Go to JCI Insight
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Alerts
  • Advertising/recruitment
  • Subscribe
  • Contact
  • Current Issue
  • Past Issues
  • By specialty
    • COVID-19
    • Cardiology
    • Gastroenterology
    • Immunology
    • Metabolism
    • Nephrology
    • Neuroscience
    • Oncology
    • Pulmonology
    • Vascular biology
    • All ...
  • Videos
    • Conversations with Giants in Medicine
    • Author's Takes
  • Reviews
    • View all reviews ...
    • 100th Anniversary of Insulin's Discovery (Jan 2021)
    • Hypoxia-inducible factors in disease pathophysiology and therapeutics (Oct 2020)
    • Latency in Infectious Disease (Jul 2020)
    • Immunotherapy in Hematological Cancers (Apr 2020)
    • Big Data's Future in Medicine (Feb 2020)
    • Mechanisms Underlying the Metabolic Syndrome (Oct 2019)
    • Reparative Immunology (Jul 2019)
    • View all review series ...
  • Viewpoint
  • Collections
    • Recently published
    • In-Press Preview
    • Commentaries
    • Concise Communication
    • Editorials
    • Viewpoint
    • Top read articles
  • Clinical Medicine
  • JCI This Month
    • Current issue
    • Past issues

  • Current issue
  • Past issues
  • Specialties
  • Reviews
  • Review series
  • Conversations with Giants in Medicine
  • Author's Takes
  • Recently published
  • In-Press Preview
  • Commentaries
  • Concise Communication
  • Editorials
  • Viewpoint
  • Top read articles
  • About
  • Editors
  • Consulting Editors
  • For authors
  • Alerts
  • Advertising/recruitment
  • Subscribe
  • Contact
Top
  • View PDF
  • Download citation information
  • Send a letter
  • Share this article
  • Terms of use
  • Standard abbreviations
  • Need Help? E-mail the JCI
  • Top
  • Abstract
  • Version history
  • Article usage
  • Citations to this article

Advertisement

Research Article Free access | 10.1172/JCI1168

Cyclic AMP suppresses the inhibition of glycolysis by alternative oxidizable substrates in the heart.

C Depre, S Ponchaut, J Deprez, L Maisin, and L Hue

Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, and Division of Cardiology, Louvain University Medical School, Brussels, Belgium.

Find articles by Depre, C. in: JCI | PubMed | Google Scholar

Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, and Division of Cardiology, Louvain University Medical School, Brussels, Belgium.

Find articles by Ponchaut, S. in: JCI | PubMed | Google Scholar

Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, and Division of Cardiology, Louvain University Medical School, Brussels, Belgium.

Find articles by Deprez, J. in: JCI | PubMed | Google Scholar

Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, and Division of Cardiology, Louvain University Medical School, Brussels, Belgium.

Find articles by Maisin, L. in: JCI | PubMed | Google Scholar

Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, and Division of Cardiology, Louvain University Medical School, Brussels, Belgium.

Find articles by Hue, L. in: JCI | PubMed | Google Scholar

Published January 15, 1998 - More info

Published in Volume 101, Issue 2 on January 15, 1998
J Clin Invest. 1998;101(2):390–397. https://doi.org/10.1172/JCI1168.
© 1998 The American Society for Clinical Investigation
Published January 15, 1998 - Version history
View PDF
Abstract

In normoxic conditions, myocardial glucose utilization is inhibited when alternative oxidizable substrates are available. In this work we show that this inhibition is relieved in the presence of cAMP, and we studied the mechanism of this effect. Working rat hearts were perfused with 5.5 mM glucose alone (controls) or together with 5 mM lactate, 5 mM beta-hydroxybutyrate, or 1 mM palmitate. The effects of 0.1 mM chlorophenylthio-cAMP (CPT-cAMP), a cAMP analogue, were studied in each group. Glucose uptake, flux through 6-phosphofructo-1-kinase, and pyruvate dehydrogenase activity were inhibited in hearts perfused with alternative substrates, and addition of CPT-cAMP completely relieved the inhibition. The mechanism by which CPT-cAMP induced a preferential utilization of glucose was related to an increased glucose uptake and glycolysis, and to an activation of phosphorylase, pyruvate dehydrogenase, and 6-phosphofructo-2-kinase, the enzyme responsible for the synthesis of fructose 2,6-bisphosphate, the well-known stimulator of 6-phosphofructo-1-kinase. In vitro phosphorylation of 6-phosphofructo-2-kinase by cAMP-dependent protein kinase increased the Vmax of the enzyme and decreased its sensitivity to the inhibitor citrate. Therefore, in hearts perfused with various oxidizable substrates, cAMP induces a preferential utilization of glucose by a concerted stimulation of glucose transport, glycolysis, glycogen breakdown, and glucose oxidation.

Version history
  • Version 1 (January 15, 1998): No description

Article tools

  • View PDF
  • Download citation information
  • Send a letter
  • Share this article
  • Terms of use
  • Standard abbreviations
  • Need Help? E-mail the JCI

Metrics

  • Article usage
  • Citations to this article

Go to

  • Top
  • Abstract
  • Version history
Advertisement
Advertisement
Follow JCI:
Copyright © 2021 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

Sign up for email alerts