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. 1986 Jul;83(14):5067–5070. doi: 10.1073/pnas.83.14.5067

Intracellular site of insulin action: mitochondrial Krebs cycle.

S P Bessman, C Mohan, I Zaidise
PMCID: PMC323891  PMID: 3523482

Abstract

Effect of insulin on the oxidation of carbons-1,4 and -2,3 of succinate and their incorporation into protein were studied in isolated rat hepatocytes and diaphragm muscle pieces. Oxidation of carbons-2,3 of succinate and their incorporation into hepatocyte protein were stimulated significantly by insulin. Insulin had only a trivial effect on 14CO2 formation from the carboxyl carbons of succinate. These data suggest that insulin affects only those carbons of succinate that are metabolized in the intramitochondrial Krebs cycle.

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Selected References

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

  1. BESSMAN S. P. Diabetes mellitus: observations, theoretical and practical. J Pediatr. 1960 Feb;56:191–203. doi: 10.1016/s0022-3476(60)80119-9. [DOI] [PubMed] [Google Scholar]
  2. Bessman S. P. A molecular basis for the mechanism of insulin action. Am J Med. 1966 May;40(5):740–749. doi: 10.1016/0002-9343(66)90155-0. [DOI] [PubMed] [Google Scholar]
  3. Bessman S. P., Geiger P. J. Compartmentation of hexokinase and creatine phosphokinase, cellular regulation, and insulin action. Curr Top Cell Regul. 1980;16:55–86. doi: 10.1016/b978-0-12-152816-4.50007-8. [DOI] [PubMed] [Google Scholar]
  4. Bessman S. P. Hexokinase acceptor theory of insulin action. New evidence. Isr J Med Sci. 1972 Mar;8(3):344–352. [PubMed] [Google Scholar]
  5. CAHILL G. F., Jr, ASHMORE J., EARLE A. S., ZOTTU S. Glucose penetration into liver. Am J Physiol. 1958 Mar;192(3):491–496. doi: 10.1152/ajplegacy.1958.192.3.491. [DOI] [PubMed] [Google Scholar]
  6. Krebs H. A., Eggleston L. V. The effect of insulin on oxidations in isolated muscle tissue. Biochem J. 1938 May;32(5):913–925. doi: 10.1042/bj0320913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Marshall S. Dual pathways for the intracellular processing of insulin. Relationship between retroendocytosis of intact hormone and the recycling of insulin receptors. J Biol Chem. 1985 Nov 5;260(25):13524–13531. [PubMed] [Google Scholar]
  9. Mohan C., Bessman S. P. Anabolic regulation of gluconeogenesis by insulin in isolated rat hepatocytes. Arch Biochem Biophys. 1985 Nov 1;242(2):563–573. doi: 10.1016/0003-9861(85)90244-9. [DOI] [PubMed] [Google Scholar]
  10. Mohan C., Bessman S. P. In vitro protein degradation measured by differential loss of labeled methionine and 3-methylhistidine: The effect of Insulin. Anal Biochem. 1981 Nov 15;118(1):17–22. doi: 10.1016/0003-2697(81)90150-0. [DOI] [PubMed] [Google Scholar]
  11. Mohan C., Bessman S. P. Insulin "inhibition" of gluconeogenesis by stimulation of protein synthesis. Biochem Med. 1981 Dec;26(3):403–426. doi: 10.1016/0006-2944(81)90016-8. [DOI] [PubMed] [Google Scholar]
  12. Seglen P. O. Preparation of isolated rat liver cells. Methods Cell Biol. 1976;13:29–83. doi: 10.1016/s0091-679x(08)61797-5. [DOI] [PubMed] [Google Scholar]

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