Superoxide activates mitochondrial uncoupling proteins

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 and Martin D. Brand ()
Additional contact information
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

Nature, 2002, vol. 415, issue 6867, 96-99

Abstract: 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.

Date: 2002
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/415096a Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:415:y:2002:i:6867:d:10.1038_415096a

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/415096a

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().