Korean Journal of Fisheries and Aquatic Sciences (한국수산과학회지)

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Molecular Cloning and Expression Pattern of Abalone (Haliotis discus hannai) Myostatin cDNA

참전복(Haliotis discus hannai) Myostatin 유전자의 cDNA 동정 및 발현 분석

  • Lee, Sang-Beum (Division of Marine Molecular Biotechnology, Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University) ;
  • Kim, Jeong-Hwan (Department of Biotechnology, Pukyong National University) ;
  • Jo, Mi-Jin (Division of Marine Molecular Biotechnology, Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University) ;
  • Oh, Mi-Young (Division of Marine Molecular Biotechnology, Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University) ;
  • Park, Heum-Gi (Division of Marine Food Science & Technology, Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University) ;
  • Jin, Hyung-Joo (Division of Marine Molecular Biotechnology, Faculty of Marine Bioscience and Technology, Kangnung-Wonju National University)
  • 이상범 (강릉원주대학교 해양생명공학부 해양분자생명) ;
  • 김정환 (부경대학교 생물공학과) ;
  • 조미진 (강릉원주대학교 해양생명공학부 해양분자생명) ;
  • 오미영 (강릉원주대학교 해양생명공학부 해양분자생명) ;
  • 박흠기 (강릉원주대학교 해양생명공학부 해양자원육성) ;
  • 진형주 (강릉원주대학교 해양생명공학부 해양분자생명)
  • Received : 2009.01.30
  • Accepted : 2009.04.09
  • Published : 2009.04.30
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Abstract

We cloned and sequenced the open reading frame (ORF) cDNA encoding myostatin from the muscle of abalone (Haliotis discus hannai). The ORF cDNA of the abalone myostatin is 1134 bp and encoded 377 amino acid residues that were 60-96% homologous with the amino acids of other organism myostatins. In addition, the ORF contained a conserved proteolytic cleavage site (RXRR) and nine conserved cysteine residues in the C-terminus. Semi-quantitative RT-PCR revealed the presence of myostatin mRNA in various tissues. The strongest expression was observed in the mantle of female abalone, and the gills and heart of male abalone.

