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Protein phosphorylation in bovine oocytes following fertilisation andparthenogenetic activation in vitro

Published online by Cambridge University Press:  01 May 1999

R. C. Chian ,
S. L. Tan  and
M. A. Sirard
R. C. Chian
Affiliation:
McGill Reproductive Center, Department of Obstetrics and Gynecology, McGill University, Montreal, Quebec, Canada H3A 1A1.
S. L. Tan
Affiliation:
McGill Reproductive Center, Department of Obstetrics and Gynecology, McGill University, Montreal, Quebec, Canada H3A 1A1.
M. A. Sirard
Affiliation:
Centre de Recherche en Biologie de la Reproduction, Département des sciences animales, Université Laval, Quebec, Canada G1K 7P4.
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Abstract

This study examined the event of protein phosphorylation in bovine oocytes in response to sperm penetration and parthenogenetic activation. In vitro matured oocytes were labelled with [32P]orthophosphate at 3 h intervals from 3 h to 18 h or from 0 h to 12 h following in vitro fertilisation and parthenogenetic activation, respectively. The level of protein dephosphorylation, at approximately 43 kDa, was similar in fertilised and parthenogenetically activated bovine oocytes. However, the level of protein phosphorylation at 40 kDa, 23 kDa and 18 kDa was different between these two samples. There were no such changes of protein phosphorylation and dephosphorylation in the control oocytes. Further, by two-dimensional gel electrophoresis there is a difference in the level of protein phosphorylation at 18 kDa between the fertilised and activated oocytes. These results suggest that this protein phosphorylation may be related to the formation of the male pronucleus in bovine oocytes.

Keywords

ActivationFertilisationOocytePhosphorylationSperm
Type
Research Article
Information
Zygote , Volume 7 , Issue 2 , May 1999 , pp. 135 - 142
Copyright
1999 Cambridge University Press

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