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Capacity of mouse oocytes to become activated depends on completion of cytoplasmic but not nuclear meiotic maturation

Published online by Cambridge University Press:  26 September 2008

Joise M.L. McConnell ,
Liz Campbell  and
Caroline Vincent
Joise M.L. McConnell*
Affiliation:
Department of Anatomy, University of Cambridge, Cambridge, UK.
Liz Campbell
Affiliation:
Department of Anatomy, University of Cambridge, Cambridge, UK.
Caroline Vincent
Affiliation:
Department of Anatomy, University of Cambridge, Cambridge, UK.
*
Dr J.M.L. McConnell, Department of Anatomy, Dowing street, Cambridge CB2 3DY, UK Telephone: (0223) 333755. Fax: (0223) 333786.
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Summary

The ability of mouse oocytes to become activated after exposure too the calcium ionophore A23187 has been investigated at different stages of meiotic maturation. The potential to respond to ionophore has been studied in relation to the time since resumption of meiotic maturation, the chromosomal conformation of the DNA within each cell and the protein synthetic profile of the maturing oocyte. Our studies demonstrate that when maturing oocytes from an MF1 strain of mice were treated with A23187 activation occured only in oocytes which had reached second meiotic metaphase (MII). However, development of the ability to respond to ionophore was not dependent on an orderly progression through normal chromosomal rearrangements such as separation at metaphase I (MI) and subsequent polar body extrusion, since there process could be prevented and the capacity to be activated became apparent in such oocytes at a time when control cells had reached MII. These data suggest that the ability to respond to ionophore depends on the development of a cytoplasmic or complex capable of monitoring the time since initiation of germinal vesicle breakdown. Metabolic radiolabelling of oocytes which were able to respond to calcium ionophore, even though they had been prevented from undergoing normal chromosomal rearrangements, showed them to be synthesising a group of proteins known as the 35 kDa complex.

Keywords

ActivationCalcium ionophoreMouseoocyte
Type
Article
Information
Zygote , Volume 3 , Issue 1 , February 1995 , pp. 45 - 55
Copyright
Copyright © Cambridge University Press 1995

