The DOI matches its Crossref record; 202 of the 202 references it cites were found in a registry or an index.
Effect of fatty acids on energy coupling processes in mitochondria
Abstract
Long-chain fatty acids are natural uncouplers of oxidative phosphorylation in mitochondria. The protonophoric mechanism of this action is due to transbilayer movement of undissociated fatty acid in one direction and the passage of its anion in the opposite direction. The transfer of the dissociated form of fatty acid can be, at least in some kinds of mitochondrion, facilitated by adenine nucleotide translocase. Apart from dissipating the electrochemical proton gradient, long-chain fatty acids decrease the activity of the respiratory chain by mechanism(s) not fully understood. In intact cells and tissues fatty acids operate mostly as excellent respiratory substrates, providing electrons to the respiratory chain. This function masks their potential uncoupling effect which becomes apparent only under special physiological or pathological conditions characterized by unusual fatty acid accumulation. Short- and medium-chain fatty acids do not have protonophoric properties. Nevertheless, they contribute to energy dissipation because of slow intramitochondrial hydrolysis of their activation products, acyl-AMP and acyl-CoA. Long-chain fatty acids increase permeability of mitochondrial membranes to alkali metal cations. This is due to their ionophoric mechanism of action. Regulatory function of fatty acids with respect to specific cation channels has been postulated for the plasma membrane of muscle cells, but not demonstrated in mitochondria. Under cold stress, cold acclimation and arousal from hibernation the uncoupling effect of fatty acids may contribute to increased thermogenesis, especially in the muscle tissue. In brown adipose tissue, the special thermogenic organ of mammals, long-chain fatty acids promote operation of the unique natural uncoupling protein, thermogenin. As anionic amphiphiles, long-chain fatty acids increase the negative surface charge of biomembranes, thus interfering in their enzymic and transporting functions.
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“Experiments performed on liposomes enriched in UCP-1 showed that FFAs are a required co-factor for UCP-1-catalyzed proton transport [29]”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [29]
In the citing paper
“First, they stimulate directly mitochondrial respiration, as seen in intact isolated brown adipocytes or mitochondria isolated from these cells [28,29].”
From Mitochondrial Uncoupling: A Key Controller of Biological Processes in Physiology and Diseases (2019) · cites this paper as [29]
Citations
Cites
Thermogenic mechanisms in brown fat.
Nicholls, D. G., & Locke, R. M. (1984) · Physiological Reviews · doi:10.1152/physrev.1984.64.1.1 · Cited by 1,602
The Interaction of Human Serum Albumin with Long-chain Fatty Acid Anions
Goodman, D. S. (1958) · Journal of the American Chemical Society · doi:10.1021/ja01548a024 · Cited by 766
ATP-sensitive K+ channel in the mitochondrial inner membrane
Inoue, I., Nagase, H., Kishi, K., & Higuti, T. (1991) · Nature · doi:10.1038/352244a0 · Cited by 751
Nicholls, D. G. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03899.x · Cited by 723
Effect of surface active agents on the latent ATPASE of mitochondira
Pressman, B. C., & Lardy, H. A. (1956) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(56)90182-2 · Cited by 478
Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation
Skulachev, V. P. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80658-p · Cited by 467
Adenine Nucleotide Translocation of Mitochondria
Pfaff, E., & Klingenberg, M. (1968) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1968.tb00420.x · Cited by 429
Direct regulation of ion channels by fatty acids
Ordway, R. W., Singer, J. J., & Walsh, J. V. (1991) · Trends in Neurosciences · doi:10.1016/0166-2236(91)90069-7 · Cited by 408
Transport of protons across membranes by weak acids.
McLaughlin, S., & Dilger, J. P. (1980) · Physiological Reviews · doi:10.1152/physrev.1980.60.3.825 · Cited by 400
The Optimal Efficiency and the Economic Degrees of Coupling of Oxidative Phosphorylation
Stucki, J. W. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04792.x · Cited by 394
Research works printed but not linked: 6
- Takeuchi, 1991, A possible mechanism of mitochondrial dysfunction during cerebral ischemia: Inhibition of mitochondrial respiration by arachidonic acid, Arch. Biochem. Biophys., 289, 33, 10.1016/0003-9861(91)90438-O · DOI
- Asimakis, 1980, In vitro alteration of the size of the liver mitochondrial nucleotide pool: correlation with respiratory functions, Arch. Biochem. Biophys., 203, 307, 10.1016/0003-9861(80)90181-2 · DOI
- Gregersen, 1981, The specific inhibition of the pyruvate dehydrogenase complex from pig kidney by propionyl-CoA and isovaleryl-CoA, Biochem. Med., 26, 20, 10.1016/0006-2944(81)90026-0 · DOI
- Kocherginsky, 1987, Physico-chemical mechanism of ionophoric activity of fatty acids as stimulants of transmembrane monovalent cation exchange, Biol. Membrany, 4, 838
- Skulachev, 1963, Regulation of the coupling of oxidation and phosphorylation, Vol. 5, 365
- Wojtczak, 1985, The surface potential of membranes: its effect on membrane-bound enzymes and transport processes, Vol. 2, 215
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Self-citationDiggle, C. P. (2002) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00025-x · Cited by 84
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Tyni, T. A., Paetau, A. E., Strauss, A. W., Middleton, B., & Kivelä, T. (2004) · Pediatric Research · doi:10.1203/01.pdr.0000141967.52759.83 · Cited by 80
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LOSKOVICH, M. V., Grivennikova, V. G., Cecchini, G., & Vinogradov, A. D. (2005) · Biochemical Journal · doi:10.1042/bj20041703 · Cited by 75
Metadata
- Authors
- Wojtczak, L., & Schönfeld, P.
- Affiliations
- Instytut Biologii Doświadczalnej im. Marcelego Nenckiego (PL)
- Corresponding author
- Wojtczak, Lech
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 1993-11
- Volume
- 1183
- Issue
- 1
- Pages
- 41-57
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W1967880167
- Cited by
- 363
- References
- 200
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 8 · 2023: 8 · 2022: 13 · 2021: 9 · 2020: 8 · 2019: 10 · 2018: 4 · 2017: 13 · 2016: 20 · 2015: 22 · 2014: 17 · 2013: 12 · 2012: 8
- FWCI
- 0.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- long-chain fatty acids, mitochondrial uncoupling, adenine nucleotide translocase, electron transport inhibition, short- and medium-chain fatty acids, acyl-CoA, mitochondrial membrane permeability, alkali metal cations, thermogenesis, brown adipose tissue, thermogenin, membrane surface charge, fatty acid accumulation
- MeSH terms
- Uncoupling Protein 1, Animals, Adipose Tissue, Brown, Carrier Proteins, Fatty Acids, Ion Channels, Membrane Proteins, Mitochondria, Muscles, Oxidation-Reduction, Uncoupling Agents, Mitochondrial Proteins
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