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The effect of a cold environment on protein and energy metabolism in calves

Published online by Cambridge University Press:  09 March 2007

Shannon L. Scott ,
Robert J. Christopherson ,
James R. Thompson  and
Vickie E. Baracos
Shannon L. Scott
Affiliation:
Deparment of Animal Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
Robert J. Christopherson
Affiliation:
Deparment of Animal Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
James R. Thompson
Affiliation:
Deparment of Animal Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
Vickie E. Baracos
Affiliation:
Deparment of Animal Science, University of Alberta, Edmonton, Alberta T6G 2P5, Canada
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Abstract

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Eleven Holstein bull calves 35 d of age were assigned to one of three treatment groups: (1) W72, warm environment (20°), 72 g feed/kg body weight (BW)0.75 per d, (2) C72, cold environment (−5°), 72 g feed/kg BW0·75 per d, or (3) C90, cold environment (−5°), 90 g feed/kg BW0·75 per d. Fractional synthesis rates (FSR) of protein in the rumen wall, rumen papillae, omasum, duodenum, kidney, liver,heart, longissimus dorsi, biceps femoris and skin were determined following a continuous infusion of[3H]phenylalanine. Phenylalanine flux was elevated in both groups of cold-adapted calves. FSR of protein in the two muscles and skin were reduced along with N retention in the calves in the C72 group compared with the other two groups. Muscle protein degradation, estimated from urinary Nτ-methylhistidine excretion, tended to be elevated in both groups of cold-adapted calves. Reduced protein synthesis and increased protein degradation in the C72 group contributed to reduced muscle protein gain. It appears that when feed intake is limited in cold-adapted animals, muscle and skin have a lower priority for nutrients than other organs and tissues, resulting in reduced protein synthesis, it seems unlikely that thermogenesis due to enhanced protein synthesis contributed to the increased heat production in the cold.

Keywords

Cold environmentProtein synthesisProtein metabolismEnergy metabolismCalves
Type
Environmental Effects on Protein and Energy Metabolism
Information
British Journal of Nutrition , Volume 69 , Issue 1 , January 1993 , pp. 127 - 139
Copyright
Copyright © The Nutrition Society 1993

