Hostname: page-component-5db58dd55d-8lnk4 Total loading time: 0 Render date: 2026-07-07T22:09:47.096Z Has data issue: false hasContentIssue false
  • English
  • Français

Nutrient Regulation of Skeletal Muscle Protein Metabolism in Animals. The Involvement of Hormones and Substrates

Published online by Cambridge University Press:  14 December 2007

Jean Grizard ,
Dominique Dardevet ,
Isabelle Papet ,
Laurent Mosoni ,
Philippe Patureau Mirand ,
Didier Attaix ,
Igor Tauveron ,
Danielle Bonin  and
Maurice Arnal
Jean Grizard
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Dominique Dardevet
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Isabelle Papet
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Laurent Mosoni
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Philippe Patureau Mirand
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Didier Attaix
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Igor Tauveron
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Danielle Bonin
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Maurice Arnal
Affiliation:
Laboratoire d'Etude du Métabolisme Azoté, Institut National de la Recherche Agronomique, Centre de Clermont-Ferrand – Theix, Centre de Recherche en Nutrition Humaine d'Auvergne, 63122 Saint-Genès-Champanelle, France
Rights & Permissions [Opens in a new window]

Abstract

An abstract is not available for this content so a preview has been provided. As you have access to this content, a full PDF is available via the ‘Save PDF’ action button.
Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'

Information

Type
Research Article
Information
Nutrition Research Reviews , Volume 8 , Issue 1 , January 1995 , pp. 67 - 91
Copyright
Copyright © The Nutrition Society 1995

References

1Ahlersova, E., Ahlens, I., Milanova, R., Datelinka, I. & Toropila, M. (1984). Circadian oscillations of thyroid hormones, insulin and glucagon in the blood of laboratory rats in the course of the year. Physiologica Bohemoslovaca 33, 309–319.Google ScholarPubMed
2Angerås, U. & Hasselgren, P.-O. (1987). Protein degradation in skeletal muscle during experimental hyperthyroidism in rats and the effect of β-blocking agents. Endocrinology 120, 1417–1421.CrossRefGoogle ScholarPubMed
3Arnal, M., Obled, C., Attaix, D., Patureau Mirand, P. & Bonin, D. (1987). Dietary control of protein turnover. Diabète et Métabolisme 13, 630–642.Google ScholarPubMed
4Attaix, D., Manghebati, A., Grizard, J. & Arnal, M. (1986). Assessment of in vivo protein synthesis in lamb tissues with [3H]valine flooding doses. Biochimica et Biophysica Acta 882, 389–397.CrossRefGoogle ScholarPubMed
5Attaix, D., Taillandier, D., Temparis, S., Larbaud, D., Aurousseau, E., Combaret, L. & Voisin, L. (1994). Regulation of ATP-ubiquitin-dependent proteolysis in muscle wasting. Reproduction Nutrition Development 34, 583–597.CrossRefGoogle ScholarPubMed
6Baillie, A. G. S. & Garlick, P. J. (1992). Attenuated responses of muscle protein synthesis to fasting and insulin in adult female rats. American Journal of Physiology 262, E1–E5.Google ScholarPubMed
7Balage, M., Grizard, J., Hui-Bon-Hoa, D. & Rosselin, G. (1986). Effect of dietary protein level on the first steps of glucagon action in rat liver plasma membranes. Journal of Nutrition 116, 1810–1819.CrossRefGoogle ScholarPubMed
8Balage, M., Grizard, J. & Manin, M. (1990 a). Effect of calorie restriction on skeletal muscle and liver insulin binding in growing rat. Hormone and Metabolic Research 22, 207–214.CrossRefGoogle ScholarPubMed
9Balage, M., Grizard, J., Sornet, C., Simon, J., Dardevet, D. & Manin, M. (1990 b). Insulin binding and receptor tyrosine kinase activity in rat liver and skeletal muscle: effect of starvation. Metabolism 39, 366–373.CrossRefGoogle ScholarPubMed
10Bauman, D. E., Eisemann, J. H. & Currie, W. B. (1982). Hormonal effects on partitioning of nutrients for tissue growth: role of growth hormone and prolactin. Federation Proceedings 41, 2538–2544.Google Scholar
