Indoleamine 2,3-dioxygenase: Difference between revisions
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== Inhibitors == |
== Inhibitors == |
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[[Norharmane]], via inhibition of indoleamine 2,3-dioxygenase exerts neuroprotective properties by suppressing [[kynurenine]] neurotoxic metabolites such as [[quinolinic acid]], 3-hydroxy-kynurenine and [[nitric oxide synthase]].<ref name="pmid10947071">{{cite journal | author = Chiarugi A, Dello Sbarba P, Paccagnini A, Donnini S, Filippi S, Moroni F | title = Combined inhibition of indoleamine 2,3-dioxygenase and nitric oxide synthase modulates neurotoxin release by interferon-gamma-activated macrophages | journal = J. Leukoc. Biol. | volume = 68 | issue = 2 | pages = 260–6 |date=August 2000 | pmid = 10947071 | doi = | url = http://www.jleukbio.org/content/68/2/260.long }}</ref> [[Rosmarinic acid]] inhibits the expression of indoleamine 2,3-dioxygenase via its [[cyclooxygenase]]-inhibiting properties.<ref name="pmid17229401">{{cite journal | author = Lee HJ, Jeong YI, Lee TH, ''et al.'' | title = Rosmarinic acid inhibits indoleamine 2,3-dioxygenase expression in murine dendritic cells | journal = Biochem. Pharmacol. | volume = 73 | issue = 9 | pages = 1412–21 |date=May 2007 | pmid = 17229401 | doi = 10.1016/j.bcp.2006.12.018 }}</ref> [[COX-2 inhibitors]] down-regulate indoleamine 2,3-dioxygenase, leading to a reduction in [[kynurenine]] levels as well as reducing proinflammatory cytokine activity.<ref name="pmid21517752">{{cite journal |author=Cesario A, Rocca B, Rutella S |title=The interplay between indoleamine 2,3-dioxygenase 1 (IDO1) and cyclooxygenase (COX)-2 in chronic inflammation and cancer |journal=Curr. Med. Chem. |volume=18 |issue=15 |pages=2263–71 |year=2011 |pmid=21517752 |doi=10.2174/092986711795656063}}</ref> |
[[Norharmane]], via inhibition of indoleamine 2,3-dioxygenase exerts neuroprotective properties by suppressing [[kynurenine]] neurotoxic metabolites such as [[quinolinic acid]], 3-hydroxy-kynurenine and [[nitric oxide synthase]].<ref name="pmid10947071">{{cite journal | author = Chiarugi A, Dello Sbarba P, Paccagnini A, Donnini S, Filippi S, Moroni F | title = Combined inhibition of indoleamine 2,3-dioxygenase and nitric oxide synthase modulates neurotoxin release by interferon-gamma-activated macrophages | journal = J. Leukoc. Biol. | volume = 68 | issue = 2 | pages = 260–6 |date=August 2000 | pmid = 10947071 | doi = | url = http://www.jleukbio.org/content/68/2/260.long }}</ref> [[Rosmarinic acid]] inhibits the expression of indoleamine 2,3-dioxygenase via its [[cyclooxygenase]]-inhibiting properties.<ref name="pmid17229401">{{cite journal | author = Lee HJ, Jeong YI, Lee TH, ''et al.'' | title = Rosmarinic acid inhibits indoleamine 2,3-dioxygenase expression in murine dendritic cells | journal = Biochem. Pharmacol. | volume = 73 | issue = 9 | pages = 1412–21 |date=May 2007 | pmid = 17229401 | doi = 10.1016/j.bcp.2006.12.018 }}</ref> [[COX-2 inhibitors]] down-regulate indoleamine 2,3-dioxygenase, leading to a reduction in [[kynurenine]] levels as well as reducing proinflammatory cytokine activity.<ref name="pmid21517752">{{cite journal |author=Cesario A, Rocca B, Rutella S |title=The interplay between indoleamine 2,3-dioxygenase 1 (IDO1) and cyclooxygenase (COX)-2 in chronic inflammation and cancer |journal=Curr. Med. Chem. |volume=18 |issue=15 |pages=2263–71 |year=2011 |pmid=21517752 |doi=10.2174/092986711795656063}}</ref> Alpha-Methyl-Tryptophan also inhibits indoleamine dioxygenase.<ref>http://cancerres.aacrjournals.org/content/67/2/792.abstract</ref> |
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Revision as of 01:55, 8 August 2014
Template:PBB Indoleamine-pyrrole 2,3-dioxygenase (IDO or INDO EC 1.13.11.52) is an enzyme that in humans is encoded by the IDO1 gene.[1][2] This enzyme catalyzes the degradation of the essential amino acid L-tryptophan to N-formylkynurenine.[3]
Function
Indoleamine 2,3-dioxygenase is the first and rate-limiting enzyme of tryptophan catabolism through kynurenine pathway, thus causing depletion of tryptophan which can cause halted growth of microbes as well as T cells.
