Hostname: page-component-78c5997874-dh8gc Total loading time: 0 Render date: 2024-11-18T05:39:39.794Z Has data issue: false hasContentIssue false
  • English
  • Français

Metabolic control and future opportunities for growth regulation

Published online by Cambridge University Press:  02 September 2010

P. J. Reeds
P. J. Reeds
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB2 9SB
Get access

Extract

The last 10 years have seen a significant expansion in the scope of attempts to manipulate the growth of animals (Buttery, Lindsay and Haynes, 1986). The expansion of interest has been driven by a number of factors, both economic and theoretical. At the economic level the need to develop energetically and economically efficient strategies of animal production has been coupled with a renewed awareness of the implications for human health of excessive intakes of saturated fats. Emphasis then has switched from the maximization of weight gain as an end in itself towards a need to promote protein deposition at any given intake and, at the same time, to reduce the fat content of meat and meat products. These twin objectives might be achieved by one of three strategies: the promotion of protein deposition alone, because at any given rate of weight gain this will tend to minimize the rate of fat deposition (the so-called repartitioning effect); the reduction of fat gain (an approach that has received particularly close attention by those concerned primarily with human obesity); or ideally the simultaneous promotion of protein accretion and depression of that of fat.

Type
Invited paper
Information
Animal Production , Volume 45 , Issue 2 , October 1987 , pp. 149 - 169
Copyright
Copyright © British Society of Animal Science 1987

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Abdel-Latif, A. A. 1986. Calcium-mobilizing receptors, polyphosphoinositides, and the generation of second messengers. Pharmacological Reviews 42: 227–272.Google Scholar
Abdel-Latif, A. A., Akhtar, R. A. and Hawthorne, J. N. 1977. Acetylcholine increases the breakdown of triphosphoinositide of rabbit iris muscle prelabelled with [32P] phosphate. Biochemical Journal 162: 61–73.CrossRefGoogle ScholarPubMed
Baker, P. K., Dalrymple, R. H., Ingle, D. L. and Ricks, C. A. 1984. Use of a (β-adrenergic agonist to alter muscle and fat deposition in lambs. Journal of Animal Science 59: 1256–1261.CrossRefGoogle Scholar
Begum, N., Thpperman, H. M. and Tepperman, J. 1985. Studies on the possible involvement of prostaglandins in insulin generation of pyruvate dehydrogenase activater. Diabetes 34: 29–37.CrossRefGoogle Scholar
Berridge, M. J. 1984. Inositol trisphosphate and diacylglycerol as second messengers. Biochemical Journal 220: 345–360.CrossRefGoogle ScholarPubMed
Berridge, M. J., Heslop, J. P., Irvine, R. F. and Brown, K. D. 1984. Inositol trisphosphate formation and calcium mobilization in Swiss 3T3 cells in response to platelet derived growth factor. Biochemical Journal 222: 195–201.CrossRefGoogle ScholarPubMed
Berridge, M. J. and Irvine, R. F. 1984. Inositol trisphosphate, a novel second messenger in cellular signal transduction. Nature, London 312: 315–321.CrossRefGoogle ScholarPubMed
Beynon, R. J. and Bond, J. S. 1986. Catabolism of intracellular protein: molecular aspects. American Journal of Physiology 251: C141–C152.CrossRefGoogle ScholarPubMed
Bolt, D. J., PurseL, V. G., Hammer, R. E., Wall, R. J., Palmiter, R. D. and Brinster, R. L. 1986. Plasma concentrations of human growth hormone and porcine growth hormone in transgenic pigs. Journal of Animal Science 54: Suppl. 1, p. 220 (Abstr.).Google Scholar
