The Full Wiki

More info on UCP2

UCP2: Wikis


Note: Many of our articles have direct quotes from sources you can cite, within the Wikipedia article! This article doesn't yet, but we're working on it! See more info or our list of citable articles.


From Wikipedia, the free encyclopedia

Uncoupling protein 2 (mitochondrial, proton carrier)
Symbols UCP2; SLC25A8; UCPH
External IDs OMIM601693 MGI109354 HomoloGene2516 GeneCards: UCP2 Gene
RNA expression pattern
PBB GE UCP2 208998 at tn.png
PBB GE UCP2 208997 s at tn.png
More reference expression data
Species Human Mouse
Entrez 7351 22228
Ensembl ENSG00000175567 ENSMUSG00000033685
UniProt P55851 Q549J5
RefSeq (mRNA) NM_003355 NM_011671
RefSeq (protein) NP_003346 NP_035801
Location (UCSC) Chr 11:
73.36 - 73.37 Mb
Chr 7:
100.37 - 100.38 Mb
PubMed search [1] [2]

Mitochondrial uncoupling protein 2 is a protein that in humans is encoded by the UCP2 gene.[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 and diabetes, 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]

See also


  1. ^ 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. PMID 9196039. 
  2. ^ 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. PMID 11101840. 
  3. ^ "Entrez Gene: UCP2 uncoupling protein 2 (mitochondrial, proton carrier)". 

Further reading

  • Ricquier D, Bouillaud F (2000). "The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP.". Biochem. J. 345 Pt 2: 161–79. doi:10.1042/0264-6021:3450161. PMID 10620491. 
  • 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. PMID 11935148. 
  • Muzzin P (2002). "The uncoupling proteins.". Ann. Endocrinol. (Paris) 63 (2 Pt 1): 106–10. PMID 11994670. 
  • 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. PMID 12787871. 
  • 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. PMID 14659466. 
  • 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. PMID 8125298. 
  • 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. PMID 9054939. 
  • 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. PMID 9133562. 
  • 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. PMID 9180264. 
  • 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. PMID 9373149. 
  • 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. PMID 9559644. 
  • 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. PMID 9568704. 
  • 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. PMID 10027754. 
  • 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. PMID 10082652. 
  • Jezek P, Urbánková E (2000). "Specific sequence of motifs of mitochondrial uncoupling proteins.". IUBMB Life 49 (1): 63–70. PMID 10772343. 
  • 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. PMID 10785390. 
  • 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. PMID 11381268. 
  • Echtay KS, Roussel D, St-Pierre J, et al. (2002). "Superoxide activates mitochondrial uncoupling proteins.". Nature 415 (6867): 96–9. doi:10.1038/415096a. PMID 11780125. 
  • 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. 
  • Bai Y, Onuma H, Bai X, et al. (2005). "Persistent nuclear factor-KB activation in Ucp2-/- mice leads to enhanced nitric oxide and inflammatory cytokine production.". J Biol Chem 280 (May 13): 19062–9. doi:10.1074/jbc.M500566200. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



Got something to say? Make a comment.
Your name
Your email address