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The effect of clenbuterol on basal protein turnover and endogenous nitrogen loss of sheep

Published online by Cambridge University Press:  09 March 2007

J. E. Inkster ,
F. D. Deb.Hovell ,
D. J. Kyle ,
D. S. Brown  and
G. E. Lobley
J. E. Inkster
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
F. D. Deb.Hovell
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
D. J. Kyle
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
D. S. Brown
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
G. E. Lobley
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
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Abstract

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Seven measurements of the effect of clenbuterol on basal nitrogen excretion (UNE), and protein turnover were made in six female sheep. The sheep were sustained by the intraruminal infusion of energy as volatile fatty acids to provide maintenance, but given no protein (N-free) for 12 d (6 d control, 6 d clenbuterol). Clenbuterol reduced UNE by 20 %, but only on day 2 of the 6 d subperiod. Protein flux (equivalent to degradation on N-free nutrition), measured on day 6 by the irreversible loss of leucine was significantly increased (12%) by clenbuterol. Amino-N oxidation measured by N excretion was unchanged and, therefore, protein synthesis was also increased. During the 12 d N-free period, the recovery of urinary total N (Kjeldahl) as the sum of urea, ammonia, creatinine and purine derivatives, declined from 87.7 to 74.2 %. The form of this missing N was not identified. The effect of clenbuterol of increasing both degradation and synthesis is unlike that reported in the literature for animals receiving protein when, in general, synthesis is unchanged and degradation reduced. This could be due to a different effect of clenbuterol in the N-free state, or to unchanged effects on protein pools other than muscle whose relative contribution to protein metabolism is different in the N-free state.

Keywords

Clenbuterol Nitrogen lossProtein turnoverNitrogen lossSheep
Type
Amino Acids and Proteins: Metabolism and Requirements
Information
British Journal of Nutrition , Volume 62 , Issue 2 , September 1989 , pp. 285 - 296
Copyright
Copyright © The Nutrition Society 1989

