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The relation between dietary restriction or clenbuterol (a selective β2 agonist) treatment on muscle growth and calpain proteinase (EC 3.4.22.17) and calpastatin activities in lambs

Published online by Cambridge University Press:  09 March 2007

Janet A. Higgins ,
Yvonne V. Lasslett ,
R. G. Bardsley  and
P. J. Buttery
Janet A. Higgins
Affiliation:
Department of Applied Biochemistry and Food Science, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics. LE12 5RD
Yvonne V. Lasslett
Affiliation:
Department of Applied Biochemistry and Food Science, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics. LE12 5RD
R. G. Bardsley
Affiliation:
Department of Applied Biochemistry and Food Science, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics. LE12 5RD
P. J. Buttery
Affiliation:
Department of Applied Biochemistry and Food Science, University of Nottingham School of Agriculture, Sutton Bonington, Loughborough, Leics. LE12 5RD
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Abstract

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1. Lamb growth trials were designed to modify growth and protein content of muscle by diet and also by β-agonist treatment, and to correlate any changes to the activities of calpain proteinases (EC 3.4.22.17) and their inhibitor calpastatin.

2. Wether lambs in a control group were fed on a barley-based diet designed to give a growth rate of 350 g/d; a second group was fed on the same diet but the intake was restricted to give an expected gain of 44 g/d; a third group was fed on the same diet as the first group but the diet included 2 mg clenbuterol/g. At the end of a 6-week trial, longissimus dorsi wet weights were 635 (n6), 377 (n4) and 788 g (n6) (standard error of difference 53.0) in the three groups respectively.

3. Minced L. dorsi was extracted in low-salt buffers and analysed by a fast protein liquid-chromatographic system for calpain I (low calcium-requiring), calpain II (high Ca2+-requiring) and calpastatin activities. No significant changes in the three activities were associated with reduced muscle weight in the restricted-intake group. The inclusion of clenbuterol in the diet, however, led to highly significant increases (P < 0.001) in calpain II and calpastatin to approximately double the control values.

4. The results did not support a direct relation between these activities and muscle growth, except when protein accretion was stimulated by a β-agonist, suggesting a role for this enzyme system in the mechanism by which these agents exert their effect.

Type
General Nutrition papers
Information
British Journal of Nutrition , Volume 60 , Issue 3 , November 1988 , pp. 645 - 652
Copyright
Copyright © The Nutrition Society 1988