IDO is an immunomodulatory enzyme produced by some alternatively activated macrophages and other immunoregulatory cells (also used as an immune subversion strategy by many tumors). Interferon-gamma has an antiproliferative effect on many tumor cells and inhibits intracellular pathogens such as Toxoplasma and chlamydia, at least partly because of the induction of indoleamine 2,3-dioxygenase.
It has been shown that IDO permits tumor cells to escape the immune system by depletion of L-Trp in the microenvironment of cells. Indeed, wide range of human cancers such as prostatic, colorectal, pancreatic, cervical, gastric, ovarian, head, lung, etc. overexpress human IDO (hIDO).[4]
Inhibitors
Norharmane, via inhibition of indoleamine 2,3-dioxygenase exerts neuroprotective properties by suppressing kynurenine neurotoxic metabolites such as quinolinic acid, 3-hydroxy-kynurenine and nitric oxide synthase.[5] Rosmarinic acid inhibits the expression of indoleamine 2,3-dioxygenase via its cyclooxygenase-inhibiting properties.[6] COX-2 inhibitors down-regulate indoleamine 2,3-dioxygenase, leading to a reduction in kynurenine levels as well as reducing proinflammatory cytokine activity.[7] Alpha-Methyl-Tryptophan also inhibits indoleamine dioxygenase.[8]
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See also
References
- ^ Dai W, Gupta SL (April 1990). "Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA". Biochem. Biophys. Res. Commun. 168 (1): 1–8. doi:10.1016/0006-291X(90)91666-G. PMID 2109605.
- ^ Najfeld V, Menninger J, Muhleman D, Comings DE, Gupta SL (1993). "Localization of indoleamine 2,3-dioxygenase gene (INDO) to chromosome 8p12-->p11 by fluorescent in situ hybridization". Cytogenet. Cell Genet. 64 (3–4): 231–2. doi:10.1159/000133584. PMID 8404046.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ "Entrez Gene: INDO indoleamine-pyrrole 2,3 dioxygenase".
- ^ Uyttenhove,C.; Pilotte, L.; Théate, I.; Stroobant, V.; Colau, D.; Parmentier,N.; Boon, T.; Van den Eynde, B. J. Naturemedicine 2003,9, 1269-74
- ^ Chiarugi A, Dello Sbarba P, Paccagnini A, Donnini S, Filippi S, Moroni F (August 2000). "Combined inhibition of indoleamine 2,3-dioxygenase and nitric oxide synthase modulates neurotoxin release by interferon-gamma-activated macrophages". J. Leukoc. Biol. 68 (2): 260–6. PMID 10947071.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Lee HJ, Jeong YI, Lee TH; et al. (May 2007). "Rosmarinic acid inhibits indoleamine 2,3-dioxygenase expression in murine dendritic cells". Biochem. Pharmacol. 73 (9): 1412–21. doi:10.1016/j.bcp.2006.12.018. PMID 17229401.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - ^ Cesario A, Rocca B, Rutella S (2011). "The interplay between indoleamine 2,3-dioxygenase 1 (IDO1) and cyclooxygenase (COX)-2 in chronic inflammation and cancer". Curr. Med. Chem. 18 (15): 2263–71. doi:10.2174/092986711795656063. PMID 21517752.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ http://cancerres.aacrjournals.org/content/67/2/792.abstract
Further reading
- Grohmann U, Fallarino F, Puccetti P (2004). "Tolerance, DCs and tryptophan: much ado about IDO". Trends Immunol. 24 (5): 242–8. doi:10.1016/S1471-4906(03)00072-3. PMID 12738417.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Takikawa O (2005). "Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism". Biochem. Biophys. Res. Commun. 338 (1): 12–9. doi:10.1016/j.bbrc.2005.09.032. PMID 16176799.
- Puccetti P (2007). "On watching the watchers: IDO and type I/II IFN". Eur. J. Immunol. 37 (4): 876–9. doi:10.1002/eji.200737184. PMID 17393386.
