Chapter 29: Inhibition of the kynurenine pathway of tryptophan metabolism

Targeting the Broadly Pathogenic Kynurenine Pathway

Volumn , Issue , 2015, Pages 393-406

  Frédérick, Raphaël ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

3 HAO; IDO; Inhibitors; KAT; KMO; Kynureninase; Kynurenine pathway; Medicinal chemistry; TDO

Indexed keywords

EID: 84956978784     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-319-11870-3_29     Document Type: Chapter

References (48)

1. Peters JC. Tryptophan nutrition and metabolism: an overview. Adv Exp Med Biol. 1991;294:345-58.
2. Bender DA. Biochemistry of tryptophan in health and disease. Mol Aspects Med. 1983;6(2):101-97.
3. Platten M, Wick W, Van den Eynde BJ. Tryptophan catabolism in cancer: beyond IDO and tryptophan depletion. Cancer Res. 2012;72(21):5435-40. doi: 10.1158/0008-5472.CAN- 12-0569.
4. Vecsei L, Szalardy L, Fulop F, Toldi J. Kynurenines in the CNS: recent advances and new questions. Nat Rev Drug Discov. 2013;12(1):64-82. doi: 10.1038/nrd3793.
5. Dolusic E, Frederick R. Indoleamine 2,3-dioxygenase inhibitors: a patent review (2008-2012). Expert Opin Ther Pat. 2013;23(10):1367-81. doi: 10.1517/13543776.2013.827662.
6. Cady SG, Sono M. 1-methyl-DL-tryptophan, β-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and β-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Arch Biochem Biophys. 1991; 291(2):326-33.
7. Lob S, Konigsrainer A, Schafer R, Rammensee HG, Opelz G, Terness P. Levo- but not dextro- 1- methyl tryptophan abrogates the IDO activity of human dendritic cells. Blood. 2008;111(4):2152-4.
8. Qian F, Villella J, Wallace PK, Mhawech-Fauceglia P, Tario Jr JD, Andrews C, et al. Efficacy of levo-1-methyl tryptophan and dextro-1-methyl tryptophan in reversing indoleamine-2,3- dioxygenase- mediated arrest of T-cell proliferation in human epithelial ovarian cancer. Cancer Res. 2009;69(13):5498-504.
9. Metz R, DuHadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC. Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan. Cancer Res. 2007; 67(15):7082-7.
10. Platten M, Wick W, Van Den Eynde BJ. Tryptophan catabolism in cancer: beyond IDO and tryptophan depletion. Cancer Res. 2012;72(21):5435-40.
11. Eguchi N, Watanabe Y, Kawanishi K, Hashimoto Y, Hayaishi O. Inhibition of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase by beta-carboline and indole derivatives. Arch Biochem Biophys. 1984;232(2):602-9.
12. Gaspari P, Banerjee T, Malachowski WP, Muller AJ, Prendergast GC, DuHadaway J, et al. Structure-activity study of brassinin derivatives as indoleamine 2,3-dioxygenase inhibitors. J Med Chem. 2006;49(2):684-92.
13. Dolusic E, Larrieu P, Blanc S, Sapunaric F, Norberg B, Moineaux L, et al. Indol-2-yl ethanones as novel indoleamine 2,3-dioxygenase (IDO) inhibitors. Bioorg Med Chem. 2011;19(4):1550-61. doi: 10.1016/j.bmc.2010.12.032.
14. Dolusic E, Larrieu P, Blanc S, Sapunaric F, Pouyez J, Moineaux L, et al. Discovery and preliminary SARs of keto-indoles as novel indoleamine 2,3-dioxygenase (IDO) inhibitors. Eur J Med Chem. 2011;46(7):3058-65. doi: 10.1016/j.ejmech.2011.02.049.
15. Brastianos HC, Vottero E, Patrick BO, Van Soest R, Matainaho T, Mauk AG, et al. Exiguamine A, an indoleamine-2,3-dioxygenase (IDO) inhibitor isolated from the marine sponge Neopetrosia exigua. J Am Chem Soc. 2006;128(50):16046-7.
16. Carr G, Chung MKW, Mauk AG, Andersen RJ. Synthesis of indoleamine 2,3-dioxygenase inhibitory analogues of the sponge alkaloid exiguamine A. J Med Chem. 2008;51(9):2634-7.
