The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
The Biology of Mitochondrial Uncoupling Proteins
Abstract
Uncoupling proteins (UCPs) are mitochondrial transporters present in the inner membrane of mitochondria. They are found in all mammals and in plants. They belong to the family of anion mitochondrial carriers including adenine nucleotide transporters. The term “uncoupling protein” was originally used for UCP1, which is uniquely present in mitochondria of brown adipocytes, the thermogenic cells that maintain body temperature in small rodents. In these cells, UCP1 acts as a proton carrier activated by free fatty acids and creates a shunt between complexes of the respiratory chain and ATP synthase. Activation of UCP1 enhances respiration, and the uncoupling process results in a futile cycle and dissipation of oxidation energy as heat. UCP2 is ubiquitous and highly expressed in the lymphoid system, macrophages, and pancreatic islets. UCP3 is mainly expressed in skeletal muscles. In comparison to the established uncoupling and thermogenic activities of UCP1, UCP2 and UCP3 appear to be involved in the limitation of free radical levels in cells rather than in physiological uncoupling and thermogenesis. Moreover, UCP2 is a regulator of insulin secretion and UCP3 is involved in fatty acid metabolism.
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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
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
Enerbäck, S., Jacobsson, A., Simpson, E. M., Guerra, C., Yamashita, H., Harper, M.-E., & Kozak, L. P. (1997) · Nature · doi:10.1038/387090a0 · Cited by 1,379
Mitochondria, oxygen free radicals, disease and ageing
Raha, S., & Robinson, B. H. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01674-1 · Cited by 1,066 · cited 1×
“Respiration is associated with production of reactive oxygen species (ROS) because the oxygen molecule is capable of accepting an additional electron to create the superoxide ion, a more reactive form of oxygen (34).”
BackgroundEnergy metabolism in uncoupling protein 3 gene knockout mice
Vidal-Puig, A. J., Grujic, D., Zhang, C.-Y., Hagen, T., Boss, O., Ido, Y., Szczepanik, A., Wade, J., Mootha, V., Cortright, R., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910179199 · Cited by 677
Transport function and regulation of mitochondrial uncoupling proteins 2 and 3
Jabůrek, M., Vařecha, M., Gimeno, R. E., Dembski, M., Ježek, P., Zhang, M., Burn, P., Tartaglia, L. A., & Garlid, K. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.37.26003 · Cited by 321
Skeletal muscle respiratory uncoupling prevents diet-induced obesity and insulin resistance in mice
Li, B., Nolte, L. A., Ju, J.-S., Ho Han, D., Coleman, T., Holloszy, J. O., & Semenkovich, C. F. (2000) · Nature Medicine · doi:10.1038/80450 · Cited by 291
Mitochondrial proton leak and the uncoupling protein 1 homologues
Stuart, J. A., Cadenas, S., Jekabsons, M. B., Roussel, D., & Brand, M. D. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00243-7 · Cited by 169
Couplan, E., del Mar Gonzalez-Barroso, M., Alves-Guerra, M. C., Ricquier, D., Goubern, M., & Bouillaud, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202535200 · Cited by 161
Self-citationDiehl, A. M., & Hoek, J. B. (1999) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1005452624640 · Cited by 95
Hesselink, M. K. C., Greenhaff, P. L., Constantin-Teodosiu, D., Hultman, E., Saris, W. H. M., Nieuwlaat, R., Schaart, G., Kornips, E., & Schrauwen, P. (2003) · Journal of Clinical Investigation · doi:10.1172/jci16653 · Cited by 82
Cited by
den Besten, G., Bleeker, A., Gerding, A., van Eunen, K., Havinga, R., van Dijk, T. H., Oosterveer, M. H., Jonker, J. W., Groen, A. K., Reijngoud, D.-J., et al. (2015) · Diabetes · doi:10.2337/db14-1213 · Cited by 1,125
Oxidative Stress and the Pathogenesis of Alzheimer's Disease
Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855
Sirt1 Regulates Insulin Secretion by Repressing UCP2 in Pancreatic β Cells
Bordone, L., Motta, M. C., Picard, F., Robinson, A., Jhala, U. S., Apfeld, J., McDonagh, T., Lemieux, M., McBurney, M., Szilvasi, A., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040031 · Cited by 715
Thermogenic Mechanisms and Their Hormonal Regulation
Silva, J. E. (2006) · Physiological Reviews · doi:10.1152/physrev.00009.2005 · Cited by 687
Is Alzheimer’s disease a type 3 diabetes? A critical appraisal
Kandimalla, R., Thirumala, V., & Reddy, P. H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.018 · Cited by 621
Metadata
- Authors
- Rousset, S., Alves-Guerra, M.-C., Mozo, J., Miroux, B., Cassard-Doulcier, A.-M., Bouillaud, F., & Ricquier, D.
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2004-02-01
- Volume
- 53
- Issue
- suppl_1
- Pages
- S130-S135
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2104645520
- Cited by
- 553
- References
- 11
- FWCI
- 11.92
- Type
- journal article
- Language
- en
- Open access
- closed
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