UCP2: Difference between revisions

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Template:PBB Mitochondrial uncoupling protein 2 is a protein that in humans is encoded by the UCP2 gene.^[1]

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References

^ 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

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. PMID 11101840.
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. PMC 1382174. PMID 15757894.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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

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[pmid9196039-1] 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.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[1]

@@ Line 5: / Line 5: @@
 {{PBB_Summary
 | section_title =
-| summary_text = 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.<ref name="pmid11101840">{{cite journal |author=Arsenijevic D, Onuma H, Pecqueur C, ''et al.'' |title=Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production |journal=Nat. Genet. |volume=26 |issue=4 |pages=435–9 |date=December 2000 |pmid=11101840 |doi=10.1038/82565 |url=}}</ref> Chromosomal order is 5'-UCP3-UCP2-3'.<ref>{{cite web | title = Entrez Gene: UCP2 uncoupling protein 2 (mitochondrial, proton carrier)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7351| accessdate = }}</ref>
+| summary_text = 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.<ref name="pmid11101840">{{cite journal  |vauthors=Arsenijevic D, Onuma H, Pecqueur C, etal |title=Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production |journal=Nat. Genet. |volume=26 |issue=4 |pages=435–9 |date=December 2000 |pmid=11101840 |doi=10.1038/82565 |url=}}</ref> Chromosomal order is 5'-UCP3-UCP2-3'.<ref>{{cite web | title = Entrez Gene: UCP2 uncoupling protein 2 (mitochondrial, proton carrier)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7351| accessdate = }}</ref>
 }}
@@ Line 23: / Line 23: @@
 *{{cite journal  | author=Muzzin P |title=The uncoupling proteins. |journal=Ann. Endocrinol. (Paris) |volume=63 |issue= 2 Pt 1 |pages= 106–10 |year= 2002 |pmid= 11994670 |doi=  }}
 *{{cite journal  | author=Horvath TL, Diano S, Barnstable C |title=Mitochondrial uncoupling protein 2 in the central nervous system: neuromodulator and neuroprotector. |journal=Biochem. Pharmacol. |volume=65 |issue= 12 |pages= 1917–21 |year= 2003 |pmid= 12787871 |doi=10.1016/S0006-2952(03)00143-6  }}
-*{{cite journal  | author=Paradis E, Clavel S, Bouillaud F, ''et al.'' |title=Uncoupling protein 2: a novel player in neuroprotection. |journal=Trends in molecular medicine |volume=9 |issue= 12 |pages= 522–5 |year= 2004 |pmid= 14659466 |doi=10.1016/j.molmed.2003.10.009  }}
+*{{cite journal   |vauthors=Paradis E, Clavel S, Bouillaud F, etal |title=Uncoupling protein 2: a novel player in neuroprotection. |journal=Trends in molecular medicine |volume=9 |issue= 12 |pages= 522–5 |year= 2004 |pmid= 14659466 |doi=10.1016/j.molmed.2003.10.009  }}
 *{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
-*{{cite journal  | author=Fleury C, Neverova M, Collins S, ''et al.'' |title=Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 269–72 |year= 1997 |pmid= 9054939 |doi= 10.1038/ng0397-269 }}
+*{{cite journal   |vauthors=Fleury C, Neverova M, Collins S, etal |title=Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 269–72 |year= 1997 |pmid= 9054939 |doi= 10.1038/ng0397-269 }}
