Reproductive and Developmental Biology

The Korean Society of Animal Reproduction (한국동물번식학회)
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Effect of Vitrification on In Vitro Maturation and Development and Gene Expression in Canine Oocytes

  • Park, Ji-Hoon (College of Veterinary Medicine, Chungnam National University) ;
  • Kim, Sang-Keun (College of Veterinary Medicine, Chungnam National University)
  • Received : 2011.03.30
  • Accepted : 2011.05.23
  • Published : 2011.06.30
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Abstract

The in vitro maturation rate of vitrified-thawed canine oocytes was $30.8{\pm}3.4%$. The in vitro maturation rate of vitrified oocytes was lower than that of the control ($52.0{\pm}2.5%$, p<0.05). The in vitro maturation rate of vitrified-thawed oocytes were significantly (p<0.05) lower than those of fresh oocytes. The in vitro maturation and developmental rates of the vitrified-thawed oocytes were $17.5{\pm}2.5%$ and $8.8{\pm}3.4%$, respectively. This results were lower than the control group ($43.6{\pm}3.2%$ vs $20.0{\pm}3.0%$). SOD1 gene expression of 1~2 mm of follicle size were higher than those of above 6 mm follicle size. SOD2 gene expression of 1~2 mm of follicle size were significantly higher than those of above 6 mm follicle size (p<0.01). The expression pattern of SOD1, 2 was constantly expressed in both groups but strongly expressed in follicles (1~2 mm) group when compared to the above 6 mm follicles. SOD gene expression between groups the fresh and vitrified oocytes groups were significant differences in rates. However, RGS gene expression between groups the fresh and vitrified oocytes groups were no significant differences in rates.