17. Kumar S, Malachowski WP, DuHadaway JB, LaLonde JM, Carroll PJ, Jaller D, et al. Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone- based inhibitors. J Med Chem. 2008;51(6):1706-18.
18. Sono M, Cady SG. Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands. Biochemistry. 1989;28(13):5392-9.
19. Sugimoto H, Oda SI, Otsuki T, Hino T, Yoshida T, Shiro Y. Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase. Proc Natl Acad Sci USA. 2006;103(8):2611-6.
20. Kumar S, Jaller D, Patel B, LaLonde JM, DuHadaway JB, Malachowski WP, et al. Structure based development of phenylimidazole-derived inhibitors of indoleamine 2,3-dioxygenase. J Med Chem. 2008;51(16):4968-77.
21. Jaipuri F, Kesharwani T, Kumar S, Mautino M, J. W, inventors; Newlink Genetics, assignee. Fused imidazole derivatives useful as ido inhibitors. USA patent WO2012142237. 2012 20110415.
22. Yue EW, Douty B, Wayland B, Bower M, Liu X, Leffet L, et al. Discovery of potent competitive inhibitors of indoleamine 2,3-dioxygenase with in vivo pharmacodynamic activity and efficacy in a mouse melanoma model. J Med Chem. 2009;52(23):7364-7.
23. Meininger D, Zalameda L, Liu Y, Stepan LP, Borges L, McCarter JD, et al. Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors. Biochim Biophys Acta. 2011;1814(12):1947-54. doi: 10.1016/j.bbapap.2011.07.023.
24. Tojo S, Kohno T, Tanaka T, Kamioka S, Ota Y, Ishii T, et al. Crystal structures and structureactivity relationships of imidazothiazole derivatives as IDO1 inhibitors. ACS Med Chem Lett. 2014;5(10):1119-23. doi: 10.1021/ml500247w.
25. Opitz CA, Litzenburger UM, Sahm F, Ott M, Tritschler I, Trump S, et al. An endogenous tumour-promoting ligand of the human aryl hydrocarbon receptor. Nature. 2011; 478(7368):197-203.
26. Pilotte L, Larrieu P, Stroobant V, Colau D, Dolušić E, Frédérick R, et al. Reversal of tumoral immune resistance by inhibition of tryptophan 2,3-dioxygenase. Proc Natl Acad Sci USA. 2012;109(7):2497-502.
27. Dolušić E, Larrieu P, Moineaux L, Stroobant V, Pilotte L, Colau D, et al. Tryptophan 2,3- dioxygenase (TDO) inhibitors. 3-(2-(pyridyl)ethenyl)indoles as potential anticancer immunomodulators. J Med Chem. 2011;54(15):5320-34.
28. Yu P, Di Prospero NA, Sapko MT, Cai T, Chen A, Melendez-Ferro M, et al. Biochemical and phenotypic abnormalities in kynurenine aminotransferase II-deficient mice. Mol Cell Biol. 2004;24(16):6919-30. doi: 10.1128/MCB.24.16.6919-6930.2004.
29. Guidetti P, Okuno E, Schwarcz R. Characterization of rat brain kynurenine aminotransferases I and II. J Neurosci Res. 1997;50(3):457-65.
30. Han Q, Robinson H, Cai T, Tagle DA, Li J. Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K. J Med Chem. 2009;52(9):2786-93. doi: 10.1021/jm9000874.
31. Pellicciari R, Filosa R, Fulco MC, Marinozzi M, Macchiarulo A, Novak C, et al. Synthesis and preliminary biological evaluation of 2′-substituted 2-(3′-carboxybicyclo[1.1.1]pentyl)glycine derivatives as group I selective metabotropic glutamate receptor ligands. ChemMedChem. 2006;1(3):358-65. doi: 10.1002/cmdc.200500071.
32. Pellicciari R, Venturoni F, Bellocchi D, Carotti A, Marinozzi M, Macchiarulo A, et al. Sequence variants in kynurenine aminotransferase II (KAT II) orthologs determine different potencies of the inhibitor S-ESBA. ChemMedChem. 2008;3(8):1199-202. doi: 10.1002/cmdc.200800109.
33. Henderson JL, Sawant-Basak A, Tuttle JB, Dounay AB, McAllister LA, Pandit J, et al. Discovery of hydroxamate bioisosteres as KAT II inhibitors with improved oral bioavailability and pharmacokinetics. MedChemComm. 2013;4(1):125-9. doi: 10.1039/C2MD20166F.
