Hostname: page-component-cd9895bd7-gvvz8 Total loading time: 0 Render date: 2024-12-28T03:31:03.507Z Has data issue: false hasContentIssue false

Correlation between the urinary excretion of acid-soluble peptides, fractional synthesis rate of whole body proteins, and plasma immunoreactive insulin-like growth factor-l/somatomedin C concentration in the rat

Published online by Cambridge University Press:  09 March 2007

Taek Jeong Nam
Affiliation:
Department of Agricultural Chemistry. Faculty of Agriculture, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Tadashi Noguchi
Affiliation:
Department of Agricultural Chemistry. Faculty of Agriculture, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Ryuhei Funabiki
Affiliation:
Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University, Fuchu-shi 183, Japan
Hisanori Kato
Affiliation:
Department of Agricultural Chemistry. Faculty of Agriculture, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Yutaka Miura
Affiliation:
Department of Agricultural Chemistry. Faculty of Agriculture, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Hiroshi Naito
Affiliation:
Department of Agricultural Chemistry. Faculty of Agriculture, University of Tokyo, Bunkyo-ku, Tokyo 113, Japan
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The relations between the urinary excretion of acid-soluble peptide (ASP)-form amino acids, the rate of whole body protein synthesis and plasma immunoreactive insulin-like growth factor-1/somatomedin C concentration were investigated in rats. The urinary ASP-form leucine plus valine excretion correlated well with the rate of whole body protein synthesis and with the plasma immunoreactive insulin-like growth factor-1 concentration. The results provide further evidence for the hypothesis that urinary excretion of ASP is an excellent index of the status of protein metabolism in animals.

Type
Protein Nutrition and Metabolism
Copyright
Copyright © The Nutrition Society 1990