References

REFERENCES

Attaix, D., Aurousseau, E., Manghebati, A. & Arnal, M. (1988). Contribution of liver, skin and skeletal muscle to whole-body protein synthesis in the young lamb. British Journal of Nutrition 60, 77–88.CrossRefGoogle ScholarPubMed
Beerman, D.H., Boyd, R.D., Fishell, V.K. & Ross, D.A. (1987). A comparison of the repartitioning effects of cimaterol and somatotrophin on skeletal muscle. Federation Proceedings 29, 1375–1378.Google Scholar
Bohorov, O., Buttery, P.J., Correia, J. H. R. D. & Soar, J.B. (1987). The effect of the β-2-adrenergic agonist clenbuterol or implantation with oestradiol plus trenbolone acetate on protein metabolism in wether lambs. British Journal of Nutrition 57, 99–107.CrossRefGoogle ScholarPubMed
Brockway, J.M., MacRae, J.C. & Williams, P. E. V. (1987). Side effects of clenbuterol as a repartitioning agent. Veterinary Record 120, 381–383.CrossRefGoogle ScholarPubMed
Buttery, P.J. & Dawson, J.M. (1987). The mode of action of beta-agonists as manipulators of carcass composition. In Beta-agonists and Their Effects on Animal Growth and Carcass Quality, pp. 29–43 [Hanrahan, J.P., editor]. London: Elsevier Applied Science.Google Scholar
Davidson, J., Mathieson, J. & Boyne, A.W. (1970). The use of automation in determining nitrogen by the Kjeldahl method, with final calculation by computer. Analyst, London 95, 181–193.CrossRefGoogle ScholarPubMed
Davis, S.R., Barry, T.N. & Hughson, G.A. (1981). Protein synthesis of growing lambs. British Journal of Nutrition 46, 409–419.CrossRefGoogle ScholarPubMed
Emery, P.W., Rothwell, N.J., Stock, M.J. & Winter, P.D. (1984). Chronic effects of β2-adrenergic agonists on body composition and protein synthesis in the rat. Bioscience Reports 4, 83–91.CrossRefGoogle Scholar
Fawcett, J.K. & Scott, J.E. (1960). The determination of urea and ammonia in biological fluids. Journal of Clinical Pathology 13, 156–159.CrossRefGoogle Scholar
Fujihara, T., Chen, X.B., Ørskov, E. R. & Hovell, F.D.DeB. (1988). The possible use of purine derivatives in the urine to estimate rumen microbial protein production. Proceedings of the 5th International Symposium on Protein Metabolism and Nutrition. European Association for Animal Production Publication no. 35, pp. 2-S, 17–18.Google Scholar
Herbert, F., Hovell, F. D.DeB. & Reeds, P.J. (1985). Some preliminary observations on the immediate effects of clenbuterol on heart rate, body temperature and nitrogen retention in lambs wholly nourished by intragastric infusion. Proceedings of the Nutrition Society 44, 150A.Google Scholar
Hovell, F.D.DeB., Kyle, D.J., Reeds, P.J. & Beerman, D.H. (1989). The effect of clenbuterol and cimaterol on the basal nitrogen excretion of sheep. Nutrition Reports International 39, 1177–1182.Google Scholar
Hovell, F. D. DeB., Ørskov, E. R., Kyle, D.J. & MacLeod, N.A. (1987). Undernutrition in sheep. Nitrogen repletion by N-depleted sheep. British Journal of Nutrition 57, 77–88.CrossRefGoogle ScholarPubMed
Kendell, M.G. & Stuart, A. (1963). The Advanced Theory of Statistics, vol. 1. pp. 232–233. London: Charles Griffen.Google Scholar
Kim, Y.S., Lee, Y.B. & Dalrymple, R.H. (1987). Effect of the repartitioning agent cimaterol on growth, carcass and skeletal muscle characteristics in lambs. Journal of Animal Science 65, 1392–1399.CrossRefGoogle ScholarPubMed
Krishnamurti, C.R. & Janssens, S.M. (1988). Determination of leucine metabolism and protein turnover in sheep using gas chromatography–mass spectrometry. British Journal of Nutrition 59, 155–164.CrossRefGoogle Scholar
Lobley, G.E., Connel, A. & Buchan, V. (1987). Effect of food intake on protein and energy metabolism in finishing beef steers. British Journal of Nutrition 57, 457–465.CrossRefGoogle ScholarPubMed
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
McNurlan, M.A., Fern, E.B. & Garlick, P.J. (1982). Failure of leucine to stimulate protein synthesis in vivo. Biochemical Journal 204, 831–838.CrossRefGoogle ScholarPubMed
MacRae, J.C., Skene, P.A., Connell, A., Buchan, V. & Lobley, G.E. (1988). The action of the β-agonist clenbuterol on protein and energy metabolism in fattening wether lambs. British Journal of Nutrition 59, 457–465.CrossRefGoogle ScholarPubMed
Maltin, C.A., Hay, S.M., Delday, M.J., Smith, F.G., Lobley, G.E. & Reeds, P.J. (1987). Clenbuterol, a beta agonist, induces growth in innervated and denervated muscle via apparently different mechanisms. Bioscience Reports 7, 525–532.CrossRefGoogle ScholarPubMed
Maltin, C.A., Reeds, P.J., Delday, M.J., Hay, S.M., Smith, F.G. & Lobley, G.E. (1986). Inhibition and reversal of denervation induced atrophy by the β-agonist growth promoter, clenbuterol. Bioscience Reports 6, 811–817.CrossRefGoogle ScholarPubMed
Marsh, W.H., Fingerhut, B. & Miller, H. (1965). Automated and manual methods for determination of blood ureaxy. Clinical Chemistry 11, 624–627.CrossRefGoogle Scholar
Pell, J.M., Bates, P.C., Elcock, C., Lane, S.E. & Simmonds, A.D. (1987). Growth hormone and clenbuterol: action and interaction on muscle growth, protein turnover and serum IGF-1 concentrations in dwarf mice. Journal of Endocrinology 115, Suppl. 68 Abstr.Google Scholar
Pentz, E.I. (1969). Adaptation of the Rimini-Schryver reaction for the measurement of allantoin in urine to the autoanalyser. Analytical Biochemistry 27, 333–342.CrossRefGoogle Scholar
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., Hay, S.M., Dorwood, P.M. & Palmer, R.M. (1986). Stimulation of muscle growth by clenbuterol: lack of effect on muscle protein biosynthesis. British Journal of Nutrition 56, 249–258.CrossRefGoogle ScholarPubMed
Reeds, P.J., Hay, S.M., Dorwood, P.M. & Palmer, R.M. (1988). The effect of β-agonists and antagonists on muscle growth and body composition of young rats (Rattus sp.). Comparative Biochemistry and Physiology 89C, 337–341.Google ScholarPubMed
Sainz, R.D. & Wolff, J.E. (1988). Effects of the β-agonist, cimaterol, on growth, body composition and energy expenditure in rats. British Journal of Nutrition 60, 84–90.CrossRefGoogle ScholarPubMed
Technicon Instruments Corp. (1965). Creatinine. Method no. N11-A. Tarrytown, NY: Technicon Instruments Corp.Google Scholar
Technicon Instruments Corp. (1979). Uric acid. Method no. SD4-0013FM9. Tarrytown, NY: Technicon Instruments Corp.Google Scholar
Wang, S.Y. & Beerman, D.H. (1988). Reduced calcium dependent proteinase activity in cimaterol-induced muscle hypertrophy in lambs. Journal of Animal Science 66, 2545–2550.CrossRefGoogle ScholarPubMed
Williams, P. E. V. (1987). The use of β-agonists as a means of altering body composition in livestock species. Nutrition Abstracts and Reviews 57, 453–464.Google Scholar