Abstract
Patients with acute renal failure are often severely catabolic (1–3) and may manifest marked muscle protein wasting. Although muscle is the major endogenous source of protein and amino acids for the organism, there are little data concerning muscle protein and amino acid metabolism in acute uremia. Since hepatic uptake of amino acids, gluconeogenesis and urea synthesis are increased in rats with experimental acute uremia (4–7), it is likely that muscle provides increased amounts of amino acids for the enhanced metabolic activity of the liver.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Silva, H., J. Pomeroy, A.I. Rae, S.M. Rosen, and S. Shaldon. Daily haemodialysis in “hypercatabolic” acute renal failure. 1964. Br. Med. J. 2: 407–410.
Leonard, C.D., R.G. Luke, and R.R. Siegel. 1973. Parenteral essential amino acids in acute renal failure. Urology 6: 154–157.
Feinstein, E.I., M.J. Blumenkrantz, M. Healy, A. Koffler, H. Silberman, S.G. Massry, and J.D. Kopple. 1981. Clinical and metabolic response to parenteral nutrition in acute renal failure: a controlled double-blind study. Medicine 60: 124–137.
Sellers, A.L., J. Katz, and J. Marmorston. 1957. Effect of bilateral nephrectomy on urea formation in rat liver slices. Am. J. Physiol. 191(2): 345–349.
Lacy, W.W. 1969. Effect of acute uremia on amino acid uptake and urea production by perfused rat liver. Am. J. Physiol. 216: 1300–1305.
Lacy, W.W. 1970. Uptake of individual amino acids by perfused rat liver: effect of acute uremia. Am. J. Physiol. 219: 649–653.
Frohlich, J., J. Scholmerich, G. Hoppe-Seyler, K.P. Maier, H. Talke, P. Schollmeyer, and W. Gerok. 1974. The effect of acute uremia on gluconeogenesis in isolated perfused rat livers. Eur. J. Clin. Invest. 4: 453–458.
Mitch, W.E. 1981. Amino acid release from the hindquarter and urea appearance in acute uremia. Am. J. Physiol. 241: E415–E419.
Shear, L. 1969. Internal redistribution of tissue protein synthesis in uremia. J. Clin. Invest. 48: 1252–1257.
Pils, P., W. Jettmar, D. Adamiker, and K.H. Tragl. 1981. Insulin and the in vitro protein synthesis of liver and skeletal muscle ribosomes in experimental acute uraemia. Horm. Metab. Res. 13: 89–91.
Jefferson, L.S. 1975. A technique for perfusion of an isolated preparation of rat hemicorpus. Methods Enzymol. 39: 73–82.
Krebs, M.A., and K. Henseleit. 1932. Hoppe-Seylers. J. Physiol. Chem. 210: 33–66.
Jefferson, L.S., J.B. Li, and S.R. Rannels. 1977. Regulation by insulin of amino acid release and protein turnover in the perfused rat hemicorpus. J. Biol. Chem. 252: 1476–1483.
Kopple, J.D. 1981. Nutritional therapy in kidney failure. Nutr. Rev. 39: 193–206.
Lamprecht, W., and I. Trautschold. 1974. In Methods of Enzymatic Analysis. H.V. Bergmeyer, editor. 2nd English Edition, Vol. 4. Academic Press, New York. 2101–2110.
Torikai, S., M.S. Wang, K.L. Klein, and K. Kurokawa. 1981. Adenylate cyclase and cell cyclic AMP of rat cortical thick ascending limb of Henle. Kidney Int. 20: 649–654.
Barrett, A.J. 1972. A new assay for cathepsin B1 and other thiol proteinases. Anal. Biochem. 47: 280–293.
Anson, M.L. 1938. The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin. J. Gen. Physiol. 22: 79–89.
Mayer, M., R. Amin, and E. Shafrir. 1974. Rat myofibrillar protease: Enzyme properties and adaptive changes in conditions of muscle protein degradation. Arch. Biochem. Biophys. 161: 20–25.
Pennington, R.J., and J.E. Robinson. 1968. Cathepsin activity in normal and dystrophic human muscle. Enzym. Biol. Clin. 9: 175–182.
Flugel-Link, R.M., I. B. Salusky, M. R. Jones, and J. D. Kopple. Protein and amino acid metabolism in the posterior hemicorpus of acutely uremic rats. Am. J. Physiol. (In press).
Kar, N. C., and C. M. Pearson. 1972. Acid, neutral and alkaline cathepsins in normal and diseased human muscle. Enzyme 13: 188–196.
Li, J. B. 1980. Protein synthesis and degradation in skeletcal muscle of normal and dystrophic hamsters. Am. J. Physiol. 239: E401–E406.
Mayer, M. R., R. Amin, R. J. Milholland, and F. Rosen. 1976. Possible significance of myofibrillar protease in muscle catabolism. Enzyme activity in dystrophic, tumor-bearing, and glucocorticoid-treated animals. Exper. Molec. Pathol. 25: 9–19.
Lundholm, K., A.-C. Bylund, J. Holm, and T. Schersten. 1976. Skeletal muscle metabolism in patients with malignant tumor. Euro. J. Cancer 12: 465–473.
Horl, W. H., and A. Heidland. 1980. Enhanced proteolytic activity — cause of protein catabolism in acute renal failure. Am. J. Clin. Nutr. 33: 1423–1427.
Libby, P., and A. L. Goldberg. 1980. Effects of chymostatin and other proteinase inhibitors on protein breakdown and proteolytic activities in muscle. Biochem. J. 188: 213–220.
Tischler, M. D., and A. L. Goldberg. 1980. Leucine degradation and release of glutamine and alanine by adipose tissue. J. Biol. Chem. 255: 8074–8081.
Feinstein, E. I., J. D. Kopple, H. Silberman, and S. G. Massry. 1983. Parenteral nutrition with increased nitrogen intake in the treatment of acute renal failure. Kidney Int 23: 123 (abstract).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1984 Plenum Press, New York
About this chapter
Cite this chapter
Flugel-Link, R.M., Salusky, I.B., Jones, M.R., Kopple, J.D. (1984). Enhanced Muscle Protein Degradation and Amino Acid Release from the Hemicorpus of Acutely Uremic Rats. In: Hörl, W.H., Heidland, A. (eds) Proteases. Advances in Experimental Medicine and Biology, vol 167. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9355-3_48
Download citation
DOI: https://doi.org/10.1007/978-1-4615-9355-3_48
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-9357-7
Online ISBN: 978-1-4615-9355-3
eBook Packages: Springer Book Archive