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Published June 1993 | Published
Journal Article Open

Full activation of the rat oocyte by protein synthesis inhibition requires protein phosphatase activity


The rat oocyte provides an interesting system in which to dissect the control mechanisms involved in the transition between a meiotic M phase and a mitotic interphase. In this study, we show that in rat oocytes activated parthenogenetically by puromycin, okadaic acid (a potent inhibitor of protein phosphatases 1 and 2A) induced an increase in histone H1 kinase activity suggesting that MPF was reactivated. However, the inhibition of phosphatases 1 and 2A shortly after second polar body extrusion did not allow the formation of a metaphase-like spindle, although microtubule polymerization was not inhibited. Instead, the chromatin remained condensed as a single mass and a large aster formed around it.

Additional Information

© UPV/EHU Press 1993. Accepted for publication: January 1993. We thank Prof. Andrzej K. Tarkowski. Dr. Jacek Kubiak and Dr. Nicola Winston for critical reading of the manuscript, Richard Schwartzmann and Gérard Géraud for their expert photographic work. We are grateful to Dr. J.C. Courvalin for the gift of the anti-lamin B antibody and to Dr. J. Kilmartin for the gift of the YL1/ 2 antibody. This work was supported by grants from the Institut National pour la Sante et la Recherche Medicate , the Ligue Nationale contre le Cancer, the Association pour la Recherche contre le Cancer and the Fondation pour la Recherche Médicale to B.M. M.Z. G. was the recipient of a CNRS fellowship.

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