Mitochondrial uncoupling protein 2 is a protein that in humans is encoded by the UCP2gene.[5]
Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate, or uncouple, oxidative phosphorylation from ATP synthesis by dissipating the mitochondrial membrane potential as heat, also referred to as the mitochondrial proton leak. UCPs facilitate the transfer of anions from the inner to the outer mitochondrial membrane and the return transfer of protons from the outer to the inner mitochondrial membrane. They also reduce the mitochondrial membrane potential in mammalian cells, which reduces production of reactive oxygen species (ROS).
In contrast to UCP1 and UCP3, which are primarily expressed in adipose and smooth muscle, UCP2 is expressed on many different tissues[6] including the kidney, liver, GI tract, brain, and skeletal muscle.
The exact mechanisms of anion transfer by UCPs are not known.[7] UCPs contain the three homologous protein domains of MACPs. Although it was originally thought to play a role in non-shivering thermogenesis, obesity, diabetes and atherosclerosis, it now appears that the main function of UCP2 is the control of mitochondria-derived reactive oxygen species.[8]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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^Garlid, Keith D.; Jabůrek, Martin; Ježek, Petr; Vařecha, Miroslav (2000-08-15). "How do uncoupling proteins uncouple?". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459 (2–3): 383–389. doi:10.1016/S0005-2728(00)00175-4. ISSN0005-2728. PMID11004454.
^Arsenijevic D, Onuma H, Pecqueur C, et al. (December 2000). "Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production". Nat. Genet. 26 (4): 435–9. doi:10.1038/82565. PMID11101840. S2CID29831657.
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Paradis E, Clavel S, Bouillaud F, et al. (2004). "Uncoupling protein 2: a novel player in neuroprotection". Trends in Molecular Medicine. 9 (12): 522–5. doi:10.1016/j.molmed.2003.10.009. PMID14659466.
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Gimeno RE, Dembski M, Weng X, et al. (1997). "Cloning and characterization of an uncoupling protein homolog: a potential molecular mediator of human thermogenesis". Diabetes. 46 (5): 900–6. doi:10.2337/diabetes.46.5.900. PMID9133562.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Argyropoulos G, Brown AM, Peterson R, et al. (1998). "Structure and organization of the human uncoupling protein 2 gene and identification of a common biallelic variant in Caucasian and African-American subjects". Diabetes. 47 (4): 685–7. doi:10.2337/diabetes.47.4.685. PMID9568704. S2CID38803735.
Tu N, Chen H, Winnikes U, et al. (1999). "Structural organization and mutational analysis of the human uncoupling protein-2 (hUCP2) gene". Life Sci. 64 (3): PL41–50. doi:10.1016/S0024-3205(98)00555-4. PMID10027754.
Pecqueur C, Cassard-Doulcier AM, Raimbault S, et al. (1999). "Functional organization of the human uncoupling protein-2 gene, and juxtaposition to the uncoupling protein-3 gene". Biochem. Biophys. Res. Commun. 255 (1): 40–6. doi:10.1006/bbrc.1998.0146. PMID10082652.
Pierrat B, Ito M, Hinz W, et al. (2000). "Uncoupling proteins 2 and 3 interact with members of the 14.3.3 family". Eur. J. Biochem. 267 (9): 2680–7. doi:10.1046/j.1432-1327.2000.01285.x. PMID10785390.
Esterbauer H, Schneitler C, Oberkofler H, et al. (2001). "A common polymorphism in the promoter of UCP2 is associated with decreased risk of obesity in middle-aged humans". Nat. Genet. 28 (2): 178–83. doi:10.1038/88911. PMID11381268. S2CID29550924.
