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Effect of trichostatin A on fertilization and embryo development during extended culture of mouse oocyte

Published online by Cambridge University Press:  27 January 2011

Byung Chul Jee
Affiliation:
Department of Obstetrics and Gynecology, Seoul National University Bundang Hospital, Seongnam, 463–707, Korea Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul, 110–744, Korea
Jun Woo Jo
Affiliation:
Department of Obstetrics and Gynecology, Seoul National University Bundang Hospital, Seongnam, 463–707, Korea
Jung Ryeol Lee
Affiliation:
Department of Obstetrics and Gynecology, Seoul National University Bundang Hospital, Seongnam, 463–707, Korea
Chang Suk Suh*
Affiliation:
Department of Obstetrics and Gynecology, Seoul National University Bundang Hospital, 300 Gumi-dong Bundang-gu Seongnam, 463–707, Korea. Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul, 110–744, Korea
Seok Hyun Kim
Affiliation:
Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul, 110–744, Korea
Shin Yong Moon
Affiliation:
Department of Obstetrics and Gynecology, Seoul National University College of Medicine, Seoul, 110–744, Korea
*
All correspondence to: Chang Suk Suh. Department of Obstetrics and Gynecology, Seoul National University Bundang Hospital, 300 Gumi-dong Bundang-gu Seongnam, 463–707, Korea. Tel: +82 31 787 7251. Fax: +82 31 787 4054. e-mail: [email protected]

Summary

We performed this study to investigate the effect of histone deacetylase inhibition during extended culture of in vitro matured mouse oocytes. In vitro matured mouse (BDF1) oocytes were cultured in vitro for 6, 12, and 24 h, respectively, and then inseminated. During in vitro culture for 6 and 12 h, two doses of trichostatin A (TSA), a histone deacetylase inhibitor, were added (100 nM and 500 nM) to the culture medium and the oocytes were then inseminated. During the 24-h in vitro culture, two doses of TSA were added (100 nM and 500 nM) to the medium and the oocytes were activated with 10 mM SrCl2. After the 6-h culture, the fertilization rate was similar to that of the control group, but the blastocyst formation rate was significantly decreased. After the 12-h culture, both the fertilization and blastocyst formation rates were significantly decreased. After the 24-h culture, total fertilization failure occurred. In the oocytes cultured for 6 and 12 h, the fertilization and blastocyst formation rates did not differ between the TSA-supplemented and control groups. Although extended culture of the mouse oocytes significantly affected their fertilization and embryo development, TSA supplementation did not overcome their decreased developmental potential.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2011