11Bennet, W. M., Connacher, A. A., Scrimgeour, C. M., Smith, K. & Rennie, M. J. (1989). Increase in anterior tibialis muscle protein synthesis in healthy man during mixed amino and infusion: studies of incorporation of [1-13C]leucine. Clinical Science 76, 447–454.CrossRefGoogle ScholarPubMed
12Bois-Joyeux, B., Chanez, M., Azzout, B. & Peret, J. (1986). Comparison between starvation and consumption of a high protein diet: plasma insulin and glucagon and hepatic activities of gluconeogenic enzymes during the first 24 hours. Diabète et Métabolisme 12, 21–27.Google Scholar
13Bondey, C. A., Underwood, L. E., Clemmons, D. R., Guler, H. P., Bach, M. E. & Skarulis, M. (1994). Clinical uses of insulin-like growth factor I. Annals of Internal Medicine 120, 593–601.CrossRefGoogle Scholar
14Brown, J. G. & Millward, D. J. (1983). Dose response of protein turnover in rat skeletal muscle to triiodothyronine treatment. Biochimica et Biophysica Acta 757, 182–190.CrossRefGoogle ScholarPubMed
15Buse, M. G. & Reid, S. S. (1975). Leucine. A possible regulator of protein turnover in muscle. Journal of Clinical Investigation 56, 1250–1261.CrossRefGoogle ScholarPubMed
16Carter, W. J., Benjamin, W. S.van der, W. & Faas, F. H. (1984). Effect of a protein-free diet on muscle protein turnover and nitrogen conservation in euthyroid and hyperthyroid rats. Biochemical Journal 217, 471–476.CrossRefGoogle ScholarPubMed
17Castellino, P., Luzi, L., Del Prato, S. & DeFronzo, R. A. (1990). Dissociation of the effects of epinephrine and insulin on glucose and protein metabolism. American Journal of Physiology 258, E117–E125.Google ScholarPubMed
18Chatterjee, V. K. K. (1994). Thyroid hormone receptors: molecular and functional aspects. In the thyroid and tissues. Merck European Thyroid Symposium, February 1994, pp. 37–44 [ J., Orgiazzi and J., Leclère, editors]. Stuttgart: Schattauer.Google Scholar
19Chen, L., Komiya, I., Inman, L., O'Neil, J., Appel, M., Alam, T. & Unger, R. H. (1989). Effects of hypoglycemia and prolonged fasting on insulin and glucagon gene expression. Studies with in situ hybridization. Journal of Clinical Investigation 84, 711–714.CrossRefGoogle ScholarPubMed
20Chérel, Y., Attaix, D., Rosolowska-Huszcz, D., Belkhou, R., Robin, J. P., Arnal, M. & Le Maho, Y. (1991). Whole-body and tissue protein synthesis during brief and prolonged fasting in the rat. Clinical Science 81, 611–619.CrossRefGoogle ScholarPubMed
21Condorelli, G., Formisano, P., Miele, C. & Beguinot, F. (1992). Thyrotropin regulates autophosphorylation and kinase activity of both the insulin and the insulin-like growth factor-I receptors in FRTL5 cells. Endocrinology 130, 1615–1625.Google ScholarPubMed
22Cortamira, N. O., Sève, B., Lebreton, Y. & Ganier, P. (1991). Effect of dietary tryptophan on muscle, liver and whole-body protein synthesis in weaned piglets: relationship to plasma insulin. British Journal of Nutrition 66, 423–435.CrossRefGoogle ScholarPubMed
23Costa, A. P. D., Ingram, R. L., Lenham, J. E. & Sonntag, W. E. (1993). The regulation and mechanisms of action of growth hormone and insulin-like growth factor 1 during normal ageing. Journal of Reproduction and Fertility, Supplement 46, 87–98.Google ScholarPubMed
24Crace, C. J., Swenne, I., Kohn, P. G., Strain, A. J. & Milner, R. D. G. (1990). Protein–energy malnutrition induces changes in insulin sensitivity. Diabète et Métabolisme 16, 484–491.Google Scholar
25Dardevet, D., Manin, M., Balage, M., Sornet, C. & Grizard, J. (1991). Influence of low- and high-protein diets on insulin and insulin-like growth factor-1 binding to skeletal muscle and liver in the growing rat. British Journal of Nutrition 65, 47–60.CrossRefGoogle ScholarPubMed
26Dardevet, D., Sornet, C., Attaix, D., Baracos, V. E. & Grizard, J. (1994). Insulin-like growth factor-I and insulin resistance in skeletal muscles of adult and old rats. Endocrinology 134, 1475–1484.CrossRefGoogle ScholarPubMed