Keywords

References

  1. Ali AA, Bilodeau JF, Sirard MA (2003): Antioxidant requirements for bovine oocytes varies during in vitro maturation, fertilization and development. Theriogenology 59:939-949. https://doi.org/10.1016/S0093-691X(02)01125-1
  2. Bedford SJ, Kurokawa M, Hinrichs K, Fissore RA (2003): Intracellular calcium oscillations and activation in horse oocytes injected with stallion sperm extracts or spermatozoa. Reproduction 126:489-499. https://doi.org/10.1530/rep.0.1260489
  3. Berman DM, Gilman AG (1998): Mammalian RGS proteins: Barbarians at the gate. J BioI Chem 273 (3):1269-1272. https://doi.org/10.1074/jbc.273.3.1269
  4. Clark P, Rahy GM, Karow Jr AM (1984): Factor influencing renal cryopreservation. II. Toxic effects of three cryopreservation in combination with three vehicle solutions in non-frozen rabbit cortical slices. Cryobiology 21:260-273. https://doi.org/10.1016/0011-2240(84)90322-5
  5. Covarrubias L, Hernandez-Garcia D, Schnabel D, Salas-Vidal E, Castro-Obregon S (2008): Function of reactive oxygen species during animal development: passive or active? Developmental Biology 320:1-11. https://doi.org/10.1016/j.ydbio.2008.04.041
  6. Dhali A, Manik RS, Singla SK, Palta P (2000): Vitrification of buffalo (Bubalus bubalis) oocytes. Theriogenology 53:1295-1303. https://doi.org/10.1016/S0093-691X(00)00273-9
  7. Fahy GM, Macfarlane DR, Angell CA, Meryman HT (1984): Vitrification as an approach to cryopreservation. Cryobiology 21:407-426. https://doi.org/10.1016/0011-2240(84)90079-8
  8. Gagnon AW, Murray DL, Leadley RJ (2002): Cloning and characterization of a novel regulator of G protein signalling in human platelets. Cell Signal, 14(7):595-606. https://doi.org/10.1016/S0898-6568(02)00012-8
  9. Garcia A, Prabhakar S, Hughan S, Anderson TW, Brock CJ, Pearce AC, Dwek RA, Watson SP, Hebestreit HF, Zitzmann N (2004): Differential proteome analysis of TRAP activated platelets: Involvement of DOK-2 and phosphorylation of RGS proteins. Blood 103(6):2088-2095. https://doi.org/10.1182/blood-2003-07-2392
  10. Hao J, Michalek C, Zhang W, Zhu M, Xu X, Mende U (2006): Regulation of cardiomyocyte signaling by RGS proteins: differential selectivity towards G proteins and susceptibility to regulation. J Mol Cell Cardiol 41:51-61. https://doi.org/10.1016/j.yjmcc.2006.04.003
  11. Hewitt DA, England GCW. 1997. Effect of preovulatory endocrine events upon maturation of oocytes of domestic bitches. J Reprod Fertil (Supp), 151:83-91.
  12. Hurst JH, Mendpara N, Hooks SB (2009): Regulator of G-protein signalling expression and function in ovarian cancer cell lines. Cell Mol BioI Lett 14:153-174. https://doi.org/10.2478/s11658-008-0040-7
  13. Krumins AM (2004): Differentially regulated expression of endogenous RGS4 and RGS7. J BioI Chem 279:2593-2599.
  14. Krumins AM, Barker SA, Huang C, Sunahara RK, Yu K, Wilkie TM, Gold SJ, Mumby SM (2004): Differentially regulated expression of endogenous RGS-4 and RGS7. J BioI Chem 279:2593-2599. https://doi.org/10.1074/jbc.M311600200
  15. Lee MJ (2005): RGS4 and RGS5 are in vivo substrates of the N-end rule pathway. Proc Natl Acad Sci 102:15030-15035. https://doi.org/10.1073/pnas.0507533102
  16. Martin CB, Mahon GM, Klinger MB, Kay RJ, Symons M, Der CJ, Whitehead IP (2001): The thrombin receptor, PAR-1, causes transformation by activation of Rho-mediated signaling pathways. Oncogene 20(16):1953-1963. https://doi.org/10.1038/sj.onc.1204281
  17. Mittmann C (2002): Expression of ten RGS proteins in human myocardium: functional characterization of an upregulation of RGS4 in heart failure. Cardiovasc Res 55:778-786. https://doi.org/10.1016/S0008-6363(02)00459-5
  18. Nikolova DN (2008): Genome-wide gene expression profiles of thyroid carcinoma: identification of molecular targets for treatment of thyroid carcinoma. Oncol Rep 20:105-121.
  19. Otoi T, Shimizu R, Naoi H, Wongsrikeao P, Agung B, Taniguchi M (2005): Meiotic competence of canine oocytes embedded in collagen gel. Reprod Domest Anim 41:17-21.
  20. Rodrigues BA, Carboneiro dos Santos L, Rodrigues JL (2004): Embryonic development of in vitro matured and in vitro fertilized dog oocytes. Mol Reprod Dev 67:215-223. https://doi.org/10.1002/mrd.10394
  21. Ross EM, Wilkie TM (2000): GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu Rev Biochem 69:795-827. https://doi.org/10.1146/annurev.biochem.69.1.795
  22. Songsasen N, Yu I, Leibo SP (2002): Nuclear maturation of canine oocytes cultured in protein-free media. Mol Reprod Dev 62:407-415. https://doi.org/10.1002/mrd.10130
  23. Songsasen N, Wildt DE (2005): Size of the donor follicle, but not stage of reproductive cycle or seasonality, influences meiotic competency of selected domestic dog oocytes. Mol Reprod Dev 72:113-119. https://doi.org/10.1002/mrd.20330
  24. Srinivasa SP, Bernstein LS, Blumer KJ, Linder ME (1998): Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae. Proc Natl Acad Sci 95(10):5584-589. https://doi.org/10.1073/pnas.95.10.5584
  25. Sutton RL (1992): Critical cooling rates for aqueous cryoprotectants in the presence of sugars and polysaccharides. Cryobiology 29:585-598. https://doi.org/10.1016/0011-2240(92)90063-8
  26. Tatemoto H, Muto N, Sunagawa I, Shinjo A, Nakada T (2004): Protection of porcine oocytes against cell damage caused by oxidative stress during in vitro maturation: role of superoxide dismutase activity in porcine follicular fluid. Biology of Reproduction 71: 1150-1157. https://doi.org/10.1095/biolreprod.104.029264
  27. Turathum B, Saikhun K, Sangsuwan P, Kitiyanant Y (2010): Effects of vitrification on nuclear maturation, ultrastructural changes and gene expression of canine oocytes. Reprod BioI Endocrinol 22:70-83.
  28. Utsumi K, Hochi S, lritani A (1982): Cryopretective effect of polyols on rat embryos during two-step freezing. Cryobiology 29:332-341.
  29. Watson N, Linder ME, Druey KM, Kehrl JH, Blumer KJ (1996): RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits. Nature 383(6596):172-175. https://doi.org/10.1038/383172a0
  30. Xie Y (2009): Breast cancer migration and invasion depend on proteasome degradation of regulator of G-protein signaling 4. Cancer Res 69:5743-5751. https://doi.org/10.1158/0008-5472.CAN-08-3564