Brown, J. G. and Millward, D. J. 1983. Dose response of protein turnover in rat skeletal muscle to triiodothyronine treatment. Biochimica Biophysica Acta 757: 182–186.CrossRefGoogle ScholarPubMed
Buttery, P. J., Lindsay, D. B. and Haynes, N. B. 1986. Control and Manipulation of Animal Growth. Butterworths, London.Google Scholar
Canalis, E. 1983. The hormonal and local regulation of bone formation. Endocrinological Reviews 4: 62–11.CrossRefGoogle ScholarPubMed
Centrella, M. and Canalis, E. 1985. Local regulators of skeletal growth; a perspective. Endocrinological Reviews 6: 544–551.CrossRefGoogle ScholarPubMed
Chung, C. S., Etherton, T. D. and Wiggins, J. P. 1985. Stimulation of swine growth by porcine growth hormone. Journal of Animal Science 60: 118–130.CrossRefGoogle ScholarPubMed
Clegg, J. S. 1984. Properties and metabolism of the aqueous-cytoplasm and its boundaries. American Journal of Physiology 246: R133–R151.Google ScholarPubMed
Cohen, R., Pacifici, M., Rubinstein, N., Biehl, J. and Holtzer, H. 1977. Effect of tumour promoter on myogenesis. Nature, London 266: 538–540.CrossRefGoogle ScholarPubMed
Conde, R. D. and Scornik, O. A. 1976. Role of protein degradation in the growth of livers after a nutritional shift. Biochemical Journal 158: 385–390.CrossRefGoogle ScholarPubMed
Coughlin, S. R., Moskowitz, M. A., Zetter, B. R., Antoniaoes, H. N. and Levine, L. 1981. Platelet-dependent stimulation of prostacyclin synthesis by platelet-derived growth factor. Nature, London 288: 600–602.CrossRefGoogle Scholar
Crabtree, B. and Newsholme, E. A. 1985. A quantitative approach to metabolic control. Current Topics in Cellular Regulation 25: 21–76.CrossRefGoogle ScholarPubMed
Damuni, Z., Caudwell, B. and Cohen, P. 1982. Regulation of the aminoacyl-tRNA synthctase complex of rat liver by phosphorylation-dephosphorylation in vitro and in vivo. European Journal of Biochemistry 129: 57–65.CrossRefGoogle Scholar
Darnell, J., Lodish, H. and Baltimore, D. 1986. Molecular Cell Biology, pp. 476–486. Scientific American, New York.Google Scholar
Dulloo, A. G. and Miller, D. S. 1984. Thermogenic drugs for the treatment of obesity: sympathetic stimulants in animal models. British Journal of Nutrition 52: 179–196.CrossRefGoogle ScholarPubMed
Eiswmann, J. H., Hammond, A. C., Rumsey, T. S. and Bauman, D. E. 1986. Tissue protein synthesis rates in beef steers injected with placebo or bovine growth hormone. Journal of Animal Science 63: Suppl. 1, p. 217 (Abstr.).Google Scholar
Ernst, V., Levin, D. H., Foulkes, J. G. and London, I. M. 1982. Effects of skeletal muscle protein phosphatase inhibitor-2 on protein synthesis and protein phosphorylation in rabbit reticulocyte lysates. Proceedings of the National Academy of Sciences, USA 79: 7092–7096.CrossRefGoogle ScholarPubMed
Fagan, J. M. and Goldberg, A. L. 1985. Inhibitors of protein and RNA synthesis cause a rapid block of prostaglandin production at the prostaglandin synthase step. Proceedings of the National Academy of Sciences, USA 83: 2771–2775.CrossRefGoogle Scholar
Fagan, J. M., Waxman, L. and Goldberg, A. L. 1987. Skeletal muscle and liver contain a soluble ATP+ubiquitin-dependent proteolytic system. Biochemical Journal 243: 335–343.CrossRefGoogle ScholarPubMed
Farese, R. V. 1985. The phosphatidate-phosphoinositide cycle: an intracellular messenger system in the actions of hormones and neurotransmitters. Metabolism 32: 628–641.CrossRefGoogle Scholar