27Dardevet, D., Sornet, C., Taillandier, D., Savary, I., Attaix, D. & Grizard, J. (1995). Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Journal of Clinical Investigation 96, in press.CrossRefGoogle ScholarPubMed
28Dimitriadis, G., Parry-Billings, M., Bevan, S., Dunger, D., Piva, T., Krause, U., Wegener, G. & Newsholme, E. A. (1992). Effects of insulin-like growth factor 1 on the rates of glucose transport and utilization in rat skeletal muscle in vitro. Biochemical Journal 285, 269–274.CrossRefGoogle ScholarPubMed
29Douglas, R. G., Gluckman, P. D., Ball, K., Breier, B. & Shaw, J. H. F. (1991). The effects of infusion of insulin-like growth factor (IGF)I, IGF-II, and insulin on glucose and protein metabolism in fasted lambs. Journal of Clinical Investigation 88, 614–622.CrossRefGoogle ScholarPubMed
30Dümmler, K., Müller, St & Seitz, H. J. (1994). hyroid hormones and protein metabolism. In the thyroid and tissues. Merck European Thyroid Symposium, pp. 61–78 [ J., Orgiazzi and J., Leclère, editors]. Stuttgart: Schattauer.Google Scholar
31Flakoll, P. J., Kulaylat, M., Frexes-Steed, M., Hourani, H., Brown, L. L., Hill, J. O. & Abumrad, N. N. (1989). Amino acids augment insulin's suppression of whole body proteolysis. American Journal of Physiology 257, E839–E847.Google ScholarPubMed
32Flakoll, P. J., VandeHaar, M. J., Kuhlman, G. & Nissen, S. (1991). Influence of α-ketoisocaproate on lamb growth, feed conversion, and carcass composition. Journal of Animal Science 69, 1461–1467.CrossRefGoogle ScholarPubMed
33Florini, J. R. (1987). Hormonal control of muscle growth. Review. Muscle and Nerve 10, 577–598.CrossRefGoogle Scholar
34Fryoesch, E. R., Schmid, C., Schwander, J. & Zapf, J. (1985). Actions of insulin-like growth factors. Annual Review of Physiology 47, 443–467.CrossRefGoogle Scholar
35Fryburg, D. A., Gelfand, R. A. & Barrett, E. J. (1991). Growth hormone acutely stimulates forearm muscle protein synthesis in normal humans. American Journal of Physiology 260, E499–E504.Google ScholarPubMed
36Fryburg, D. A., Louard, R. J., Gerow, K. E., Gelfand, R. A. & Barrett, E. J. (1992). Growth hormone stimulates skeletal muscle protein synthesis and antagonizes insulin's antiproteolytic action in humans. Diabetes 41, 424–429.CrossRefGoogle ScholarPubMed
37Galbraith, R. A. & Buse, M. G. (1981). Effects of serine on protein synthesis and insulin receptors. American Journal of Physiology 241, C167–C171.CrossRefGoogle ScholarPubMed
38Garlick, P. J., Fern, M. & Preedy, V. R. (1983). The effect of insulin infusion and food intake on muscle protein synthesis in postabsorptive rats. Biochemical Journal 210, 669–676.CrossRefGoogle ScholarPubMed
39Garlick, P. J. & Grant, I. (1988). Amino acid infusion increases the sensitivity of muscle protein synthesis in vivo to insulin. Effect of branched-chain amino acids. Biochemical Journal 254, 579–584.CrossRefGoogle ScholarPubMed
40Garlick, P. J., McNurlan, M. A., Essén, P. & Wernerman, J. (1994). Measurement of tissue protein synthesis rates in vivo: a critical analysis of contrasting methods. American Journal of Physiology 266, E287–E297.Google ScholarPubMed
41Garlick, P. J., McNurlan, M. A. & Preedy, V. R. (1980). A rapid and convenient technique for measuring the rate of protein synthesis in tissues by injection of [3H]phenylalanine. Biochemical Journal 192, 719–723.CrossRefGoogle ScholarPubMed
42Gelfand, R. A. & Barrett, E. J. (1987). Effect of physiologic hyperinsulinemia on skeletal muscle protein synthesis and breakdown in man. Journal of Clinical Investigation 80, 1–6.CrossRefGoogle ScholarPubMed
43Gelfand, R. A., Glickman, M. G., Jacob, R., Sherwin, R. S. & DeFronzo, R. A. (1986). Removal of infused amino acids by splanchnic and leg tissues in humans. American Journal of Physiology 250, E407–E413.Google ScholarPubMed
