Localization of Cyclin B and Erk1/2 in Ovine Oocytes and MPF and MAPK Activities in Cytoplast and Karyoplast following Enucleation

  • Lee, Joon-Hee (Department of Animal Bioscience, College of Agriculture and Life Sciences, Gyeongsang National University) ;
  • Campbell, Keith H.S. (Division of Animal Physiology, School of Biosciences, The University of Nottingham)
  • 투고 : 2011.10.22
  • 심사 : 2011.10.31
  • 발행 : 2011.12.31

초록

The development of embryos reconstructed by somatic cell nuclear transfer (SCNT) is dependent upon numerous factors. Central to development is the quality and developmental competence of the recipient cytoplast and the type of the donor nucleus. Typically metaphase of the second meiotic division (MII) has become the cytoplast of choice. Production of a cytoplast requires removal of the recipient genetic material, however, it may remove proteins which are essential for development or reduce the levels of cytoplasmic proteins to influence subsequent reprogramming of the donor nucleus. In this study, enucleation at MII did not affect the activities of either MPF or MAPK kinases. Immunocytochemical staining showed that both Cyclin B1 (MPF) and Erk1/2 (MAPK) were associated with the meiotic spindle of AI/TI oocytes with little staining in the cytoplasm, however, at MII association of both proteins with the spindle had reduced and a greater degree of cytoplasmic distribution was observed. The analysis of oocyte proteins removed during enucleation is a difficult approach to the identification of factors which may be depleted in the cytoplast. This is primarily due to the large numbers of aspirated karyoplasts which would be required for the analysis.