34. Dua RK, Taylor EW, Phillips RS. 5-Aryl-L-cysteine S, S-dioxides: design, synthesis, and evaluation of a new class of inhibitors of kynureninase. J Am Chem Soc. 1993;115(4): 1264-70.
35. Pellicciari R, Natalini B, Costantino G, Mahmoud MR, Mattoli L, Sadeghpour BM, et al. Modulation of the kynurenine pathway in search for new neuroprotective agents. Synthesis and preliminary evaluation of (m-Nitrobenzoyl)alanine, a potent inhibitor of Kynurenine-3- hydroxylase. J Med Chem. 1994;37(5):647-55.
36. Fitzgerald DH, Muirhead KM, Botting NP. A comparative study on the inhibition of human and bacterial kynureninase by novel bicyclic kynurenine analogues. Bioorg Med Chem. 2001;9(4):983-9.
37. Walsh HA, Leslie PL, O'Shea KC, Botting NP. 2-Amino-4-[3′-hydroxyphenyl]-4- hydroxybutanoic acid; a potent inhibitor of rat and recombinant human kynureninase. Bioorg Med Chem Lett. 2002;12(3):361-3.
38. Lima S, Kumar S, Gawandi V, Momany C, Phillips RS. Crystal structure of the homo sapiens kynureninase-3-hydroxyhippuric acid inhibitor complex: Insights into the molecular basis of kynureninase substrate specificity. J Med Chem. 2009;52(2):389-96.
39. Carpenedo R, Chiarugi A, Russi P, Lombardi G, Carlà V, Pellicciari R, et al. Inhibitors of kynurenine hydroxylase and kynureninase increase cerebral formation of kynurenate and have sedative and anticonvulsant activities. Neuroscience. 1994;61(2):237-44.
40. Speciale C, Wu HQ, Cini M, Marconi M, Varasi M, Schwarcz R. (R, S)-3,4- dichlorobenzoylalanine (FCE 28833A) causes a large and persistent increase in brain kynurenic acid levels in rats. Eur J Pharmacol. 1996;315(3):263-7.
41. Natalini B, Mattoli L, Pellicciari R, Carpenedo R, Chiarugi A, Moroni F. Synthesis and activity of enantiopure (S) (m-nitrobenzoyl) alanine, potent kynurenine-3-hydroxylase inhibitor. Bioorg Med Chem Lett. 1995;5(14):1451-4.
42. Reinhard Jr JF. Pharmacological manipulation of brain kynurenine metabolism. Ann NY Acad Sci. 2004;1035:335-49.
43. Röver S, Cesura AM, Huguenin P, Kettler R, Szente A. Synthesis and biochemical evaluation of N-(4-phenylthiazol-2- yl)benzenesulfonamides as high-affinity inhibitors of kynurenine 3- hydroxylase. J Med Chem. 1997;40(26):4378-85.
44. Pellicciari R, Amori L, Costantino G, Giordani A, Macchiarulo A, Mattoli L, et al. Modulation of the kynurine pathway of tryptophan metabolism in search for neuroprotective agents. Focus on kynurenine-3-hydroxylase. Adv Exp Med Biol. 2003;527:621-8.
45. Heidempergher F, Pevarello P, Pillan A, Pinciroli V, Della Torre A, Speciale C, et al. Pyrrolo[3,2-c]quinoline derivatives: a new class of kynurenine-3-hydroxylase inhibitors. II. Farmaco. 1999;54(3):152-60.
46. Walsh JL, Todd WP, Carpenter BK, Schwarcz R. 4-Halo-3-hydroxyanthranilic acids: potent competitive inhibitors of 3-hydroxy-anthranilic acid oxygenase in vitro. Biochem Pharmacol. 1991;42(5):985-90.
47. Linderberg M, Hellberg S, Björk S, Gotthammar B, Högberg T, Persson K, et al. Synthesis and QSAR of substituted 3-hydroxyanthranilic acid derivatives as inhibitors of 3- hydroxyanthranilic acid dioxygenase (3-HAO). Eur J Med Chem. 1999;34(9):729-44.
48. Vallerini GP, Amori L, Beato C, Tararina M, Wang XD, Schwarcz R, et al. 2-Aminonicotinic acid 1-oxides are chemically stable inhibitors of quinolinic acid synthesis in the mammalian brain: a step toward new antiexcitotoxic agents. J Med Chem. 2013;56(23):9482-95. doi: 10.1021/jm401249c.