44Ginsberg, B. H., Brown, T. J., Simon, I. & Spector, A. A. (1981). Effect of the membrance lipid environment on the properties of insulin receptors. Diabetes 30, 773–780.CrossRefGoogle Scholar
45Goldspink, D. F., EI Haj, A. J., Lewis, S. E. M., Merry, B. J. & Holehan, A. M. (1987). The influence of chronic dietary intervention on protein turnover and growth of the diaphragm and extensor digitorum longus muscles of the rat. Experimental Gerontology 22, 67–78.CrossRefGoogle ScholarPubMed
46Green, A., Bustillos, D. P. & Misbin, R. I. (1984). β-Hydroxybutyrate increases the insulin sensitivity of adipocyte glucose transport at a postreceptor level. Diabetes 33, 1045–1050.CrossRefGoogle Scholar
47Grizard, J., Prugnaud, J., Arnal, M. & Pion, R. (1975). [Effect of insulin on body composition and free amino acid levels in blood, liver and muscle of the growing rat subjected to energy restriction.] Annales de Biologie Animale, Biochimie, Biophysique 15, 569–582.CrossRefGoogle Scholar
48Grizard, J., Prugnaud, J. & Pion, R. (1977). [Effect of insulin excess on body composition and free amino acid levels in blood, liver and muscle of growing rats fed a control diet or subjected to nitrogen restriction.] Annales de Biologie Animale, Biochimie, Biophysique 17, 373–387.CrossRefGoogle Scholar
49Harp, J. B., Goldstein, S. & Phillips, L. S. (1991). Nutrition and somatomedin. 23. Molecular regulation of IGF-I by amino acid availability in cultured hepatocytes. Diabetes 40, 95–101.CrossRefGoogle Scholar
50Hart, I. C. & Johnsson, I. D. (1986). Growth hormone and growth in meat producing animals. In Control and Manipulation of Animal Growth, pp. 135–159 [ P. J., Buttery, D. B., Lindsay and N. B., Haynes, editors]. London: Butterworths.CrossRefGoogle Scholar
51Henry, Y. (1988). Significance and limitations of the concept of dietary amino acid balance for the growing pig. INRA Productions Animales, 1, 65–74.CrossRefGoogle Scholar
52Hershko, A. & Ciechanover, A. (1992). The ubiquitin system for protein degradation. Annual Review of Biochemistry 61, 761–807.CrossRefGoogle ScholarPubMed
53Holloszy, J. O., Chen, M., Cartee, G. D. & Young, J. C. (1991). Skeletal muscle atrophy in old rats: differential changes in the three fiber types. Mechanism of Ageing and Development 60, 199–213.CrossRefGoogle ScholarPubMed
54Ilian, M. A. & Forsberg, N. E. (1992). Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits. Biochemical Journal 287, 163–171.CrossRefGoogle ScholarPubMed
55Kettelhut, I. C., Wing, S. S. & Goldberg, A. J. (1988). Endocrine regulation of protein breakdown in skeletal muscle. Diabetes/Metabolism Reviews 4, 751–772.CrossRefGoogle ScholarPubMed
56Kimball, S. R., Vary, T. C. & Jefferson, L. S. (1994). Regulation of protein synthesis by insulin. Annual Review of Physiology 56, 321–348.CrossRefGoogle ScholarPubMed
57Komori, K., Block, N. E., Robinson, K. A. & Buse, M. G. (1989). Insulin-stimulated phosphorylation of a 195K protein from muscle and liver in the presence of poly-L-lysine. Endocrinology 125, 1438–1450.CrossRefGoogle ScholarPubMed
58Larbaud, D., Debras, E., Rallière, C., Taillandier, D., Grizard, J. & Attaix, D. (1995). Insulin down regulates ubiquitin gene expression in skeletal muscle in vivo. Advanced workshop on proteasomes and related complexes, Clermont Ferrand, Abstract.Google Scholar
59Laurent, B. C., Moldawer, L. L., Young, V. R., Bistrian, B. R. & Blackburn, G. L. (1984). Whole-body leucine and muscle protein kinetics in rats fed varying protein intakes. American Journal of Physiology 246, E444–E451.Google ScholarPubMed
60Liu, S., Baracos, V. E., Quinney, H. A. & Clandinin, M. T. (1994). Dietary ω-3 and polyunsaturated fatty acids modify fatty acyl composition and insulin binding in skeletal-muscle sarcolemma. Biochemical Journal 299, 831–837.CrossRefGoogle ScholarPubMed
61Lobley, G. E. (1990). Energy metabolism reactions in ruminant muscle: responses to age, nutrition and hormonal status. Reproduction, Nutrition, Development 30, 13–34.CrossRefGoogle ScholarPubMed
