The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
UCP2 and UCP3 rise in starved rat skeletal muscle but mitochondrial proton conductance is unchanged
Abstract
The relationship between UCP2 and UCP3 expression and mitochondrial proton conductance of rat skeletal muscle was examined. Rats were starved for 24 h and the levels of UCP2 and UCP3 mRNA and UCP3 protein were determined by Northern and Western blots. Proton conductance was measured by titrating mitochondrial respiration rate and membrane potential with malonate. Starvation increased UCP2 and UCP3 mRNA levels more than 5‐fold and 4‐fold, respectively, and UCP3 protein levels by 2‐fold. However, proton conductance remained unchanged. These results suggest either that Northern and Western blots do not reflect the levels of active protein or that these UCPs do not catalyse the basal proton conductance in skeletal muscle mitochondria.
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In the citing paper
“fasting has been quite convincingly shown to increase UCP3 protein levels in animal studies (36,37).”
From Prolonged fasting identifies skeletal muscle mitochondrial dysfunction as consequence rather than cause of human insulin resistance (2010) · cites this paper as [37]
In the citing paper
“Regarding UCP-3, several groups reported that UCP-3 has no clear uncoupling effect as it does, for instance, in CHO cells overexpressing this protein [19] or in rat skeletal muscles [20].”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [20]
In the citing paper
“This resembles the discordance in UCP3 expression and proton-leak activity seen in rodents subject to starvation (44) or lipopolysaccharide-induced free fatty acid release (344).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [44]
In the citing paper
“UCP3 is known to be upregulated under conditions of increased free fatty acid delivery to mitochondria, including fasting (44), insulin-deficient diabetes (134), and high-fat feeding (135).”
From Mitochondrial Dysfunction in Diabetes: From Molecular Mechanisms to Functional Significance and Therapeutic Opportunities (2010) · cites this paper as [44]
Citations
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Self-citationSuperoxide activates mitochondrial uncoupling proteins
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Metadata
- Authors
- Cadenas, S., Buckingham, J. A., Samec, S., Seydoux, J., Din, N., Dulloo, A. G., & Brand, M. D.
- Affiliations
- University of Cambridge (GB)
- University of Geneva (CH)
- Novo Nordisk (Denmark) (DK)
- University of Fribourg (CH)
- Corresponding author
- Brand, Martin D.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-11-30
- Volume
- 462
- Issue
- 3
- Pages
- 257-260
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2072444935
- Cited by
- 227
- References
- 25
- Citations by year
- 2024: 2 · 2023: 1 · 2021: 3 · 2019: 6 · 2018: 5 · 2017: 2 · 2016: 4 · 2015: 8 · 2014: 3 · 2013: 12 · 2012: 5
- FWCI
- 6.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (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, uncoupling proteins, skeletal muscle, starvation, mRNA expression, protein abundance, mitochondrial respiration, membrane potential
- MeSH terms
- Uncoupling Protein 2, Uncoupling Protein 3, Animals, Carrier Proteins, Electrophysiology, Female, Food Deprivation, Ion Channels, Kinetics, Mitochondria, Proteins, Protons, RNA, Messenger, Uncoupling Agents, Blotting, Northern, Blotting, Western, Rats, Wistar, Muscle, Skeletal, Mitochondrial Proteins, Membrane Transport Proteins, Rats
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