- Kadoya A, Tone S, Maeda H; et al. (1992). "Gene structure of human indoleamine 2,3-dioxygenase". Biochem. Biophys. Res. Commun. 189 (1): 530–6. doi:10.1016/0006-291X(92)91590-M. PMID 1449503.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Kamimura S, Eguchi K, Yonezawa M, Sekiba K (1991). "Localization and developmental change of indoleamine 2,3-dioxygenase activity in the human placenta". Acta Med. Okayama. 45 (3): 135–9. PMID 1716396.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Tone S, Takikawa O, Habara-Ohkubo A; et al. (1990). "Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA". Nucleic Acids Res. 18 (2): 367. doi:10.1093/nar/18.2.367. PMC 330282. PMID 2326172.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Werner-Felmayer G, Werner ER, Fuchs D; et al. (1990). "Tumour necrosis factor-alpha and lipopolysaccharide enhance interferon-induced tryptophan degradation and pteridine synthesis in human cells". Biol. Chem. Hoppe-Seyler. 370 (9): 1063–9. PMID 2482041.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Carlin JM, Borden EC, Byrne GI (1989). "Interferon-induced indoleamine 2,3-dioxygenase activity inhibits Chlamydia psittaci replication in human macrophages". J. Interferon Res. 9 (3): 329–37. doi:10.1089/jir.1989.9.329. PMID 2501398.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Kobayashi K, Hayashi K, Sono M (1989). "Effects of tryptophan and pH on the kinetics of superoxide radical binding to indoleamine 2,3-dioxygenase studied by pulse radiolysis". J. Biol. Chem. 264 (26): 15280–3. PMID 2549057.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Daley-Yates PT, Powell AP, Smith LL (1989). "Pulmonary indoleamine 2,3-dioxygenase activity and its significance in the response of rats, mice, and rabbits to oxidative stress". Toxicol. Appl. Pharmacol. 96 (2): 222–32. doi:10.1016/0041-008X(88)90082-8. PMID 2848333.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Burkin DJ, Kimbro KS, Barr BL; et al. (1993). "Localization of the human indoleamine 2,3-dioxygenase (IDO) gene to the pericentromeric region of human chromosome 8". Genomics. 17 (1): 262–3. doi:10.1006/geno.1993.1319. PMID 8406467.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Malina HZ, Martin XD (1996). "Indoleamine 2,3-dioxygenase: antioxidant enzyme in the human eye". Graefes Arch. Clin. Exp. Ophthalmol. 234 (7): 457–62. doi:10.1007/BF02539413. PMID 8817290.
- Munn DH, Zhou M, Attwood JT; et al. (1998). "Prevention of allogeneic fetal rejection by tryptophan catabolism". Science. 281 (5380): 1191–3. doi:10.1126/science.281.5380.1191. PMID 9712583.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Takikawa O, Littlejohn TK, Truscott RJ (2001). "Indoleamine 2,3-dioxygenase in the human lens, the first enzyme in the synthesis of UV filters". Exp. Eye Res. 72 (3): 271–7. doi:10.1006/exer.2000.0951. PMID 11180976.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Kudo Y, Boyd CA (2001). "The role of l-tryptophan transport in l-tryptophan degradation by indoleamine 2,3-dioxygenase in human placental explants". J. Physiol. (Lond.). 531 (Pt 2): 417–23. doi:10.1111/j.1469-7793.2001.0417i.x. PMC 2278460. PMID 11230514.
- Terentis AC, Thomas SR, Takikawa O; et al. (2002). "The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions". J. Biol. Chem. 277 (18): 15788–94. doi:10.1074/jbc.M200457200. PMID 11867636.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - Kvirkvelia N, Vojnovic I, Warner TD; et al. (2002). "Placentally derived prostaglandin E2 acts via the EP4 receptor to inhibit IL-2-dependent proliferation of CTLL-2 T cells". Clin. Exp. Immunol. 127 (2): 263–9. doi:10.1046/j.1365-2249.2002.01718.x. PMC 1906325. PMID 11876748.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) - Sedlmayr P, Blaschitz A, Wintersteiger R; et al. (2002). "Localization of indoleamine 2,3-dioxygenase in human female reproductive organs and the placenta". Mol. Hum. Reprod. 8 (4): 385–91. doi:10.1093/molehr/8.4.385. PMID 11912287.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link)
External links
- Indoleamine-Pyrrole+2,3,-Dioxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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