Fisher, S. K., Hootman, S. R., Heacock, A. M., Ernst, S. A. and Agranoff, B. W. 1983. Muscarinic stimulation of phospholipid turnover in dissociated avian salt glands. Federation of European Biochemical Societies Letters 155: 43–46.CrossRefGoogle Scholar
Flint, D. J. and Futter, C. E. 1985. Immunological manipulation of body fat. Hannah Research 1985, pp. 123–127. Hannah Research Institute, Ayr.Google Scholar
Foulkes, J. G., Jefferson, L. S. and Cohen, P. 1980. The hormonal control of glycogen metabolism: dephosphorylation of protein-phosphatase inhibitor-1 in vivo in response to insulin. Federation of European Biochemical Societies Letters 112: 21–24.CrossRefGoogle ScholarPubMed
Fuller, M. F., Reeds, P. J., Cadenhead, A., Seve, B. and Preston, T. 1986. Effects of the amount and quality of dietary protein on amino acid, nitrogen and energy metabolism and their interrelationships in growing pigs. In Energy Metabolism of Farm Animals (ed. Moe, P. W., Tyrell, H. J. and Reynolds, P. J.), pp. 2–5. Rowman and Littlefield, Totowa, New Jersey.Google Scholar
Fuller, M. F., Weekes, T. E. C., Cadenhead, A. and Bruce, J. B. 1977. The protein-sparing effect of carbohydrate. 2. The role of insulin. British Journal of Nutrition 38: 489–496.CrossRefGoogle ScholarPubMed
Garlick, P. J. 1980. Protein turnover in the whole animal and in specific tissues. In Comprehensive Biochemistry (ed. Florkin, M., Neuberger, A. and Deeman, L. L. M. Van), Vol. 19B. Protein Metabolism, pp. 77–152. Elsevier, Amsterdam.Google Scholar
Garlick, P. J., Fern, M. and Preedy, V. R. 1983. The effect of insulin infusion and food intake on muscle protein synthesis in postabsorptive rat. Biochemical Journal 210: 669–676.CrossRefGoogle Scholar
Goldspink, D. F., Garlick, P. J. and McNurlan, M. A. 1983. Protein turnover measured in vivo and in vitro in muscles undergoing compensatory growth and subsequent denervation atrophy. Biochemical Journal 210: 89–98.CrossRefGoogle ScholarPubMed
Goldspink, D. F. and Kelly, F. J. 1984. Protein turnover and growth in the whole-body, liver and kidney of the rat from foetus to senility. Biochemical Journal 217: 507–516.CrossRefGoogle ScholarPubMed
Goldspink, D. F., Lewis, S. E. M. and Kelly, F. J. 1984. Protein synthesis during developmental growth of the small and large intestine of the rat. Biochemical Journal 217: 527–535.CrossRefGoogle ScholarPubMed
Goodman, M. N. 1987. Differential effects of acute changes in Ca2 concentrations of myofibrillar and non-myofibrillar protein breakdown in the rat extensor digitorum longus muscle in vitro. Biochemical Journal 244: 121–125.CrossRefGoogle Scholar
Hammer, R. E., Brinster, R. L., Rosenfeld, M. G., Evans, R. M. and Mayo, K. E. 1985. Expressions of human growth hormone-releasing factor in transgenic mice results in increased somatic growth. Nature, London 315: 413–416.CrossRefGoogle ScholarPubMed
Harris, R. A., Powell, S. M., Paxton, R., Gillim, G. E. and Nagak, H. 1985. Physiological covalent regulation of rat liver branched chain a-keto acid dehydrogenase. Archives of Biochemistry and Biophysics 243: 542–548.CrossRefGoogle Scholar
Hart, I. C. and Johnsson, I. D. 1986. Growth hormone and growth in meat producing animals. In Control and Manipulation of Animal Growth (ed. Buttery, P. J., Lindsay, D. B. and Haynes, N. B.), pp. 135–161. Butterworths, London.CrossRefGoogle Scholar
Hassid, A. 1982. Regulation of prostaglandin biosynthesis in cultured cells. American Journal of Physiology 243: C203–C211.CrossRefGoogle ScholarPubMed
Hecker, E. 1968. Carcinogenic principles from the seed-oil of Croton Tiglium and from other Euphorbiacaeae. Cancer Research 28: 2338–2349.Google Scholar
