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词条 Indoleamine 2,3-dioxygenase 2
释义

  1. Function

  2. References

  3. Further reading

{{Infobox_gene}}Indoleamine 2,3-dioxygenase 2 (IDO2) is a protein that in humans is encoded by the IDO2 gene.[1]

Function

IDO2 (indolamine-2,3-dioxygenase) is an enzyme with protein size of 420 amino acids (47 kDa) that is used for catabolism of tryptophan. In organisms, other enzymes participate in L-tryptophan cleavage, namely IDO1 and TDO. Despite of IDO1 and IDO2 are closely related enzymes originating by gene duplication and sharing high level (43%) of sequence homology,[2][3] they differentiate by their kinetics, function and expression pattern. Genes encoding IDO1 and IDO2 have similar genomic structure and are situated closely to each other on chromosome 8.[4] IDO2 is produced in a very limited type of tissues as kidney, liver or antigen presenting cells.[5] IDO2 is less active on substrates of IDO1, better catabolizing other Trp derivates as 5-methoxytryptophan. There are several isoforms in population that comes from alternative splicing.[6] As well as IDO1, IDO2 has been reported in Treg differentiation in vitro,[7] suggesting a role in tolerance maintenance. Its expression has been found in several cancers, gastric, colon or renal tumores.[8]

References

1. ^{{cite web | title = Entrez Gene: Indoleamine 2,3-dioxygenase 2 | url = https://www.ncbi.nlm.nih.gov/gene/169355 }}
2. ^{{cite journal | vauthors = Yuasa HJ, Mizuno K, Ball HJ | title = Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable | journal = The FEBS Journal | volume = 282 | issue = 14 | pages = 2735–45 | date = July 2015 | pmid = 25950090 | doi = 10.1111/febs.13316 }}
3. ^{{cite journal | vauthors = Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH | title = Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice | journal = Gene | volume = 396 | issue = 1 | pages = 203–13 | date = July 2007 | pmid = 17499941 | doi = 10.1016/j.gene.2007.04.010 }}
4. ^{{cite journal | vauthors = Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH | title = Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice | journal = Gene | volume = 396 | issue = 1 | pages = 203–13 | date = July 2007 | pmid = 17499941 | doi = 10.1016/j.gene.2007.04.010 }}
5. ^{{cite journal | vauthors = Merlo LM, Mandik-Nayak L | title = IDO2: A Pathogenic Mediator of Inflammatory Autoimmunity | journal = Clinical Medicine Insights. Pathology | volume = 9 | issue = Suppl 1 | pages = 21–28 | date = 2016 | pmid = 27891058 | pmc = 5119657 | doi = 10.4137/CPath.S39930 }}
6. ^{{cite journal | vauthors = Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC | title = Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan | journal = Cancer Research | volume = 67 | issue = 15 | pages = 7082–7 | date = August 2007 | pmid = 17671174 | doi = 10.1158/0008-5472.CAN-07-1872 }}
7. ^{{cite journal | vauthors = Metz R, Smith C, DuHadaway JB, Chandler P, Baban B, Merlo LM, Pigott E, Keough MP, Rust S, Mellor AL, Mandik-Nayak L, Muller AJ, Prendergast GC | title = IDO2 is critical for IDO1-mediated T-cell regulation and exerts a non-redundant function in inflammation | journal = International Immunology | volume = 26 | issue = 7 | pages = 357–67 | date = July 2014 | pmid = 24402311 | pmc = 4432394 | doi = 10.1093/intimm/dxt073 }}
8. ^{{cite journal | vauthors = Löb S, Königsrainer A, Zieker D, Brücher BL, Rammensee HG, Opelz G, Terness P | title = IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism | journal = Cancer Immunology, Immunotherapy | volume = 58 | issue = 1 | pages = 153–7 | date = January 2009 | pmid = 18418598 | doi = 10.1007/s00262-008-0513-6 }}
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Further reading

