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.

• MeSH
• iontové kanály MeSH
• kvasinky metabolismus   MeSH
• lidé MeSH
• mastné kyseliny metabolismus   MeSH
• membránové transportní proteiny * MeSH
• mitochondriální proteiny * MeSH
• mitochondrie metabolismus   MeSH
• proteiny metabolismus   MeSH
• transportní proteiny metabolismus   MeSH
• uncoupling protein 2 MeSH
• uncoupling protein 3 MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• přehledy MeSH
• Research Support, U.S. Gov't, Non-P.H.S. MeSH
• Názvy látek
• iontové kanály MeSH
• mastné kyseliny MeSH
• membránové transportní proteiny * MeSH
• mitochondriální proteiny * MeSH
• proteiny MeSH
• transportní proteiny MeSH
• UCP2 protein, human MeSH Prohlížeč
• UCP3 protein, human MeSH Prohlížeč
• uncoupling protein 2 MeSH
• uncoupling protein 3 MeSH