Hostname: page-component-848d4c4894-cjp7w Total loading time: 0 Render date: 2024-06-19T16:14:29.102Z Has data issue: false hasContentIssue false
  • English
  • Français

Age-related changes and nutritional regulation of myosin heavy-chain composition in longissimus dorsi of commercial pigs

Published online by Cambridge University Press:  14 June 2013

X. M. Men ,
B. Deng ,
Z. W. Xu ,
X. Tao  and
K. K. Qi
X. M. Men
Affiliation:
Institute of Animal Husbandry and Veterinary Science, Zhejiang Academy of Agricultural Science, Hangzhou 310021, China
B. Deng
Affiliation:
Institute of Animal Husbandry and Veterinary Science, Zhejiang Academy of Agricultural Science, Hangzhou 310021, China
Z. W. Xu*
Affiliation:
Institute of Animal Husbandry and Veterinary Science, Zhejiang Academy of Agricultural Science, Hangzhou 310021, China
X. Tao
Affiliation:
Institute of Animal Husbandry and Veterinary Science, Zhejiang Academy of Agricultural Science, Hangzhou 310021, China
K. K. Qi
Affiliation:
Institute of Animal Husbandry and Veterinary Science, Zhejiang Academy of Agricultural Science, Hangzhou 310021, China
*
†E-mail: xzwfyz@sina.com
Get access

Abstract

The objective of this study is to investigate the age-related changes of and the effects of dietary conjugated linoleic acid (CLA) on muscle-fibre types in commercial pigs. We divided 25 crossbred male pigs into five age groups (7, 30, 60, 100 and 180 days) and 30 finishing pigs into two dietary groups (one fed a CLA-enriched diet and the other fed a control diet for 30 days). We analysed the composition (%) of myosin heavy-chain (MyHC) mRNA according to the absolute copies of each MyHC (I, IIa, IIb and IIx) mRNA, and the activities of succinate dehydrogenase (SDH) and malate dehydrogenase (MDH) in the longissimus muscle. From days 7 to 180, the MyHC I mRNA abundance and SDH and MDH activities presented a decreasing trend, the MyHC IIb mRNA abundance presented a steady trend and the MyHC IIa and IIx mRNA abundances presented an increasing trend. On day 30, MyHC I and IIb mRNA abundances were at their lowest (P < 0.05), and the MyHC IIa and IIx mRNA abundances were at their highest (P < 0.05). In the CLA group, the MyHC I mRNA abundance and the activities of SDH and MDH were improved in the longissimus muscle, whereas pressure loss, drip loss and average back fat depth significantly decreased (P < 0.01) and shear force significantly increased (P < 0.01). Loin eye area, feed conversion rate and meat colour showed some tendency to be improved. These results indicated that more oxidative fibres might convert to glycolytic fibres with increasing age or weight, and that the early developmental stage might be a key stage for this conversion. During the finishing stage, the proportion of oxidative fibres might be increased by dietary CLA supplementation, which may contribute to the water-holding capacity of meat. The results would provide an important basis for the application of muscle-fibre types in the improvement of pork quality.