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References

Cascio, S.M.. & Wassarman, P.M.. (1982). Program of early development in the mammal: post-transcriptional control of a class of proteins synthesized by mouse oocytes and early embryos. Dev. Biol. 89, 397–408.Google Scholar
Clarke, H.J.. & Masui, Y.. (1983). The induction of reversible and irreversible chromosome decondensation by protein synthesis inhibition during meiotic maturation. Dev. Biol. 97, 291–301.Google Scholar
Clarke, H.J.. & Masui, Y.. (1988). Suppression of chromosome cindensation during meiotic maturation induces parthenogenic development of mouse oocytes. Development 104, 97–103.Google Scholar
Gautier, J., Norbury, C., Lohka, M., Nurse, P.. & Maller, J.. (1988). Purified maturation-promoting factor contains the product of a Xenopus homolog of the fission yeast cell cycle control gene cdc2+. Cell 54, 433–9.Google Scholar
Gautier, J., Minshull, J., Lohka, M.G., Glotzer, M., Hunt, T.. & Maller, J.L.. (1990). Cyclin is a component of maturation promoting factor from Xenopus. Cell 60, 487–94.Google Scholar
Howlett, S.K.. (1986). A Set of proteins showing cell cycle dependent modifications in the early mouse embryo. Cell. 45, 387–9.Google Scholar
Hunt, T.. (1989). Under arrest in the cell cycle. Nature 342, 483–4.CrossRefGoogle ScholarPubMed
Kilmartin, J., Wright, B.. & Milestein, C.. (1982). Rat monoclonal anti-tubulin antibodies derived by using a new nonsecreting rat cell line. J. Cell Biol. 22, 699–707.Google Scholar
Kubiak, J.Z.. (1989). Mouse oocytes gradually develop the capacity for activation during the methaphase II arrest. Dev. Biol. 136, 537–45.Google Scholar
Kubiak, J.Z., Weber, M., Pennart, H., Winston, N.J.. & Maro, B.. (1993). The metaphase II arrest in mouse oocyte is controlled through microtubule dependent destruction of cyclin B in the presence of CSF. EMBO J. 12, 3773–8.CrossRefGoogle ScholarPubMed
Lohka, M.J., Haynes, M.K.. & Maller, J.L.. (1988). Purification of maturation-promoting factor, an intracellular regulator of early mitotic events. Proc. Nalt. Acad. Sci. USA 85, 3009–13.Google Scholar
Lorca, T., Galas, S., Fesquet, D., Devault, A., Cavadore, J.C.. & Doree, M.. (1991). Degradation of the proto-oncogene product p39mos is not necessary for cyclin proteolysis and exit from meiotic metaphase: requirement for Ca2+ calmodulin even. EMBO J. 10, 2087–93.Google Scholar
Maro, B., Johnson, M.H., Pickering, S.J.. & Flach, G.. (1984). Changes in actin distribution during fertilization of the mouse eggs. J. Embryol. Exp. Morphol. 81, 211–37.Google Scholar
Masui, Y.. & Market, C.L.. (1971). Cytoplasmic control of nuclear behaviour during meiotic maturation of frog oocytes. J. Exp. Zool. 117, 129–46.Google Scholar
McConnell, J.. (1990). Cell cycle control in early mouse development. J.Reprod. Fert. Suppl. 42, 205–13.Google ScholarPubMed
Murray, A.W.. (1989). The cell cycle as a cdc2 cycle. Nature 342, 14–15.CrossRefGoogle ScholarPubMed
Murray, A.W., Solomon, M.J.. & Kirschner, M.W.. (1989). The role of cyclin synthesis and degradation in the control of maturation promoting factor activity. Nature 339, 280–5.CrossRefGoogle ScholarPubMed
Nasr-Esfahani, M., Johnson, M.H.. & Aitkin, R.J.. (1990). The effect of iron and iron chelators on the in vitro block to development of the preimplantation embryp: BAT6 a new medium for improved culture of mouse embrys in vitro. Hum. Reprod.. 5, 997–1003.CrossRefGoogle Scholar
Pennart, H.de., Verlhac, M.H., Cibert, C., Santa-Maria, A.. & Maro, B.. (1993). Okadaic acid induces spindle lengthening and disrupts the interaction of microtubules with the kinetochores in metaphase II arrested mouse oocytes. Dev. Biol. 157, 170–81.CrossRefGoogle ScholarPubMed
Szollosi, M.S., Kubiak, J.Z., Debey, P., Pennart, H., Szollosi, D.. & Maro, B.. (1993). Inhibition of protein kinases by 6-dmap accelerates the transition to interphase in activated mouse oocytes. J. Cell Sci. 104, 861–72.CrossRefGoogle ScholarPubMed
Tarkowski, A.K.. (1966). An air-drying method for chromosome preparations from mouse eggs. Cytogenetics 5, 394–400.CrossRefGoogle Scholar
Tombes, R.M., Simerly, G.G.. & Schatten, G.. (1992). Meiosis egg activation, and nuclear envelope breakdown are differntially reliant on Ca2+, whereas germinal vesicle breakdown is Ca2+ independent in the mouse oocyte. J. Cell Biol. 117, 799–811.Google Scholar
Van Blerkom, J.. & Bell, H.. (1986). Regulation of development in the fully grown mouse oocyte: chromosome-mediated temporal and spatial differentiation of the cytoplasm and plasma membrane. J. Embryol. Exp. Morphol. 93, 213–38.Google ScholarPubMed
Van de Velden, H.W.M.. & Lohka, M.J.. (1993). Mitotic arrest caused by the amino terminus of cyclin B2. Mol. Cell Biol. 13, 1480–8.Google Scholar
Vincent, C., Cheek, T.R.. & Johnson, M.H.. (1992). Cell cycle progression of parthogenetically activated mouse oocytes to interphase is dependent on the level of internal calcium. J. Cell Sci. 103, 389–96.Google Scholar
Watanabe, N., Van de Woude, G.F., Ikawa, Y.. & Sagata, N.. (1989). Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilisation of Xenopus eggs. Nature 342, 505–11.Google Scholar
Winston, N.J., McGuinness, O., Johnson, M.H.. & Maro, B.. (1994). The exit of activated mouse oocytes from meiotic M-phase requires an intact spindle during intracellular calcium release. J. Cell Sci (in press).Google Scholar