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Allosteric activation of pyruvate kinase via NAD+ in rat liver cells.

Abstract : In isolated rat hepatocytes, it has previously been reported that a rise in the ATP content induces a proportional increase in cytosolic NAD+ concentration [Devin, A., Guérin, B. & Rigoulet, M. (1997) FEBS Lett. 410, 329-332]. This occurs under physiological conditions such as various substrates or different energetic states. To investigate the effect of a physiological rise in cytosolic [NAD+] per se on glycolysis and gluconeogenesis, an increase in [NAD+] induced by exogenous nicotinamide addition was obtained without a change in redox potential, ATP/ADP ratio and ATP concentration. Using dihydroxyacetone as substrate, we found that an increase in cytosolic [NAD+] decreases gluconeogenesis and enhances glycolysis without significant alteration of dihydroxyacetone consumption rate. These modifications are the consequence of an allosteric activation of pyruvate kinase via cytosolic NAD+ content. Thus, in addition to the well-known thermodynamic control of glycolysis by pyridine-nucleotide redox status, our study points to a new mechanism of glycolytic flux regulation by NAD+ concentration at the level of pyruvate kinase activity.
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Contributor : Sarah Hamant <>
Submitted on : Saturday, June 6, 2009 - 12:36:20 PM
Last modification on : Wednesday, December 4, 2019 - 11:14:05 AM


  • HAL Id : inserm-00389993, version 1
  • PUBMED : 11453987




Anne Devin, Véronique Nogueira, Xavier Leverve, Bernard Guérin, Michel Rigoulet. Allosteric activation of pyruvate kinase via NAD+ in rat liver cells.. European Journal of Biochemistry, Wiley, 2001, 268 (14), pp.3943-9. ⟨inserm-00389993⟩



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