{{refbegin|32em}}
  • {{cite journal | vauthors = Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH | title = Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice | journal = Gene | volume = 396 | issue = 1 | pages = 203–13 | date = July 2007 | pmid = 17499941 | doi = 10.1016/j.gene.2007.04.010 }}
  • {{cite journal | vauthors = Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC | title = Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan | journal = Cancer Research | volume = 67 | issue = 15 | pages = 7082–7 | date = August 2007 | pmid = 17671174 | doi = 10.1158/0008-5472.CAN-07-1872 }}
  • {{cite journal | vauthors = Witkiewicz AK, Costantino CL, Metz R, Muller AJ, Prendergast GC, Yeo CJ, Brody JR | title = Genotyping and expression analysis of IDO2 in human pancreatic cancer: a novel, active target | journal = Journal of the American College of Surgeons | volume = 208 | issue = 5 | pages = 781–7; discussion 787-9 | date = May 2009 | pmid = 19476837 | pmc = 3176891 | doi = 10.1016/j.jamcollsurg.2008.12.018 }}
  • {{cite journal | vauthors = Witkiewicz AK, Costantino CL, Metz R, Muller AJ, Prendergast GC, Yeo CJ, Brody JR | title = Genotyping and expression analysis of IDO2 in human pancreatic cancer: a novel, active target | journal = Journal of the American College of Surgeons | volume = 208 | issue = 5 | pages = 781–7; discussion 787-9 | date = May 2009 | pmid = 19476837 | pmc = 3176891 | doi = 10.1016/j.jamcollsurg.2008.12.018 }}
  • {{cite journal | vauthors = Huttunen R, Syrjänen J, Aittoniemi J, Oja SS, Raitala A, Laine J, Pertovaara M, Vuento R, Huhtala H, Hurme M | title = High activity of indoleamine 2,3 dioxygenase enzyme predicts disease severity and case fatality in bacteremic patients | journal = Shock | volume = 33 | issue = 2 | pages = 149–54 | date = February 2010 | pmid = 19487973 | doi = 10.1097/SHK.0b013e3181ad3195 }}
  • {{cite journal | vauthors = Cetindere T, Nambiar S, Santourlidis S, Essmann F, Hassan M | title = Induction of indoleamine 2, 3-dioxygenase by death receptor activation contributes to apoptosis of melanoma cells via mitochondrial damage-dependent ROS accumulation | journal = Cellular Signalling | volume = 22 | issue = 2 | pages = 197–211 | date = February 2010 | pmid = 19799997 | doi = 10.1016/j.cellsig.2009.09.013 }}
  • {{cite journal | vauthors = Mao R, Zhang J, Jiang D, Cai D, Levy JM, Cuconati A, Block TM, Guo JT, Guo H | title = Indoleamine 2,3-dioxygenase mediates the antiviral effect of gamma interferon against hepatitis B virus in human hepatocyte-derived cells | journal = Journal of Virology | volume = 85 | issue = 2 | pages = 1048–57 | date = January 2011 | pmid = 21084489 | pmc = 3019998 | doi = 10.1128/JVI.01998-10 }}
  • {{cite journal | vauthors = Sørensen RB, Køllgaard T, Andersen RS, van den Berg JH, Svane IM, Straten P, Andersen MH | title = Spontaneous cytotoxic T-Cell reactivity against indoleamine 2,3-dioxygenase-2 | journal = Cancer Research | volume = 71 | issue = 6 | pages = 2038–44 | date = March 2011 | pmid = 21406395 | doi = 10.1158/0008-5472.CAN-10-3403 }}
  • {{cite journal | vauthors = Meininger D, Zalameda L, Liu Y, Stepan LP, Borges L, McCarter JD, Sutherland CL | title = Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors | journal = Biochimica et Biophysica Acta | volume = 1814 | issue = 12 | pages = 1947–54 | date = December 2011 | pmid = 21835273 | doi = 10.1016/j.bbapap.2011.07.023 }}
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