References

REFERENCES

Bates, P. C. & Millward, D. J. (1981). Characteristics of skeletal muscle growth and protein turnover in a fast-growing rat strain. British Journal of Nulrition 46, 713.CrossRefGoogle Scholar
Binoux, M., Lassarre, C. & Hardouin, N. (1982). Somatomedin production by rat liver in organ culture. III. Studies on the release of insulin-like growth factor and its carrier protein measured by radioligand assays. Effects of growth hormone, insulin and cortisol. Acta Endocrinologica 99, 422430.Google ScholarPubMed
Clemmons, D. R., Klibanski, A., Underwood, L. E., Macarthur, J. W., Ridgway, E. C., Beitins, I. Z. & Van wyk, J. J. (1981). Reduction of plasma immunoreactive somatomedin-C during fasting in humans. Journal of Clinical Endocrinology and Metabolism 53, 12471250.CrossRefGoogle ScholarPubMed
Clemmons, D. R., Seek, M. M. & Underwood, L. E. (1985). Supplemental essential amino acids augment the somatomedin-C/insulin-like growth factor I response to refeeding after fasting. Metabolism 34, 391395.CrossRefGoogle ScholarPubMed
Conde, R. D. (1979). Effect of hypophysectomy on the rates or protein synthesis and degradation in rat liver. Biochemical Journal 178, 725731.CrossRefGoogle ScholarPubMed
Daughaday, W. W. (1983). The somatomedin hypothesis: origins and recent developments. In Insulin-Like Growth Factors/Somatomedins, pp. 311 [Spencer, E. M. editor]. Berlin and New York: Walter de Gruyter.Google Scholar
Funabiki, R., Yagasaki, K., Nyumura, N. & Takeda, A. (1986). Development of an intraperitoneal large-dose alanyltyrosine method for the measurement of protein synthesis in vivo. Reports of The Research Committee on Essential Amino Acids (Japan), no. 109, pp. 3133. Tokyo: The Research Committee of Essential Amino Acids (Japan).Google Scholar
Garlick, 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, 719723.CrossRefGoogle ScholarPubMed
Garlick, P. J. & Marshall, I. (1972). A technique for measuring brain protein syntehsis. Journal of Neurochemistry 19, 577583.CrossRefGoogle Scholar
Goldspink, D. F. & Kelly, F. J. (1984). Protein turnover and growth in the whole body, liver and kidney of the rat from the foetus to senility. Biochemical Journal 217, 507516.CrossRefGoogle ScholarPubMed
Macdonald, M. L. & Swick, R. W. (1981). The effect of protein depletion and repletion on muscle-protein turnover in the chick. Biochemical Journal 194, 811819.CrossRefGoogle ScholarPubMed
Maes, M., Underwood, L. E., Gerard, G. & Ketelslegers, J. M. (1984). Relationship between plasma somatomedin-C and liver somatogenic binding sites in neonatal rats during malnutrition and after short and long term refeeding. Endocrinology 115, 786792.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J., Nnanyelugo, D. O. & Waterlow, J. C. (1976). The relative importance of muscle protein synthesis and breakdown in the regulation of muscle mass. Biochemical Journal 156, 185188.Google Scholar
Millward, D. J., Garlick, P. J., Stewart, R. J. C., Nnanyehgo, D. O. & Waterlow, J. C. (1975). Skeletal muscle growth and protein turnover. Biochemical Journal 150, 235243.CrossRefGoogle ScholarPubMed
Millward, D. J. & Waterlow, J. C. (1978). Effect of nutrition on protein turnover in skeletal muscle. Federation Proceedings 37, 22832290.Google ScholarPubMed
Nam, T. J., Noguchi, T. & Naito, H. (1990). Changes in the urinary excretion of acid-soluble peptides in rats injected with streptozotocin or dexamethasone: a trial to estimate the changes in the rate of whole-body protein degradation in those rats. British Journal of Nutrition (In the Press).Google Scholar
Nishizawa, N., Shimbo, M., Noguchi, T., Hareyama, S. & Funabiki, R. (1978). Effect of starvation, refeeding and hydrocortisone administration on turnover of myofibrillar proteins estimated by urinary excretion of NT-methylhistidine in the rat. Agricultural and Biological Chemistry 42, 20832089.Google Scholar
Noguchi, T., Okiyama, A., Naito, H., Kaneko, K. & Koike, G. (1982). Some nutritional and physiological factors affecting the urinary excretion of acid soluble peptides in rats and women. Agricultural and Biological Chemistry 46, 28212828.Google Scholar
Noguchi, T., Nam, T. J., Kato, H. & Naito, H. (1988). Further studies on the nutritional factors affecting the urinary excretion of acid-soluble peptides in rats. British Journal of Nutrition 60, 321337.CrossRefGoogle ScholarPubMed
Odedra, 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, 617627.CrossRefGoogle ScholarPubMed
Odedra, B. R. & Millward, D. J. (1982). Effect of corticosterone treatment on muscle protein turnover in adrenalectomized rats and diabetic rats maintained on insulin. Biochemical Journal 204, 663672.CrossRefGoogle ScholarPubMed
Prewitt, T. E., D'Ercole, A. J., Switzer, B. R. & Van wyk, J. J. (1982). Relationship of serum immunoreactive somatomedin-C to dietary protein and energy in growing rats. Journal of Nutrition 112, 144150.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, 445455.CrossRefGoogle ScholarPubMed
Reeves, R. D., Dickinson, L., Lee, J., Kilgore, B., Branham, B. & Elders, M. J. (1979). Effects of dietary composition on somatomedin activity in growing rats. Journal of Nutrition 109, 613620.Google Scholar
Reichlin, S. (1988). Control of GH secretion: an overview. In Growth Hormone, Growth Factor, and Acromegaly. pp. 111 [Ludecke, D. K. and Tolis, G. editors]. New York: Raven Press.Google Scholar
Rogers, Q. R. & Harper, A. E., (1965). Amino acid diets and maximal growth in the rat. Journal of Nutrition 87, 217225.CrossRefGoogle ScholarPubMed
Schwander, J. C., Hauri, C., Zapf, J. & Froesch, E. R. (1983). Synthesis and secretion of insulin-like growth factor and its binding protein by the perfused rat liver. Dependence of growth hormone status. Endocrinology 113, 297305.CrossRefGoogle ScholarPubMed
Shimatsu, A. & Rotwein, P. (1987). Mosaic evolution of the insulin-like growth factors. Organization, sequence, and expression of the rat insulin-like growth factor I gene. Journal of Biological Chemistry 262, 78947900.CrossRefGoogle ScholarPubMed
Snedecor, G. W. & Cochran, W. G.. (1967). One-way classifications. Analysis of variance. In Statistical Methods, 6th ed, pp. 271273. Ames, Iowa: Iowa State University Press.Google Scholar
Takahashi, S.-I., Kato, H., Seki, T., Noguchi, T., Naito, H., Aoyagi, T. & Umezawa, H. (1985). Bestatin, a microbial aminopeptidase inhibitor, inhibits DNA synthesis induced by insulin or epidermal growth factor in primary cultured rat hepatocytes. Journal of Antibiotics 38, 17671773.CrossRefGoogle ScholarPubMed
Waalkes, T. P. & Udenfriend, S. (1957). A fluorometric method for the estimation of tyrosine in plasma and tissues. Journal of Luboratory and Clinical Medicine 50, 733736.Google ScholarPubMed
Yahya, Z. A. H., Bates, P. C., Dalal, S. S., Morell, D., Holder, A. T., Taylor, A. & Millward, D. J. (1986). The effect of dietary protein con entration on bone and muscle growth and immunoreactive somatomedin C in the rat. Proceeding of the Nutrition Society 45, 107A.Google Scholar
Yamashita, S. & Melmed, S. (1986). Insulin-like growth factor I action on rat anterior pituitary cells: suppression of growth hormone secretion and messenger ribonucleic acid levels. Endocrinology 118, 176182.Google Scholar