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Phosphorylation of p90rsk during meiotic maturation and parthenogenetic activation of rat oocytes: correlation with MAP kinases

Published online by Cambridge University Press:  06 August 2001

Xin Tan ,
Da-Yuan Chen ,
Zhe Yang ,
Yong-Chao Wang ,
Manyu Li ,
Heide Schatten  and
Qing-Yuan Sun
Xin Tan
Affiliation:
State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, P.R. China. Beijing Normal University, The Key Laboratory of Cell Proliferation and Regulation of Educational Ministry of China, Beijing 100875, P.R. China. Capital University of Medical Sciences, Beijing 100054, P.R. China.
Da-Yuan Chen
Affiliation:
State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, P.R. China.
Zhe Yang
Affiliation:
State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, P.R. China.
Yong-Chao Wang
Affiliation:
Beijing Normal University, The Key Laboratory of Cell Proliferation and Regulation of Educational Ministry of China, Beijing 100875, P.R. China.
Manyu Li
Affiliation:
State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, P.R. China.
Heide Schatten
Affiliation:
Department of Veterinary Pathobiology, University of Missouri-Columbia, Columbia, MO 65211, USA.
Qing-Yuan Sun
Affiliation:
State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100080, P.R. China.
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Abstract

This paper reports on the activation of p90rsk during meiotic maturation and the inactivation of p90rsk after electrical parthenogenetic activation of rat oocytes. In addition, the correlation between p90rsk and MAP kinases after different treatments was studied. We assessed p90rsk activity by examining its electrophoretic mobility shift on SDS-PAGE and evaluated ERK1+2 activity by both mobility shift and a specific antibody against phospho-MAP kinase. The phosphorylation of p90rsk during rat oocyte maturation was a sequential process that may be divided into two stages: the first stage was partial phosphorylation, which was irrelevant with MAP kinases because p90rsk phosphorylation took place prior to activation of MAP kinases. The second stage inferred full activation occurred at the time when MAP kinases began to be activated (3 h after germinal visicle breakdown). Evidence for the involvement of MAP kinases in the p90rsk phosphorylation was further obtained by the following approaches: (1) okadaic acid (OA) accelerated the phosphorylation of both MAP kinases and p90rsk; (2) OA induced phosphorylation of both MAP kinases and p90rsk in the presence of IBMX; (3) when activation of MAP kinases was inhibited by cycloheximide, p90rsk phosphorylation was also abolished; (4) dephosphorylation of p90rsk began to take place at 3 h post-activation, temporally correlated with the completion of MAP kinase inactivation; (5) phosphorylation of both kinases was maintained in oocytes that failed to form pronuclei after stimulation; (6) OA abolished the dephosphorylation of both kinases after parthenogenetic activation. Our data suggest that MAP kinases are not required for early partial activation of p90rsk but are required for full activation of p90rsk during rat oocyte maturation, and that p90rsk dephosphorylation occurs following MAP kinase inactivation after parthenogenetic activation of rat oocytes.

Keywords

Cell cycleMAP kinaseOocytep90rskRat
Type
Research Article
Information
Zygote , Volume 9 , Issue 3 , August 2001 , pp. 269 - 276
Copyright
© 2001 Cambridge University Press

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