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Mitochondrial ATP synthase--a possible target protein in the regulation of energy metabolism in vitro and in vivo.

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Author

Summary, in English

The increasing prevalence of obesity in the Western world has stimulated an intense search for mechanisms regulating food intake and energy balance. A number of appetite-regulating peptides have been identified, their receptors cloned and the intracellular events characterized. One possible energy-dissipating mechanism is the mitochondrial uncoupling of ATP-synthesis from respiratory chain oxidation through uncoupling proteins, whereby energy derived from food could be dissipated as heat, instead of stored as ATP. The exact role of the uncoupling proteins in energy balance is, however, uncertain. We show here that mitochondrial F1F0-ATP synthase itself is a target protein for an anorectic peptide, enterostatin, demonstrated both after affinity purification of rat brain membranes and through a direct physical interaction between enterostatin and purified F1-ATP synthase. In insulinoma cells (INS-1) enterostatin was found to target F1F0-ATP synthase, causing an inhibition of ATP production, an increased thermogenesis and increased oxygen consumption. The experiments suggest a role of mitochondrial F1F0-ATP synthase in the suppressed insulin secretion induced by enterostatin. It could be speculated that this targeting mechanism is involved in the decreased energy efficiency following enterostatin treatment in rat.

Publishing year

2002

Language

English

Pages

201-210

Publication/Series

Nutritional Neuroscience

Volume

5

Issue

3

Document type

Journal article review

Publisher

Taylor & Francis

Topic

  • Basic Medicine

Keywords

  • Ins-1
  • Enterostatin
  • Insulin
  • Thermogenesis
  • Uncoupling Protein

Status

Published

Research group

  • Insulin Signal Transduction
  • Molecular Endocrinology
  • Molecular Nutrition
  • Cellular Biomechanics
  • Appetite Regulation

ISBN/ISSN/Other

  • ISSN: 1476-8305