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'''Mitochondrial uncoupling protein 2''' is a [[protein]] that in humans is encoded by the ''UCP2'' [[gene]].<ref name="pmid9196039">{{cite journal | vauthors = Vidal-Puig A, Solanes G, Grujic D, Flier JS, Lowell BB | title = UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue | journal = Biochem Biophys Res Commun | volume = 235 | issue = 1 | pages = 79–82 |date=Jul 1997 | pmid = 9196039 |
'''Mitochondrial uncoupling protein 2''' is a [[protein]] that in humans is encoded by the ''UCP2'' [[gene]].<ref name="pmid9196039">{{cite journal | vauthors = Vidal-Puig A, Solanes G, Grujic D, Flier JS, Lowell BB | title = UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue | journal = Biochem Biophys Res Commun | volume = 235 | issue = 1 | pages = 79–82 |date=Jul 1997 | pmid = 9196039 | doi = 10.1006/bbrc.1997.6740 }}</ref> |
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Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate, or uncouple, [[oxidative phosphorylation]] from [[ATP synthase|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). |
Mitochondrial uncoupling proteins (UCP) are members of the larger family of mitochondrial anion carrier proteins (MACP). UCPs separate, or uncouple, [[oxidative phosphorylation]] from [[ATP synthase|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). |
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In contrast to UCP1 and UCP3, which are primarily expressed in adipose and smooth muscle, UCP2 is expressed on many different tissues<ref>{{Cite web|title=Tissue expression of UCP2 - Summary - The Human Protein Atlas|url=https://www.proteinatlas.org/ENSG00000175567-UCP2/tissue|access-date=2020-08-20|website=www.proteinatlas.org}}</ref> including the kidney, liver, GI tract, brain, and skeletal muscle. |
In contrast to UCP1 and UCP3, which are primarily expressed in adipose and smooth muscle, UCP2 is expressed on many different tissues<ref>{{Cite web|title=Tissue expression of UCP2 - Summary - The Human Protein Atlas|url=https://www.proteinatlas.org/ENSG00000175567-UCP2/tissue|access-date=2020-08-20|website=www.proteinatlas.org}}</ref> including the kidney, liver, GI tract, brain, and skeletal muscle. |
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The exact mechanisms of anion transfer by UCPs are not known.<ref>{{Cite journal|date=2000-08-15|title=How do uncoupling proteins uncouple?|url=https://www.sciencedirect.com/science/article/pii/S0005272800001754|journal=Biochimica et Biophysica Acta (BBA) - Bioenergetics|language=en|volume=1459|issue=2–3|pages=383–389|doi=10.1016/S0005-2728(00)00175-4|issn=0005-2728|last1=Garlid|first1=Keith D.|last2=Jabůrek|first2=Martin|last3=Ježek|first3=Petr|last4=Vařecha|first4=Miroslav|pmid=11004454}}</ref> 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.<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 |s2cid=29831657 |
The exact mechanisms of anion transfer by UCPs are not known.<ref>{{Cite journal|date=2000-08-15|title=How do uncoupling proteins uncouple?|url=https://www.sciencedirect.com/science/article/pii/S0005272800001754|journal=Biochimica et Biophysica Acta (BBA) - Bioenergetics|language=en|volume=1459|issue=2–3|pages=383–389|doi=10.1016/S0005-2728(00)00175-4|issn=0005-2728|last1=Garlid|first1=Keith D.|last2=Jabůrek|first2=Martin|last3=Ježek|first3=Petr|last4=Vařecha|first4=Miroslav|pmid=11004454}}</ref> 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.<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 |s2cid=29831657 }}</ref> |
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Chromosomal order is 5'-UCP3-UCP2-3'.<ref>{{cite web | title = Entrez Gene: UCP2 uncoupling protein 2 (mitochondrial, proton carrier)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7351 |
Chromosomal order is 5'-UCP3-UCP2-3'.<ref>{{cite web | title = Entrez Gene: UCP2 uncoupling protein 2 (mitochondrial, proton carrier)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7351}}</ref> |
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[[File:MMDB_ID_92271_PDB_ID_2LCK_Mitochondrial_Uncoupling_Protein_2.png|thumb|286px|Mitochondrial Uncoupling Protein 2]] |
[[File:MMDB_ID_92271_PDB_ID_2LCK_Mitochondrial_Uncoupling_Protein_2.png|thumb|286px|Mitochondrial Uncoupling Protein 2]] |
