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http://dx.doi.org/10.5713/ajas.2007.1612

Developmental Proteomic Profiling of Porcine Skeletal Muscle during Postnatal Development  

Kim, Nam-Kuk (Department of Applied Biochemistry, College of Biomedical & Health Science Konkuk University)
Lim, Jong-Hyun (Department of Applied Biochemistry, College of Biomedical & Health Science Konkuk University)
Song, Min-Jin (Department of Applied Biochemistry, College of Biomedical & Health Science Konkuk University)
Kim, Oun-Hyun (Department of Animal Science, College of Natural Science, Konkuk University)
Park, Beom-Young (National Institute of Animal Science, Rural Development Admistration)
Kim, Myung-Jick (National Institute of Animal Science, Rural Development Admistration)
Hwang, In-Ho (Department of Animal Resources and Biotechnology, Chonbuk National University)
Lee, Chang-Soo (Department of Applied Biochemistry, College of Biomedical & Health Science Konkuk University)
Publication Information
Asian-Australasian Journal of Animal Sciences / v.20, no.10, 2007 , pp. 1612-1617 More about this Journal
Abstract
In this study, we have compared the skeletal muscle proteome at various stages of porcine postnatal development. Korean native pigs were divided into five postnatal stages of 30, 70, 130, 170 and 300 d and their loin muscles were analyzed for muscle proteome by using two-dimensional electrophoresis and mass spectrometry. We found 5 proteins showing a consistent pattern during skeletal muscle growth. Four proteins were identified as myosin light chain 1 slow-twitch (MLC1sa) isoform, troponin T, triosephosphate isomerase (TIP) and DJ-1 protein. The remaining protein was not identified. Two muscle fiber proteins of MLC1sa isoform and troponin T showed a high expression level at an early postnatal stage and then their levels were decreased markedly during growth stages. On the other hand, the expression of TIP and DJ-1 protein, which are well known as catalysis enzyme and antioxidant-related protein, respectively, were linearly increased during growth stages. Thus, the stage-related muscle proteins may be useful as parameters for understanding the developmental characteristics of biochemical and physiological properties in Korean native pig skeletal muscle.
Keywords
Muscle Proteome; Growth; Two-dimensional Electrophoresis;
Citations & Related Records
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Times Cited By Web Of Science : 4  (Related Records In Web of Science)
Times Cited By SCOPUS : 3
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1 Pontier, P. J. and N. H. Hart. 1981. Developmental expression of glucose and triose phosphate isomerase genes in teleost fishes (brachydanio). J. Exp. Zool. 217:53-71.   DOI   ScienceOn
2 Sabry, M. A. and G. K. Dhoot. 1991. Identification and pattern of transitions of fast skeletal muscle-like developmental and adult isoforms of troponin T in some rat and human skeletal muscle. J. Muscle Res. Cell Motil. 12:447-454.   DOI
3 Sharma, P. M. 1996. Muscle molecular genetics of human. In: Meyers, R. A. Encyclopedia of molecular biology and molecular medicine. Vol 4. Wiley-VCH Verlag-GmbH, Weinheim, Federal Republic of Germany. pp. 133-142.
4 Stadtman, E. R. 1992. Protein oxidation and aging. Science 257:1220-1224.   DOI
5 Millward, D. J., P. J. Garlick, R. J. C. Stewart, D. O. Nnanyelugo and J. C. Waterlow. 1975. Skeletal-muscle growth and protein turnover. Biochem. J. 150:235-243.   DOI
6 Choi, B. H., J. S. Lee, G. W. Jang, H. Y. Lee, J. W. Lee, H. Y. Chung, H. S. Park, S. J. Oh, S. S. Sun, K. H. Myung, I. C. Cheong and T. H. Kim. 2006. Mapping of the porcine calpastatin gene and association study of its variance with economic traits in pigs. Asian-Aust. J. Anim. Sci. 19:1085-1089.   과학기술학회마을   DOI
7 Lefaucheur, L. and P. Vigneron. 1986. Post-natal changes in some histochemical and enzymatic characteristics of three pig muscles. Met Sci. 16:199-216.
