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Κυριακή 23 Ιουλίου 2017

Nitric oxide (NO) inhibition of meiotic G2-M1 transition in Anabas testudineus oocytes: Participation of cAMP-dependent protein kinase (PKA) in regulation of intra-oocyte signaling events

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Publication date: Available online 23 July 2017
Source:Molecular and Cellular Endocrinology
Author(s): Poulomi Nath, Debabrata Das, Soumojit Pal, Sudipta Maitra
Nitric oxide (NO) regulation of ovarian function in mammals has been studied extensively. However, relatively less information is available on NO action on meiotic G2-M1 transition in teleost oocytes. In the present study using follicle-enclosed oocytes of Anabas testudineus, NO regulation of intra-oocyte signaling events during meiotic G2-M1 transition were examined. Priming with NO donor, sodium nitroprusside (SNP) prevented 17α,20β-dihydroxy-4-pregenen-3-one (17,20β-P)-induced germinal vesicle break down (GVBD) in dose- and duration-dependent manner. Impaired GVBD response in SNP-treated groups corroborated well with reduced p34Cdc2 (Thr161) phosphorylation. Immunoblot analysis revealed that congruent with elevated cAMP-dependent protein kinase (PKA) phosphorylation (activation), NO inhibition of meiotic maturation involves down regulation of Cdc25 activation, Mos synthesis and MAPK3/1 (p-ERK1/2) phosphorylation. However, priming with PKA inhibitor (H89) could reverse SNP attenuation of oocyte GVBD significantly. Collectively our results indicate that negative influence of NO on meiotic G2-M1 transition in perch oocytes might involve PKA activation.



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