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• W2018294925 endingPage "308" @default.
• W2018294925 startingPage "301" @default.
• W2018294925 abstract "Protein phosphorylation catalyzed by the cAMP-dependent protein kinase is implicated in transcriptional activation of the embryonic genome in the two-cell mouse embryo, while heat shock protein (hsp70) has been identified as one of the first products of zygotic gene activation. Using reverse transcription-polymerase chain reaction we have analyzed relative changes in the amount of hsp70 mRNA during oocyte maturation and early embryogenesis. We report that the amount of hsp70 mRNA decreases after germinal vesicle breakdown, while inhibiting germinal vesicle breakdown inhibits this maturation-associated decrease. The amount of hsp70 mRNA increases between the one- and two-cell stages. This increase is inhibited by either α-amanitin or the cAMP-dependent protein kinase inhibitor H-8; the same concentration of H-7, which is a more potent inhibitor of protein kinase C, has little inhibitory effect on this increase in the relative amount of hsp70 mRNA. Last, addition of cycloheximide to one-cell embryos late in G2 inhibits neither cleavage to the two-cell stage nor the increase in the relative amount of hsp70 mRNA. These results strengthen the previous proposal that protein phosphorylation is involved in zygotic gene activation in the two-cell mouse embryo." @default.
• W2018294925 created "2016-06-24" @default.
• W2018294925 creator A5002886426 @default.
• W2018294925 creator A5041471920 @default.
• W2018294925 creator A5043825479 @default.
• W2018294925 date "1991-04-01" @default.
• W2018294925 modified "2023-10-18" @default.
• W2018294925 title "Regulation of hsp70 mRNA levels during oocyte maturation and zygotic gene activation in the mouse" @default.
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• W2018294925 doi "https://doi.org/10.1016/0012-1606(91)90423-z" @default.
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