References

REFERENCES

Allison, J. B. & Wannemacher, R. W. Jr (1965). The concept and significance of labile and overall protein reserves of the body. American Journal of Clinical Nutrition 16, 445–452.CrossRefGoogle ScholarPubMed
Ames, D. R., Brink, D. R. & Willms, C. L. (1980). Adjusting protein in feed lot diets during thermal stress. Journal of Animal Science 50, 1–6.CrossRefGoogle Scholar
Aoyagi, Y., Tasaki, I., Okumura, J.-I. & Muramatsu, T. (1988). Effect of low ambient temperature on protein turnover and heat production in chicks. Comparative Biochemistry and Physiology 89A, 433–436.CrossRefGoogle Scholar
Association of Official Analytical Chemists (1984). Official Methods of Analysis, 14th ed. Arlington: AOAC.Google Scholar
Attaix, D. & Arnal, M. (1987). Protein synthesis and growth in the gastrointestinal tract of the young preruminant lamb. British Journal of Nutrition 58, 159–169.CrossRefGoogle Scholar
Baracos, V. E., Brun-Bellut, J. & Marie, M. (1991). Tissue protein synthesis in lactating and dry goats. British Journal of Nutrition 66, 451–465.CrossRefGoogle ScholarPubMed
Brown, J. G., Van Bueren, J. & Millward, D. J. (1984). Differential changes in free and total 3,5,3'-triiodothyronine in cold exposed rats. Proceedings of the Nutrition Society 43, 74A.Google Scholar
Buttery, P. J. & Bryan, L. (1986). Effect of diet and hormones on protein metabolism in muscle. In Nuclear and Related Techniques in Animal Production and Health, pp. 457–468. Vienna: International Atomic Energy Agency.Google Scholar
Fuller, M. F. (1965). The effect of environmental temperature on the nitrogen metabolism and growth of the young pig. British Journal of Nutrition 19, 531–546.CrossRefGoogle ScholarPubMed
Garlick, P. J. & Lobley, G. E. (1987). Dietary intake and protein turnover. Wissenschaftliche Zeitschrift der Wilhelm-Pieck-Universitaet Rostock, Naturwissenschaftliche Reihe 36, 18–21.Google Scholar
Garlick, P. J., Millward, D. J. & James, W. P. T. (1973). The diurnal response of muscle and liver protein synthesis in vivo in meal-fed rats. Biochemical Journal 136, 935–945.CrossRefGoogle ScholarPubMed
Harris, C. I. & Milne, G. (1981). The urinary excretion of N'-methylhistidine by cattle: validation as an index of muscle protein breakdown. British Journal of Nutrition 45, 411–422.CrossRefGoogle Scholar
Hartree, E. F. (1972). Determination of protein: a modification of the Lowry method that gives a linear photometric response. Analytical Biochemistry 48, 422–427.CrossRefGoogle ScholarPubMed
Johnston, D. M., Moody, W. G., Boling, J. A. & Bradley, N. W. (1981). Influence of breed type, sex, feeding systems, and muscle bundle size on bovine fiber type characteristics. Journal of Food Science 46, 1760–1765.CrossRefGoogle Scholar
Jones, B. N. & Gilligan, J. P. (1983). α-Phthaldialdehyde precolumn derivatization and reversed-phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids. Journal of Chromatography 266, 471–482.CrossRefGoogle ScholarPubMed
Lindsay, D. B., Dauncey, M. J., Barker, P. J. & Ingram, D. L. (1988). Protein synthesis and degradation after acclimation to different environmental temperatures and energy intakes. Journal of Thermal Biology 13, 79–83.CrossRefGoogle Scholar
Lobley, G. E., Milne, V., Lovie, J. M., Reeds, P. J. & Pennie, K. (1980). Whole body and tissue protein synthesis in cattle. British Journal of Nutrition 43, 491–502.CrossRefGoogle ScholarPubMed
McAllister, T. (1987). Effect of temperature on protein turnover in the laboratory rat. MSc Thesis, University of Alberta.Google Scholar
McBride, B. W., Early, R. J. & Ball, R. O. (1989). Protein synthesis and the energy costs of Na+, K+-transport in tissues of somatotropin treated steers. In Energy Metabolism of Farm Animals. European Associationfor Animal Production Publication no. 43, pp. 107–110. [van der Honing, Y. and Close, W. H., editors]. Wageningen: Pudoc.Google Scholar
Mclean, J. A. (1972). On the calculation of heat production from open-circuit calorimetric measurements. British Journal of Nutrition 27, 597–600.CrossRefGoogle ScholarPubMed
Nakamura, H. & Pisano, J. J. (1976). Fluorescamine derivatives of histidine, histamine, and certain related imidazoles: unique fluorescence after heating in acid. Archives of Biochemistry and Biophysics 177, 334–335.CrossRefGoogle ScholarPubMed