62Lobley, G. E. (1992). Control of the metabolic fate of amino acids in ruminants: a review. Journal of Animal Science 70, 3264–3275.CrossRefGoogle ScholarPubMed
63Lobley, G. E. (1993). Protein metabolism and turnover. In Quantitative Aspects of Ruminant Digestion and Metabolism, pp. 313–339 [ J. M., Forbes and J., France, editors]. Wallingford: C. A. B. International.Google Scholar
64Lobley, G. E., Harris, P. M., Skene, P. A., Brown, D., Milne, E., Calder, A. G., Anderson, S. E., Garlick, P. J., Nevison, I. & Connell, A. (1992). Responses in tissue protein synthesis to sub- and supra-maintenance intake in young growing sheep: comparison of large-dose and continuous-infusion techniques. British Journal of Nutrition 68, 373–388.CrossRefGoogle ScholarPubMed
65Louard, R. J., Bhushan, R., Gelfand, R. A., Barrett, E. J. & Sherwin, R. S. (1994). Glucocorticoids antagonize insulin's antiproteolytic action on skeletal muscle in humans. Journal of Clinical Endocrinology and Metabolism 79, 278–284.Google ScholarPubMed
66Lowe, W. L., Adamo, M., Werner, H., Roberts, C. T. & LeRoith, D. (1989). Regulation by fasting of rat insulin- like growth factor I and its receptor. Effects on gene expression and binding. Journal of Clinical Investigation 84, 619–626.CrossRefGoogle ScholarPubMed
67Lowell, B. B. & Goodman, M. N. (1987). Protein sparing in skeletal muscle during prolonged starvation. Dependence on lipid fuel availability. Diabetes 36, 14–19.CrossRefGoogle ScholarPubMed
68Lunn, P. G., Whitehead, R. G., Cole, T. J. & Austin, S. (1979). The relationship between hormonal balance and growth in malnourished children and rats. British Journal of Nutrition 41, 73–84.CrossRefGoogle ScholarPubMed
69Machlin, L. J. (1972). Effect of porcine growth hormone on growth and carcass composition of the pig. Journal of Animal Science 35, 794–800.CrossRefGoogle ScholarPubMed
70McNulty, P. H., Young, L. H. & Barrett, E. J. (1993). Response of rat heart and skeletal muscle protein in vivo to insulin and amino acid infusion. American Journal of Physiology 264, E958–E965.Google ScholarPubMed
71McNurlan, M. A. & Garlick, P. J. (1989). Influence of nutrient intake on protein turnover. Diabetes/Metabolism Reviews 5, 165–189.CrossRefGoogle ScholarPubMed
72MacRae, J. C. & Lobley, G. E. (1991). Physiological and metabolic implications of conventional and novel methods for the manipulation of growth and production. Livestock Production Science 27, 43–59.CrossRefGoogle Scholar
73Makrides, S. C. (1983). Protein synthesis and degradation during aging and senescence. Biological Reviews of the Cambridge Philosophical Society 58, 343–422.CrossRefGoogle ScholarPubMed
74Masoro, E. J. (1992). Aging and proliferative homeostasis: modulation by food restriction in rodents. Laboratory Animal Science 42, 132–137.Google ScholarPubMed
75Medina, R., Wing, S. S., Kettelhut, I. & Goldberg, A. L. (1992). Regulation of different proteolytic systems in muscle by insulin and food intake. In Protein Metabolism in Diabetes Mellitus, pp. 111–123 [ K. S., Nair, editor]. Nishimura: Smith-Gordon.Google Scholar
76Millward, D. J., Brown, J. G. & van Bueren, J. (1988). The influence of plasma concentrations of triiodothyronine on the acute increases in insulin and muscle protein synthesis in the refed fasted rat. Journal of Endocrinology 118, 417–422.CrossRefGoogle ScholarPubMed
77Millward, D. J., Odedra, B. & Bates, P. C. (1983). Role of insulin, corticosterone and other factors in the acute recovery of muscle protein synthesis on refeeding food-deprived rats. Biochemical Journal 216, 583–587.CrossRefGoogle ScholarPubMed
78Millward, D. J. & Rivers, J. P. W. (1989). The needs for indispensable amino acids: the concept of the anabolic drive. Diabetes/Metabolism Reviews 5, 191–211.CrossRefGoogle Scholar
