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Developmental Proteomic Profiling of Porcine Skeletal Muscle during Postnatal Development
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 Title & Authors
Developmental Proteomic Profiling of Porcine Skeletal Muscle during Postnatal Development
Kim, Nam-Kuk; Lim, Jong-Hyun; Song, Min-Jin; Kim, Oun-Hyun; Park, Beom-Young; Kim, Myung-Jick; Hwang, In-Ho; Lee, Chang-Soo;
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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.
Muscle Proteome;Growth;Two-dimensional Electrophoresis;
 Cited by
한우 등심조직 내 succinate dehydrogenase 및 triosephosphate isomerase 발현이 근내 지방함량에 미치는 영향에 관한 연구,김남국;이승환;임다정;윤두학;이창수;김언현;김형철;오성종;홍성구;

생명과학회지, 2012. vol.22. 1, pp.31-35 crossref(new window)
Identification of Differentially Expressed Proteins at Four Growing Stages in Chicken Liver,Lee, K.Y.;Jung, K.C.;Jang, B.G.;Choi, K.D.;Jeon, J.T.;Lee, J.H.;

Asian-Australasian Journal of Animal Sciences, 2008. vol.21. 10, pp.1383-1388 crossref(new window)
Differential Proteome Analysis of Breast and Thigh Muscles between Korean Native Chickens and Commercial Broilers,Liu, Xian De;Jayasena, Dinesh D.;Jung, Yeon-Kuk;Jung, Samooel;Kang, Bo-Seok;Heo, Kang-Nyeong;Lee, Jun-Heon;Jo, Cheo-Run;

Asian-Australasian Journal of Animal Sciences, 2012. vol.25. 6, pp.895-902 crossref(new window)
Expression Analysis of miRNAs in Porcine Fetal Skeletal Muscle on Days 65 and 90 of Gestation,Chen, Jian-hai;Wei, Wen-Juan;Xiao, Xiao;Zhu, Meng-Jin;Fan, Bin;Zhao, Shu-Hong;

Asian-Australasian Journal of Animal Sciences, 2008. vol.21. 7, pp.954-960 crossref(new window)
Beal, M. F. 2002. Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32:797-803. crossref(new window)

Bendixen, E. 2005. The use of Proteomics in meat science. Meat Sci. 71:138-149. crossref(new window)

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. crossref(new window)

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.

Dickerson, J. W. T. and E. M. Widdowson. 1960. Chemical changes in skeletal muscle during development. Bochem. J. 74:247-257.

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. crossref(new window)

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. crossref(new window)

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.

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. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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.

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.

Lefaucheur, L. and P. Vigneron. 1986. Post-natal changes in some histochemical and enzymatic characteristics of three pig muscles. Met Sci. 16:199-216.

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.

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.

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. crossref(new window)

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. crossref(new window)

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. crossref(new window)

Perry, S. V. 1998. Troponin-T: Genetics, properties, and function. J. Muscle Res. Cell Motil. 19:575-602. crossref(new window)

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. crossref(new window)

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. crossref(new window)

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.

Stadtman, E. R. 1992. Protein oxidation and aging. Science 257:1220-1224. crossref(new window)

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. crossref(new window)

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. crossref(new window)