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Mitochondrial uncoupling protein 2 is a protein that in humans is encoded by the UCP2gene.[1]
Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate oxidative phosphorylation from ATP synthesis with energy dissipated 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. Tissue specificity occurs for the different UCPs and the exact methods of how UCPs transfer H+/OH- are not known. UCPs contain the three homologous protein domains of MACPs. This gene is expressed in many tissues, with the greatest expression in skeletal muscle. Although it was originally thought to play a role in nonshivering thermogenesis, obesity, diabetes and atherosclerosis, it now appears that the main function of UCP2 is the control of mitochondria-derived reactive oxygen species.[2] Chromosomal order is 5'-UCP3-UCP2-3'.[3]
↑Vidal-Puig A, Solanes G, Grujic D, Flier JS, Lowell BB (Jul 1997). "UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue". Biochem Biophys Res Commun. 235 (1): 79–82. doi:10.1006/bbrc.1997.6740. PMID9196039.
↑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.
Saleh MC, Wheeler MB, Chan CB (2002). "Uncoupling protein-2: evidence for its function as a metabolic regulator". Diabetologia. 45 (2): 174–87. doi:10.1007/s00125-001-0737-x. PMID11935148.
Muzzin P (2002). "The uncoupling proteins". Ann. Endocrinol. Paris. 63 (2 Pt 1): 106–10. PMID11994670.
Horvath TL, Diano S, Barnstable C (2003). "Mitochondrial uncoupling protein 2 in the central nervous system: neuromodulator and neuroprotector". Biochem. Pharmacol. 65 (12): 1917–21. doi:10.1016/S0006-2952(03)00143-6. PMID12787871.
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.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Fleury C, Neverova M, Collins S, et al. (1997). "Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia". Nat. Genet. 15 (3): 269–72. doi:10.1038/ng0397-269. PMID9054939.
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.
Boss O, Samec S, Paoloni-Giacobino A, et al. (1997). "Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression". FEBS Lett. 408 (1): 39–42. doi:10.1016/S0014-5793(97)00384-0. PMID9180264.
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.
Hodný Z, Kolárová P, Rossmeisl M, et al. (1998). "High expression of uncoupling protein 2 in foetal liver". FEBS Lett. 425 (2): 185–90. doi:10.1016/S0014-5793(98)00230-0. PMID9559644.
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.
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.
Jezek P, Urbánková E (2000). "Specific sequence of motifs of mitochondrial uncoupling proteins". IUBMB Life. 49 (1): 63–70. doi:10.1080/713803586. PMID10772343.
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.
Arsenijevic D, Onuma H, et al. (2000). "Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production". Nature Genetics. 26 (Dec): 435–9. doi:10.1038/82565. PMID11101840.