Reconstitution of novel mitochondrial uncoupling proteins UCP2 and UCP3
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Review
- MeSH
- Ion Channels MeSH
- Yeasts metabolism MeSH
- Humans MeSH
- Fatty Acids metabolism MeSH
- Membrane Transport Proteins * MeSH
- Mitochondrial Proteins * MeSH
- Mitochondria metabolism MeSH
- Proteins metabolism MeSH
- Carrier Proteins metabolism MeSH
- Uncoupling Protein 2 MeSH
- Uncoupling Protein 3 MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Names of Substances
- Ion Channels MeSH
- Fatty Acids MeSH
- Membrane Transport Proteins * MeSH
- Mitochondrial Proteins * MeSH
- Proteins MeSH
- Carrier Proteins MeSH
- UCP2 protein, human MeSH Browser
- UCP3 protein, human MeSH Browser
- Uncoupling Protein 2 MeSH
- Uncoupling Protein 3 MeSH
Reconstitution of novel mitochondrial uncoupling proteins, human UCP2 and UCP3, expressed in yeast, was performed to characterize fatty acid (FA)-induced H+ efflux in the resulted proteoliposomes. We now demonstrate for the first time that representatives of physiologically abundant long chain FAs, saturated or unsaturated, activate H+ translocation in UCP2- and UCP3-proteoliposomes. Efficiency of lauric, palmitic or linoleic acid was roughly the same, but oleic acid induced faster H+ uniport. We have confirmed that ATP and GTP inhibit such FA-induced H+ uniport mediated by UCP2 and UCP3. Coenzyme Q10 did not further significantly activate the observed H+ efflux. In conclusion, careful instant reconstitution yields intact functional recombinant proteins, UCP2 and UCP3, the activity of which is comparable with UCP1.
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