Abstract
Many investigators1,2 have demonstrated that starvation or dietary protein deprivation produces an immediate fall in synthesis of albumin which returns promptly to normal or above normal levels within 24 hours of refeeding an adequate diet, and there are suggestions that the changes in albumin synthetic rate are mediated by the availability of amino acids to the hepatic cells1. Such observations have triggered widespread interest in the effects of amino acid supply on the cellular organelles involved in protein biosynthesis. Hepatic cytoplasmic ribosomes, as in most mammalian cells, exist either as free ribosomes or bound to membranes of the rough endoplasmic reticulum3.
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References
Kirsch, R. E., Frith, L., Black, E. G. and Hoffenberg, R. Regulation of albumin synthesis and catabolism by alteration of dietary protein. Nature 217 (1968), 578
Morgan, E. H. and Peters, T. Jr. The biosynthesis of rat serum albumin. V. Effect of protein depletion and refeeding on albumin and transferrin synthesis. J. Biol. Chem., 246 (1971), 3500
Fawcett, D. W. (1966) The Cell: Its Organelles and Inclusions. W. B. Saunders Co., Philadelphia
Martin, T. E. A simple general method to determine the proportion of active ribosomes in eukaryotic cells. Exptl. Cell Res., 80 (1973), 496
Zylber, E. A. and Penman, S. The effect of high ionic strength on monomers, polyribosomes, and puromycin-treated polyribosomes. Biochim. Biophys. Acta, 204 (1970), 221
Falvey, A. K. and Staehelin, T. Structure and function of mammalian ribosomes. I. Isolation and characterisation of active liver ribosomal subunits. J. Mol. Biol., 53 (1970), 1
Rogers, Q. R. and Harper, A. E. Amino acid diets and maximal growth in the rat. J. Nutr., 87 (1965), 267
Miller, L. L., Bly, C. G., Watson, M. L. and Bale, W. F. The dominant role of the liver in plasma protein synthesis: a direct study of the isolated perfused rat liver with the aid of lysine-e-C14. J. Exp. Med., 94 (1951), 431
Miller, L. L. (1973) Technique of isolated rat liver perfusion. In: Isolated Liver Perfusion and Its Applications, I. Bartošek, A. Guaitani and L. L. Miller, eds., Raven Press, New York, p. 11
Ross, B. D. (1972) Perfusion Techniques in Biochemistry. Clarendon Press, Oxford.
Seglen, P. O. and Jervell, K. F. A simple perfusion technique applied to glucocorticoid regulation of tryptophan oxygenase turnover and bile production in the isolated rat liver. Hoppe–Seyler’s Z. physiol. Chem., 350 (1969), 308
Jefferson, L. S. and Korner, A. Influence of amino acid supply on ribosomes and protein synthesis of perfused rat liver. Biochem. J., 111 (1969), 703
Clemens, M. J. and Korner, A. Amino acid requirement for the growth-hormone stimulation of incorporation of precursors into protein and nucleic acids of liver slices. Biochem. J., 119, (1970), 629
Anthony, L. E. and Faloona, G. R. Plasma insulin and glucagon levels in protein-malnourished rats. Metabolism, 23 (1974), 303
Anthony, L., Geller, S. and Edozien, J. C. Liver protein synthesis in chronic protein–calorie malnutrition. Fed. Proc., 28 (1968), 756
Enwonwu, C. O. and Jacobson, K. Relation between adrenal cortex and hepatic protein synthesis in protein–calorie-deficient rats. J. Nutr., 103 (1973), 290
Enwonwu, C. O. Distribution of free and membrane-bound ribosomes in livers of protein–calorie-deficient rats. Lab. Invest., 26 (1972), 626
Enwonwu, C. O. and Sreebny, L. M. Studies of hepatic lesions of experimental protein–calorie malnutrition in rats and immediate effects of refeeding an adequate protein diet. J. Nutr., 101 (1971), 501
Enwonwu, C. O. and Sreebny, L. M. Experimental protein–calorie malnutrition in rats. Biochemical and ultrastructural studies. Exptl. Mol. Pathol. 12 (1970), 332
Drysdale, J. W. and Munro, H. N. Polysome profiles obtained from mammalian tissues by an improved procedure. Biochim. Biophys. Acta, 138 (1967), 616
Sarma, D. S. R., Reid, I. M., Verney, E. and Sidransky, H. Studies on the nature of attachment of ribosomes to membranes in liver. I. Influence of ethionine, sparsomycin, carbon tetrachloride, and puromycin on membrane-bound polyribosomal disaggregation and on detachment of membrane-bound ribosomes. Lab. Invest., 27 (1972), 39
Blobel, G. and Potter, V. R. Studies on free and membrane-bound ribosomes in rat liver. I. Distribution as related to total cellular RNA. J. Mol. Biol., 26 (1967), 293
Wunner, W. H., Bell, J. and Munro, H. N. The effect of feeding a tryptophan-free amino acid mixture on rat-liver polysomes and ribosomal ribonucleic acid. Biochem. J., 101 (1966), 417
Enwonwu, C. O. Restitution of secretory proteins as reflected by changes in polyribosomal organisation in salivary glands of rats treated with isoproterenol. Lab. Invest., 27 (1972) 199
Enwonwu, C. O. and Munro, H. N. Changes in liver polyribosome patterns following administration of hydrocortisone and actinomycin D. Biochim. Biophys. Acta, 238 (1971), 264
Enwonwu, C. O. and Munro, H. N. Rate of RNA turnover in rat liver in relation to intake of protein. Arch. Biochem. Biophys., 138 (1970), 532
