Mitochondrial proton leak and the uncoupling protein 1 homologues
Open accessAbstract
Mitochondrial proton leak is the largest single contributor to the standard metabolic rate (SMR) of a rat, accounting for about 20% of SMR. Yet the mechanisms by which proton leak occurs are incompletely understood. The available evidence suggests that both phospholipids and proteins in the mitochondrial inner membrane are important determinants of proton conductance. The uncoupling protein 1 homologues (e.g. UCP2, UCP3) may play a role in mediating proton leak, but it is unlikely they account for all of the observed proton conductance. Experimental data regarding the functions of these proteins include important ambiguities and contradictions which must be addressed before their function can be confirmed. The physiological role of the proton leak, and of the uncoupling protein 1 homologues, remains similarly unclear.
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The single-electron transfers are tightly controlled and quickly coupled with the second electron transfer.
“However, the single-electron transfers are tightly controlled and quickly coupled with the second electron transfer (107, 293, 294).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [294]
In brown adipose tissue, UCP1 functions as a proton leak.
“However, it is now widely accepted that, in brown adipose tissue (BAT), UCP1 does function in this way.”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [300]
UCP1 overexpression in BAE cells is clearly not physiologic.
“However, this overexpression is clearly not physiologic (300).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [300]
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- Authors
- Stuart, J. A., Cadenas, S., Jekabsons, M. B., Roussel, D., & Brand, M. D.
- Affiliations
- University of Cambridge (GB)
- MRC Mitochondrial Biology Unit (GB)
- Corresponding author
- Brand, M.D
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2001-03
- Volume
- 1504
- Issue
- 1
- Pages
- 144-158
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W2051826214
- Cited by
- 169
- References
- 74
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 7 · 2019: 4 · 2018: 6 · 2017: 3 · 2016: 2 · 2015: 4 · 2014: 2 · 2013: 5 · 2012: 5
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- 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
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- mitochondrial proton leak, UCP2, UCP3, inner mitochondrial membrane, proton conductance, standard metabolic rate, mitochondrial membrane phospholipids, mitochondrial membrane proteins
- MeSH terms
- Uncoupling Protein 2, Uncoupling Protein 3, Uncoupling Protein 1, Amino Acid Sequence, Animals, Basal Metabolism, Carrier Proteins, Diffusion, Humans, Intracellular Membranes, Ion Channels, Membrane Proteins, Mitochondria, Molecular Sequence Data, Proteins, Protons, RNA, Messenger, Sequence Alignment, Sequence Homology, Models, Animal, Mitochondrial Proteins, Membrane Transport Proteins, Animals, Genetically Modified
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