79Morrison, W. L., Gibson, J. N. A., Jung, R. T. & Rennie, M. J. (1988). Skeletal muscle and whole body protein turnover in thyroid disease. European Journal of Clinical Investigation 18, 62–68.CrossRefGoogle ScholarPubMed
80Mortimore, G. E., Pösö, A. R., Kadowaki, M. & Wert, J. J. (1987). Multiphasic control of hepatic protein degradation by regulatory amino acids. General features and hormonal modulation. Journal of Biological Chemistry 262, 16322–16327.CrossRefGoogle ScholarPubMed
81Mortimore, G. E., Pösö, A. R. & Lardeux, B. R. (1989). Mechanism and regulation of protein degradation in liver. Diabetes/Metabolism Reviews 5, 49–70.CrossRefGoogle ScholarPubMed
82Mosoni, L., Houlier, M. L., Patureau Mirand, P., Bayle, G. & Grizard, J. (1993 a). Effect of amino acids alone or with insulin on muscle and liver protein synthesis in adult and old rats. American Journal of Physiology 264, E614–E620.Google ScholarPubMed
83Mosoni, L., Patureau Mirand, P., Houlier, M. L. & Arnal, M. (1993 b). Age related changes in protein synthesis measured in vivo in rat liver and gastrocnemius muscle. Mechanism of Ageing and Development 68, 209–220.CrossRefGoogle ScholarPubMed
84Mosoni, L., Valluy, M.-C., Serrurier, B., Prugnaud, J., Obled, C., Guézennec, C. Y. & Patureau Mirand, P. (1995). Altered response of protein synthesis to nutritional state and endurance training in old rats. American Journal of Physiology 268, E328–E335.Google ScholarPubMed
85Moundras, C., Rémésy, C. & Demigné, C. (1993). Dietary protein paradox – decrease of amino acid availability induced by high-protein diets. American Journal of Physiology 264, G1057–G1065.Google ScholarPubMed
86Obled, C., Arnal, M. & Grizard, J. (1977). [Circadian rhythm of plasma corticosterone in growing rats. Effect of feeding schedule.] Comptes Rendus Hebdomadaires des Séances de l' Académie des Sciences D 284, 195–198.Google Scholar
87O'Brien, R. M. & Granner, D. K. (1991). Regulation of gene expression by insulin. Biochemical Journal 278, 609–619.CrossRefGoogle ScholarPubMed
88Odedra, B. R., Bates, P. C. & Millward, D. J. (1983). Time course of the effect of catabolic doses of corticosterone on protein turnover in rat skeletal muscle and liver. Biochemical Journal 214, 617–627.CrossRefGoogle ScholarPubMed
89Okitolonda, W., Brichard, S. M., Pottier, A. M. & Henquin, J. C. (1988). Influence of low- and high-protein diets on glucose homeostasis in the rat. British Journal of Nutrition 60, 509–516.CrossRefGoogle ScholarPubMed
90Ostaszewski, P., Papet, I., Nissen, S., Grizard, J., Glomot, F. & Arnal, M. (1994). Effect of 3-hydroxy-3-methylbutyrate on protein metabolism in growing lambs. In Proceedings of the Society of Nutrition Physiology, VII International Symposium on Ruminant Physiology, pp. 25–30 [ D., Giesecke, editor]. Willingen, Germany.Google Scholar
91Pacy, P. J., Price, G. M., Halliday, D., Quevedo, M. R. & Millward, D. J. (1994). Nitrogen homoeostasis in man: the diurnal responses of protein synthesis and degradation and amino acid oxidation to diets with increasing protein intakes. Clinical Science 86, 103–118.CrossRefGoogle ScholarPubMed
92Papet, I., Glomot, F., Grizard, J. & Arnal, M. (1992). Leucine excess under conditions of low or compensated aminoacidemia does not change skeletal muscle and whole-body protein synthesis in suckling lambs during the postprandial period. Journal of Nutrition 122, 2307–2315.CrossRefGoogle Scholar
93Parr, T., Bardsley, R. G., Gilmour, R. S. & Buttery, P. J. (1992). Changes in calpain and calpastatin messenger RNA induced by β-adrenergic stimulation of bovine skeletal muscle. European Journal of Biochemistry 208, 333–339.CrossRefGoogle ScholarPubMed
94Pell, J. M. & Bates, P. C. (1987). Collagen and non-collagen protein turnover in skeletal muscle of growth hormone-treated lambs. Journal of Endocrinology 115, R1–R4.CrossRefGoogle ScholarPubMed
95Poggi, C., Le Marchand-Brustel, Y., Zapf, J., Froesch, E. R. & Freychet, P. (1979). Effects and binding of insulin- like growth factor I in the isolated soleus muscle of lean and obese mice: comparison with insulin. Endocrinology 105, 723–730.CrossRefGoogle ScholarPubMed