Wunner, W. H. The time sequence of RNA and protein synthesis in cellular compartments following an acute dietary challenge with amino acid mixtures. Proc. Nutr. Soc. (England), 26 (1967), 153
Ekren, T., Jervell, K. F. and Seglen, P. O. Insulin and amino acid regulation of polysomes in perfused, diabetic rat liver. Nature New Biology, 229 (1971), 244
Reader, R. W. and Stanners, C. P. On the significance of ribosome dimers in extracts of animal cells. J. Mol. Biol., 28 (1967), 211
Faber, A. J. and Tamaoki, T. Isolation of active ribosomal subunits from L5178Y mouse lymphoma cells. Arch. Biochem. Biophys., 149 (1972), 289
Pilkis, S. J. and Korner, A. Effect of diabetes and insulin treatment on protein synthetic activity of rat liver ribosomes. Biochim. Biophys. Acta, 247 (1971), 597
Enwonwu, C. O. Biochemical and morphologic changes in rat submandibular gland in experimental protein–calorie malnutrition. Exptl. Mol. Pathol., 16 (1972), 244
Martin, T. E. and Wool, I. G. Active hybrid 80S particles formed from subunits of rat, rabbit and protozoan (Tetrahymena pyriformis) ribosomes. J. Mol. Biol., 43 (1969), 151
Enwonwu, C. O. Alterations in ninhydrin-positive substances and cytoplasmic protein synthesis in the brains of ascorbic acid deficient guinea pigs. J. Neurochem., 21 (1973), 69
Enwonwu, C. O., Stambaugh, R. V. and Jacobson, K. L. Protein-energy deficiency in nonhuman primates: biochemical and morphological alterations. Am. J. Clin. Nutr., 26 (1973), 1287
Baliga, B. S., Pronczuk, A. W. and Munro, H. N. Regulation of polysome aggregation in a cell-free system through amino acid supply. J. Mol. Biol., 34 (1968), 199
Enwonwu, C. O. and Glover, V. Alterations in cerebral protein metabolism in the progeny of protein–calorie-deficient rats. J. Nutr., 103 (1973), 61
Edozien, J. C. Experimental kwashiorkor and marasmus. Nature, 220 (1968), 917
Enwonwu, C. O. Experimental protein–calorie malnutrition in the guinea pig and evaluation of the role of ascorbic acid status. Lab. Invest., 29 (1973), 17
Gaetani, S., Massotti, D. and Spadoni, M. A. Studies of dietary effects on free and membrane-bound polysomes in rat liver. J. Nutr., 99 (1969), 307
Reiss, U. and Tappel, A. L. Decreased activity in protein synthesis systems from liver of vitamin-E-deficient rats. Biochim. Biophys. Acta, 312 (1973), 608
Storb, U. and Martin, T. E. Number and activity of free and membrane-bound spleen ribosomes during the course of the immune response. Biochim. Biophys. Acta, 281 (1972), 406
Levitan, I. B. and Webb, T. E. Regulation of tyrosine transaminase in the isolated perfused rat liver. J. Biol. Chem., 244 (1969), 4684
McGown, E., Richardson, A. G., Henderson, L. M. and Swan, P. B. Effect of amino acids on ribosome aggregation and protein synthesis in perfused rat liver. J. Nutr., 103 (1973), 109
Tavill, A. S., East, A. G., Black, E. G., Nadkarni, D. and Hoffenberg, R. (1973) Regulatory factors in the synthesis of plasma proteins by the perfused rat liver. In: Protein Turnover. Ciba Foundation Symposium 9 (New Series). Elsevier, Amsterdam.
Norman, M., Gamulin, S. and Clark, K. The distribution of ribosomes between different functional states in livers of fed and starved mice. Biochem. J., 134 (1973), 387
Horie, Y. and Ashida, K. Stimulation of hepatic protein synthesis in rats fed an adequate protein diet after a low protein diet. J. Nutr., 101 (1971), 1319
Gan, J. C. and Jeffay, H. Origins and metabolism of the intracellular amino acid pools in rat liver and muscle. Biochim. Biophys. Acta, 148 (1967), 448
Wannamacher, Jr., R. W., Ribosomal RNA synthesis and function as influenced by amino acid supply and stress. Proc. Nutr. Soc. (England), 31 (1972), 281
Oratz, M., Rothschild, M. A., Burks, A., Mongelli, J. and Schreiber, S. S. (1973) The influence of amino acids and hepatotoxic agents on albumin synthesis, polysomal aggregation and RNA turnover. In: Protein Turnover. Ciba Foundation Symposium 9 (New Series). Elsevier. Amsterdam
Pronczuk, A. W., Rogers, Q R. and Munro, H. N. Liver polysome patterns of rats fed amino acid imbalanced diets. J. Nutr., 100 (1970), 1249
Ip, C. C. Y. and Harper, A. E. Effect of threonine supplementation on hepatic polysome patterns and protein synthesis of rats fed a threonine-deficient diet. Biochim. Biophys. Acta, 331 (1973), 251
Miller, L. L. and John, D. W. (1970) Nutritional, hormonal and temporal factors regulating net plasma protein biosynthesis in the isolated perfused rat liver. In: Plasma Protein Metabolism: Regulation of Synthesis, Distribution and Degradation, M. R. Rothschild and T. Waldmann, eds., Academic Press, New York, p. 207
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Enwonwu, C.O. (1976). Protein synthesis in the perfused liver: Comparative evaluation of the influence of amino acid supply on ribosomal activity of intact and isolated perfused rat liver. In: Bianchi, R., Mariani, G., McFarlane, A.S. (eds) Plasma Protein Turnover. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-02644-9_17
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DOI: https://doi.org/10.1007/978-1-349-02644-9_17
Publisher Name: Palgrave Macmillan, London
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