Journal of Embryo Transfer (한국수정란이식학회지)

The Korean Society of Embryo Transfer (한국수정란이식학회)
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Study on Chemicals for Post-activation in Porcine Somatic Cell Nuclear Transfer

  • Min, Kyuhong (College of Veterinary Medicine, Chungnam National University) ;
  • Na, Seungwon (College of Veterinary Medicine, Chungnam National University) ;
  • Lee, Euncheol (College of Veterinary Medicine, Chungnam National University) ;
  • Kim, Ghangyong (College of Veterinary Medicine, Chungnam National University) ;
  • Yu, Youngkwang (College of Veterinary Medicine, Chungnam National University) ;
  • Roy, Pantu Kumar (College of Veterinary Medicine, Chungnam National University) ;
  • Fang, Xun (College of Veterinary Medicine, Chungnam National University) ;
  • Salih, MB (College of Veterinary Medicine, Chungnam National University) ;
  • Cho, Jongki (College of Veterinary Medicine, Chungnam National University)
  • Received : 2016.06.24
  • Accepted : 2016.06.28
  • Published : 2016.07.01
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Abstract

Since the first success of animal cloning, somatic cell nuclear transfer presented various ideas in many research areas such as regenerative medicine. However, SCNT embryos has poor survival rate. Therefore, numerous researches carried out to enhance the developmental capability of porcine nuclear transfer embryos. Cytochalasin B, demecolcine, latrunculin A, cycloheximide and 6-dimethylaminopurine are efficient chemicals treated in post-activation procedure to increase the efficiency of SCNT. This review study is aim to investigate the effects of these chemicals applied to post-activation in porcine SCNT. Cytochalasin B, demecolcine, latrunculin A are cytoskeletal manuplators inhibit extrusion of pseudo-polar body. Cytochalasin B and demecolcine showed considerably higher blastocyst formation proportion (26-28%) compared to when they are not treated (16%). And when latrunculin A was treated for postactivation, blastocyst formation proportion was increased in SCNT embryos exposed to LA (38%) than those in control (14%). On the other hand, cycloheximide and 6-dimethylaminopurine are protein synthesis and kinase inhibitors. And they help to maintain $Ca^{2+}$ fluctuation in oocytes. Cleavage and blastocyst rates of NT embryos were increased when they were exposed to CHX (16.9% and 5.4% with no CHX).And 6-DMAP also showed higher blastocyst formation (21.5% compared to 15.7%, control). Although all these chemicals have different mechanisms, they showed developmental competence enhancement in NT embryos. However, there are only few studies comparing each chemical's post-activation effect. Therefore, further research and study should be conducted to find optimal chemical for improving the efficiency of SCNT.

