Hostname: page-component-76fb5796d-dfsvx Total loading time: 0 Render date: 2024-04-29T02:16:06.727Z Has data issue: false hasContentIssue false
  • English
  • Français

Effects of amino acid analogues on protein synthesis and degradation in isolated cells

Published online by Cambridge University Press:  09 March 2007

S. E. Knowles  and
F. J. Ballard
S. E. Knowles
Affiliation:
CSIRO Division of Human Nutrition, Kintore Avenue, Adelaide, South Australia 5000, Australia
F. J. Ballard
Affiliation:
CSIRO Division of Human Nutrition, Kintore Avenue, Adelaide, South Australia 5000, Australia
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.

1. Naturally-occurring and synthetic analogues of phenylalanine, tyrosine, histidine, arginine, proline, tryptophan and the sulphur amino acids have been tested in rat reticulocytes and in the Reuber H35 hepatoma for effects on protein synthesis and protein degradation and on the heat lability of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) in the hepatoma cells. The experiments were designed to test whether the analogues could be incorporated into mammalian proteins and whether the resultant proteins would be degraded at an accelerated rate.

2. Several analogues, including thiazolylalanine, triazolalanine and selenocystine both stimulated protein synthesis and produced labile protein in reticulocytes. Other analogues, such as dihydroxyphenylalanine, thioproline and pipecolic acid accelerated protein breakdown but probably indirectly via an inhibition of protein synthesis. Azetidine-2-carboxylic acid had the largest effect on protein breakdown in reticulocytes.

3. Labile protein was produced in hepatoma cells incubated in the presence of azetidine-2-carboxylic acid, canavanine, indospicine, triazolalanine, 2-, 3- and 4-fluorophenylalanine. These same analogues, together with 3, 4-dehydroproline, β-2-thienylalanine, dihydroxyphenylalanine, histidinol, 5- and 6-fluorotryptophan, selenocystine and selenomethionine produced heat-labile phosphoenolpyruvate carboxykinase. Enzyme induced in the presence of selenomethionine or indospicine showed the largest increases in heat lability, and for these analogues equimolar concentrations of methionine and arginine respectively were needed to nullify the enzyme abnormality.

4. The toxicity of the same naturally-occurring analogues has been discussed in terms of their ability to be incorporated into cell proteins.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 40 , Issue 2 , September 1978 , pp. 275 - 287
Copyright
Copyright © The Nutrition Society 1978

References

Allende, C. C. & Allende, J. E. (1964). J. biol. Chem. 239, 1102.CrossRefGoogle Scholar
Ballard, F. J. & Hanson, R. W. (1969). J. biol. Chem. 244, 5625.CrossRefGoogle Scholar
Baum, B. J., Johnson, L. S., Franzblau, C. & Troxler, R. F. (1975). J. biol. Chem. 250, 1464.CrossRefGoogle Scholar
Bell, E. A. (1976). FEBS Lett. 64, 29.CrossRefGoogle Scholar
Bell, E. A. & Janzen, D. H. (1971). Nature, Lond. 229, 136.CrossRefGoogle Scholar
Christie, G. S., Wilson, M. & Hegarty, M. P. (1975). J. Path. 117, 195.CrossRefGoogle Scholar
Eagle, H. (1959). Science, N.Y. 130, 432.CrossRefGoogle Scholar
Fowden, L. (1959). Biochem. J. 71, 643.CrossRefGoogle Scholar
Fowden, L. (1974). Rec. Adv. Phytochem. 8, 95.CrossRefGoogle Scholar
Fowden, L., Lewis, D. & Tristram, H. (1967). Adv. Enzym. 29, 89.Google Scholar
Goldberg, A. L. & Dice, J. F. (1974). A. Rev. Biochem. 43, 835.CrossRefGoogle Scholar
Hegarty, M. P., Court, R. D. & Thorne, P. M. (1964). Aust. J. agric. Res. 15, 168.CrossRefGoogle Scholar
Hegarty, M. P. & Pound, A. W. (1970). Aust. J. biol. Sci. 23, 831.CrossRefGoogle Scholar
Hegarty, M. P., Schinckel, P. G. & Court, R. D. (1964). Aust. J. agric. Res. 15, 153.CrossRefGoogle Scholar
Knowles, S. E., Gunn, J. M., Hanson, R. W. & Ballard, F. J. (1975). Biochem. J. 146, 595.CrossRefGoogle Scholar
Knowles, S. E., Gunn, J. M., Reshef, L., Hanson, R. W. & Ballard, F. J. (1975). Biochem. J. 146, 585.CrossRefGoogle Scholar
Kruse, P. F., White, P. B., Carter, H. A. & McCoy, T. A. (1959). Cancer Res. 19, 122.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). J. biol. Chem. 193, 265.CrossRefGoogle Scholar
Schimke, R. T. (1970). Meth. Enzym. 17A, 313.CrossRefGoogle Scholar