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Effect of feeding butoxybutyl alcohol on the growth performance and status of skeletal muscle proteolysis in broiler chickens

Published online by Cambridge University Press:  18 February 2015

T. KAMIZONO ,
D. SAPUTRA ,
I. MIURA ,
M. KIKUSATO ,
K. HAYASHI  and
M. TOYOMIZU
T. KAMIZONO
Affiliation:
Animal Nutrition, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan
D. SAPUTRA
Affiliation:
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan
I. MIURA
Affiliation:
Otsuka Pharmaceutical Co., Ltd., 224-18 Ebisuno, Hiraishi, Kagasuno, Tokushima 771-0182, Japan
M. KIKUSATO
Affiliation:
Animal Nutrition, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan
K. HAYASHI
Affiliation:
Department of Biochemical Science and Technology, Faculty of Agriculture, Kagoshima University, 1-21-24 Korimoto, Kagoshima 890-0065, Japan
M. TOYOMIZU*
Affiliation:
Animal Nutrition, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiyamachi, Aoba-ku, Sendai 981-8555, Japan
*
*To whom all correspondence should be addressed. Email: [email protected]
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Summary

Butoxybutyl alcohol (BBA) is a possible growth promoter contained in the fermentation and distillation by-products of a traditional Japanese spirit, shochu. In the present study, BBA was synthesized and its chemical structure was confirmed by gas chromatography mass spectrometry and nuclear magnetic resonance. Then, two studies were conducted to investigate the effects of feeding the synthesized BBA on the growth and skeletal muscle proteolysis of broiler chickens. Ross male broiler chickens were divided into two groups, control (basal diet: 219 g crude protein/kg and 12·66 MJ metabolizable energy/kg) and BBA diet (30 mg BBA/kg basal diet), with the experimental diets being provided from 15 to 27 days and 0 to 27 days of age, for Studies 1 and 2, respectively. Butoxybutyl alcohol supplementation increased final body weight in both studies, whereas feed intake was unchanged, thereby indicating significantly increased feed efficiency. Furthermore, the synthesized BBA increased the weights of the pectoralis superficialis and profundus muscles, and the leg. The BBA decreased the Nτ-methylhistidine concentration in the excrement and plasma, which are indices of the rate of skeletal muscle protein degradation. It also decreased the mRNA levels of μ-calpain large subunit, atrogin-1/muscle atrophy F-box (MAFbx), ubiquitin and 20S proteasome C2 subunit. These suggest that growth promotion due to the feeding of synthesized BBA is caused by the suppression of skeletal muscle protein degradation, which is related to a decrease in gene expression in the calpain and ubiquitin–proteasome systems.

Type
Animal Research Papers
Information
The Journal of Agricultural Science , Volume 153 , Issue 5 , July 2015 , pp. 920 - 928
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Copyright
Copyright © Cambridge University Press 2015 

