Differential effects of heat stress on oxidative status of skeletal muscle with different muscle fibre compositions in broiler chicken
M. Kikusato 1  
,   M. Toyomizu 1
More details
Hide details
Tohoku University, Graduate School of Agricultural Science, Division of Life Sciences, Laboratory of Animal Nutrition, 980-8572 Sendai, Japan
M. Kikusato   

Tohoku University, Graduate School of Agricultural Science, Division of Life Sciences, Laboratory of Animal Nutrition, 980-8572 Sendai, Japan
Publication date: 2019-01-31
J. Anim. Feed Sci. 2019;28(1):78–82
Skeletal muscles are composed of two major muscle fibre types, glycolytic and oxidative, which can be differentiated using their mitochondrial content. Mitochondria are a major generator of reactive oxygen species, and muscles have adapted them to possess oxidative resistance to counteract the oxidative damage. The present study aims to clarify the oxidative tolerance of heat stress (HS) in different types of skeletal muscles of broiler chickens. Exposure of 3-week-old broiler chickens to HS conditions (34 °C, 12 h) resulted in significantly higher lipid peroxidation in Musculus pectoralis (Pec), which consists entirely of glycolytic muscle fibres (type IIB), than in thermoneutral (TN) birds. This increase did not occur in gastrocnemius (Gas) muscle, which has a lower proportion of type IIB fibres (65–80%). HS treatment resulted in significantly higher mitochondrial H2O2 production in Pec muscle but not in Gas muscle. In both muscles, HS treatment did not alter the gene expression levels of cytosolic antioxidative enzymes, superoxide dismutase (SOD) 1, catalase and glutathione peroxidase-4. In Pec muscle, there was no difference in SOD2 mRNA levels between TN and HS birds, while avian uncoupling protein (avUCP) was significantly down-regulated by HS treatment. Conversely, in the Gas muscle of HS birds, SOD2 mRNA level was significantly increased while avUCP mRNA level was unchanged. Based on this evidence, it is suggested that the glycolytic muscle (e.g., Gas muscle) in broiler chickens is more susceptible to HS-induced oxidative disturbance, in which avUCP and SOD2 may be involved.
Cantó C., Auwerx J., 2009. PGC-1α, SIRT1 and AMPK, an energy sensing network that controls energy expenditure. Curr. Opin. Lipidol. 20, 98–105,
Hakamata Y., Watanabe K., Amo T., Toyomizu M., Kikusato M., 2018. Characterization of mitochondrial content and respiratory capacities of broiler chicken skeletal muscles with different muscle fiber compositions. J. Poult. Sci. 55, 210–216,
Kikusato M., Nanto F., Mukai K., Toyomizu M., 2016. Effects of trehalose supplementation on the growth performance and intestinal innate immunity of juvenile chicks. Br. Poult. Sci. 57, 375–380,
Kikusato M., Ramsey J.J., Amo T., Toyomizu M., 2010. Application of modular kinetic analysis to mitochondrial oxidative phosphorylation in skeletal muscle of birds exposed to acute heat stress. FEBS Lett. 584, 3143–3148,
Kikusato M., Toyomizu M., 2013. Crucial role of membrane potential in heat stress-induced overproduction of reactive oxygen species in avian skeletal muscle mitochondria. PLoS ONE 8, e64412,
Kikusato M., Toyomizu M., 2015. Moderate dependence of reactive oxygen species production on membrane potential in avian muscle mitochondria oxidizing glycerol 3-phosphate. J. Physiol. Sci. 65, 555–559,
Kikusato M., Yoshida H., Furukawa K., Toyomizu M., 2015. Effect of heat stress-induced production of mitochondrial reactive oxygen species on NADPH oxidase and heme oxygenase-1 mRNA levels in avian muscle cells. J. Thermal. Biol. 52, 8–13,
National Research Council (NRC), 1994. Nutrient Requirements of Poultry: 9th Revised Edition. The National Academies Press. Washington, DC (USA),
Picard M., Hepple R.T., Burelle Y., 2012. Mitochondrial functional specialization in glycolytic and oxidative muscle fibres: tailoring the organelle for optimal function. Am. J. Physiol. Cell Physiol. 302, C629–C641,
Rosado Montilla S.I., Johnson T.P., Pearce S.C., Gardan-Salmon D., Gabler N.K., Ross J.W., Rhoads R.P., Baumgard L.H., Lonergan S.M., Selsby J.T., 2014. Heat stress causes oxidative stress but not inflammatory signaling in porcine skeletal muscle. Temperature 1, 42–50,
Tamura Y., Matsunaga Y., Kitaoka Y., Hatta H., 2017. Effects of heat stress treatment on age-dependent unfolded protein response in different types of skeletal muscle. J. Gerontol. Ser. A Biol. Sci. Med. Sci. 72, 299–308,
Valle I., Álvarez-Barrientos A., Arza E., Lamas S., Monsalve M., 2005. PGC-1α regulates the mitochondrial antioxidant defense system in vascular endothelial cells. Cardiovasc. Res. 66, 562–573,
Williams K., Dhoot G.K., 1992. Heterogeneity and distribution of fast myosin heavy chains in some adult vertebrate skeletal muscles. Histochemistry 97, 361–370,
Yamaguchi T., Suzuki T., Arai H., Tanabe S., Atomi Y., 2010. Continuous mild heat stress induces differentiation of mammalian myoblasts, shifting fiber type from fast to slow. Am. J. Physiol. Cell Physiol. 298, C140–C148,
Zhang L., Zhou Y., Wu W., Hou L., Chen H., Zuo B., Xiong Y., Yang J., 2017. Skeletal muscle-specific overexpression of PGC-1α induces fiber-type conversion through enhanced mitochondrial respiration and fatty acid oxidation in mice and pigs. Int. J. Biol. Sci. 13, 1152–1162,
Nutritional regulation of mitochondrial ROS production of chickens exposed to acute and chronic heat stress
M. Toyomizu, A. Mujahid, R. Hirakawa, K. Furukawa, M.A.K. Azad, M. Taciak, M. Kikusato
Energy and protein metabolism and nutrition
Effects of plant-derived isoquinoline alkaloids on growth performance and intestinal function of broiler chickens under heat stress
Motoi Kikusato, Guangda Xue, Anja Pastor, Theo Niewold, Masaaki Toyomizu
Poultry Science