National Research Council (1978). Nutrient Requirements of Dairy Cattle, 5th ed. Washington, DC: National Academy of Sciences.Google Scholar
Newsholme, E. A. (1987). Substrate cycles and energy metabolism: their biochemical, biological, physiological and pathological importance. In Energy Metabolism of Farm Animals. European Association for Animal Production Publication no. 32, pp. 174–186 [Moe, P. W., Tyrrell, H. F. and Reynolds, P. J., editors]. Totowa, NJ: Rowman and Littlefield.Google Scholar
Nishizawa, N., Toyoda, Y., Noguchi, T., Hareyama, S., Itabashi, H. & Funabiki, R. (1979). N'-Methylhistidine content of organs and tissues of cattle and an attempt to estimate fractional catabolic and synthetic rates of myofibrillar proteins of skeletal muscle during growth by measuring urinary output of N'-methylhistidine. British Journal of Nutrition 42, 247–252.CrossRefGoogle Scholar
Preedy, V. R., McNurlan, M. A. & Garlick, P. J. (1983). Protein synthesis in skin and bone of the young rat. British Journal of Nutrition 49, 511–523.CrossRefGoogle ScholarPubMed
Rannels, D. E., Wartell, S. A. & Watkins, C. A. (1982). The measurement of protein synthesis in biological systems. Life Sciences 30, 1679–1690.CrossRefGoogle ScholarPubMed
Reeds, P. J., Cadenhead, A., Fuller, M. F., Lobley, G. E. & McDonald, J. D. (1980). Protein turnover in growing pigs. Effects of age and food intake. British Journal of Nutrition 43, 445–455.CrossRefGoogle ScholarPubMed
Reeds, P. J. & Fuller, M. F. (1983). Nutrient intake and protein turnover. Proceedings of the Nutrition Society 42, 463–471.CrossRefGoogle ScholarPubMed
SAS Institute Inc. (1985). SAS User's Guide; Statisrics, Version 5 edition. Cary, NC: SAS Institute.Google Scholar
Schaefer, A. L., Davis, S. R. & Hughson, G. A. (1986). Estimation of tissue protein synthesis in sheep during sustained elevation of plasma leucine concentration by intravenous infusion. British Journal of Nutrition 56, 281–288.CrossRefGoogle ScholarPubMed
SPSS Inc. (1988). SPSS-X User's Guide, 3rd ed. Chicago: SPSS Inc.Google Scholar
Steele, R. G. D. & Torrie, J. H. (1980). Principles and Procedures of Statistics. New York: McGraw-Hill Book co.Google Scholar
Suzuki, O. & Yagi, K. (1976). A fluorimetric assay for β-phenylethylamine in rat brain. Analytical Biochemistry 75, 192–200.CrossRefGoogle Scholar
Thompson, J. R., Christopherson, R. J. & Early, R. J. (1987). Cold environmental temperatures increase the rate of skeletal muscle protein breakdown. 66th Annual Feeder's Day Report. Agriculture and Forestry Bulletin of the University of Alberta, pp. 52–54. Edmonton: University of Alberta.Google Scholar
Ugarte, J., Peron, N. & Preston, T. R. (1974). Rearing dairy calves by restricted suckling. V. Carcass composition and ruminal development of calves reared by restricted suckling. Cuban Journal of Agricultural Science 8, 211–218.Google Scholar
Wassner, S. J., Schlitzer, J. R. & Li, J. B. (1980). A rapid, sensitive method for the determination of 3-methylhistidine levels in urine and plasma using high-pressure liquid chromatography. Analytical Biochemistry 104, 284–289.CrossRefGoogle ScholarPubMed
Waterlow, J. C., Garlick, P. J. & Millward, D. J. (1978). Protein Turnover in Mammalian Tissues and in the Whole Body. Amsterdam: Elsevier North Holland.Google Scholar
Webster, A. J. F., Gordon, J. G. & McGregor, R. (1978). The cold tolerance of beef and dairy type calves in the first weeks of life. Animal Production 26, 85–92.Google Scholar
Westra, R. & Christopherson, R. J. (1976). Effects of cold on digestibility, retention time of digesta, reticulum motility and thyroid hormones in sheep. Canadian Journal of Animal Science 56, 699–708.CrossRefGoogle Scholar
Young, B. A., Fenton, T. W. & McLean, J. A. (1984). Calibration methods in respiratory calorimetry. Journal of Applied Physiology 56. 1120–1125.CrossRefGoogle ScholarPubMed
Young, B. A., Kerrigan, B. & Christopherson, R. J. (1975). A versatile respiratory pattern analyzer for studies of energy metabolism of livestock. Canadian Journal of Animal Science 55, 17–22.CrossRefGoogle Scholar