96Pomposelli, J. J., Palombo, J. D., Hamawy, K. J., Bistrian, B. R., Blackburn, G. L. & Moldawer, L. L. (1985). Comparison of different techniques for estimating rates of protein synthesis in vivo in healthy and bacteraemic rats. Biochemical Journal 226, 37–42.CrossRefGoogle ScholarPubMed
97Preedy, V. R. & Garlick, P. J. (1985). The effect of glucagon administration on protein synthesis in skeletal muscles, heart and liver in vivo. Biochemical Journal 228, 575–581.CrossRefGoogle ScholarPubMed
98Price, G. M., Halliday, D., Pacy, P. J., Quevedo, M. R. & Millward, D. J. (1994). Nitrogen homoeostasis in man. 1. Influence of protein intake on the amplitude of diurnal cycling of body nitrogen. Clinical Science 86, 91–102.CrossRefGoogle ScholarPubMed
99Rathmacher, J. A., Link, G. & Nissen, S. (1993). Measurement of 3-methylhistidine production in lambs by using compartmental-kinetic analysis. British Journal of Nutrition 69, 743–755.CrossRefGoogle ScholarPubMed
100Redpath, N. T. & Proud, C. G. (1994). Molecular mechanisms in the control of translation by hormones and growth factors. Biochimica et Biophysica Acta – Molecular Cell Research 1220, 147–162.CrossRefGoogle ScholarPubMed
101Reeds, P. J., & Fuller, M. F. (1983). Nutrient intake and protein turnover. Proceedings of the Nutrition Society 42, 463–471.CrossRefGoogle ScholarPubMed
102Reeds, 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
103Rennie, M. J., Smith, K. & Watt, P. W. (1994 a). Measurement of human tissue protein synthesis: an optimal approach. Review. American Journal of Physiology 266, E298–E307.Google Scholar
104Rennie, M. J., Tadros, L., Khogal, S., Ahmed, A. & Taylor, P. M. (1994 b). Glutamine transport and its metabolic effects. Journal of Nutrition 124, 1503S–1508S.CrossRefGoogle ScholarPubMed
105Rivett, A. J. (1993). Proteasomes: multicatalytic proteinase complexes. Biochemical Journal 291, 1–10.CrossRefGoogle ScholarPubMed
106Rossetti, L., Rothman, D. L., DeFronzo, R. A. & Shulman, G. I. (1989). Effect of dietary protein on in vivo insulin action and liver glycogen repletion. American Journal of Physiology 257, E212–E219.Google ScholarPubMed
107Sabatino, F., Masoro, E. J., McMahan, C. A. & Kuhn, R. W. (1991). Assessment of the role of the glucocorticoid system in aging processes and in the action of food restriction. Journal of Gerontology 46, B171–B179.CrossRefGoogle ScholarPubMed
108Salter, D. N., Montgomery, A. I., Hudson, A., Quelch, D. B. & Elliott, R. J. (1990). Lysine requirements and whole-body protein turnover in growing pigs. British Journal of Nutrition 63, 503–513.CrossRefGoogle ScholarPubMed
109Sève, B., Reeds, P. J., Fuller, M. F., Cadenhead, A. & 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, Dévelopment 26, 849–861.CrossRefGoogle Scholar
110Straus, D. S. & Takemoto, C. D. (1990). Effect of dietary protein deprivation on insulin-like growth factor (IGF)-I and -II, IGF binding protein-2, and serum albumin gene expression in rat. Endocrinology 127, 1849–1860.CrossRefGoogle ScholarPubMed
111Taillandier, D., Bigard, X., Desplanches, D., Attaix, D., Guezennec, C. Y. & Arnal, M. (1993). Role of protein intake on protein synthesis and fiber distribution in the unweighted soleus muscle. Journal of Applied Physiology 75, 1226–1232.CrossRefGoogle ScholarPubMed
112Tauveron, I., Charrier, S., Champredon, C., Bonnet, Y., Berry, C., Bayle, G., Prugnaud, J., Obled, C., Grizard, J. & Thiéblot, P. (1995). Response of leucine metabolism to hyperinsulinemia under amino acid replacement in experimental hyperthyroidism. American Journal of Physiology 269, E499–E507.Google ScholarPubMed
113Tauveron, I., Grizard, J., Thiéblot, Ph. & Bonin, D. (1992). [Metabolic adaptation to hyperthyroidism – implication of insulin.] Diabète et Métabolisme 18, 131–136.Google ScholarPubMed