-*{{cite journal  | author=Gimeno RE, Dembski M, Weng X, ''et al.'' |title=Cloning and characterization of an uncoupling protein homolog: a potential molecular mediator of human thermogenesis. |journal=Diabetes |volume=46 |issue= 5 |pages= 900–6 |year= 1997 |pmid= 9133562 |doi=10.2337/diabetes.46.5.900  }}
+*{{cite journal   |vauthors=Gimeno RE, Dembski M, Weng X, etal |title=Cloning and characterization of an uncoupling protein homolog: a potential molecular mediator of human thermogenesis. |journal=Diabetes |volume=46 |issue= 5 |pages= 900–6 |year= 1997 |pmid= 9133562 |doi=10.2337/diabetes.46.5.900  }}
-*{{cite journal  | author=Boss O, Samec S, Paoloni-Giacobino A, ''et al.'' |title=Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression. |journal=FEBS Lett. |volume=408 |issue= 1 |pages= 39–42 |year= 1997 |pmid= 9180264 |doi=10.1016/S0014-5793(97)00384-0  }}
+*{{cite journal   |vauthors=Boss O, Samec S, Paoloni-Giacobino A, etal |title=Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression. |journal=FEBS Lett. |volume=408 |issue= 1 |pages= 39–42 |year= 1997 |pmid= 9180264 |doi=10.1016/S0014-5793(97)00384-0  }}
-*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
+*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  }}
-*{{cite journal  | author=Hodný Z, Kolárová P, Rossmeisl M, ''et al.'' |title=High expression of uncoupling protein 2 in foetal liver. |journal=FEBS Lett. |volume=425 |issue= 2 |pages= 185–90 |year= 1998 |pmid= 9559644 |doi=10.1016/S0014-5793(98)00230-0  }}
+*{{cite journal   |vauthors=Hodný Z, Kolárová P, Rossmeisl M, etal |title=High expression of uncoupling protein 2 in foetal liver. |journal=FEBS Lett. |volume=425 |issue= 2 |pages= 185–90 |year= 1998 |pmid= 9559644 |doi=10.1016/S0014-5793(98)00230-0  }}
-*{{cite journal  | author=Argyropoulos G, Brown AM, Peterson R, ''et al.'' |title=Structure and organization of the human uncoupling protein 2 gene and identification of a common biallelic variant in Caucasian and African-American subjects. |journal=Diabetes |volume=47 |issue= 4 |pages= 685–7 |year= 1998 |pmid= 9568704 |doi=10.2337/diabetes.47.4.685  }}
+*{{cite journal   |vauthors=Argyropoulos G, Brown AM, Peterson R, etal |title=Structure and organization of the human uncoupling protein 2 gene and identification of a common biallelic variant in Caucasian and African-American subjects. |journal=Diabetes |volume=47 |issue= 4 |pages= 685–7 |year= 1998 |pmid= 9568704 |doi=10.2337/diabetes.47.4.685  }}
-*{{cite journal  | author=Tu N, Chen H, Winnikes U, ''et al.'' |title=Structural organization and mutational analysis of the human uncoupling protein-2 (hUCP2) gene. |journal=Life Sci. |volume=64 |issue= 3 |pages= PL41–50 |year= 1999 |pmid= 10027754 |doi=10.1016/S0024-3205(98)00555-4  }}
+*{{cite journal   |vauthors=Tu N, Chen H, Winnikes U, etal |title=Structural organization and mutational analysis of the human uncoupling protein-2 (hUCP2) gene. |journal=Life Sci. |volume=64 |issue= 3 |pages= PL41–50 |year= 1999 |pmid= 10027754 |doi=10.1016/S0024-3205(98)00555-4  }}
-*{{cite journal  | author=Pecqueur C, Cassard-Doulcier AM, Raimbault S, ''et al.'' |title=Functional organization of the human uncoupling protein-2 gene, and juxtaposition to the uncoupling protein-3 gene. |journal=Biochem. Biophys. Res. Commun. |volume=255 |issue= 1 |pages= 40–6 |year= 1999 |pmid= 10082652 |doi= 10.1006/bbrc.1998.0146 }}