Keywords

References

  1. Amali, A.A., C.J. Lin, Y.H. Chen, W.L. Wang, H.Y. Gong, C.Y. Lee, Y.L. Ko, J.K. Lu, G.M. Her, T.T. Chen and J.L. Wu. 2004. Up-regulation of muscle-specific transcription factors during embryonic somitogenesis of zebrafish (Danio rerio) by knock-down of myostatin-1. Dev. Dyn., 229, 847-856 https://doi.org/10.1002/dvdy.10454
  2. Acosta, J., Y. Carpio, I. Borroto, O. Gonzalez and M.P. Estrada. 2005. Myostatin gene silenced by RNAi show a zebrafish giant phenotype. J. Biotechnol., 119, 324-331 https://doi.org/10.1016/j.jbiotec.2005.04.023
  3. Biga, P.R., S.B. Roberts, D.B. Iliev, L.A. McCauley, J.S. Moon, P. Collodi and F.W. Goetz. 2005. The isolation, characterization, and expression of a novel GDF11 gene and a second myostatin form in zebrafish, Danio rerio. Comp. Biochem. Physiol. B Biochem. Mol. Biol., 141, 218-230 https://doi.org/10.1016/j.cbpc.2005.03.004
  4. Chenna, R., H. Sugawara, T. Koike, R. Lopez, T.J. Gibson, D.G. Higgins and J.D. Thompson. 2003. Multiple sequence alignment with the clustal series of programs. Nucleic Acids Res., 31, 3497-3500 https://doi.org/10.1093/nar/gkg500
  5. Grobet, L., L.J. Marvtin, D. Poncelet, D. Pirottin, B. Brouwers, J. Riquet, A. Schoeberlein, S. Dunner, F. Menissier, J. Massabanda, R. Fries, R. Hanset and M. Georges. 1997. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. NAT. Genet., 17, 71-74 https://doi.org/10.1038/ng0997-71
  6. Delgado, I., E. Fuentes, S. Escobar, C. Navarro, T. Corbeaux, A.E. Reyes, M.I. Vera, M. Alvarez and A. Molina. 2008. Temporal and spatial expression pattern of the myostatin gene during larval and juvenile stages of the Chilean flounder (Paralichthys adspersus). Comp. Biochem. Physiol. B., 151, 197-202 https://doi.org/10.1016/j.cbpb.2008.07.003
  7. Gonzalez-Cadavid, N.F., W.E. Taylor, K. Yarasheski, I. Sinha-Hikim, K. Ma, S. Ezzat, R. Shen, R. Lalani, S. Asa, M. Mamita, G. Nair, S. Arver and S. Bhasin. 1998. Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. Proc. Natl. Acad. Sci. USA, 95, 14938-14943 https://doi.org/10.1073/pnas.95.25.14938
  8. Hall, T.A. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser., 41, 95-98
  9. Kambadur, R., M. Sharma, T.P. Smith and J.J. Bass. 1977. Mutations in myostatin (GDF8) in double-muscled Belgian blue and Piedmontese cattle. Genome Res., 7, 910-916
  10. Kimurá, M. 1980. A simple method for estimating evolutionary rate of base substitution through comparative studies of nucleotide sequences. J. Mol. Evol., 16, 116-120
  11. Kocamis, H., D.C. Kirkpatrick-Keller, J. Richter and J. Killefer. 1999. The ontogeny of myostatin, follistatin andactivin-B mRNA expression during chicken embryonic development. Growth Dev. Aging, 63, 143-150
  12. Kumar, S., K. Tamura and M. Nei. 2004. MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform., 5, 150-163 https://doi.org/10.1093/bib/5.2.150
  13. Lin, J., H.B. Arnold and M.A. Della-Fera. 2002. Myostatin knockout in mice increases myogenesis and decreases adipogenesis. Biochme. Biophys. Res. Commun., 291, 701-706 https://doi.org/10.1006/bbrc.2002.6500
  14. Lee, S.B., Y.S. Kim, M.G. Yoon, S.K. Kim, I.K. Jang, H.J. Lim and H.J. Jin. 2007. Characterization and expression pattern of the partial myostatin cDNA in shrimp, Fenneropenaeus chinensis J. Marin Biotech. Biosci., 2, 224-229
  15. McPherron, A.C. and S.J. Lee. 1997. Double muscling in cattle due to mutations in the myostatin gene. Proc. Natl. Acad. Sci. USA, 94, 12457-12461 https://doi.org/10.1073/pnas.94.23.12457
  16. McPherron, A.C. and S.J. Lee. 2002. Suppression of body fat accumulation in myostatin deficient mice. J. Clin. Invest., 109, 595-601 https://doi.org/10.1172/JCI0213562
  17. Robert, S.B. and F.W. Goetz. 2003. Myostatin protein and RNA transcript levels in adult and developing brook trout. Mol. Cell. Endocrinol., 210, 9-20 https://doi.org/10.1016/j.mce.2003.09.002
  18. Sambrook, T., E.F. Fritsch and T. Maniatis. 1989. Molecular Cloning: A Laboratory Manual. Cold Spring Habor Laboratory Press, New York
  19. Sharma, M., R. Kambadur, K.G. Matthews, W.G. Somers, G.P. Devlin, J.V. Conaglen, P.J. Fowke and J.J. Bass. 1999. Myostatin, a transforming growth factor-beta superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct. J. Cell. Physiol., 180, 1-9 https://doi.org/10.1002/(SICI)1097-4652(199907)180:1<1::AID-JCP1>3.0.CO;2-V
  20. Tomas, M., B. Langley, C. Berry, M. Sharma, S. Kirk, J. Bass and R. Kambadur. 2000. Myostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation J. Biol. Chem., 275, 40235-40243 https://doi.org/10.1074/jbc.M004356200
  21. Xu, C., G. Wu, Y. Zohar and S.J. Du. 2003. Analysis of myostatin gene structure, expression and function in zebrafish. J. Exp. Biol., 206, 4067-4079 https://doi.org/10.1242/jeb.00635

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