Reconstitution of Novel Mitochondrial Uncoupling Proteins UCP2 and UCP3

Žáčkova, Markéta; Ježek, Petr

doi:10.1023/a:1016009022186

Cited by 25Mitochondrial Function and PathologyATP Synthase and ATPases ResearchAdipose Tissue and Metabolism

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Reconstitution of Novel Mitochondrial Uncoupling Proteins UCP2 and UCP3

Žáčkova, Markéta, Ježek, Petr·2002·Bioscience Reports

DOI 10.1023/a:1016009022186

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Abstract

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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Activating ω-6 Polyunsaturated Fatty Acids and Inhibitory Purine Nucleotides Are High Affinity Ligands for Novel Mitochondrial Uncoupling Proteins UCP2 and UCP3
Žáčková, M., Škobisová, E., Urbánková, E., & Ježek, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212850200 · Cited by 91
Self-citation
Polyunsaturated fatty acids activate human uncoupling proteins 1 and 2 in planar lipid bilayers
Beck, V., Jabůrek, M., Demina, T. V., Rupprecht, A., Porter, R. K., Ježek, P., & Pohl, E. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-7489com · Cited by 121
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A structure–activity study of fatty acid interaction with mitochondrial uncoupling protein
Ježek, P., Modrianský, M., & Garlid, K. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00335-9 · Cited by 74
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Uncoupling proteins 2 and 3 are highly active H + transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)
Echtay, K. S., Winkler, E., Frischmuth, K., & Klingenberg, M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1416 · Cited by 313
Substitutional mutations in the uncoupling protein-specific sequences of mitochondrial uncoupling protein UCP1 lead to the reduction of fatty acid-induced H+ uniport
Urbánková, E., Hanák, P., Škobisová, E., Růžička, M., & Ježek, P. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00131-0 · Cited by 20
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Authors: Žáčkova, M., & Ježek, P.
Affiliations: Institute of Physiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, 14220, Prague 4, Czech Republic
Czech Academy of Sciences (CZ)
ORCID: Ježek, Petr
Venue: Bioscience Reports
Publisher: Portland Press Ltd.
Published: 2002-02-01
Volume: 22
Issue: 1
Pages: 33-46
ISSN: 0144-8463 (ISSN-L)
1573-4935
DOI: 10.1023/a:1016009022186
OpenAlex: W190962978
Cited by: 25
References: 57
Citations by year: 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1
FWCI: 0.81
Type: journal article
Language: en
Open access: closed
Locations: Bioscience Reports (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
Keywords: UCP2, UCP3, mitochondrial uncoupling proteins, proteoliposomes, long-chain fatty acids, oleic acid, ATP inhibition, GTP inhibition, coenzyme Q10, UCP1
MeSH terms: Uncoupling Protein 2, Uncoupling Protein 3, Carrier Proteins, Fatty Acids, Humans, Ion Channels, Mitochondria, Proteins, Yeasts, Mitochondrial Proteins, Membrane Transport Proteins

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Reconstitution of Novel Mitochondrial Uncoupling Proteins UCP2 and UCP3

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