Article ID Journal Published Year Pages File Type
2196031 Molecular and Cellular Endocrinology 2014 8 Pages PDF
Abstract

•In vitro oocyte maturation (OM) in Tenualosa ilisha was induced by 17,20β-P.•17,20β-P induction of OM was dose- and time-dependent.•PI3 kinase shown to be the initial signal molecule for 17,20β-P induced OM.•MAP kinase although was activated during 17,20β-P induced OM.•MAP kinase activation is not involved in induction of OM.

Fully grown fish and amphibian oocytes exposed to a maturation-inducing steroid (MIS) activates multiple signal transduction pathways, leading to formation and activation of maturation-promoting factor (MPF) and induction of germinal vesicle breakdown (GVBD). The present study was to investigate if phosphatidylinositol 3 kinase (PI3 kinase) and mitogen-activated protein kinase (MAP kinase) activation are required for naturally occurring MIS, 17α,20β-dihydroxy-4-pregnen-3-one (17,20β-P)-induced cdc2 activation and oocyte maturation (OM) in Tenualosa ilisha. We observed that17,20β-P-induced OM was significantly inhibited by PI3 kinase inhibitors Wortmannin and LY29400. 17,20β-P was shown to activate PI3 kinase maximally at 90 min and cdc2 kinase at 16 h of treatment. Relative involvement of PI3 kinase, MAP kinase and cdc2 kinase in 17,20β-P-induced OM was examined. MAP kinase was rapidly phosphorylated and activated (60–120 min) after MIS treatment and this response preceded the activation of cdc2 kinase by several hours. A selective inhibitor of MAP kinase (MEK), PD98059, sufficiently blocked the phosphorylation and activation of MAP kinase. Inhibition of MAP kinase activity using PD98059 however, had no effect on MIS-induced cdc2 kinase activation and GVBD. These results demonstrate that activation of the PI3 kinase is required for 17,20β-P-induced cdc2 kinase activation and OM in T. ilisha. MAP kinase although was activated in response to 17,20β-P and PI3 kinase activation, it is not necessary for cdc2 activation and OM in this species.

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