Keywords

age-related changesMyHCCLAmuscle-fibre typespork quality
Type
Physiology and functional biology of systems
Information
animal , Volume 7 , Issue 9 , September 2013 , pp. 1486 - 1492
Copyright
Copyright © The Animal Consortium 2013 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Abreu, E, Quiroz-Rothe, E, Mayoral, AI, Vivo, JM, Robina, A, Guillen, MT, Aguera, E, Rivero, JL 2006. Myosin heavy chain fibre types and fibre sizes in nuliparous and primiparous ovariectomized Iberian sows: interaction with two alternative rearing systems during the fattening period. Meat Science 74, 359–372.CrossRefGoogle ScholarPubMed
Baldwin, KM, Haddad, F 2001. Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. Journal of Applied Physiology 90, 345–357.Google Scholar
Bassaganya-Riera, J, Reynolds, K, Martino-Catt, S, Cui, Y, Hennighausen, L, Gonzalez, F, Rohrer, J, Benninghoff, AU, Hontecillas, R 2004. Activation of PPAR gamma and delta by conjugated linoleic acid mediates protection from experimental inflammatory bowel disease. Gastroenterology 127, 777–791.Google Scholar
Bassel-Duby, R, Olson, EN 2006. Signaling pathways in skeletal muscle remodeling. Annual Review of Biochemistry 75, 19–37.Google Scholar
Bee, G, Guex, G, Herzog, W 2004. Free-range rearing of pigs during the winter: adaptations in muscle fiber characteristics and effects on adipose tissue composition and meat quality traits. Journal of Animal Science 82, 1206–1218.CrossRefGoogle ScholarPubMed
Bertram, HC, Purslow, PP, Andersen, HJ 2002. Relationship between meat structure, water mobility and distribution: a low field nuclear magnetic resonance study. Journal of Agriculture and Food Chemistry 50, 824–829.CrossRefGoogle ScholarPubMed
Bigard, X, Sanchez, H, Zoll, J, Mateo, P, Rousseau, V, Veksler, V, Ventura-Clapier, R 2000. Calcineurin co-regulates contractile and metabolic components of slow muscle phenotype. Journal of Biological Chemistry 275, 19653–19660.CrossRefGoogle ScholarPubMed
Bottinelli, R, Reggiani, C 2000. Human skeletal muscle fibres: molecular and functional diversity. Progress in Biophysics and Molecular Biology 73, 195–262.CrossRefGoogle ScholarPubMed
Chang, KC 2007. Key signaling factors and pathways in the molecular determination of skeletal muscle phenotype. Animal 1, 681–698.Google Scholar
Chang, KC, 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, 1429–1437.Google Scholar
Chang, KC, Fernander, K, Dauncey, MJ 1995. Molecular characterization of a developmentally regulated porcine skeletal myosin heavy chain gene and its 5′ regulatory region. Journal of Cell Science 108, 1779–1789.Google Scholar
Chang, KC, Fernander, K, Gldspink, G 1993. In vivo expression and molecular characterization of the porcine slow myosin heavy chain. Journal of Cell Science 106, 331–341.Google Scholar
Choi, YM, Kim, BC 2009. Muscle fiber characteristics, myofibrillar protein isoforms and meat quality. Livestock Science 122, 105–118.Google Scholar
Clark, KA, McElhinny, AS, Beckerle, MC, Gregorio, CC 2002. Striated muscle cytoarchitecture: an intricate web of form and function. Annual Review of Cell Developmental Biology 18, 637–706.CrossRefGoogle ScholarPubMed
Delling, U, Tureckova, J, Lim, HW, De Windt, LJ, Rotwein, P, Molkentin, JD 2000. A calcineurin-NFATc3-dependent pathway regulates skeletal muscle differentiation and slow myosin heavy-chain expression. Molecular and Cellular Biology 20, 6600–6611.Google Scholar
Dugan, MER, Aalhus, JL, Kramer, JKG 2004. Conjugated linoleic acid pork research. American Journal of Clinic Nutrition 79, 1212S–1216S.Google Scholar
Gondret, F, Combes, S, Lefaucheur, L, Lebret, B 2005. Effects of exercise during growth and alternative rearing systems on muscle fibers and collagen properties. Reproduction Nutrition Development 45, 69–86.Google Scholar
Guo, J, Shan, T, Wu, T, Zhu, LN, Ren, Y, An, S, Wang, YZ 2011. Comparisons of different muscle metabolic enzymes and muscle fiber types in Jinhua and Landrace pigs. Journal of Animal Science 89, 185–191.Google Scholar
