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Publication : Function of the Mos/MAPK pathway during oocyte maturation in the Japanese brown frog Rana japonica.

First Author  Yoshida N Year  2000
Journal  Mol Reprod Dev Volume  57
Issue  1 Pages  88-98
PubMed ID  10954860 Mgi Jnum  J:63854
Mgi Id  MGI:1861860 Doi  10.1002/1098-2795(200009)57:1<88::AID-MRD12>3.0.CO;2-9
Citation  Yoshida N, et al. (2000) Function of the Mos/MAPK pathway during oocyte maturation in the japanese brown frog rana japonica. Mol Reprod Dev 57(1):88-98
abstractText  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. Mol. Reprod. Dev. 57:88-98, 2000. Copyright 2000 Wiley-Liss, Inc.
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