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Dev Biol. 1990 Sep;141(1):115-22.

Protein phosphatases are involved in the in vivo activation of histone H1 kinase in mouse oocyte.

Author information

1
Laboratoire de physiologie de la Reproduction, INRA-CNRS, UA 555, Université Pierre et Marie Curie, France.

Abstract

Histone H1 kinase and protein phosphorylation have been studied in mouse oocyte. Histone H1 kinase activity increases when the oocyte enters M-phase at the time of GVBD and is paralleled with a burst of protein phosphorylation. This activity dramatically drops after parthenogenetic activation induced by puromycin. Okadic acid (OA), a potent inhibitor of protein phosphatases, induces GVBD when oocytes are arrested in the first meiotic prophase by dbc-AMP; the continuous presence of the phosphatase inhibitor, however, inhibits the polymerization of metaphase microtubules. Following activation of metaphase II-arrested mouse eggs by puromycin, OA can induce the breakdown of the nuclear envelope and the activation of histone H1 kinase. This indicates that in the absence of protein synthesis, and therefore of cyclin synthesis, inhibition of protein phosphatases may be sufficient to induce the entry into M-phase during the first cell cycle of the mouse parthenogenetic activated oocyte.

PMID:
2167856
DOI:
10.1016/0012-1606(90)90106-s
[Indexed for MEDLINE]

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