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*{{cite journal | vauthors=Ricquier D, Bouillaud F |title=The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. |journal=Biochem. J. |volume=345 |issue= 2|pages= 161–79 |year= 2000 |pmid= 10620491 |doi=10.1042/0264-6021:3450161 | pmc=1220743 }} |
*{{cite journal | vauthors=Ricquier D, Bouillaud F |title=The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. |journal=Biochem. J. |volume=345 |issue= 2|pages= 161–79 |year= 2000 |pmid= 10620491 |doi=10.1042/0264-6021:3450161 | pmc=1220743 }} |
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*{{cite journal | vauthors=Saleh MC, Wheeler MB, Chan CB |title=Uncoupling protein-2: evidence for its function as a metabolic regulator. |journal=Diabetologia |volume=45 |issue= 2 |pages= 174–87 |year= 2002 |pmid= 11935148 |doi= 10.1007/s00125-001-0737-x |doi-access= free }} |
*{{cite journal | vauthors=Saleh MC, Wheeler MB, Chan CB |title=Uncoupling protein-2: evidence for its function as a metabolic regulator. |journal=Diabetologia |volume=45 |issue= 2 |pages= 174–87 |year= 2002 |pmid= 11935148 |doi= 10.1007/s00125-001-0737-x |doi-access= free }} |
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*{{cite journal | author=Muzzin P |title=The uncoupling proteins. |journal=Ann. Endocrinol. |volume=63 |issue= 2 Pt 1 |pages= 106–10 |year= 2002 |pmid= 11994670 |
*{{cite journal | author=Muzzin P |title=The uncoupling proteins. |journal=Ann. Endocrinol. |volume=63 |issue= 2 Pt 1 |pages= 106–10 |year= 2002 |pmid= 11994670 }} |
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*{{cite journal | vauthors=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 | vauthors=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 }} |
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*{{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 |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 }} |
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Revision as of 12:35, 5 December 2020
Mitochondrial uncoupling protein 2 is a protein that in humans is encoded by the UCP2 gene.[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]
Chromosomal order is 5'-UCP3-UCP2-3'.[9]
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000175567 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000033685 – Ensembl, May 2017
- ^ "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.
- ^ 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.
- ^ "Tissue expression of UCP2 - Summary - The Human Protein Atlas". www.proteinatlas.org. Retrieved 2020-08-20.
- ^ 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. ISSN 0005-2728. PMID 11004454.
- ^ 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. S2CID 29831657.
- ^ "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 (2): 161–79. doi:10.1042/0264-6021:3450161. PMC 1220743. 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. 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. S2CID 13421247.
- 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. S2CID 33808140.
- 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. S2CID 35050170.
- 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. doi:10.1080/713803586. PMID 10772343. S2CID 8541209.
- 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. S2CID 29550924.
- 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. S2CID 4349744.
- Rupprecht A, Sittner D, Smorodchenko A, Hilse KE, Goyn J, Moldzio R, Seiler AE, Bräuer AU, Pohl EE (2014). "Uncoupling protein 2 and 4 expression pattern during stem cell differentiation provides new insight into their putative function". PLOS ONE. 9 (2): e88474. doi:10.1371/journal.pone.0088474. PMC 3921169. PMID 24523901.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Rupprecht A, Bräuer AU, Smorodchenko A, Goyn J, Hilse KE, Shabalina IG, Infante-Duarte C, Pohl EE (2012). "Quantification of uncoupling protein 2 reveals its main expression in immune cells and selective up-regulation during T-cell proliferation". PLOS ONE. 7 (8): e41406. doi:10.1371/journal.pone.0041406. PMC 3411681. PMID 22870219.
{{cite journal}}: CS1 maint: unflagged free DOI (link)
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