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

Berger, Karin LU ; Sivars, Ulf; Sörhede Winzell, Maria LU ; Johansson, Peter LU ; Hellman, Ulf; Rippe, Catarina LU and Erlanson-Albertsson, Charlotte LU (2002) In Nutritional Neuroscience 5(3). p.201-210
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Ins-1, Enterostatin, Insulin, Thermogenesis, Uncoupling Protein
in
Nutritional Neuroscience
volume
5
issue
3
pages
201 - 210
publisher
Taylor & Francis
external identifiers
  • wos:000177387600004
  • pmid:12041876
  • scopus:0036014865
ISSN
1476-8305
DOI
10.1080/10284150290008604
language
English
LU publication?
yes
id
e0b6df51-dfb3-4364-bce3-d4d995346b20 (old id 108636)
date added to LUP
2007-07-10 12:00:32
date last changed
2017-01-01 04:54:52
@article{e0b6df51-dfb3-4364-bce3-d4d995346b20,
  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.},
  author       = {Berger, Karin and Sivars, Ulf and Sörhede Winzell, Maria and Johansson, Peter and Hellman, Ulf and Rippe, Catarina and Erlanson-Albertsson, Charlotte},
  issn         = {1476-8305},
  keyword      = {Ins-1,Enterostatin,Insulin,Thermogenesis,Uncoupling Protein},
  language     = {eng},
  number       = {3},
  pages        = {201--210},
  publisher    = {Taylor & Francis},
  series       = {Nutritional Neuroscience},
  title        = {Mitochondrial ATP synthase--a possible target protein in the regulation of energy metabolism in vitro and in vivo.},
  url          = {http://dx.doi.org/10.1080/10284150290008604},
  volume       = {5},
  year         = {2002},
}