114Tauveron, I., Larbaud, D., Champredon, C., Debras, E., Tesseraud, S., Bayle, G., Bonnet, Y., Thiéblot, P. & Grizard, J. (1994). Effect of hyperinsulinemia and hyperaminoacidemia on muscle and liver protein synthesis in lactating goats. American Journal of Physiology 267, E877–E885.Google ScholarPubMed
115Tawa, N. E. & Goldberg, A. L. (1993). Protein and amino acid metabolism in muscle. In Myology, 2nd edn, pp. 683–707. [ A. G., Engel and C., Franzini-Armstrong, editors]. New York: McGraw-Hill Book Co.Google Scholar
116Tawa, N. E., Kettelhut, I. C. & Goldberg, A. L. (1992). Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle. American Journal of Physiology 263, E326–E334.Google ScholarPubMed
117Tessari, P., Inchiostro, S., Biolo, G., Vincenti, E. & Sabadin, L. (1991). Effects of acute systemic hyperinsulinemia on forearm muscle proteolysis in healthy man. Journal of Clinical Investigation 88, 27–33.CrossRefGoogle ScholarPubMed
118Tesseraud, S., Grizard, J., Debras, E., Papet, I., Bonnet, Y., Bayle, G. & Champredon, C. (1993). Leucine metabolism in lactating and dry goats: effect of insulin and substrate availability. American Journal of Physiology 265, E402–E413.Google ScholarPubMed
119Tesseraud, S., Larbier, M., Chagneau, A. M. & Geraert, P. A. (1992). Effect of dietary lysine on muscle protein turnover in growing chickens. Reproduction, Nutrition Dévelopment 32, 163–171.CrossRefGoogle ScholarPubMed
120Thissen, J. P., Ketelslegers, J. M. & Underwood, L. E. (1994). Nutritional regulation of the insulin-like growth factors. Endocrine Reviews 15, 80–101.Google ScholarPubMed
121Thissen, J. P., Triest, S., Moats-States, B. M., Underwood, L. E., Mauerhoff, T., Maiter, D. & Ketelslegers, J. M. (1991). Evidence that pretranslational and translational defects decrease serum insulin-like growth factor- I concentrations during dietary protein restriction. Endocrinology 129, 429–435.CrossRefGoogle ScholarPubMed
122Van Koevering, M. & Nissen, S. (1992). Oxidation of leucine and α-ketoisocaproate to beta-hydroxy-beta-methylbutyrate in vivo. American Journal of Physiology 262, E27–E31.Google ScholarPubMed
123Wang, T. C. & Fuller, M. F. (1989). The optimum dietary amino acid pattern for growing pigs. 1. Experiments by amino acid deletion. British Journal of Nutrition 62, 77–89.CrossRefGoogle ScholarPubMed
124Watt, P. W., Corbett, M. E. & Rennie, M. J. (1992). Stimulation of protein synthesis in pig skeletal muscle by infusion of amino acids during constant insulin availability. American Journal of Physiology 262, E453–E460.Google Scholar
125Webster, B. A., Vigna, S. R. & Paquette, T. (1986). Acute exercise, epinephrine, and diabetes enhance insulin binding to skeletal muscle. American Journal of Physiology 250, E186–E197.Google ScholarPubMed
126Wing, S. S. & Banville, D. (1994). 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. American Journal of Physiology 267, E39–E48.Google ScholarPubMed
127Wing, S. S. & Goldberg, A. L. (1993). Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. American Journal of Physiology 264, E668–E676.Google ScholarPubMed
128Wolfe, R. R., Jahoor, F. & Hartl, W. H. (1989). Protein and amino acid metabolism after injury. Diabetes/Metabolism Reviews 5, 149–164.CrossRefGoogle ScholarPubMed
129Yahya, Z. A. H., & Millward, D. J. (1994). Dietary protein and the regulation of long bone and muscle growth in the rat. Clinical Science 87, 213–224.CrossRefGoogle ScholarPubMed
130Yahya, Z. A. H., Tirapegui, J. O., Bates, P. C. & Millward, D. J. (1994). Influence of dietary protein, energy and corticosteroids on protein turnover, proteoglycan sulphation and growth of long bone and skeletal muscle in the rat. Clinical Science 87, 607–618.CrossRefGoogle ScholarPubMed
131Young, V. R., Yu, Y. M. & Fukagawa, N. K. (1992). Energy and protein turnover. In Energy Metabolism, pp. 439–466 [ J. M., Kinney and H. N., Tucker, editors]. New York: Raven Press.Google Scholar