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Superoxide activates mitochondrial uncoupling proteins

Author

Listed:
  • Karim S. Echtay

    (Medical Research Council Dunn Human Nutrition Unit)

  • Damien Roussel

    (Medical Research Council Dunn Human Nutrition Unit)

  • Julie St-Pierre

    (Medical Research Council Dunn Human Nutrition Unit)

  • Mika B. Jekabsons

    (Medical Research Council Dunn Human Nutrition Unit)

  • Susana Cadenas

    (Medical Research Council Dunn Human Nutrition Unit)

  • Jeff A. Stuart

    (Medical Research Council Dunn Human Nutrition Unit)

  • James A. Harper

    (Medical Research Council Dunn Human Nutrition Unit)

  • Stephen J. Roebuck

    (Medical Research Council Dunn Human Nutrition Unit)

  • Alastair Morrison

    (Departments of Comparative Genomics)

  • Susan Pickering

    (Departments of Comparative Genomics)

  • John C. Clapham

    (Departments of Vascular Biology, GlaxoSmithKline)

  • Martin D. Brand

    (Medical Research Council Dunn Human Nutrition Unit)

Abstract

Uncoupling protein 1 (UCP1) diverts energy from ATP synthesis to thermogenesis in the mitochondria of brown adipose tissue by catalysing a regulated leak of protons across the inner membrane1,2. The functions of its homologues, UCP2 and UCP3, in other tissues are debated3,4. UCP2 and UCP3 are present at much lower abundance than UCP1, and the uncoupling with which they are associated is not significantly thermogenic5,6. Mild uncoupling would, however, decrease the mitochondrial production of reactive oxygen species, which are important mediators of oxidative damage7,8. Here we show that superoxide increases mitochondrial proton conductance through effects on UCP1, UCP2 and UCP3. Superoxide-induced uncoupling requires fatty acids and is inhibited by purine nucleotides. It correlates with the tissue expression of UCPs, appears in mitochondria from yeast expressing UCP1, and is absent in skeletal muscle mitochondria from UCP3 knockout mice. Our findings indicate that the interaction of superoxide with UCPs may be a mechanism for decreasing the concentrations of reactive oxygen species inside mitochondria.

Suggested Citation

  • Karim S. Echtay & Damien Roussel & Julie St-Pierre & Mika B. Jekabsons & Susana Cadenas & Jeff A. Stuart & James A. Harper & Stephen J. Roebuck & Alastair Morrison & Susan Pickering & John C. Clapham , 2002. "Superoxide activates mitochondrial uncoupling proteins," Nature, Nature, vol. 415(6867), pages 96-99, January.
    • Handle: RePEc:nat:nature:v:415:y:2002:i:6867:d:10.1038_415096a
    DOI: 10.1038/415096a
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    Cited by:

    1. Weronika Wasyluk & Patrycja Nowicka-Stążka & Agnieszka Zwolak, 2021. "Heart Metabolism in Sepsis-Induced Cardiomyopathy—Unusual Metabolic Dysfunction of the Heart," IJERPH, MDPI, vol. 18(14), pages 1-20, July.
    2. Erminia Donnarumma & Michael Kohlhaas & Elodie Vimont & Etienne Kornobis & Thibault Chaze & Quentin Giai Gianetto & Mariette Matondo & Maryse Moya-Nilges & Christoph Maack & Timothy Wai, 2022. "Mitochondrial Fission Process 1 controls inner membrane integrity and protects against heart failure," Nature Communications, Nature, vol. 13(1), pages 1-24, December.
    3. Maura Calvani & Claudio Favre, 2019. "Antioxidant Nutraceutical approach to Ewing Sarcoma - Where is the Trap?," Biomedical Journal of Scientific & Technical Research, Biomedical Research Network+, LLC, vol. 17(3), pages 12805-12814, April.

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