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Expression of the cell cycle control protein cdc25 in cleavage stage bovine embryos

Published online by Cambridge University Press:  26 September 2008

J.M. Jones
Affiliation:
Department of Meat and Animal ScienceUniversity of WisconsinMadison, Wisconsin, USA.
N.L. First*
Affiliation:
Department of Meat and Animal ScienceUniversity of WisconsinMadison, Wisconsin, USA.
*
Dr Neal First, Department of Meat and Animal Science, University of Wisconsin-Madison, Madison, WI 53706, USA. Telephone: (608) 263-4307. Fax: (608) 262-5157.

Summary

We have examined the synthesis and expression of a homologue of the cell cycle protein cdc25 by early cleavage stage bovine embryos. cdc25 is the protein phosphatase responsible for activating p34cdc2 by dephosphorylating the threonine 14 (Thr 14) and tyrosine 15 (Tyr 15) residues of p34cdc2. Human cdc25 antibody was utilised in western blots immunoprecipitations to examine the presence and synthesis of cdc25 in bovine embryos. cdc25 is present as a 52 kDa non-phosphorylated and a 66 kDa presumably phosphorylated form in bovine 1−, 2−, 4− and 8−cell embryos. However, cdc25 is actively synthesised only in 8-Cell embryos, indicating that the cdc25 present prior to this stage is inherited from the oocyte. In addition, the synthesis of cdc25 was induced in 2-cell embryos in which cleavage was blocked with the DNA synthesis inhibitor aphidicolin.