Hesketh, J. E. and Campbell, G. 1987. Effects of insulin, pertussis and cholera toxins on protein synthesis and diacylglycerol production in 3T3 fibroblasts. Bioscience Reports 7: In press.Google Scholar
Hesketh, J. E., Campbell, G. and Reeds, P. J. 1986. Rapid response of protein synthesis to insulin in 3T3 cells. Effect of protein kinase-C depletion and difference from the response to serum. Bioscience Reports 6: 797–804.CrossRefGoogle ScholarPubMed
Hirata, F., Matsuda, K., Notsu, Y., Hattori, T. and Carmine, R. Del. 1984. Phosphorylation at a tyrosine residue of lipomodulin in mitogen-stimulated murine thymocytes. Proceedings of the National Academy of Sciences, USA 18: 4717–4721.CrossRefGoogle Scholar
Hokin, M. R. and Hokin, L. E. 1953. Enzyme secretion and the incorporation of P32 into phospholipids of pancreas slices. Journal of Biological Chemistry 203: 967–977.CrossRefGoogle ScholarPubMed
Houslay, M. D. 1984. A family of guanine nucleotide regulatory proteins. Trends in Biochemical Science 9: 39–40.CrossRefGoogle Scholar
Houslay, M. D. and Heyworth, C. M. 1983. Insulin: in search of a mechanism. Trends in Biochemical Science 8: 449–452.CrossRefGoogle Scholar
Houslay, M. D., Wakelam, M. J. O. and Pyne, N. J. 1986. The mediator is the message: is it part of insulin's action. Trends in Biochemical Science 11: 393–395.CrossRefGoogle Scholar
Ingebritsen, T. S. and Cohen, P. 1983. Protein phosphatases: properties and role in cellular regulation. Science, Washington 221: 331–338.CrossRefGoogle ScholarPubMed
Irvine, R. F. 1984. How is the level of free arachidonic acid controlled? Biochemical Journal 204: 3–16.CrossRefGoogle Scholar
Jacobs, F. A., Bird, R. C. and Sells, B. H. 1985. Differentiation of rat myoblasts. Regulation of turnover of ribosomal proteins and their mRNA's. European Journal of Biochemistry 150: 255–263.CrossRefGoogle Scholar
Jarett, L. and Seals, J. R. 1979. Pyruvate dehydrogenase activation in adipocyte mitochondria by an insulin-generated mediator from muscle. Science, Washington 206: 1407–1408.CrossRefGoogle ScholarPubMed
Kishimoto, A., Kajikawa, N., Shiota, M. and Nishizuka, Y. 1983. Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by a calcium dependent neutral protease. Journal of Biological Chemistry 258: 1156–1164.CrossRefGoogle ScholarPubMed
Krebs, E. G. and Beavo, J. A. 1979. Phosphorylation and dephosphorylation of enzymes. Annual Review of Biochemistry 48: 923–959.CrossRefGoogle ScholarPubMed
Larner, J., Cheng, K., Schwartz, C., Kikuchi, K., Tamura, S., Creacy, S., Dubler, R., Galasko, G., Pullin, C. and Katz, M. 1982. Insulin mediators and their control of metabolism through protein phosphorylation. Recent Progress in Hormone Research 38: 511–556.Google ScholarPubMed
Larner, J., Cheng, K., Schwartz, C., Rubler, K., Creacy, S., Kikuchi, K., Tamura, K., Galasko, G., Pullin, C. and Katz, M. 1981. Chemical mechanism of insulin action via proteolytic formation of mediator peptides. Molecular and Cellular Biochemistry 40: 155–161.CrossRefGoogle ScholarPubMed
Larner, J., Galasko, G., Cheng, K., Depaoli-Roach, A. A., Huang, L., Daggy, P. and Kellogg, J. 1979. Generation by insulin of a chemical mediator that controls protein phosphorylation and dephosphorylation. Science, Washington 206: 1408–1410.CrossRefGoogle ScholarPubMed
Laurent, G. J., Sparrow, M. P. and Millward, D. J. 1978. Turnover of muscle protein in the fowl. Changes in the rates of protein synthesis and breakdown during hypertrophy of the anterior and posterior latissimus dorsi muscles. Biochemical Journal 176: 407–417.CrossRefGoogle ScholarPubMed