8 Perry, S. V. 1998. Troponin-T: Genetics, properties, and function. J. Muscle Res. Cell Motil. 19:575-602.   DOI   ScienceOn
9 Zhang, Y., K. U. Yuksel and R. W. Gracy. 1995. Terminal marking of avian triosephosphate isomerase by deamination and oxidation. Arch. Biochem. Biophys. 317:112-120.   DOI   ScienceOn
10 Hwang, I. H., B. Y. Park, J. H. Kim, S. H. Cho and J. M. Lee. 2005. Assement of postmortem proteolysis by gel-based proteome analysis and its relationship to meat quality traits in pig longissimus. Meat Sci. 69:79-91.   DOI   ScienceOn
11 Jurie, C., J. Robelin, B. Picard and Y. Geay. 1995. Post-natal changes in the biological characteristics of semitendinosus muscle in male limousin cattle. Meat Sci. 41:125-135.   DOI   ScienceOn
12 Kyprianou, P., A. Madgwick, M. Morgan, K. Krishan and G. K. Dhoot. 1997. Expression pattern of troponin I and distinct alternatively spliced developmental isoforms of troponin T in vitro and in neonatally denervated rat skeletal muscles. Basic Appl. Myol. 7:287-293.
13 Moss, R. L., G. M. Diffee and M. L. Greaser. 1995. Contractile properties of skeletal muscle fibers in relation to myofibrillar protein isoforms. Rev. Physiol. Biochem. Pharmac. 126:1-63.   DOI
14 Mahan, D. C. and R. G. Shields, Jr. 1998. Macro- and micromineral composition of pigs from birth to 145 kilograms of body weight. J. Anim. Sci. 76:506-512.
15 Kim, T. H., B. H. Choi, H. K. Lee, H. S.Park, H. Y. Lee, D. H. Yoon, J. W. Lee, G. J. Jeon, I. C. Cheong, S. J. Oh and J. Y. Han. 2005. Identification of quantitative traits loci (QTL) affecting growth traits in pigs. Asian-Aust. J. Anim. Sci. 18:1524-1528.   과학기술학회마을   DOI
16 Mitsumoto, A. and Y. Nakagawa. 2001. DJ-1 is an indicator for endogenous reactive oxygen species elicited by endotoxin. Free Radic. Res. 35:85-893.   DOI   ScienceOn
17 Nagakubo, D., T. Taira, H. Kitaura, M. Ikeda, K. Tamai, S. M. Iguchi-Ariga and H. Ariga. 1997. DJ-1, a novel oncogene which transforms mouse HIH3T3 cells in cooperation with ras. Biochem. Biophys. Res. Commun. 231:509-513.   DOI   ScienceOn
18 Taira, T., Y. Saito, T. Niki, S. M. M. Iguchi-Ariga and K. Takahashi. 2004. DJ-1 has a role in antioxidative stress to prevent cell death. EMBO reports 5:213-218.   DOI   ScienceOn
19 Beal, M. F. 2002. Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32:797-803.   DOI   ScienceOn
20 Bertram, H. C., M. Rasmussen, H. Busk, N. Oksbjerg, A. H. Karlsson and H. J. Andersen. 2002. Change in porcine muscle water characteristics during growth: An in vitro low-field NMR relaxation study. J. Magn. Reson. 157:267-276.   DOI   ScienceOn
21 Bendixen, E. 2005. The use of Proteomics in meat science. Meat Sci. 71:138-149.   DOI   ScienceOn
22 Dickerson, J. W. T. and E. M. Widdowson. 1960. Chemical changes in skeletal muscle during development. Bochem. J. 74:247-257.   DOI
23 Doherty, M. K., L. McLean, J. R. Hayter, J. M. Pratt, D. H. L. Robertson, A. El-Shafei, S. J. Gaskell and R. J. Beynon. 2004. The proteome of chicken skeletal muscle: Changes in soluble protein expression during growth in a layer strain. Proteomics 4:2082-2093.   DOI   ScienceOn
24 Gracy, R. W., J. M. Talent and A. I. Zvaigzne. 1998. Molecular wear and tear leads to terminal marking and the unstable isoforms of aging. J. Exp. Zool. 282:18-27.   DOI   ScienceOn
25 Hailstones, D. L. and P. W. Gunning. 1990. Characterization of human myosin light chains 1sa and 3 nm: Implications for isoform evolution and function. Mol. Cell. Biol. 10:1095-1104.   DOI
26 Hochstrasser, D. F., M. G. Harrington, A. C. Hochstrasser, M. J. Miller and C. R. Merril. 1988. Methods for increasing the resolution of two-dimensional protein electrophoresis. Anal. Biochem. 173:424-435.   DOI   ScienceOn
27 Jin, J. P., A. Chen and Q. Q. Huang. 1998. Three alternatively spliced mouse slow skeletal muscle troponin T isoforms: Conserved primary structure and regulated expressed during postnatal development. Gene 214:121-129.   DOI   ScienceOn