocyte maturation accelerated and delayed MPF activation, respectively. Furthermore, Mos induced a low level of cyclin B protein synthesis in immature oocytes without the aid of MAPK. These results suggest that the general function of the Mos/MAPK pathway, which is not essential for MPF activation and GVBD in Rana oocytes, is to enhance cyclin B translation by Mos itself and to stabilize cyclin B protein by MAPK during oocyte maturation.
Insights
The Mos/mitogen-activated protein kinase (MAPK) pathway is not essential for frog oocyte maturation. It enhances cyclin B translation and stabilizes cyclin B protein, but does not initiate maturation-promoting factor (MPF) activation or germinal vesicle breakdown (GVBD).
Area of Science:
- Cell Biology
- Developmental Biology
- Molecular Biology
Background:
- Oocyte maturation is crucial for fertilization and involves meiotic maturation, driven by maturation-promoting factor (MPF).
- The Mos/mitogen-activated protein kinase (MAPK) pathway is activated during vertebrate oocyte maturation, but its specific role varies across species.
Purpose of the Study:
- To investigate the function of the Mos/MAPK pathway in the oocyte maturation of the frog Rana japonica.
- To determine the pathway's necessity for maturation-promoting factor (MPF) activation and germinal vesicle breakdown (GVBD).
Main Methods:
- Injection of c-mos mRNA to activate the Mos/MAPK pathway in immature oocytes.
- Inhibition of Mos synthesis using c-mos antisense RNA.
- Inactivation of MAPK using CL100 phosphatase.
- Progesterone induction of oocyte maturation.
Main Results:
- MAPK activation occurred concurrently with MPF activation, but did not initiate MPF activation or GVBD when artificially activated in immature oocytes.
- Inhibiting Mos synthesis or MAPK activity did not prevent progesterone-induced MPF activation and GVBD.
- Continuous MAPK activation accelerated MPF activation, while MAPK inhibition delayed it.
- Mos induced cyclin B protein synthesis independently of MAPK, and MAPK stabilized cyclin B protein.
Conclusions:
- The Mos/MAPK pathway is not essential for initiating MPF activation and GVBD in Rana oocytes.
- The pathway's primary role is to enhance cyclin B translation via Mos and stabilize cyclin B protein through MAPK activity during oocyte maturation.
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