Laycock, J. G. 1983. Identification and metabolism of polyphosphoinositides in isolated islets of Langerhans. Biochemical Journal 216: 101–106.CrossRefGoogle Scholar
Levine, L. and Hassid, A. 1977. Epidermal Growth Factor stimulated prostaglandin synthesis by canine kidney (MDCK) cells. Biochemical and Biophysical Research Communications 76: 1181–1187.CrossRefGoogle ScholarPubMed
Lewis, S. E. M., Kelly, F. J. and Goldspink, D. F. 1984. Pre- and post-natal growth and protein turnover in smooth muscle, heart and slow- and fast-twitch muscles of the rat. Biochemical Journal 111: 517–526.CrossRefGoogle Scholar
Lobley, G. E., Connell, A., Mollison, G., Brewer, A., Harris, C. I., Buchan, V. and Galbraith, H. 1985. The effects of a combined implant of trenbolone acetate and oestradiol-17β on protein and energy metabolism in finishing beef steers. British Journal of Nutrition 54: 681–694.CrossRefGoogle Scholar
Lobley, G. E., Milne, V., Lovie, J., Reeds, P. J. and Pennie, K. 1980. Whole body and tissue protein synthesis in cattle. British Journal of Nutrition 43: 491–502.CrossRefGoogle ScholarPubMed
MacAulay, S. L. and Jarett, L. 1985. Insulin mediator causes dephosphorylation of the α-subunit of pyruvate dehydrogenase by stimulating phosphatase activity. Archives of Biochemistry and Biophysics 237: 142–150.CrossRefGoogle ScholarPubMed
McGrath, J. A. and Goldspink, D. F. 1982. Glucocorticoid action on protein synthesis and protein breakdown in isolated skeletal muscles. Biochemical Journal 206: 641–645.CrossRefGoogle ScholarPubMed
McMillan, D. N. 1987. The role of prostaglandins in the control of protein turnover in the tissues of the rat and the rainbow trout (Salmo ganeri, Richardson). Ph.D. Thesis, University of Aberdeen.Google Scholar
McNuklan, M. A., Tomkins, A. M. and Garlick, P. J. 1979. The effect of starvation on the rate of protein synthesis in rat liver and small intestine. Biochemical Journal 178: 373–379.CrossRefGoogle Scholar
Mailer, J. L., Pike, L. J., Freidenberg, G. R., Cordera, R., Stith, B. J., Olefsky, J. M. and Krebs, E. G. 1986. Increased phosphorylation of ribosomal protein S6 following microinjection of insulin receptor-kinase into Xenopus oocytes. Nature, London 320: 459–461.CrossRefGoogle Scholar
Mayer, R. J. and Doherty, F. 1986. Intracellular protein catabolism: the state of the art. Federation of European Biochemical Societies Letters 198: 181–193.CrossRefGoogle Scholar
Melloni, E., Pontremolli, S., Michetti, M., Sacco, O., Sparatore, B. and Horecker, B. L. 1986. The involvement of calpain in the activation of protein kinase-C in neutrophils stimulated by phorbol myristic acid. Journal of Biological Chemistry 261: 4101–4105.CrossRefGoogle ScholarPubMed
Millward, D. J., Garlick, P. J. and Reeds, P. J. 1976. The energy cost of growth. Proceedings of the Nutrition Society 35: 339–349.CrossRefGoogle ScholarPubMed
Millward, D. J., Garlick, P. J., Stewart, R. J. C., Nnanyelugo, D. O. and Waterlow, J. C. 1975. Skeletal-muscle growth and protein turnover. Biochemical Journal 150: 235–243.CrossRefGoogle ScholarPubMed
Millward, D. J. and Waterlow, J. C. 1978. Effect of nutrition on protein turnover in skeletal muscle. Proceedings of the Federation of American Biological Societies 37: 2283–2290.Google ScholarPubMed
Moolenaar, W. H., Tertoolen, L. G. J. and Laat, S. W. De. 1984. Phorbol ester and diacylglycerol mimic growth factors in raising cytoplasmic pH. Nature, London 312: 371–374.CrossRefGoogle ScholarPubMed
Mortimore, G. E. and Mondon, C. E. 1970. Inhibition by insulin of valine turnover in liver. Journal of Biological Chemistry 245: 2375–2381.CrossRefGoogle ScholarPubMed