References

Agricultural Research Council (1980). Nutrient Requirements of Ruminant Livestock. Slough: Commonwealth Agricultural Bureaux.Google Scholar
Baker, P. K., Dalrymple, R. H., Ingle, D. L. & Ricks, C. A. (1984) Journal of Animal Science 59, 1256–1261.CrossRefGoogle Scholar
Ballard, R., Bardsley, R. G. & Buttery, P. J. (1988) British Journal of Nutrition 59, 141–147.CrossRefGoogle Scholar
Bohorov, O., Buttery, P. J., Correia, J. H. R. D. & Soar, J. B. (1987) British Journal of Nutrition 57, 99–107.CrossRefGoogle Scholar
Davidson, J., Mathison, J. & Bone, A. M. (1970) Analyst 95, 181–193.CrossRefGoogle Scholar
Dayton, W. R., Goll, D. E., Stromer, M. H., Reville, W. J., Zeece, M. G. & Robson, R. M. (1975). Cold Spring Harbor Conference on Cell Proliferation: Proteases and Biological Control pp. 551–577. [Reich, E. D. B., Rifkin E., Shaw, editors]. Cold Spring Harbor; N.Y.: The Cold Spring Harbor Laboratory.Google Scholar
Dayton, W. R., Schollmeyer, J. V., Chan, A. C. & Allen, C. E. (1979) Biochimica et Biophysica Acta 584, 216–230.CrossRefGoogle Scholar
Gates, R. E. & King, L. E. (1983) Biochemical and Biophysical Research Communications 113, 255–261.CrossRefGoogle Scholar
Gerard, K. W. & Schneider, D. L. (1980) Biochemical and Biophysical Research Communications 94, 1353–1361.CrossRefGoogle Scholar
Gopapakrishna, R. & Barsky, S. H. (1986) Journal of Biological Chemistry 261, 13936–13942.CrossRefGoogle Scholar
Inomata, M., Hayashi, M., Nakamura, M., Imahori, K. & Kawashima, S. (1983) Journal of Biochemistry 93. 291–294.CrossRefGoogle Scholar
Ishiura, S., Tsuji, S., Murofushi, S. & Suzuki, K. (1982) Biochimica et Biophysica Acta 701, 216–223.CrossRefGoogle Scholar
Kar, N. C. & Pearson, C. M. (1976) Clinica Chimica Acta 73, 293–297.CrossRefGoogle Scholar
Karlsson, J., Gustavsson, S., Hall, C. & Nilsson, E. (1985) Biochemical Journal 231, 201–204.CrossRefGoogle Scholar
Kawashima, S., Nomoto, M., Hayashi, M., Inomata, M., Nakamura, M. & Imahori, K. (1984) Journal of Biochemistry 95, 95–101.CrossRefGoogle Scholar
Kay, J. (1983). Proteases: Potential Role in Health and Disease, pp. 519–531. [Heidland, A., Horl, W.H., editors]. London: Plenum Press.Google Scholar
Lepley, R. A., Pampusch, M. & Dayton, W. R. (1985) Biochimica et Biophysica Acta 828, 95–103.CrossRefGoogle Scholar
Martinez, J. A., Buttery, P. J. & Pearson, J. T. (1984) British Journal of Nutrition 52, 515–521.CrossRefGoogle Scholar
Millward, D. J. (1985) Biochemical Society Transactions 13, 1023–1026.CrossRefGoogle Scholar
Murachi, T., Tanaka, K., Hatanaka, M. & Murakami, T. (1981) Advances in Enzyme Regulation 19, 407–424.CrossRefGoogle Scholar
Nakamura, M., Inomata, M., Hayashi, M., Imahori, K. & Kawashima, S. (1984) Journal of Biochemistry 96, 1399–1407.CrossRefGoogle Scholar
Nishizuka, Y. (1984) Nature 308, 693–698.CrossRefGoogle Scholar
Pemrick, S. M. & Grebenau, R. C. (1984) Journal of Cell Biology 99, 2297–2308.CrossRefGoogle Scholar
Pontremoli, S., Melloni, E. & Horecker, B. L. (1985) Current Topics in Cellular Regulation 27, 293–304.CrossRefGoogle Scholar
Pontremoli, S., Melloni, E., Michetti, M., Sparatore, B., Salamino, F., Sacco, O. & Horecker, B. L. (1987) Proceedings of the National Academy of Sciences, USA 84, 398–401.CrossRefGoogle Scholar
Puca, B. A., Nola, E., Sica, V. & Bresciani, F. (1977) Journal of Biological Chemistry 252, 1358–1366.CrossRefGoogle Scholar
Reeds, P. J., Hay, S. M., Dorwood, P. M. & Palmer, R. M. (1986) British Journal of Nutrition 56, 249–258.CrossRefGoogle Scholar
Ricks, C. A., Dalrymple, R. H., Baker, P. K. & Ingle, D. L. (1984) Journal of Animal Science 59, 1247–1255.CrossRefGoogle Scholar
Sinnett-Smith, P. A., Dumelow, N. W. & Buttery, P. J. (1983) British Journal of Nutrition 50, 225–234.CrossRefGoogle Scholar
Szpacenko, A., Kay, J., Goll, D. E. & Otsuka, Y. (1980). Proceinases and their Inhibitors: Structure, Function and Applied Aspects, pp. 151–161. [Turk, V., Vitale, L.J., editors]. Oxford: Pergamon Press.Google Scholar
Tsuji, S. & Imahori, K. (1981) Journal of Biochemistry 90, 233–240.CrossRefGoogle Scholar
Vedeckis, W. V., Freeman, M. R., Schrader, W. T. & O'Malley, B. (1980) Biochemistry 19, 335–343.CrossRefGoogle Scholar
Vernon, B. G. & Buttery, P. J. (1978) British Journal of Nutrition 40, 563–572.CrossRefGoogle Scholar
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