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This Article Full Text Full Text (PDF) All Versions of this Article: 69/5/1494    most recent biolreprod.103.019018v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Viveiros, M. M. Articles by Eppig, J. J. Search for Related Content PubMed PubMed Citation Articles by Viveiros, M. M. Articles by Eppig, J. J. Agricola Articles by Viveiros, M. M. Articles by Eppig, J. J.

Characterization of Protein Kinase C- in Mouse Oocytes Throughout Meiotic Maturation and Following Egg Activation¹

The Jackson Laboratory, Bar Harbor, Maine 04609

Changes in protein kinase C (PKC) activity influence the progression of meiosis; however, the specific function of the various PKC isoforms in female gametes is not known. In the current study, the protein expression and subcellular distribution profile of PKC-delta (PKC-), a novel isoform of the PKC family, was determined in mouse oocytes undergoing meiotic maturation and following egg activation. The full-length protein was observed as a doublet (76 and 78 kDa) on Western blot analysis. A smaller (47 kDa) carboxyl-terminal fragment, presumably the truncated catalytic domain of PKC-, was also strongly expressed. Both the full-length protein and the catalytic fragment became phosphorylated coincident with the resumption of meiosis and remained phosphorylated throughout metaphase II (MII) arrest. Immunofluorescence staining showed PKC- distributed diffusely throughout the cytoplasm of oocytes during maturation and associated with the spindle apparatus during the first meiotic division. Discrete foci of the protein also localized with the chromosomes in some mature eggs. Following the completion of meiosis, PKC- became dephosphorylated within 2 h of in vitro fertilization or parthenogenetic activation. The protein also accumulated in the nuclei of early embryos and was phosphorylated during M-phase of the initial mitotic cleavage division. By the two-cell stage, expression of the truncated catalytic fragment was minimal. These data demonstrate that the subcellular distribution and posttranslational modification of PKC- is cell cycle dependent, suggesting that its activity and/or function likely vary with the progression of meiosis and egg activation.

¹ This research was supported by a grant (CA62392) from the National Cancer Institute to J.J.E. Scientific resources of The Jackson Laboratory are supported in part by a Cancer Center Core Grant (CA 34196) from the National Cancer Institute.

² Correspondence. FAX: 610 925-8121; viveiros{at}vet.upenn.edu

³ Current address: University of Pennsylvania, School of Veterinary Medicine, Department of Animal Biology, Center for Animal Transgenesis and Germ Cell Research, 382 West Street Road, Kennett Square, PA 19348-1692

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