Type
Article
Copyright
Copyright © Cambridge University Press 1995

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References

Barmes, F.L. & Eyestone, W.H. (1990). Early cleavage and the maternal to zygotic transition in bovine embryos. Theriogenology 33 141–52.CrossRefGoogle Scholar
Barmes, F.L. & First, N.L. (1991). Embryonic transcription in in vitro cultured bovine embryos. Mol. Reprod. Dev. 29 117–23.CrossRefGoogle Scholar
Bensaude, O., Babinet, C., Morange, M. & Jacob, F. (1983). Heat shock proteins, first major products of zygotic gene activity Nature 305 331–3.CrossRefGoogle ScholarPubMed
Bolton, V., Oades, P. & Johnson, M. (1984). The relationship between cleavage, DNA replication, and gene expression in the mouse 2-cell embryo. J. Embryol. Exp. Morphol. 79 139–69.Google ScholarPubMed
Connover, J.C., Temelles, G.L, Zimmermann, J.W., Burke, B. & Schultz, R.M. (1991). Stage specific expression of a family of proteins that are major products of gene activation in the mouse embryos Dev. Biol. 147 403–14.Google Scholar
Dasso, M. & Newpart, J.W. (1990). Completion of DNA replication is monitored by a feedback mechanism that controls the initiation of mitosis in vitro: studies in Xenopus. Cell 61, 811–23.CrossRefGoogle Scholar
Dunphy, W.G. & Kumagi, A. (1991). The cdc25 protein contains an intrinsic phosphatase activity. Cell 67, 189–96.CrossRefGoogle ScholarPubMed
Edgar, B.A. & O'Farrell, P.H. (1989). Genetic control of cell division patterns in the Drosophila embryo. Cell 57, 177–87.CrossRefGoogle ScholarPubMed
Edgar, B.A. & O'Farrell, P.H. (1990). The three postblastoderm cell cycles of Drosophila embryogenesis are regulated in G2 by string. Cell 62, 469–80.CrossRefGoogle ScholarPubMed
Edgar, B.A. & Schubinger, G. (1986). Parameters controlling transcriptional activation during early Drosophila development. Cell 44, 871–7.CrossRefGoogle ScholarPubMed
Edgar, B.A., Kiehle, C.P. & Schubinger, G. (1986). Cell cycle control by the nucleocytoplasmic ratio in early Drosophila development. Cell 44, 365–6.CrossRefGoogle ScholarPubMed
Flach, G., Johnson, M., Braude, P., Taylor, R. & Bolton, V. (1982). The transition from maternal to embryonic control in the 2-cell mouse embryo. EMBO J. 1 681–6.CrossRefGoogle ScholarPubMed
Frei, P.G., Schultz, G.A. & Church, R.B. (1989). Qualitative and quantitative changes in protein synthesis occur at the 8–16–cell stage of embryogenesis in the cow. J. Reprod. Pert. 86, 637–41.CrossRefGoogle ScholarPubMed
Galaktionov, K. & Beach, D. (1991). Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins. Cell 67, 1181–94.CrossRefGoogle ScholarPubMed
Gautier, J., Solomon, M.J., Booher, R.N., Bazan, J.F. & Kirschner, M.W. (1991). cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2. Cell 67, 192–119.CrossRefGoogle ScholarPubMed
Girard, F., Strausfeld, U., Cavadore, J.C., Russell, P., Fernandez, A. & Lamb, N.J. (1992). cdc25 is a nuclear protein expressed constituitively throughout the cell cycle in non–transformed mammalian cells. J. Cell Biol. 118, 785–94.CrossRefGoogle Scholar
Hoffmann, I., Clarke, P.R., Jesus Marcote, M., Karsenti, E. & Draetta, G. (1993). Phosphorylation and activation of human cdc25 by cdc2-cyclin B and its involvement in the self–amplification of MPF at mitosis. EMBO J. 12, 5363.CrossRefGoogle ScholarPubMed
Jessus, C. & Beach, D. (1992). Oscillation of MPF is accompanied by periodic association between cdc25 and cdc2-cyclin B. Cell 68, 223–32.CrossRefGoogle ScholarPubMed
Jiminez, J., Alphey, L., Nurse, P. & Glover, D.M. (1991). Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two cell cycle genes from Drosophila: a cdc2 homologue and string. EMBO J. 9,3565–71.CrossRefGoogle Scholar
Kakizuka, A., Sebastion, B., Borgmeyer, U., HermansBorgmeyer, I., Bolado, J., Hunter, T., Hoekstra, M.F. & Evans, R.M. (1992). A mouse cdc25 homolog is differentially and developmentally expressed. Genes Dev. 6, 578–90.CrossRefGoogle ScholarPubMed
Kimmelman, D., Kirschner, M. & Scherson, T. (1987). The events of the midblastula transition in Xenopus are regulated by changes in the cell cycle. Cell 48, 399407.CrossRefGoogle Scholar
King, W.A., Niar, A., Chartrain, I., Betteridge, K.J. & Guay, P. (1988). The nucleolus organizer regions and nucleoli in preattachment bovine embryos. J. Reprod. Fert. 66, 8795.CrossRefGoogle Scholar
Kopecny, V., Flechon, J.E., Camous, S. & Fulka, J. (1989). Nucleologenesis and the onset of transcription in the eight-cell bovine embryo: fine-structural autoradiographic study. Mol. Reprod. Dev. 1, 7990.CrossRefGoogle ScholarPubMed