Honikel, K, Kim, C, Hamm, R 1986. Sarcomere shortening of prerigor muscles and its influence on drip loss. Meat Science 16, 267–282.CrossRefGoogle ScholarPubMed
Hu, HM, Wang, JY, Zhu, RS, Guo, JF, Wu, Y 2008. Effect of myosin heavy chain composition of muscles on meat quality in Laiwu pigs and Duroc. Science in China Series C, Life Sciences 51, 127–132.Google Scholar
Huang, JX, Yang, FY, Liu, ZH, Jiang, S, Xiao, R 2010. Effect of conjugated linoleic acid on the composition of myofiber types in skeletal muscle cells of pigs in vitro. Chinese Journal of Animal and Veterinary Sciences 41, 295–300 (in Chinese).Google Scholar
Kauffman, RG, Eikelenboom, G, van der Wal, PG, Engel, B, Zaar, M 1986. A comparison of methods to estimate water-holding capacity in post-rigor porcine muscle. Meat Science 18, 307–322.Google Scholar
Kim, NK, Lim, JH, Song, MJ, Kim, OH, Park, BY, Kim, MJ, Hwang, IH, Lee, CS 2008. Comparisons of longissimus muscle metabolic enzymes and muscle fiber types in Korean and western pig breeds. Meat Science 78, 455–460.Google Scholar
Lefaucheur, L, Ecolan, P, Barzic, YM, Marion, J, Le Dividich, J 2003. Early postnatal food intake alters myofiber maturation in pig skeletal muscle. Journal of Nutrition 133, 140–147.Google Scholar
Lundstrom, K, Malmfors, G 1985. Variation in light scatter and water-holding capacity along the porcine longissimus dorsi muscle. Meat Science 15, 203–214.Google Scholar
Meadus, WJ, MacInnis, R, Dugan, MER 2002. Prolonged dietary treatment with conjugated linoleic acid stimulates porcine muscle peroxisome proliferator activated receptor g and glutamine fructose aminotransferase gene expression in vivo. Journal of Molecular Endocrinology 28, 79–86.Google Scholar
Murphy, EF, Jewell, C, Hooiveld, GJ, Muller, M, Cashman, KD 2006. Conjugated linoleic acid enhances transepithelial calcium transport in human intestinal-like Caco-2 cells: an insight into molecular changes. Prostaglandins, Leukotrienes and Essential Fatty Acids 74, 295–301.Google Scholar
Narkar, VA, Downes, M, Yu, RT, Embler, E, Wang, YX, Banayo, E, Mihaylova, MM, Nelson, MC, Zou, YH, Juguilon, H, Kang, HJ, Shaw, RJ, Evans, RM 2008. AMPK and PPARd agonists are exercise mimetics. Cell 134, 405–415.Google Scholar
Pearce, KL, Rosenvold, K, Andersen, HJ, Hopkins, DL 2011. Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes—a review. Meat Science 89, 111–124.Google Scholar
Pette, D, Staron, RS 2000. Myosin isoforms, muscle fiber types, and transitions. Microscopy Research and Technique 50, 500–509.3.0.CO;2-7>CrossRefGoogle ScholarPubMed
Ryu, YC, Kim, BC 2005. The relationship between muscle fiber characteristics, postmortem metabolic rate, and meat quality of pig longissimus dorsi muscle. Meat Science 71, 351–357.Google Scholar
Ryu, YC, Choi, YM, Lee, SH, Shin, HG, Choe, JH, Kim, JM, Hong, KC, Kim, BC 2008. Comparing the histochemical characteristics and meat quality traits of different pig breeds. Meat Science 80, 363–369.CrossRefGoogle ScholarPubMed
Schiaffino, S, Reggiani, C 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiological Reviews 76, 371–423.Google Scholar
Schiaffino, S, Reggiani, C 2011. Fiber types in mammalian skeletal muscles. Physiological Reviews 91, 1447–1531.Google Scholar
Spangenburg, EE, Booth, FW 2003. Molecular regulation of individual skeletal muscle fibre types. Acta Physiologica Scandinavica 178, 413–424.Google Scholar
Tanabe, R, Muroya, S, Chikuni, K 1999. Expression of myosin heavy chain isoforms in porcine muscle determined by multiplex PCR. Journal of Food Science 64, 222–225.Google Scholar
Tanabe, R, Murakami, T, Kawahara, T, Yamashiro, R, Mitsumoto, M, Muroya, S, Nakajima, I, Chikuni, K 2001. Composition of myosin heavy chain isoforms in relation to meat texture in Duro, Landrace and Meishan pigs. Journal of Animal Science 72, 230–237.Google Scholar
United States National Research Council 1998. Nutrient Requirement of Swine. 10th edition. National Academy Press, Washington, DCGoogle Scholar