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

Karin Berger, Ulf Sivars, Maria Sörhede Winzell, Peter Johansson, Ulf Hellman, Catarina Rippe, Charlotte Erlanson-Albertsson

Research output: Contribution to journalReview articlepeer-review

37 Citations (SciVal)

Abstract

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.
Original languageEnglish
Pages (from-to)201-210
JournalNutritional Neuroscience
Volume5
Issue number3
DOIs
Publication statusPublished - 2002

Subject classification (UKÄ)

  • Basic Medicine

Keywords

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

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