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Dynamics of myosin heavy chain isoform transition in the longissimus muscle of domestic and wild pigs during growth: a comparative study

Published online by Cambridge University Press:  27 June 2016


G. Fazarinc
Affiliation:
Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia
M. Vrecl
Affiliation:
Veterinary Faculty, University of Ljubljana, Gerbičeva 60, 1000 Ljubljana, Slovenia
D. Škorjanc
Affiliation:
Faculty of Agriculture and Life Sciences, University of Maribor, Pivola 10, 2311 Hoče, Slovenia
T. Čehovin
Affiliation:
Administration of the Republic of Slovenia for Food Safety, Veterinary Sector and Plant Protection, Dunajska cesta 22, 1000 Ljubljana, Slovenia
M. Čandek-Potokar
Affiliation:
Agricultural Institute of Slovenia, Hacquetova ulica 17, 1000 Ljubljana, Slovenia
Corresponding

Abstract

Dynamics of myofiber differentiation/maturation in porcine skeletal muscle is associated with domestication, breeding and rearing conditions. This study was aimed to comparatively elucidate the age-dependent myosin heavy chain (MyHC) isoform expression and transition pattern in domestic and wild pig (WP) skeletal muscle from birth until adulthood. Domestic pigs (DPs) of Large White breed raised in conventional production system were compared with WPs reared in a large hunting enclosure. Muscle samples for immuno/enzyme histochemistry were taken from the longissimus dorsi muscle within 24 h postmortem at 24 to 48 h, 21 to 23 days, 7 months and ~2 years postpartum. Based on the antibody reactivity to MyHCs (NCL-MHCs, A4.74, BF-F3) and succinate dehydrogenase activity, myofibers were classified into I, I/IIa, IIa, IIx and IIb types. In addition, foetal MyHC expression was determined with the use of F158.4C10 antibody. Maturation of the longissimus dorsi muscle in the WP was characterized by an accelerated transformation of the fast to slow MyHC during the first hours postpartum, followed by differentiation towards oxidative myofibers in which type I, IIa and IIx MyHCs predominated. In the DP, the transformation shifted towards glycolytic myofibers that expressed MyHC-IIb. The expression of foetal MyHC was higher in the DP than in the WP at 1 day of age, and the decline in the foetal MyHC during the first 3 weeks was more rapid in the WP than in the DP denoting an accelerated early postnatal muscle maturation in WP than DP piglets. All foetal MyHC-positive myofibers co-expressed IIa isoform, but not vice versa. The intense myofiber hypertrophy was evident from 3 weeks until 7 months of age. In this period, the myofiber cross-sectional area increased up to 10- and 20-fold in the WP and the DP, respectively. In the DP, the hypertrophy of all myofiber types was more pronounced than in the WP, particularly the hypertrophy of IIx and IIb myofibers. To summarize, the comparison between growing DP with wild ancestors showed that genetic selection and rearing conditions lead to substantial changes in the direction and intensity of postnatal MyHC transformation as evidenced by different proportion of individual myofiber types and differences in their hypertrophic potential.