Krek, W. & Nigg, E.A. (1991a). Differential phosphorylation of vertebrate p34cdc2 kinase at the G1/S and G2/M transitions of the cell cycle: identification of major phosphorylation sites. EMBO J. 10, 305–16.CrossRefGoogle ScholarPubMed
Krek, W. & Nigg, E.A. (1991b). Mutations of p34cdc2 phosphorylation sites induce premature mitotic events in HeLa cells: evidence for a double block to p34cdc2 kinase activation in vertebrates. EMBO J. 10, 3331–41.CrossRefGoogle ScholarPubMed
Kumagi, A. & Dunphy, W.G. (1991). The cdc25 protein controls tyrosine dephosphorylation of the cdc2 protein in a cell-free system. Cell 64, 90–14.Google Scholar
Kumagi, A. & Dunphy, W.G. (1992). Regulation of the cdc25 protein during the cell cycle in Xenopus extracts. Cell 70, 139–51.CrossRefGoogle Scholar
Lee, M.S., Ogg, S., Xu, M., Parker, L.L., Donoghue, D.J., Maller, J.L. & Piwnica-Worms, H. (1992). cdc25 + encodes a protein phosphatase that dephosphorylates p34cdc2. Mol. Biol. Cell 3, 7384.CrossRefGoogle ScholarPubMed
Leibfried-Rutledge, M.L., Critser, E.S., Parrish, J.J. & First, N.L. (1989): In vitro maturation and fertilization of bovine oocytes. Theriogenology 31, 6173.CrossRefGoogle Scholar
MartinezSalaz, E., Linney, E., Hassell, J. & DePamphilus, M.L. (1989). The need for enhancers in gene expression first appears during mouse development with formation of the zygotic nucleus. Genes Dev. 3, 1493–506.CrossRefGoogle Scholar
McGowen, C. & Russell, P. (1993). Human Weel kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr 15. EMBO J. 12, 7585.CrossRefGoogle Scholar
McNight, S.L. & Miller, O.L. (1976). Ultrastructural patterns of RNA synthesis during early embryogenesis of Drosophila melanogaster. Cell 8, 305–19.CrossRefGoogle Scholar
Millar, J.B.A., Blevitt, J., Gerace, L., Sadhu, K., Featherstone, C. & Russell, P. (1991). p55cdc25 is a nuclear protein required for the initiation of mitosis in human cells. Proc. Natl. Acad. Sci. USA 88, 10500–4.CrossRefGoogle ScholarPubMed
Newport, J.W. & Kirschner, M. (1982a). A major developmental transition in early Xenopus embryos. I. Characterization and timing of cellular changes at the midblastula stage. Cell 30, 675–86.CrossRefGoogle Scholar
Newport, J.W. & Kirschner, M. (1982b). A major developmental transition in early Xenopus embryos. II. Control of the onset of transcription. Cell 30, 6896.CrossRefGoogle Scholar
Pines, J. & Hunter, T. (1991). Human cyclins A and B1 are differentially located in the cell and undergo cell cycle dependent nuclear transport. J. Cell Biol. 115, 117.CrossRefGoogle ScholarPubMed
Poueymirou, W.T. & Schultz, R.M. (1987). Differential effects of activators of cAMP-dependent protein kinase and protein kinase C on cleavage of 1-cell mouse embryos and protein synthesis and phosphorylation in 1- and 2-cell embryos. Dev. Biol. 121, 489–98.CrossRefGoogle ScholarPubMed
Rosenkrans, C.F., Zeng, Z.Q., McNamara, G.T., Schoff, P.K. & First, N.L. (1993). The development of bovine embryos is affected by energy substrates Biol. Reprod. 49 459–62.CrossRefGoogle ScholarPubMed
Russell, P. & Nurse, P. (1986). cdc25 functions as an inducer in mitotic control of fission yeast Cell 45 145–53.CrossRefGoogle ScholarPubMed
Sadhu, R., Reed, S.I., Richardson, H. & Russel, P. (1990). Human homolog of fission yeast cdc25 mitotic incucer is prodominantly expressedin G2. Proc. Natl. Acad Sci. USA 87 5139–43.CrossRefGoogle Scholar
Saeki, K., Hoshi, M., Leibfried-Rultdge, M.L. & First, N.L., (1990). In vitro fertilization and development of bovine oocytes matured with commercially available follicle stimulating hormone. Theriogenology 34 1035–9.CrossRefGoogle Scholar
Sakicki, J.A., Magnuson, T. &. Epstein, C.J., (1982). Evidence for the expression of the paternal genome in two-cell mouse embryo. Nature 294 450–1.CrossRefGoogle Scholar
Simcox, A.A. & Sang, J.H. (1992). When does determination occur in Drosophila embryos? Dev. Biol. 97 212–21.CrossRefGoogle Scholar
Smythe, C. & Newport, J.W. (1992). Coupling of mitosis to the completion of S phas in Xenopus occurs via modulation of the tyrosine kinase that phosphorylates p34cdc2. Cell 68 787–97.CrossRefGoogle Scholar
Strausfeld, U., Labbe, J.C. & Fesquet, D., Cavadore, J.C., Picard, A., Sadhu, K., Russell, M. (1991). Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human cdc25 protein Nature 351 242–5.CrossRefGoogle ScholarPubMed