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. 1988 Apr 15;251(2):621–624. doi: 10.1042/bj2510621

Effect of streptozotocin-diabetes on rat liver mitochondrial adenosine triphosphatase turnover.

A Jordá 1, E Pérez-Pastor 1, M Portolés 1
PMCID: PMC1149047  PMID: 2969728

Abstract

The apparent turnover rates of some mitochondrial enzymes can be modified in diabetes. We studied the effect of streptozotocin-diabetes on the half-life of a protein tightly bound to the inner membrane, ATPase. The half-life (t 1/2), measured by the double-isotope technique, decreased by approx. 20% in diabetes (from approximately equal to 2.56 days in controls to approximately equal to 2.06 days in diabetic rats). These results suggest that diabetes produces an increase in degradation of ATPase by a mechanism which is not yet clear, possibly influenced by alterations induced by diabetes in hepatic lysosomes that are associated with hepatic autophagy.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amherdt M., Harris V., Renold A. E., Orci L., Unger R. H. Hepatic autography in uncontrolled experimental diabetes and its relationships to insulin and glucagon. J Clin Invest. 1974 Jul;54(1):188–193. doi: 10.1172/JCI107742. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BRADLEY L. B., JACOB M., JACOBS E. E., SANADI D. R. Uncoupling of oxidative phosphorylation by cadmium ion. J Biol Chem. 1956 Nov;223(1):147–156. [PubMed] [Google Scholar]
  3. Bond J. S. Failure to demonstrate increased protein turnover and intracellular proteinase activity in livers of mice with streptozotocin-induced diabetes. Diabetes. 1980 Aug;29(8):648–654. doi: 10.2337/diab.29.8.648. [DOI] [PubMed] [Google Scholar]
  4. Catterall W. A., Pedersen P. L. Adenosine triphosphatase from rat liver mitochondria. I. Purification, homogeneity, and physical properties. J Biol Chem. 1971 Aug 25;246(16):4987–4994. [PubMed] [Google Scholar]
  5. Clarke S. A major polypeptide component of rat liver mitochondria: carbamyl phosphate synthetase. J Biol Chem. 1976 Feb 25;251(4):950–961. [PubMed] [Google Scholar]
  6. Cohen P. P. Biochemical differentiation during amphibian metamorphosis. Science. 1970 May 1;168(3931):533–543. doi: 10.1126/science.168.3931.533. [DOI] [PubMed] [Google Scholar]
  7. Dice J. F., Walker C. D., Byrne B., Cardiel A. General characteristics of protein degradation in diabetes and starvation. Proc Natl Acad Sci U S A. 1978 May;75(5):2093–2097. doi: 10.1073/pnas.75.5.2093. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Felipo V. A rat liver cell-free system for the synthesis of proteins and their transport into mitochondria. Physiol Chem Phys Med NMR. 1986;18(1):25–32. [PubMed] [Google Scholar]
  9. Felipo V., Grisolía S. Adenosine 5'-triphosphate stimulates the release of polypeptides from mitochondria. FEBS Lett. 1985 Apr 8;183(1):60–64. doi: 10.1016/0014-5793(85)80954-6. [DOI] [PubMed] [Google Scholar]
  10. Glass R. D., Doyle D. On the measurement of protein turnover in animal cells. J Biol Chem. 1972 Aug 25;247(16):5234–5242. [PubMed] [Google Scholar]
  11. Goldberg A. L., St John A. C. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976;45:747–803. doi: 10.1146/annurev.bi.45.070176.003531. [DOI] [PubMed] [Google Scholar]
  12. Grisolía S., Knecht E., Hernández-Yago J., Wallace R. Turnover and degradation of mitochondria and their proteins. Ciba Found Symp. 1979;(75):167–188. doi: 10.1002/9780470720585.ch11. [DOI] [PubMed] [Google Scholar]
  13. Jordá A., Cabo J., Grisolia S. Changes in the levels of urea cycle enzymes and in metabolites thereof in diabetes. Enzyme. 1981;26(5):240–244. doi: 10.1159/000459185. [DOI] [PubMed] [Google Scholar]
  14. Jordá A., Gomez M., Cabo J., Grisolía S. Effect of streptozotocin diabetes on some urea cycle enzymes. Biochem Biophys Res Commun. 1982 May 14;106(1):37–43. doi: 10.1016/0006-291x(82)92054-x. [DOI] [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. Lusty C. J. Carbamoylphosphate synthetase I of rat-liver mitochondria. Purification, properties, and polypeptide molecular weight. Eur J Biochem. 1978 Apr 17;85(2):373–383. doi: 10.1111/j.1432-1033.1978.tb12249.x. [DOI] [PubMed] [Google Scholar]
  17. Nicoletti M., Guerri C., Grisolia S. Turnover of carbamyl-phosphate synthase, of other mitochondrial enzymes and of rat tissues. Effect of diet and of thyroidectomy. Eur J Biochem. 1977 May 16;75(2):583–592. doi: 10.1111/j.1432-1033.1977.tb11558.x. [DOI] [PubMed] [Google Scholar]
  18. Portolés M., Miñana M. D., Jordá A., Grisolía S. Caffeine-induced changes in the composition of the free amino acid pool of the cerebral cortex. Neurochem Res. 1985 Jul;10(7):887–895. doi: 10.1007/BF00964626. [DOI] [PubMed] [Google Scholar]
  19. Pérez-Pastor E., Wallace R., Grisolía S. Turnover of adenosine triphosphatase from rat liver mitochondria. Effect of high-protein and low-protein diets. Eur J Biochem. 1982 Oct;127(2):275–278. doi: 10.1111/j.1432-1033.1982.tb06866.x. [DOI] [PubMed] [Google Scholar]
  20. Soler J., Timoneda J., de Arriaga D., Grisolía S. Participation of the inner mitochondrial membrane in the inactivation of carbamyl phosphate synthase and of adenosine triphosphatase by lysosomes. Biochem Biophys Res Commun. 1980 Nov 17;97(1):100–106. doi: 10.1016/s0006-291x(80)80140-9. [DOI] [PubMed] [Google Scholar]
  21. Timoneda J., Wallace R., Grisolía S. Isolation of a mitochondrial factor from rat liver which potentiates the inactivation of glutamate dehydrogenase by lysosomes. Biochem Biophys Res Commun. 1981 Jul 30;101(2):555–562. doi: 10.1016/0006-291x(81)91295-x. [DOI] [PubMed] [Google Scholar]
  22. Zaragozá R., Renau-Piqueras J., Portolés M., Hernández-Yago J., Jordá A., Grisolía S. Rats fed prolonged high protein diets show an increase in nitrogen metabolism and liver megamitochondria. Arch Biochem Biophys. 1987 Nov 1;258(2):426–435. doi: 10.1016/0003-9861(87)90364-x. [DOI] [PubMed] [Google Scholar]

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