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

Dev Biol. 1990 Sep;141(1):115-22. doi: 10.1016/0012-1606(90)90106-s.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Electrophoresis, Polyacrylamide Gel
  • Ethers, Cyclic / pharmacology
  • Fluorescent Antibody Technique
  • Growth Substances / biosynthesis
  • Maturation-Promoting Factor
  • Meiosis / drug effects
  • Mice
  • Mice, Mutant Strains
  • Microtubules / drug effects
  • Nuclear Envelope / drug effects
  • Nuclear Envelope / physiology
  • Okadaic Acid
  • Oocytes / drug effects
  • Oocytes / metabolism*
  • Parthenogenesis
  • Phosphoprotein Phosphatases / physiology*
  • Protamine Kinase / metabolism*
  • Protein Kinases / metabolism*
  • Puromycin / pharmacology


  • Ethers, Cyclic
  • Growth Substances
  • Okadaic Acid
  • Puromycin
  • Protein Kinases
  • Protamine Kinase
  • Maturation-Promoting Factor
  • Phosphoprotein Phosphatases