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References

REFERENCES

Asatoor, A. M. & Armstrong, M. D. (1967). 3-Methylhistidine, a component of actin. Biochemical and Biophysical Research Communications 26, 168–174.CrossRefGoogle ScholarPubMed
Ciechanover, A. (2006). The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology 66 (Suppl. 1), S7–S19.CrossRefGoogle ScholarPubMed
De Boever, S., Vangestel, C., De Backer, P., Croubels, S. & Sys, S. U. (2008). Identification and validation of housekeeping genes as internal control for gene expression in an intravenous LPS inflammation model in chickens. Veterinary Immunology and Immunopathology 122, 312–317.CrossRefGoogle Scholar
Du, J., Wang, X., Miereles, C., Bailey, J. L., Debigare, R., Zheng, B., Price, S. R. & Mitch, W. E. (2004). Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. Journal of Clinical Investigation 113, 115–123.CrossRefGoogle ScholarPubMed
Franch, H. A. & Price, S. R. (2005). Molecular signaling pathways regulating muscle proteolysis during atrophy. Current Opinion in Clinical Nutrition and Metabolic Care 8, 271–275.CrossRefGoogle ScholarPubMed
Glass, D. J. (2005). Skeletal muscle hypertrophy and atrophy signaling pathways. International Journal of Biochemistry and Cell Biology 37, 1974–1984.CrossRefGoogle ScholarPubMed
Goll, D. E., Thompson, V. F., Li, H., Wei, W. & Cong, J. (2003). The calpain system. Physiological Reviews 83, 731–801.CrossRefGoogle ScholarPubMed
Goll, D. E., Neti, G., Mares, S. W. & Thompson, V. F. (2008). Myofibrillar protein turnover: the proteasome and the calpains. Journal of Animal Science 86 (Suppl.), E19–E35.CrossRefGoogle ScholarPubMed
Hayashi, K., Maeda, Y., Toyomizu, M. & Tomita, Y. (1987). High-performance liquid chromatographic method for the analysis of Nτ-methylhistidine in food, chicken excreta, and rat urine. Journal of Nutritional Science and Vitaminology 33, 151–156.CrossRefGoogle Scholar
Johnson, P., Harris, C. I. & Perry, S. V. (1967). 3-Methylhistidine in actin and other muscle proteins. Biochemical Journal 105, 361–370.CrossRefGoogle ScholarPubMed
Kamizono, T., Nakashima, K., Ohtsuka, A. & Hayashi, K. (2010). Effects of feeding hexane-extracts of a shochu distillery by-product on skeletal muscle protein degradation in broiler chicken. Bioscience, Biotechnology, and Biochemistry 74, 92–95.CrossRefGoogle ScholarPubMed
Kamizono, T., Ohtsuka, A., Hashimoto, F. & Hayashi, K. (2013). Dibutoxybutane suppresses protein degradation and promotes growth in cultured chicken muscle cells. Journal of Poultry Science 50, 37–43.CrossRefGoogle Scholar
Mahfudz, L. D., Hayashi, K., Ikeda, M., Hamada, K., Ohtsuka, A. & Tomita, Y. (1996 a). The effective use of shochu distillery by-product as a source of broiler feed. Japanese Poultry Science 33, 1–7.CrossRefGoogle Scholar
Mahfudz, L. D., Hayashi, K., Otsuji, Y., Ohtsuka, A. & Tomita, Y. (1996 b). Separation of growth promoting factor of broiler chicken from shochu distillery by-product. Japanese Poultry Science 33, 96–103.CrossRefGoogle Scholar
Mahfudz, L. D., Nakashima, K., Ohtsuka, A. & Hayashi, K. (1997). Growth factors for a primary chick muscle cell culture from shochu distillery by-products. Bioscience, Biotechnology, and Biochemistry 61, 1844–1847.CrossRefGoogle ScholarPubMed
Mujahid, A., Akiba, Y., Warden, C. H. & Toyomizu, M. (2007). Sequential changes in superoxide production, anion carriers and substrate oxidation in skeletal muscle mitochondria of heat-stressed chickens. FEBS Letters 581, 3461–3467.CrossRefGoogle ScholarPubMed
Nakashima, K., Komatsu, T., Yamazaki, M. & Abe, H. (2005). Effects of fasting and refeeding on expression of proteolytic-related genes in skeletal muscle of chicks. Journal of Nutritional Science and Vitaminology 51, 248–253.CrossRefGoogle ScholarPubMed
Nakashima, K., Ishida, A. & Katsumata, M. (2009). Comparison of proteolytic-related gene expression in the skeletal muscles of layer and broiler chickens. Bioscience, Biotechnology, and Biochemistry 73, 1869–1871.CrossRefGoogle ScholarPubMed
Ohtsuka, A., Kawatomi, N., Nakashima, K., Araki, T. & Hayashi, K. (2011). Gene expression of muscle-specific ubiquitin ligase, atrogin-1/MAFbx, positively correlates with skeletal muscle proteolysis in food-deprived broiler chickens. Journal of Poultry Science 48, 92–96.CrossRefGoogle Scholar
Saleh, A. A., Eid, Y. Z., Ebeid, T. A., Ohtsuka, A., Yamamoto, M. & Hayashi, K. (2012). Feeding Aspergillus awamori reduces skeletal muscle protein breakdown and stimulates growth in broilers. Animal Science Journal 83, 594–598.CrossRefGoogle ScholarPubMed
Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. New York: Cold Spring Harbor Laboratory Press.Google Scholar
Sorimachi, H., Hata, S. & Ono, Y. (2011). Impact of genetic insights into calpain biology. Journal of Biochemistry 150, 23–37.CrossRefGoogle ScholarPubMed
Sultana, M. S., Kamizono, T., Furusono, K. & Hayashi, K. (2011). Shochu distillery by-product loses growth promoting activity during preservation. Journal of Warm Regional Society of Animal Science, Japan 54, 99–105.Google Scholar
Szewczyk, N. J. & Jacobson, L. A. (2005). Signal-transduction networks and the regulation of muscle protein degradation. International Journal of Biochemistry and Cell Biology 37, 1997–2011.CrossRefGoogle ScholarPubMed
Tesseraud, S., Bouvarel, I., Collin, A., Audouin, E., Crochet, S., Seiliez, I. & Leterrier, C. (2009). Daily variations in dietary lysine content alter the expression of genes related to proteolysis in chicken pectoralis major muscle. Journal of Nutrition 139, 38–43.CrossRefGoogle ScholarPubMed
Young, V. R., Alexis, S. D., Baliga, B. S., Munro, H. N. & Muecke, W. (1972). Metabolism of administered 3-methylhistidine. Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methylhistidine and its N-acetyl derivative. Journal of Biological Chemistry 247, 3592–3600.CrossRefGoogle ScholarPubMed