Mortimore, G. E. and Surmacz, C. A. 1983. The lysosomal pathway in cytoplasmic protein degradation. In Protein Metabolism and Nutrition (ed. Arnal, M., Pion, D. and Bonin, D.), pp. 97–115. Institut Nationale de la Recherche Agronomique, Paris.Google Scholar
Muira, Y., Mahmud, I., Karimi-Tari, F. and Fukui, W. 1981. The control of the arachidonic acid cascade in normal liver and in hepatoma cells. In Advances in Enzyme Regulation, Vol. 19 (ed. Weber, G.), pp. 27–36. Academic Press, New York.Google Scholar
Newsholme, E. A. 1986. Substrate cycles and energy metabolism. Their biochemical, biological, physiological and pathological importance. In Energy Metabolism of Farm Animals (ed. Moe, P. W., Tyrell, H. F. and Reynolds, P. J.), pp. 174–187. Rowman and Littlefield, Totowa, New Jersey.Google Scholar
Newsholme, E. A. and Crabtree, B. 1976. Substrate cycles in metabolic regulation and heat generation. Biochemical Society Symposia 41: 61–110.Google Scholar
Nielson, P. J., Manchester, K. L., Towbin, H., Gordon, J. and Thomas, G. 1982. The phosphorylation of ribosome protein S6 in rat tissues following cycloheximide injection, in diabetes and after denervation of the diaphragm. Journal of Biological Chemistry 257: 12316–12324.CrossRefGoogle Scholar
Nijweide, P. J., Burger, E. H. and Feyen, J. H. M. 1986. Cells of bones: proliferation, differentiation and hormonal regulation. Physiological Reviews 66: 855–886.CrossRefGoogle Scholar
Nishimura, S. and Sekiya, T. 1987. Human cancer and cellular oncogenes. Biochemical Journal 243: 313–327.CrossRefGoogle ScholarPubMed
Nishizuka, Y. 1984. The rôle of protein kinase C in cell surface signal transduction and tumour promotion. Nature, London 308: 693–698.CrossRefGoogle ScholarPubMed
Odedra, B. R. and Millward, D. J. 1982. Effect of corticosterone treatment on muscle protein turnover in adrenalectomised rats and diabetic rats maintained on insulin. Biochemical Journal 204: 663–672.CrossRefGoogle Scholar
Pain, V. M. 1986. Initiation of protein synthesis in mammalian cells. Biochemical Journal 235: 625–637.CrossRefGoogle ScholarPubMed
Pain, V. M., Albertse, E. C. and Garlick, P. J. 1983. Protein metabolism in skeletal muscle, diaphragm and heart of diabetic rats. American Journal of Physiology 245: E604–E610.Google ScholarPubMed
Palmer, R. M., Bain, Patricia A. and Reeds, P. J. 1985. The effect of insulin and intermittent mechanical stretching on rates of protein synthesis and degradation in isolated rabbit muscle. Biochemical Journal 230: 117–123.CrossRefGoogle ScholarPubMed
Palmiter, R. D., Brinster, R. L., Hammer, R. E., Trumbauer, M. E., Rosenfeld, M. G., Birnberg, N. C. and Evans, R. M. 1982. Dramatic growth of mice that develop from eggs microinjected with metallothionine-growth hormone fusion genes. Nature, London 300: 611–615.CrossRefGoogle ScholarPubMed
Pepinsky, R. B. and Sinclair, L. K. 1986. Epidermal growth factor-dependent phosphorylation of lipocortin. Nature, London 321: 81–84.CrossRefGoogle ScholarPubMed
Perisic, O. and Traugh, J. A. 1983. Protease-activated kinase II as the potential mediator of insulin-stimulated phosphorylation of ribosome protein S6. Journal of Biological Chemistry 258: 9598–9601.Google Scholar
Perisic, O. and Traligh, J. A. 1985. Protease-activated kinase II as the modulator of Epidermal Growth Factor stimulated phosphorylation of ribosomal protein S6. Federation of European Biochemical Societies Letters 183: 215–219.CrossRefGoogle Scholar
Raisz, L. G. and Kream, B. E. 1983. Regulation of bone formation. New England Journal of Medicine 309: 29–35.CrossRefGoogle ScholarPubMed