Keywords

References

  1. Bai C, Liu H, Liu Y, Wu X, Cheng L, Bou S, Li GP. 2011. Diploid oocyte formation and tetraploid embryo development induced by cytochalasin B in bovine. Cell Reprogram 13(1):37-45. https://doi.org/10.1089/cell.2010.0038
  2. Baliga BS, Pronczuk AW, Munro HN. 1969. Mechanism of cycloheximide inhibition of protein synthesis in a cell-free system prepared from rat liver. J Biol Chem 244(16):4480-4489.
  3. Cooper JA. 1987. Effects of cytochalasin and phalloidin on actin. J Cell Biol 105(4):1473-1478. https://doi.org/10.1083/jcb.105.4.1473
  4. Copeland M. 1974. The cellular response to cytochalasin B: a critical overview. Cytologia (Tokyo) 39(4):709-727. https://doi.org/10.1508/cytologia.39.709
  5. Dustin P. 1974. Some recent advances in the study of microtubules and microtubule poisons. Arch Biol (Liege) 85(2):263-288.
  6. Gordo AC, He CL, Smith S, Fissore RA. 2001. Mitogen activated protein kinase plays a significant role in metaphase II arrest, spindle morphology, and maintenance of maturation promoting factor activity in bovine oocytes. Mol Reprod Dev 59(1):106-114. https://doi.org/10.1002/mrd.1012
  7. Himaki T, Mizobe Y, Tsuda K, Suetomo M, Yamakuchi H, Miyoshi K, Takao S, Yoshida M. 2012. Effect of postactivation treatment with latrunculin A on in vitro and in vivo development of cloned embryos derived from kidney fibroblasts of an aged Clawn miniature boar. J Reprod Dev 58(4):398-403. https://doi.org/10.1262/jrd.11-083A
  8. Himaki T, Mori H, Mizobe Y, Miyoshi K, Sato M, Takao S, Yoshida M. 2010. Latrunculin A dramatically improves the developmental capacity of nuclear transfer embryos derived from gene-modified clawn miniature pig cells. Cell Reprogram 12(2):127-131. https://doi.org/10.1089/cell.2009.0066
  9. Im GS, Samuel M, Lai L, Hao Y, Prather RS. 2007. Development and calcium level changes in pre-implantation porcine nuclear transfer embryos activated with 6-DMAP after fusion. Mol Reprod Dev 74(9):1158-1164. https://doi.org/10.1002/mrd.20492
  10. Im GS, Seo JS, Hwang IS, Kim DH, Kim SW, Yang BC, Yang BS, Lai L, Prather RS. 2006. Development and apoptosis of pre-implantation porcine nuclear transfer embryos activated with different combination of chemicals. Mol Reprod Dev 73(9):1094-1101. https://doi.org/10.1002/mrd.20455
  11. Katoh M, Araki A, Ogura T, Valdivia RP. 2004. 6-Dimethylaminopurine (6-DMAP), which is used to produce most cloned animals, is mutagenic in Salmonella typhimurium TA1535. Mutat Res 560(2):199-201. https://doi.org/10.1016/j.mrgentox.2004.03.003
  12. Lai L, Kolber-Simonds D, Park KW, Cheong HT, Greenstein JL, Im GS, Samuel M, Bonk A, Rieke A, Day BN, Murphy CN, Carter DB, Hawley RJ, Prather RS. 2002. Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning. Science 295(5557):1089-1092. https://doi.org/10.1126/science.1068228
  13. Lee J, You J, Kim J, Hyun SH, Lee E. 2010. Postactivation treatment with nocodazole maintains normal nuclear ploidy of cloned pig embryos by increasing nuclear retention and formation of single pronucleus. Theriogenology 73(4):429-436. https://doi.org/10.1016/j.theriogenology.2009.09.026
  14. Liu L, Ju JC, Yang X. 1998. Parthenogenetic development and protein patterns of newly matured bovine oocytes after chemical activation. Mol Reprod Dev 49(3):298-307. https://doi.org/10.1002/(SICI)1098-2795(199803)49:3<298::AID-MRD10>3.0.CO;2-T
  15. MacLean-Fletcher S, Pollard TD. 1980. Mechanism of action of cytochalasin B on actin. Cell 20(2):329-341. https://doi.org/10.1016/0092-8674(80)90619-4
  16. Martinez Diaz MA, Suzuki M, Kagawa M, Ikeda K, Takahashi Y. 2003. Effects of cycloheximide treatment on in-vitro development of porcine parthenotes and somatic cell nuclear transfer embryos. Jpn J Vet Res 50(4):147-155.
  17. Park SJ, Park HJ, Koo OJ, Choi WJ, Moon JH, Kwon DK, Kang JT, Kim S, Choi JY, Jang G, Lee BC. 2012. Oxamflatin improves developmental competence of porcine somatic cell nuclear transfer embryos. Cell Reprogram 14(5):398-406. https://doi.org/10.1089/cell.2012.0007
  18. Rieder CL, Palazzo RE. 1992. Colcemid and the mitotic cycle. J Cell Sci 102 (Pt 3):387-392.
  19. Scherlach K, Boettger D, Remme N, Hertweck C. 2010. The chemistry and biology of cytochalasans. Nat Prod Rep 27(6):869-886. https://doi.org/10.1039/b903913a
  20. Schneider-Poetsch T, Ju J, Eyler DE, Dang Y, Bhat S, Merrick WC, Green R, Shen B, Liu JO. 2010. Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat Chem Biol 6(3):209-217. https://doi.org/10.1038/nchembio.304
  21. Song K, Hyun SH, Shin T, Lee E. 2009. Post-activation treatment with demecolcine improves development of somatic cell nuclear transfer embryos in pigs by modifying the remodeling of donor nuclei. Mol Reprod Dev 76(7):611-619. https://doi.org/10.1002/mrd.20989
  22. Susko-Parrish JL, Leibfried-Rutledge ML, Northey DL, Schutzkus V, First NL. 1994. Inhibition of protein kinases after an induced calcium transient causes transition of bovine oocytes to embryonic cycles without meiotic completion. Dev Biol 166(2):729-739. https://doi.org/10.1006/dbio.1994.1351
  23. Szollosi MS, Kubiak JZ, Debey P, de Pennart H, Szollosi D, Maro B. 1993. Inhibition of protein kinases by 6-dimethylaminopurine accelerates the transition to interphase in activated mouse oocytes. J Cell Sci 104 (Pt 3):861-872.
  24. Theodoropoulos PA, Gravanis A, Tsapara A, Margioris AN, Papadogiorgaki E, Galanopoulos V, Stournaras C. 1994. Cytochalasin B may shorten actin filaments by a mechanism independent of barbed end capping. Biochem Pharmacol 47(10):1875-1881. https://doi.org/10.1016/0006-2952(94)90318-2
  25. Wakatsuki T, Schwab B, Thompson NC, Elson EL. 2001. Effects of cytochalasin D and latrunculin B on mechanical properties of cells. J Cell Sci 114(Pt 5):1025-1036.
  26. Wang WH, Abeydeera LR, Prather RS, Day BN. 1998. Functional analysis of activation of porcine oocytes by spermatozoa, calcium ionophore, and electrical pulse. Mol Reprod Dev 51(3):346-353. https://doi.org/10.1002/(SICI)1098-2795(199811)51:3<346::AID-MRD15>3.0.CO;2-0
  27. Yarmola EG, Somasundaram T, Boring TA, Spector I, Bubb MR. 2000. Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J Biol Chem 275(36):28120-28127.