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No Evidence for a Basal, Retinoic, or Superoxide-induced Uncoupling Activity of the Uncoupling Protein 2 Present in Spleen or Lung Mitochondria
Open accessAbstract
The phenotypes observed in mice whose uncoupling protein (Ucp2) gene had been invalidated by homologous recombination (Ucp2(-/-) mice) are consistent with an increase in mitochondrial membrane potential in macrophages and pancreatic beta cells. This could support an uncoupling (proton transport) activity of UCP2 in the inner mitochondrial membrane in vivo. We used mitochondria from lung or spleen, the two organs expressing the highest level of UCP2, to compare the proton leak of the mitochondrial inner membrane of wild-type and Ucp2(-/-) mice. No difference was observed under basal conditions. Previous reports have concluded that retinoic acid and superoxide activate proton transport by UCP2. Spleen mitochondria showed a higher sensitivity to retinoic acid than liver mitochondria, but this was not caused by UCP2. In contrast with a previous report, superoxide failed to increase the proton leak rate in kidney mitochondria, where no UCP2 expression was detected, and also in spleen mitochondria, which does not support stimulation of UCP2 uncoupling activity by superoxide. Finally, no increase in the ATP/ADP ratio was observed in spleen or lung of Ucp2(-/-) mice. Therefore, no evidence could be gathered for the uncoupling activity of the UCP2 present in spleen or lung mitochondria. Although this may be explained by difficulties with isolated mitochondria, it may also indicate that UCP2 has another physiological significance in spleen and lung.
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“Moreover, mitochondria isolated from UCP3 (45, 91) or UCP2 KO mice (73, 176) do not show a decrease in basal proton conductance.”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [73]
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Metadata
- Authors
- Couplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institut National de la Recherche Agronomique (FR)
- Corresponding author
- Bouillaud, Frédéric
- ORCID
- Bouillaud, Frédéric
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-07
- Volume
- 277
- Issue
- 29
- Pages
- 26268-26275
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2032301380
- Cited by
- 161
- References
- 51
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 2 · 2020: 4 · 2019: 6 · 2018: 8 · 2017: 5 · 2016: 5 · 2015: 4 · 2014: 7 · 2013: 7 · 2012: 9
- FWCI
- 5.79
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- UCP2, mitochondrial proton leak, mitochondrial membrane potential, retinoic acid, superoxide, UCP2 knockout mice, lung mitochondria, ATP/ADP ratio, mitochondrial uncoupling
- MeSH terms
- Uncoupling Protein 2, Animals, Flow Cytometry, Ion Channels, Kidney, Lung, Membrane Potentials, Mitochondria, Oxygen Consumption, Phenotype, Proteins, RNA, Messenger, Spleen, Superoxides, Tretinoin, Mice, Knockout, Rhodamine 123, Mitochondrial Proteins, Membrane Transport Proteins, Mice
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