Reeds, P. J., Fuller, M. F. and Nicholson, B. A. 1985. Metabolic basis of energy expenditure with particular reference to protein. In Substrate and Energy Metabolism in Man (ed. Garrow, J. S. and Halliday, D.), pp. 46–67. John Libbey and Son, London.Google Scholar
Reeds, P. J. and Garlick, P. J. 1985. Nutrition and protein metabolism in man. Advances in Nutrition Research 6: 93–126.Google Scholar
Reeds, P. J., Hay, S. M., Dorwood, P. M. and 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. and Palmer, R. M. 1983. The possible involvement of PGF2α in the stimulation of muscle protein synthesis by insulin. Biochemical and Biophysical Research Communications 116: 1084–1090.CrossRefGoogle ScholarPubMed
Reeds, P. J. and Palmer, R. M. 1984. Changes in prostaglandin release associated with inhibition of muscle protein synthesis by dexmethasone. Biochemical Journal 219: 953–957.CrossRefGoogle Scholar
Reeds, P. J. and Palmer, R. M. 1986. The role of prostaglandins in the control of muscle protein turnover. In Control and Manipulation of Animal Growth (ed. Buttery, P. J., Lindsay, D. B. and Haynes, N. B.), pp. 161–185. Butterworths, London.CrossRefGoogle Scholar
Ricks, C. A., Dalrymple, R. H., Baker, P. K. and Ingle, D. L. 1984. Use of a β-agonist to alter fat and muscle deposition in steers. Journal of Animal Science 59: 1247–1252.CrossRefGoogle Scholar
Robertson, I. S., Wilson, J. C., Fraser, H. H., Innes, G. H. and Jones, A. S. 1984. Immunological castration of young bulls for beef production. In Manipulation of Growth in Farm Animals (ed. Roche, J. F. and O'Callaghan, D.), pp. 137–150. Martinus Nijhoff, Boston.CrossRefGoogle Scholar
Rodemann, H.-P. and Goldberg, A. L. 1982. Arachidonic acid, PGE2 and PGF2α influence protein turnover in skeletal and cardiac muscle. Journal of Biological Chemistry 257: 1632–1638.CrossRefGoogle ScholarPubMed
Rodriguez-Pena, A. and Rozengurt, E. 1984. Disappearance of Ca2 -sensitive, phospholipid-dependent protein kinase activity in phorbol ester-treated 3T3 cells. Biochemical and Biophysical Research Communications 120: 1053–1059.CrossRefGoogle ScholarPubMed
Rosen, O. M., Herrera, R., Olowe, Y., Petruzzelli, L. M. and Cobb, M. H. 1983. Phosphorylation activates the insulin receptor tyrosine protein kinase. Proceedings of the National Academy of Sciences, USA 80: 3237–3240.CrossRefGoogle ScholarPubMed
Rozengurt, E. 1981. Stimulation of Na+ influx, Na-K pump activity and DNA synthesis in quiescent cultured cells. In Advances in Enzyme Regulation, Vol. 19 (ed. Weber, G.), pp. 61–85. Academic Press, New York.Google Scholar
Rubin, R. P., Godfrey, P. P., Chapman, D. A. and Putney, J. W. 1984. Secretagogue induced formation of inositol phosphates in rat exocrine pancreas. Biochemical Journal 219: 655–659.CrossRefGoogle ScholarPubMed
Rucker, R. and Tinker, D. 1986. The rôle of nutrition in gene expression: a fertile field for the application of molecular biology. Journal of Nutrition 116: 177–189.CrossRefGoogle ScholarPubMed
Saltiel, A. R. and Cuatrecasas, P. 1986. Insulin stimulates the generation from hepatic plasma membranes of modulators derived from an inositol glycolipid. Proceedings of the National Academy of Sciences, USA 83: 5793–5797.CrossRefGoogle ScholarPubMed
Scornik, O. A. and Borbol, V. 1976. Rôle of changes in protein degradation in the growth of regenerating livers. Journal of Biological Chemistry 251: 2891–2896.CrossRefGoogle ScholarPubMed
Seely, J. E., Poso, H. and Pegg, A. E. 1983. Effect of androgens on turnover of ornithine decarboxylase in mouse kidney. Journal of Biological Chemistry 257: 7549–7554.CrossRefGoogle Scholar
