Indoleamine 2,3-dioxygenase 2

IDO2
Identifiers
AliasesIDO2, INDOL1, indoleamine 2,3-dioxygenase 2
External IDsMGI: 2142489 HomoloGene: 48830 GeneCards: IDO2
Gene location (Human)
Chr.Chromosome 8 (human)[1]
Band8p11.21Start39,934,614 bp[1]
End40,016,391 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

169355

209176

Ensembl

ENSG00000188676

ENSMUSG00000031549

UniProt

Q6ZQW0

Q8R0V5

RefSeq (mRNA)

NM_194294

NM_145949

RefSeq (protein)

NP_919270

NP_666061

Location (UCSC)Chr 8: 39.93 – 40.02 MbChr 8: 24.53 – 24.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Indoleamine 2,3-dioxygenase 2 (IDO2) is a protein that in humans is encoded by the IDO2 gene.[5]

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,[6][7] 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.[8] IDO2 is produced in a very limited type of tissues as kidney, liver or antigen presenting cells.[9] 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.[10] As well as IDO1, IDO2 has been reported in Treg differentiation in vitro,[11] suggesting a role in tolerance maintenance. It's expression has been found in several cancers, gastric, colon or renal tumores.[12]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000188676 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031549 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ "Entrez Gene: Indoleamine 2,3-dioxygenase 2".
  6. ↑ Yuasa HJ, Mizuno K, Ball HJ (July 2015). "Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable". The FEBS Journal. 282 (14): 2735–45. doi:10.1111/febs.13316. PMID 25950090.
  7. ↑ Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.
  8. ↑ Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (July 2007). "Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice". Gene. 396 (1): 203–13. doi:10.1016/j.gene.2007.04.010. PMID 17499941.
  9. ↑ Merlo LM, Mandik-Nayak L (2016). "IDO2: A Pathogenic Mediator of Inflammatory Autoimmunity". Clinical Medicine Insights. Pathology. 9 (Suppl 1): 21–28. doi:10.4137/CPath.S39930. PMC 5119657. PMID 27891058.
  10. ↑ Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC (August 2007). "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan". Cancer Research. 67 (15): 7082–7. doi:10.1158/0008-5472.CAN-07-1872. PMID 17671174.
  11. ↑ 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 (July 2014). "IDO2 is critical for IDO1-mediated T-cell regulation and exerts a non-redundant function in inflammation". International Immunology. 26 (7): 357–67. doi:10.1093/intimm/dxt073. PMC 4432394. PMID 24402311.
  12. ↑ Löb S, Königsrainer A, Zieker D, Brücher BL, Rammensee HG, Opelz G, Terness P (January 2009). "IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism". Cancer Immunology, Immunotherapy. 58 (1): 153–7. doi:10.1007/s00262-008-0513-6. PMID 18418598.

Further reading

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

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