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. 1968 Oct;109(5):867–875. doi: 10.1042/bj1090867

Changes in the concentrations of some phosphorylated intermediates and stimulation of glycolysis in liver slices

G Gaja 1, G Ragnotti 1, F Cajone 1, A Bernelli-Zazzera 1
PMCID: PMC1187039  PMID: 4301449

Abstract

1. The concentrations of some phosphorylated glycolytic intermediates and of NADH were measured in glycolysing rat liver slices. 2. In anaerobically incubated liver slices the concentration of hexose monophosphates decreases during the first 20min. of incubation, whereas the concentrations of fructose diphosphate and triose phosphates increase progressively. 3. In liver slices from fed rats, previously exposed to oxygen, the stimulated anaerobic glycolysis is accompanied by an increase in the concentration of hexose monophosphates; fructose diphosphate and triose phosphates maintain the concentrations reached at the end of the aerobic preincubation. 4. The same pattern in the concentration of glycolytic phosphorylated intermediates is seen under all conditions where aerobic preincubation brings about a stimulation of anaerobic glycolysis. A similar pattern is also found in liver slices from fed rats incubated anaerobically in the presence of fructose; these slices display a high glycolytic activity, which is not further affected by previous aerobic incubation. 5. The concentration of NADH decreases in liver slices during exposure to oxygen; during the subsequent anaerobic glycolysis the concentration increases but is always lower in preincubated than in non-preincubated liver slices. 6. The results of the present experiments suggest that the limiting step mainly affected by the preliminary exposure to oxygen might be at the level of the utilization of triose phosphates.

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Selected References

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

  1. Bernelli-Zazzera A., Gaja G., Ragnotti G. The stimulation of glycolysis by previous aerobiosis in rat-liver slices. Biochem J. 1966 Jul;100(1):114–119. doi: 10.1042/bj1000114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CARROLL N. V., LONGLEY R. W., ROE J. H. The determination of glycogen in liver and muscle by use of anthrone reagent. J Biol Chem. 1956 Jun;220(2):583–593. [PubMed] [Google Scholar]
  3. DIPIETRO D. L. SOME ASPECTS OF D-FRUCTOSE METABOLISM IN RAT LIVER. J Biol Chem. 1964 Dec;239:4051–4055. [PubMed] [Google Scholar]
  4. Dickens F., Greville G. D. The metabolism of normal and tumour tissue: The anaerobic conversion of fructose into lactic acid by tumour and adult normal tissues. Biochem J. 1932;26(5):1546–1556. doi: 10.1042/bj0261546. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GREENBAUM A. L., CLARK J. B., MCLEAN P. THE ESTIMATION OF THE OXIDIZED AND REDUCED FORMS OF THE NICOTINAMIDE NUCLEOTIDES. Biochem J. 1965 Apr;95:161–166. doi: 10.1042/bj0950161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gaja G., Ragnotti G., Bernelli-Zazzera A. Effect of aerobic pre-incubation of glycolysis in resting and proliferating liver cells. Nature. 1965 Jul 31;207(996):538–539. doi: 10.1038/207538a0. [DOI] [PubMed] [Google Scholar]
  7. Gaja G., Ragnotti G., Cajone F., Bernelli-Zazzera A. Further studies on the stimulation of glycolysis by previous aerobiosis. Biochem J. 1967 Nov;105(2):647–654. doi: 10.1042/bj1050647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gaja G., Ragnotti G. Variazioni dell'attività glicolitica di sezioni di fegato di ratto dopo incubazione in aerobiosi. Sperimentale. 1966 Jul-Aug;116(4):213–224. [PubMed] [Google Scholar]
  9. Gevers W., Krebs H. A. The effects of adenine nucleotides on carbohydrate metabolism in pigeon-liver homogenates. Biochem J. 1966 Mar;98(3):720–735. doi: 10.1042/bj0980720. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LOWRY O. H., PASSONNEAU J. V. THE RELATIONSHIPS BETWEEN SUBSTRATES AND ENZYMES OF GLYCOLYSIS IN BRAIN. J Biol Chem. 1964 Jan;239:31–42. [PubMed] [Google Scholar]
  11. Orr J. W., Stickland L. H. The metabolism of rat liver during carcinogenesis by butter yellow. Biochem J. 1941 Apr;35(4):479–487. doi: 10.1042/bj0350479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. PAPPIUS H. M., JOHNSON D. M., ELLIOTT K. A. Acid-labile phosphate content of incubated brain slices. Can J Biochem Physiol. 1959 Aug;37(8):999–1010. [PubMed] [Google Scholar]
  13. Rolleston F. S., Newsholme E. A. Control of glycolysis in cerebral cortex slices. Biochem J. 1967 Aug;104(2):524–533. doi: 10.1042/bj1040524. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. UNDERWOOD A. H., NEWSHOLME E. A. PROPERTIES OF PHOSPHOFRUCTOKINASE FROM RAT LIVER AND THEIR RELATION TO THE CONTROL OF GLYCOLYSIS AND GLUCONEOGENESIS. Biochem J. 1965 Jun;95:868–875. doi: 10.1042/bj0950868. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. WOODS M., BURK D. INHIBITION OF TUMOR CELL GLYCOLYSIS BY DPNH2, AND REVERSAL OF THE INHIBITION BY DPN, PYRUVATE OR METHYLENE BLUE. Z Naturforsch B. 1963 Sep;18:731–748. doi: 10.1515/znb-1963-0909. [DOI] [PubMed] [Google Scholar]
  16. Wu R. Control of glycolysis by phosphofructokinase in slices of rat liver, Novikoff hepatoma, and adenocarcinomas. Biochem Biophys Res Commun. 1964;14:79–85. doi: 10.1016/0006-291x(63)90215-8. [DOI] [PubMed] [Google Scholar]

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