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References

Akiyama, T., Kim, J.M., Nagata, M. & Aoki, F. (2004). Regulation of histone acetylation during meiotic maturation in mouse oocytes. Mol. Reprod. Dev. 69, 222–7.CrossRefGoogle ScholarPubMed
Akiyama, T., Nagata, M. & Aoki, F. (2006). Inadequate histone deacetylation during oocyte meiosis causes aneuploidy and embryo death in mice. Proc. Natl. Acad. Sci. USA 103, 7339–44.CrossRefGoogle ScholarPubMed
Bui, H.T., Van Thuan, N., Kishigami, S., Wakayama, S., Hikichi, T., Ohta, H., Mizutani, E., Yamaoka, E., Wakayama, T. & Miyano, T. (2007). Regulation of chromatin and chromosome morphology by histone H3 modifications in pig oocytes. Reproduction 133, 371–82.CrossRefGoogle ScholarPubMed
Endo, T., Naito, K., Aoki, F., Kume, S. & Tojo, H. (2005). Changes in histone modifications during in vitro maturation of porcine oocytes. Mol. Reprod. Dev. 71, 123–8.CrossRefGoogle ScholarPubMed
Endo, T., Naito, K., Kume, S., Nishimura, Y., Kashima, K. & Tojo, H. (2006). Activities of maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are not required for the global histone deacetylation observed after germinal vesicle breakdown (GVBD) in porcine oocytes. Reproduction 131, 439–47.CrossRefGoogle Scholar
Endo, T., Kano, K. & Naito, K. (2008). Nuclear histone deacetylases are not required for global histone deacetylation during meiotic maturation in porcine oocytes. Biol. Reprod. 78, 1073–80.CrossRefGoogle Scholar
Goud, P.T., Goud, A.P., Laverge, H., De Sutter, P. & Dhont, M. (1999). Effect of post-ovulatory age and calcium in the injection medium on the male pronucleus formation and metaphase entry following injection of human spermatozoa into golden hamster oocytes. Mol. Hum. Reprod. 5, 227–33.CrossRefGoogle ScholarPubMed
Goud, A.P., Goud, P.T., Diamond, M.P. & Abu-Soud, H.M. (2005). Nitric oxide delays oocyte aging. Biochemistry 44, 11361–8.CrossRefGoogle ScholarPubMed
Huang, J.C., Yan, L.Y., Lei, Z.L., Miao, Y.L., Shi, L.H., Yang, J.W., Wang, Q., Ouyang, Y.C., Sun, Q.Y. & Chen, D.Y. (2007). Changes in histone acetylation during postovulatory aging of mouse oocyte. Biol. Reprod. 77, 666–70.CrossRefGoogle ScholarPubMed
Jeseta, M., Petr, J., Krejcova, T., Chmelikova, E. & Jilek, F. (2008). In vitro ageing of pig oocytes, effects of the histone deacetylase inhibitor trichostatin A. Zygote 16, 145–52.CrossRefGoogle ScholarPubMed
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. Biol. Reprod. 63, 715–22.CrossRefGoogle ScholarPubMed
Kim, J.M., Liu, H., Tazaki, M., Nagata, M. & Aoki, F. (2003). Changes in histone acetylation during mouse oocyte meiosis. J. Cell Biol. 162, 3746.CrossRefGoogle ScholarPubMed
Liang, X.W., Zhu, J.Q., Miao, Y.L., Liu, J.H., Wei, L., Lu, S.S., Hou, Y., Schatten, H., Lu, K.H. & Sun, Q.Y. (2008). Loss of methylation imprint of Snrpn in postovulatory aging mouse oocyte. Biochem. Biophys. Res. Commun. 371, 1621.CrossRefGoogle ScholarPubMed
Ma, P. & Schultz, R.M. (2008). Histone deacetylase 1 (HDAC1) regulates histone acetylation, development, and gene expression in preimplantation mouse embryos. Dev. Biol. 319, 110–20.CrossRefGoogle ScholarPubMed
Miao, Y.L., Kikuchi, K., Sun, Q.Y. & Schatten, H. (2009). Oocyte aging: cellular and molecular changes, developmental potential and reversal possibility. Hum. Reprod. Update 15, 573–85.CrossRefGoogle ScholarPubMed
Petr, J., Chmelikova, E., Kheilova, K. & Jilek, F. (2009). Histone deacetylase inhibition improves meiotic competence but not developmental competence in growing pig oocytes. Zygote 17, 307–14.CrossRefGoogle Scholar
Rausell, F., Pertusa, J.F., Gomez-Piquer, V., Hermenegildo, C., Garcia-Perez, M.A., Cano, A. & Tarin, J.J. (2007). Beneficial effects of dithiothreitol on relative levels of glutathione S-transferase activity and thiols in oocytes, and cell number, DNA fragmentation and allocation at the blastocyst stage in the mouse. Mol. Reprod. Dev. 74, 860–9.CrossRefGoogle ScholarPubMed
Schwartz, B., Avivi-Green, C. & Polak-Charcon, S. (1998). Sodium butyrate induces retinoblastoma protein dephosphorylation, p16 expression and growth arrest of colon cancer cells. Mol. Cell. Biochem. 188, 2130.CrossRefGoogle ScholarPubMed
Spinaci, M., Seren, E. & Mattioli, M. (2004). Maternal chromatin remodeling during maturation and after fertilization in mouse oocytes. Mol. Reprod. Dev. 69, 215–21.CrossRefGoogle ScholarPubMed
Tatone, C., Amicarelli, F., Carbone, M.C., Monteleone, P., Caserta, D., Marci, R., Artini, P.G., Piomboni, P. & Focarelli, R. (2008). Cellular and molecular aspects of ovarian follicle ageing. Hum. Reprod. Update 14, 131–42.CrossRefGoogle ScholarPubMed
Wang, Q., Yin, S., Ai, J.S., Liang, C.G., Hou, Y., Chen, D.Y., Schatten, H. & Sun, Q.Y. (2006). Histone deacetylation is required for orderly meiosis. Cell Cycle 5, 766–74.CrossRefGoogle ScholarPubMed