+*{{cite journal   |vauthors=Pecqueur C, Cassard-Doulcier AM, Raimbault S, etal |title=Functional organization of the human uncoupling protein-2 gene, and juxtaposition to the uncoupling protein-3 gene. |journal=Biochem. Biophys. Res. Commun. |volume=255 |issue= 1 |pages= 40–6 |year= 1999 |pmid= 10082652 |doi= 10.1006/bbrc.1998.0146 }}
 *{{cite journal  | author=Jezek P, Urbánková E |title=Specific sequence of motifs of mitochondrial uncoupling proteins. |journal=IUBMB Life |volume=49 |issue= 1 |pages= 63–70 |year= 2000 |pmid= 10772343 |doi=10.1080/713803586  }}
-*{{cite journal  | author=Pierrat B, Ito M, Hinz W, ''et al.'' |title=Uncoupling proteins 2 and 3 interact with members of the 14.3.3 family. |journal=Eur. J. Biochem. |volume=267 |issue= 9 |pages= 2680–7 |year= 2000 |pmid= 10785390 |doi=10.1046/j.1432-1327.2000.01285.x  }}
+*{{cite journal   |vauthors=Pierrat B, Ito M, Hinz W, etal |title=Uncoupling proteins 2 and 3 interact with members of the 14.3.3 family. |journal=Eur. J. Biochem. |volume=267 |issue= 9 |pages= 2680–7 |year= 2000 |pmid= 10785390 |doi=10.1046/j.1432-1327.2000.01285.x  }}
-*{{cite journal  | author=Esterbauer H, Schneitler C, Oberkofler H, ''et al.'' |title=A common polymorphism in the promoter of UCP2 is associated with decreased risk of obesity in middle-aged humans. |journal=Nat. Genet. |volume=28 |issue= 2 |pages= 178–83 |year= 2001 |pmid= 11381268 |doi= 10.1038/88911 }}
+*{{cite journal   |vauthors=Esterbauer H, Schneitler C, Oberkofler H, etal |title=A common polymorphism in the promoter of UCP2 is associated with decreased risk of obesity in middle-aged humans. |journal=Nat. Genet. |volume=28 |issue= 2 |pages= 178–83 |year= 2001 |pmid= 11381268 |doi= 10.1038/88911 }}
-*{{cite journal  | author=Echtay KS, Roussel D, St-Pierre J, ''et al.'' |title=Superoxide activates mitochondrial uncoupling proteins. |journal=Nature |volume=415 |issue= 6867 |pages= 96–9 |year= 2002 |pmid= 11780125 |doi= 10.1038/415096a }}
+*{{cite journal   |vauthors=Echtay KS, Roussel D, St-Pierre J, etal |title=Superoxide activates mitochondrial uncoupling proteins. |journal=Nature |volume=415 |issue= 6867 |pages= 96–9 |year= 2002 |pmid= 11780125 |doi= 10.1038/415096a }}
 }}
-*{{cite journal  | author=Arsenijevic D, Onuma H, ''et al.'' |title=Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. |journal=Nature Genetics |volume=26 |issue= Dec |pages= 435–9 |year= 2000 |doi=10.1038/82565  | pmid=11101840 }}
+*{{cite journal   |vauthors=Arsenijevic D, Onuma H, etal |title=Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. |journal=Nature Genetics |volume=26 |issue= Dec |pages= 435–9 |year= 2000 |doi=10.1038/82565  | pmid=11101840 }}
-*{{cite journal  | author=Bai Y, Onuma H, Bai X, ''et al.'' |title=Persistent nuclear factor-KB activation in Ucp2-/- mice leads to enhanced nitric oxide and inflammatory cytokine production. |journal=J Biol Chem |volume=280 |issue= May 13 |pages= 19062–9 |year= 2005 |doi=10.1074/jbc.M500566200  | pmid=15757894  | pmc=1382174 }}
+*{{cite journal   |vauthors=Bai Y, Onuma H, Bai X, etal |title=Persistent nuclear factor-KB activation in Ucp2-/- mice leads to enhanced nitric oxide and inflammatory cytokine production. |journal=J Biol Chem |volume=280 |issue= May 13 |pages= 19062–9 |year= 2005 |doi=10.1074/jbc.M500566200  | pmid=15757894  | pmc=1382174 }}
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UCP2: Difference between revisions

Revision as of 13:48, 2 September 2015

See also

References

Further reading