Type
Research Article
Copyright
© The Animal Consortium 2016 

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References

Bee, G 2004. Effect of early gestation feeding, birth weight, and gender of progeny on muscle fiber characteristics of pigs at slaughter. Journal of Animal Science 82, 826836.CrossRefGoogle Scholar
Berard, J, Kalbe, C, Losel, D, Tuchscherer, A and Rehfeldt, C 2011. Potential sources of early-postnatal increase in myofibre number in pig skeletal muscle. Histochemistry and Cell Biology 136, 217225.CrossRefGoogle Scholar
Bogucka, J, Kapelanski, W, Elminowska-Wenda, G, Walasik, K and Lewandowska, KL 2008. Comparison of microstructural traits of Musculus longissimus lumborum in wild boars, domestic pigs and wild boar/domestic pig hybrids. Archiv Fur Tierzucht 51, 359365.Google Scholar
Bottinelli, R, Betto, R, Schiaffino, S and Reggiani, C 1994. Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle. Journal of Muscle Research and Cell Motility 15, 413419.CrossRefGoogle Scholar
Chang, KC and Fernandes, K 1997. Developmental expression and 5′ end cDNA cloning of the porcine 2x and 2b myosin heavy chain genes. DNA and Cell Biology 16, 14291437.CrossRefGoogle Scholar
Eizema, K, van den Burg, M, Kiri, A, Dingboom, EG, van Oudheusden, H, Goldspink, G and Weijs, WA 2003. Differential expression of equine myosin heavy-chain mRNA and protein isoforms in a limb muscle. The Journal of Histochemistry and Cytochemistry 51, 12071216.CrossRefGoogle Scholar
Fazarinc, G, Ursic, M, Kantura, V, Vukicevic, T, Skrlep, M and Candek-Potokar, M 2013. Expression of myosin heavy chain isoforms in longissimus muscle of domestic and wild pig. Slovenian Veterinary Research 50, 6774.Google Scholar
Gagniere, H, Picard, B and Geay, Y 1999. Contractile differentiation of foetal cattle muscles: intermuscular variability. Reproduction Nutrition Development 39, 637655.CrossRefGoogle ScholarPubMed
Graziotti, GH, Menendez, JMR, Rios, CM, Cossu, ME, Bosco, A, Affricano, NO, Ceschel, AP, Moisa, S and Basso, L 2011. Relationship between myosin isoforms and meat quality traits in pig semitendinosus neuromuscular compartments. Asian-Australasian Journal of Animal Sciences 24, 125129.CrossRefGoogle Scholar
Graziotti, GH, Rios, CM and Rivero, JL 2001. Evidence for three fast myosin heavy chain isoforms in type II skeletal muscle fibers in the adult llama (Lama glama). The Journal of Histochemistry and Cytochemistry 49, 10331044.CrossRefGoogle Scholar
Harrison, AP, Rowlerson, AM and Dauncey, MJ 1996. Selective regulation of myofiber differentiation by energy status during postnatal development. The American Journal of Physiology 270, R667R674.Google ScholarPubMed
Herpin, P, Lossec, G, Schmidt, I, Cohen-Adad, F, Duchamp, C, Lefaucheur, L, Goglia, F and Lanni, A 2002. Effect of age and cold exposure on morphofunctional characteristics of skeletal muscle in neonatal pigs. Pflugers Archiv – European Journal of Physiology 444, 610618.CrossRefGoogle ScholarPubMed
Lefaucheur, L, Ecolan, P, Lossec, G, Gabillard, JC, Butler-Browne, GS and Herpin, P 2001. Influence of early postnatal cold exposure on myofiber maturation in pig skeletal muscle. Journal of Muscle Research and Cell Motility 22, 439452.CrossRefGoogle ScholarPubMed
Lefaucheur, L, Ecolan, P, Plantard, L and Gueguen, N 2002. New insights into muscle fiber types in the pig. The Journal of Histochemistry and Cytochemistry 50, 719730.CrossRefGoogle ScholarPubMed
Lefaucheur, L, Edom, F, Ecolan, P and Butler-Browne, GS 1995. Pattern of muscle fiber type formation in the pig. Developmental Dynamics 203, 2741.CrossRefGoogle ScholarPubMed
Lefaucheur, L, Hoffman, RK, Gerrard, DE, Okamura, CS, Rubinstein, N and Kelly, A 1998. Evidence for three adult fast myosin heavy chain isoforms in type II skeletal muscle fibers in pigs. Journal of Animal Science 76, 15841593.CrossRefGoogle ScholarPubMed
Lefaucheur, L, Le Dividich, J, Mourot, J, Monin, G, Ecolan, P and Krauss, D 1991. Influence of environmental temperature on growth, muscle and adipose tissue metabolism, and meat quality in swine. Journal of Animal Science 69, 28442854.CrossRefGoogle ScholarPubMed