Sève, B., Reeds, P. J., Fuller, M. F., Cadenhead, A. and Hay, S. M. 1986. Protein synthesis and retention in some tissues of the young pig as influenced by dietary protein intake after early-weaning. Possible connection to the energy metabolism. Reproduction Nutrition and Developpment 26: 849–861.CrossRefGoogle Scholar
Sinnett-Smith, P. A., Dumelow, N. D. and Buttery, P. J. 1983. Effect of trenbolone acetate and zeranol on protein metabolism in male castrate and female lambs. British Journal of Nutrition 50: 225–234.CrossRefGoogle ScholarPubMed
Sivak, A. and Duuren, D. Van. 1968. Phenotypic expression of transformation. Induction in cell culture by a phorbol ester. Science, Washington 157: 1443–1444.CrossRefGoogle Scholar
Smith, R. H., Palmer, R. M., Lobley, G. E. and Reeds, P. J. 1983. Protein synthesis in isolated rabbit forelimb muscles. The possible rôle of arachidonic acid metabolites in the response to intermittent stretching. Biochemical Journal 214: 153–161.CrossRefGoogle ScholarPubMed
Spencer, G. S. G. 1986. Hormonal manipulation of animal production by immuno-neutralization. In Control and Manipulation of Animal Growth (ed. Buttery, P. J., Lindsay, D. B. and Haynes, N. B.), pp. 279–292. Butterworths, London.CrossRefGoogle Scholar
Spencer, G. S. G., Garssen, G. J. and Hart, I. C. 1983. A novel approach to growth promotion using auto-immunisation against somatostatin. I. Effects on growth and hormone levels in lambs. Livestock Production Science 10: 25–37.CrossRefGoogle Scholar
Sutherland, E. W. and Rall, T. W. 1960. The relationship of adenosine-3', 5'-phosphate and phosphorylase to the actions of catecholamines and other hormones. Pharmacological Reviews 12: 265–299.Google Scholar
Wagner, T. E. and Jochle, W. 1986. Recombinant gene transfer in animals: the potential for improving growth in livestock. In Control and Manipulation of Animal Growth (ed. Buttery, P. J., Lindsay, D. B. and Haynes, N. B.), pp. 293–314. Butterworths, London.CrossRefGoogle Scholar
Waterlow, J. C., Garlick, P. J. and Millward, D. J. 1978. Protein Turnover in Mammalian Tissues and in the Whole Body. North Holland, Amsterdam.Google Scholar
Wheatley, D. N. 1982. Significance of the rapid degradation of newly synthesised proteins in mammalian cells. A working hypothesis. Journal of Theoretical Biology 98: 286–292.CrossRefGoogle Scholar
Williams, P. E. V., Pagliani, L., Innes, G. M., Pennie, K., Harris, C. I. and Garthwaiie, P. 1987. Effects of a β-agonist (clenbuterol) on growth, carcass composition, protein and energy metabolism of veal calves. British Journal of Nutrition 57: In press.CrossRefGoogle ScholarPubMed
Wolfman, A. and MacAra, I. G. 1987. Elevated levels of diacylglycerol and decreased phorbol ester sensitivity in ras-transformed fibroblasts. Nature, London 325: 359–361.CrossRefGoogle ScholarPubMed
Wool, I. G., Striewalt, W. S., Kurihara, K., Low, R. B. and Oyer, D. 1968. Mode of action of insulin in the regulation of protein biosynthesis in muscle. Recent Progress in Hormone Research 24: 139–208.Google ScholarPubMed
Yano, K., Higashida, H., Inoue, R. and Nozawa, Y. 1984. Bradykinin-induced rapid breakdown of phosphatidyl 4,5-bisphosphate in neuroblastoma × glioma hybrid NG 108–15 cells. Journal of Biological Chemistry 259: 10201–10207.CrossRefGoogle Scholar
Zeman, R. J., Bernstein, P. L., Ludemann, R. and Etunger, J. D. 1986. Regulation of Ca23-dependent protein turnover in skeletal muscle by thyroxine. Biochemical Journal 240: 269–275.CrossRefGoogle ScholarPubMed