Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1984 Feb 15;218(1):157–163. doi: 10.1042/bj2180157

The ability of adenosine to decrease the concentration of fructose 2,6-bisphosphate in isolated hepatocytes. A cyclic AMP-mediated effect.

R Bartrons, E Van Schaftingen, H G Hers
PMCID: PMC1153319  PMID: 6324747

Abstract

The presence of adenosine (25-250 microM) or of 2-chloroadenosine (2.5-100 microM) in the incubation medium caused a marked decrease in the concentration of fructose 2,6-bisphosphate in isolated hepatocytes. This effect was accompanied by an increase in the concentration of cyclic AMP, an activation of phosphorylase and of fructose 2,6-bisphosphatase, and an inactivation of pyruvate kinase and of 6-phosphofructo-2-kinase. As a rule, the changes in the fructose 2,6-bisphosphate-modifying system were slower but more persistent than those in the activities of phosphorylase and pyruvate kinase. The effect of the nucleoside to decrease the concentration of fructose 2,6-bisphosphate was not affected by an inhibitor of adenosine transport and could not be obtained in a liver high-speed supernatant. These data indicate that the effect of adenosine to decrease the concentration of fructose 2,6-bisphosphate is mediated by the stimulation of adenylate cyclase, secondary to the binding of adenosine to membranous receptors. Like glucagon, 2-chloroadenosine stimulated gluconeogenesis in isolated hepatocytes, whereas adenosine had an opposite effect.