키워드

참고문헌

  1. Baguisi A, Behboodi E, Melican DT, Pollock JS, Destrempes MM, Cammuso C, Williams JL, Nims SD, Porter CA, Midura P, Palacios MJ, Ayres SL, Denniston RS, Hayes ML, Ziomek CA, Meade HM, Godke RA, Gavin WG, Overstrom EW, Echelard Y (1999): Production of goats by somatic cell nuclear transfer. Nature Biotechnology 17:456-461. https://doi.org/10.1038/8632
  2. Blum H, Beier H, Gross HJ (1987): Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8:93-99. https://doi.org/10.1002/elps.1150080203
  3. Campbell KHS, Alberio R (2003): Reprogramming the genome: role of the cell cycle. Reproduction Supplement 61:477-494.
  4. Campbell KHS, Loi P, Otaegui PJ, Wilmut I (1996a): Cloning mammals by nuclear transfer. Co-ordinating nuclear and cytoplasmic events. Reviews in Reproduction 1:40-46. https://doi.org/10.1530/ror.0.0010040
  5. Campbell KHS, McWhir J, Ritchie WA, Wilmut I (1996b): Sheep cloned by nuclear transfer from a cultured cell line [see comments]. Nature 380:64-66. https://doi.org/10.1038/380064a0
  6. Chesne P, Adenot PG, Viglietta C, Baratte M, Boulanger L, Renard JP (2002): Cloned rabbits produced by nuclear transfer from adult somatic cells. Nature Biotechnology 20:366-369. https://doi.org/10.1038/nbt0402-366
  7. Collas P, Balise JJ, Robl JM (1992): Influence of cell cycle stage of the donor nucleus on development of nuclear transplant rabbit embryos. Biology of Reproduction 46:492-500. https://doi.org/10.1095/biolreprod46.3.492
  8. Fulka J Jr, Motlik J, Fulka J, Crozet N (1986): Activity of maturation promoting factor in mammalian oocytes after its dilution by single and multiple fusions. Developmental Biology 118:176-181.
  9. Fulka J Jr, Ouhibi N, Fulka J, Kanka J, Moor RM (1995): Chromosome condensation activity (CCA) in bisected C57BL/6JxCBA mouse oocytes. Reproduction Fertility and Development 7:1123-1127. https://doi.org/10.1071/RD9951123
  10. Galli C, Lagutina I, Crotti G, Colleoni S, Turini P, Ponderato N, Duchi R, Lazzari G (2003): Pregnancy: a cloned horse born to its dam twin. Nature 424:635.
  11. Goto S, Naito K, Ohashi S, Sugiura K, Naruoka H, Iwamori N, Tojo H (2002): Effects of spindle removal on MPF and MAP kinase activities in porcine matured oocytes. Molecular Reproduction and Development 63:388-393. https://doi.org/10.1002/mrd.90022
  12. Greaves S (2000): Maturing ooctyes: the role of MAP kinase. Nature. Cell Biology 2: E125. https://doi.org/10.1038/35017140
  13. Horne MM, Guadagno TM (2003): A requirement for MAP kinase in the assembly and maintenance of the mitotic spindle. Journal of Cell Biology 161: 1021-1028. https://doi.org/10.1083/jcb.200304144
  14. Kikuchi K, Naito K, Noguchi J, Shimada A, Kaneko H, Yamashita M, Aoki F, Tojo H, Toyoda Y (2000): Maturation/M-phase promoting factor: a regulator of aging in porcine oocytes. Biology of Reproduction 63:715-722. https://doi.org/10.1095/biolreprod63.3.715
  15. Ledda S, Bogliolo L, Leoni G, Naitana S (2001): Cell coupling and maturation-promoting factor activity in in vitro-matured prepubertal and adult sheep oocytes. Biology of Reproduction 65:247-252. https://doi.org/10.1095/biolreprod65.1.247
  16. Lee JH, Campbell KHS (2005): Effects of enculeation and caffeine on maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) activities in ovine oocytes used as recipients cytoplasts for nuclear transfer. Biology of Reproduction 74:691-698.
  17. Li GP, White KL, Bunch TD (2004): Review of enucleation methods and procedures used in animal cloning: state of the art. Cloning and Stem Cells 6: 5-13. https://doi.org/10.1089/15362300460743781
  18. O'Keefe SJ, Kiessling AA, Cooper GM (1991): The c-mos gene product is required for cyclin B accumulation during meiosis of mouse eggs. Proceedings of the National Academy of Science U S A 88: 7869-7872. https://doi.org/10.1073/pnas.88.17.7869
  19. Pennington K, McGregor E, Beasley CL, Everall I, Cotter D, Dunn MJ (2004): Optimization of the first dimension for separation by two-dimensional gel electrophoresis of basic proteins from human brain tissue. Proteomics 4:27-30. https://doi.org/10.1002/pmic.200300624
  20. Polejaeva IA, Chen SH, Vaught TD, Page RL, Mullins J, Ball S, Dai Y, Boone J, Walker S, Ayares DL, Colman A, Campbell KHS (2000): Cloned pigs produced by nuclear transfer from adult somatic cells. Nature 407:86-90. https://doi.org/10.1038/35024082
  21. Sagata N, Watanabe N, Vande W, Ikawa Y (1989): The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 342:512-518. https://doi.org/10.1038/342512a0
  22. Salamone DF, Damiani P, Fissore RA, Robl JM, Duby RT (2001): Biochemical and developmental evidence that ooplasmic maturation of prepubertal bovine oocytes is compromised. Biology of Reproduction 64:1761-1768. https://doi.org/10.1095/biolreprod64.6.1761
  23. Simerly C, Dominko T, Navara C, Payne C, Capuano S, Gosman G, Chong KY, Takahashi D, Chace C, Compton D, Hewitson L, Schatten G (2003): Molecular correlates of primate nuclear transfer failures. Science 300:297. https://doi.org/10.1126/science.1082091
  24. Torner H, Kubelka M, Heleil B, Tomek W, Aim H, Kuzmina T, Guiard V (2001): Dynamics of meiosis and protein kinase activities in bovine oocytes correlated to prolactin treatment and follicle size. Theriogenology 55:885-899. https://doi.org/10.1016/S0093-691X(01)00451-4
  25. Wakayama T, Perry AC, Zuccotti M, Johnson KR, Yanagimachi R (1998): Full-term development of mice from enucleated oocytes injected with cumulus cell nuclei. Nature 394:369-374. https://doi.org/10.1038/28615
  26. Wells DN, Misica PM, Tervit HR (1999): Production of cloned calves following nuclear transfer with cultured adult mural granulosa cells. Biology of Reproduction 60:996-1005. https://doi.org/10.1095/biolreprod60.4.996
  27. Woods GL, White KL, Vanderwall DK, Li GP, Aston KI, Bunch TD, Meerdo LN, Pate BJ (2003): A mule cloned from fetal cells by nuclear transfer. Science 301:1063. https://doi.org/10.1126/science.1086743
  28. Zhou Q, Renard JP, Le Friec G, Brochard V, Beaujean N, Cherifi Y, Fraichard A, Cozzi J (2003): Generation of fertile cloned rats by regulating oocyte activation. Science 302:1179. https://doi.org/10.1126/science.1088313