Losel, D, Franke, A and Kalbe, C 2013. Comparison of different skeletal muscles from growing domestic pigs and wild boars. Archiv Fur Tierzucht 56, 766777.Google Scholar
Mascarello, F, Stecchini, ML, Rowlerson, A and Ballocchi, E 1992. Tertiary myotubes in postnatal growing pig muscle detected by their myosin isoform composition. Journal of Animal Science 70, 18061813.CrossRefGoogle ScholarPubMed
Muller, E, Rutten, M, Moser, G, Reiner, G, Bartenschlager, H and Geldermann, H 2002. Fibre structure and metabolites in M. longissimus dorsi of wild boar, Pietrain and Meishan pigs as well as their crossbred generations. Journal of Animal Breeding and Genetics 119, 125137.CrossRefGoogle Scholar
Nachlas, MM, Tsou, KC, de Souza, E, Cheng, CS and Seligman, AM 1957. Cytochemical demonstration of succinic dehydrogenase by the use of a new p-nitrophenyl substituted ditetrazole. The Journal of Histochemistry and Cytochemistry 5, 420436.CrossRefGoogle Scholar
Pette, D and Staron, RS 2000. Myosin isoforms, muscle fiber types, and transitions. Microscopy Research and Technique 50, 500509.3.0.CO;2-7>CrossRefGoogle ScholarPubMed
Rehfeldt, C, Henning, M and Fiedler, I 2008. Consequences of pig domestication for skeletal muscle growth and cellularity. Livestock Science 116, 3041.CrossRefGoogle Scholar
Ruusunen, M and Puolanne, E 2004. Histochemical properties of fibre types in muscles of wild and domestic pigs and the effect of growth rate on muscle fibre properties. Meat Science 67, 533539.CrossRefGoogle ScholarPubMed
Schiaffino, S, Gorza, L, Pitton, G, Saggin, L, Ausoni, S, Sartore, S and Lomo, T 1988. Embryonic and neonatal myosin heavy chain in denervated and paralyzed rat skeletal muscle. Developmental Biology 127, 111.CrossRefGoogle ScholarPubMed
Schiaffino, S, Gorza, L, Sartore, S, Saggin, L, Ausoni, S, Vianello, M, Gundersen, K and Lomo, T 1989. Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. Journal of Muscle Research and Cell Motility 10, 197205.CrossRefGoogle ScholarPubMed
Smerdu, V, Cehovin, T, Strbenc, M and Fazarinc, G 2009. Enzyme- and immunohistochemical aspects of skeletal muscle fibers in brown bear (Ursus arctos). Journal of Morphology 270, 154161.CrossRefGoogle Scholar
Smerdu, V, Karsch-Mizrachi, I, Campione, M, Leinwand, L and Schiaffino, S 1994. Type IIx myosin heavy chain transcripts are expressed in type IIb fibers of human skeletal muscle. The American Journal of Physiology 267, C1723C1728.Google ScholarPubMed
Strbenc, M, Smerdu, V, Zupanc, M, Tozon, N and Fazarinc, G 2004. Pattern of myosin heavy chain isoforms in different fibre types of canine trunk and limb skeletal muscles. Cells, Tissues, Organs 176, 178186.CrossRefGoogle Scholar
Szentkuti, L and Schlegel, O 1985. Genetic and functional effects on fiber type composition and fiber diameters in the longissimus muscle of the thorax and the semitendinous muscle of swine. Studies of exercised domestic swine and wild swine kept under restricted mobility. Deutsche Tierärztliche Wochenschrift 92, 9397.Google ScholarPubMed
Talmadge, RJ, Grossman, EJ and Roy, RR 1996. Myosin heavy chain composition of adult feline (Felis catus) limb and diaphragm muscles. The Journal of Experimental Zoology 275, 413420.3.0.CO;2-R>CrossRefGoogle ScholarPubMed
Tanabe, R, Muroya, S and Chikuni, K 1998. Sequencing of the 2a, 2x, and slow isoforms of the bovine myosin heavy chain and the different expression among muscles. Mammalian Genome 9, 10561058.CrossRefGoogle ScholarPubMed
Weiler, U, Appell, HJ, Kremser, M, Hofacker, S and Claus, R 1995. Consequences of selection on muscle composition. A comparative study on gracilis muscle in wild and domestic pigs. Anatomia Histologia Embryologia 24, 7780.CrossRefGoogle ScholarPubMed
Wilson, SJ, McEwan, JC, Sheard, PW and Harris, AJ 1992. Early stages of myogenesis in a large mammal: formation of successive generations of myotubes in sheep tibialis cranialis muscle. Journal of Muscle Research and Cell Motility 13, 534550.CrossRefGoogle Scholar
Wimmers, K, Ngu, NT, Jennen, DG, Tesfaye, D, Murani, E, Schellander, K and Ponsuksili, S 2008. Relationship between myosin heavy chain isoform expression and muscling in several diverse pig breeds. Journal of Animal Science 86, 795803.CrossRefGoogle ScholarPubMed

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