Full text

PDF
157

Selected References

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

  1. Arch J. R., Newsholme E. A. Activities and some properties of 5'-nucleotidase, adenosine kinase and adenosine deaminase in tissues from vertebrates and invertebrates in relation to the control of the concentration and the physiological role of adenosine. Biochem J. 1978 Sep 15;174(3):965–977. doi: 10.1042/bj1740965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Arch J. R., Newsholme E. A. The control of the metabolism and the hormonal role of adenosine. Essays Biochem. 1978;14:82–123. [PubMed] [Google Scholar]
  3. Bartrons R., Hue L., Van Schaftingen E., Hers H. G. Hormonal control of fructose 2,6-bisphosphate concentration in isolated rat hepatocytes. Biochem J. 1983 Sep 15;214(3):829–837. doi: 10.1042/bj2140829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bontemps F., Van den Berghe G., Hers H. G. Evidence for a substrate cycle between AMP and adenosine in isolated hepatocytes. Proc Natl Acad Sci U S A. 1983 May;80(10):2829–2833. doi: 10.1073/pnas.80.10.2829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. CLARKE D. A., DAVOLL J., PHILIPS F. S., BROWN G. B. Enzymatic deamination and vasodepressor effects of adenosine analogs. J Pharmacol Exp Ther. 1952 Nov;106(3):291–302. [PubMed] [Google Scholar]
  6. El-Maghrabi M. R., Claus T. H., Pilkis J., Fox E., Pilkis S. J. Regulation of rat liver fructose 2,6-bisphosphatase. J Biol Chem. 1982 Jul 10;257(13):7603–7607. [PubMed] [Google Scholar]
  7. Fain J. N., Shepherd R. E. Adenosine, cyclic AMP metabolism, and glycogenolysis in rat liver cells. J Biol Chem. 1977 Nov 25;252(22):8066–8070. [PubMed] [Google Scholar]
  8. Felíu J. E., Hue L., Hers H. G. Regulation in vitro and in vivo of adenosine 3':5'-monophosphate-dependent inactivation of rat-liver pyruvate kinase type L. Eur J Biochem. 1977 Dec;81(3):609–617. doi: 10.1111/j.1432-1033.1977.tb11988.x. [DOI] [PubMed] [Google Scholar]
  9. Henderson J. F., Paterson A. R., Caldwell I. C., Paul B., Chan M. C., Lau K. F. Inhibitors of nucleoside and nucleotide metabolism. Cancer Chemother Rep 2. 1972 Nov;3(1):71–85. [PubMed] [Google Scholar]
  10. Hers H. G., Hue L. Gluconeogenesis and related aspects of glycolysis. Annu Rev Biochem. 1983;52:617–653. doi: 10.1146/annurev.bi.52.070183.003153. [DOI] [PubMed] [Google Scholar]
  11. Hers H. G., Van Schaftingen E. Fructose 2,6-bisphosphate 2 years after its discovery. Biochem J. 1982 Jul 15;206(1):1–12. doi: 10.1042/bj2060001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hue L., Bontemps F., Hers H. The effects of glucose and of potassium ions on the interconversion of the two forms of glycogen phosphorylase and of glycogen synthetase in isolated rat liver preparations. Biochem J. 1975 Oct;152(1):105–114. doi: 10.1042/bj1520105. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hue L., Felíu J. E., Hers H. G. Control of gluconeogenesis and of enzymes of glycogen metabolism in isolated rat hepatocytes. A parallel study of the effect of phenylephrine and of glucagon. Biochem J. 1978 Dec 15;176(3):791–797. doi: 10.1042/bj1760791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Londos C., Cooper D. M., Wolff J. Subclasses of external adenosine receptors. Proc Natl Acad Sci U S A. 1980 May;77(5):2551–2554. doi: 10.1073/pnas.77.5.2551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lund P., Cornell N. W., Krebs H. A. Effect of adenosine on the adenine nucleotide content and metabolism of hepatocytes. Biochem J. 1975 Dec;152(3):593–599. doi: 10.1042/bj1520593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Marchand J. C., Lavoinne A., Giroz M., Matray F. The influence of adenosine on intermediary metabolism of isolated hepatocytes. Biochimie. 1979;61(11-12):1273–1282. doi: 10.1016/s0300-9084(80)80286-0. [DOI] [PubMed] [Google Scholar]
  17. Miller R. L., Adamczyk D. L., Miller W. H., Koszalka G. W., Rideout J. L., Beacham L. M., 3rd, Chao E. Y., Haggerty J. J., Krenitsky T. A., Elion G. B. Adenosine kinase from rabbit liver. II. Substrate and inhibitor specificity. J Biol Chem. 1979 Apr 10;254(7):2346–2352. [PubMed] [Google Scholar]
  18. Olaus T. H., Anand-Srivastava M. B., Johnson R. A. Regulation of hepatocyte cAMP and pyruvate kinase by site-specific analogs of adenosine. Mol Cell Endocrinol. 1982 May;26(3):269–279. doi: 10.1016/0303-7207(82)90116-2. [DOI] [PubMed] [Google Scholar]
  19. Steiner A. L., Parker C. W., Kipnis D. M. Radioimmunoassay for cyclic nucleotides. I. Preparation of antibodies and iodinated cyclic nucleotides. J Biol Chem. 1972 Feb 25;247(4):1106–1113. [PubMed] [Google Scholar]
  20. Van Schaftingen E., Hers H. G. Formation of fructose 2,6-bisphosphate from fructose 1,6-bisphosphate by intramolecular cyclisation followed by alkaline hydrolysis. Eur J Biochem. 1981 Jul;117(2):319–323. doi: 10.1111/j.1432-1033.1981.tb06339.x. [DOI] [PubMed] [Google Scholar]
  21. Van Schaftingen E., Lederer B., Bartrons R., Hers H. G. A kinetic study of pyrophosphate: fructose-6-phosphate phosphotransferase from potato tubers. Application to a microassay of fructose 2,6-bisphosphate. Eur J Biochem. 1982 Dec;129(1):191–195. doi: 10.1111/j.1432-1033.1982.tb07039.x. [DOI] [PubMed] [Google Scholar]
  22. Van den Berghe G., Bontemps F., Hers H. G. Purine catabolism in isolated rat hepatocytes. Influence of coformycin. Biochem J. 1980 Jun 15;188(3):913–920. doi: 10.1042/bj1880913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. van Schaftingen E., Davies D. R., Hers H. G. Fructose-2,6-bisphosphatase from rat liver. Eur J Biochem. 1982 May;124(1):143–149. doi: 10.1111/j.1432-1033.1982.tb05917.x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES