Những điểm nổi bật tại cổng chuyển hóa tryptophan: một bài tổng quan về các cơ chế hoạt hóa và điều hòa của indoleamine 2,3-dioxygenase (IDO), một mục tiêu mới trong bệnh ung thư

Austin CJ, Astelbauer F, Kosim-Satyaputra P, Ball HJ, Willows RD, Jamie JF, Hunt NH (2008) Mouse and human indoleamine 2,3-dioxygenase display some distinct biochemical and structural properties. Amino Acids (in press) Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH (2007) Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice. Gene 396:203–213 Ball HJ, Yuasa HJ, Austin CJ, Weiser S, Hunt NH (2008) Indoleamine 2,3-dioxygenase-2; a new enzyme in the kynurenine pathway. Int J Biochem Cell Biol (in press) Batabyal D, Yeh SR (2007) Human tryptophan dioxygenase: a comparison to indoleamine 2,3-dioxygenase. J Am Chem Soc 129:15690–15701 Bendall DS (1996) Protein electron transfer. BIOS Scientific Publishers, Oxford Brastianos HC, Vottero E, Patrick BO, Soest RV, Matainaho T, Mauk AG, Andersen RJ (2006) Exiguamine A, an indoleamine-2,3-dioxygenase (IDO) inhibitor isolated from the marine sponge Neopetrosia exigua. J Am Chem Soc 128:16046–16047 Cady SG, Sono M (1991) 1-Methyl-dl-tryptophan, beta-(3-benzofuranyl)-dl-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-dl-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Arch Biochem Biophys 291:326–333 Carr G, Chung MK, Mauk AG, Andersen RJ (2008) Synthesis of indoleamine 2,3-dioxygenase inhibitory analogues of the sponge alkaloid exiguamine A. J Med Chem 51:2634–2637 Chauhan N, Basran J, Efimov I, Svistunenko DA, Seward HE, Moody PC, Raven EL (2008) The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase. Biochemistry 47:4761–4769 Eguchi N, Watanabe Y, Kawanishi K, Hashimoto Y, Hayaishi O (1984) Inhibition of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase by beta-carboline and indole derivatives. Arch Biochem Biophys 232:602–609 Fallarino F, Grohmann U, Hwang KW, Orabona C, Vacca C, Bianchi R, Belladonna ML, Fioretti MC, Alegre ML, Puccetti P (2003) Modulation of tryptophan catabolism by regulatory T cells. Nat Immunol 4:1206–1212 Gaspari P, Banerjee T, Malachowski WP, Muller AJ, Prendergast GC, DuHadaway J, Bennett S, Donovan AM (2006) Structure-activity study of brassinin derivatives as indoleamine 2,3-dioxygenase inhibitors. J Med Chem 49:684–692 Grohmann U, Fallarino F, Puccetti P (2003) Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol 24:242–248 Hayaishi O (1993) My life with tryptophan-never a dull moment. Protein Sci 2:472–475 Hayaishi O, Hirata F, Ohnishi T, Henry JP, Rosenthal I, Katoh A (1977) Indoleamine 2,3-dioxygenase: incorporation of 18O2 and 18O2 into the reaction products. J Biol Chem 252:3548–3550 Higuchi K, Kuno S, Hayaishi O (1963) Enzymatic formation of d-kynurenin. Federation Proc 22:243 (abstr.) Hirata F, Hayaishi O (1975) Studies on indoleamine 2,3-dioxygenase. I. Superoxide anion as substrate. J Biol Chem 250:5960–5966 Hirata F, Ohnishi T, Hayaishi O (1977) Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2-complex. J Biol Chem 252:4637–4642 Hou DY, Muller AJ, Sharma MD, DuHadaway J, Banerjee T, Johnson M, Mellor AL, Prendergast GC, Munn DH (2007) Inhibition of indoleamine 2,3-dioxygenase in dendritic cells by stereoisomers of 1-methyl-tryptophan correlates with antitumor responses. Cancer Res 67:792–801 Katz JB, Muller AJ, Prendergast GC (2008) Indoleamine 2,3-dioxygenase in T-cell tolerance and tumoral immune escape. Immunol Rev 222:206–221 Kumar S, Malachowski WP, DuHadaway JB, LaLonde JM, Carroll PJ, Jaller D, Metz R, Prendergast GC, Muller AJ (2008) Indoleamine 2,3-dioxygenase is the anticancer target for a novel series of potent naphthoquinone-based inhibitors. J Med Chem 51:1706–1718 Lob S, Konigsrainer A, Schafer R, Rammensee HG, Opelz G, Terness P (2008a) Levo- but not dextro-1-methyl tryptophan abrogates the IDO activity of human dendritic cells. Blood 111:2152–2154 Lob S, Konigsrainer A, Zieker D, Brucher BL, Rammensee HG, Opelz G, Terness P (2008b) IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism. Cancer Immunol Immunother. In press Macchiarulo A, Nuti R, Bellocchi D, Camaioni E, Pellicciari R (2007) Molecular docking and spatial coarse graining simulations as tools to investigate substrate recognition, enhancer binding and conformational transitions in indoleamine-2,3-dioxygenase (IDO). Biochim Biophys Acta 1774:1058–1068 Maghzal GJ, Thomas SR, Hunt NH, Stocker R (2008) Cytochrome b5, not superoxide anion radical, is a major reductant of indoleamine 2,3-dioxygenase in human cells. J Biol Chem 283:12014–12025 Malachowski WP, Metz R, Prendergast GC, Muller AJ (2005) A new cancer immunosuppression target: indoleamine 2,3-dioxygenase (IDO). A review of the IDO mechanism, inhibition and therapeutic applications. Drugs Future 30:897–909 Mellor AL, Munn DH (2004) IDO expression by dendritic cells: tolerance and tryptophan catabolism. Nat Rev Immunol 4:762–774 Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC (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 Res 67:7082–7087 Muller AJ, DuHadaway JB, Donover PS, Sutanto-Ward E, Prendergast GC (2005a) Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat Med 11:312–319 Muller AJ, Malachowski WP, Prendergast GC (2005b) Indoleamine 2,3-dioxygenase in cancer: targeting pathological immune tolerance with small-molecule inhibitors. Expert Opin Ther Targets 9:831–849 Muller AJ, Prendergast GC (2007) Indoleamine 2,3-dioxygenase in immune suppression and cancer. Curr Cancer Drug Targets 7:31–40 Muller AJ, Scherle PA (2006) Targeting the mechanisms of tumoral immune tolerance with small-molecule inhibitors. Nat Rev Cancer 6:613–625 Munn DH, Zhou M, Attwood JT, Bondarev I, Conway SJ, Marshall B, Brown C, Mellor AL (1998) Prevention of allogeneic fetal rejection by tryptophan catabolism. Science 281:1191–1193 Ozaki Y, Nichol CA, Duch DS (1987) Utilization of dihydroflavin mononucleotide and superoxide anion for the decyclization of l-tryptophan by murine epididymal indoleamine 2,3-dioxygenase. Arch Biochem Biophys 257:207–216 Ozaki Y, Reinhard JF Jr, Nichol CA (1986) Cofactor activity of dihydroflavin mononucleotide and tetrahydrobiopterin for murine epididymal indoleamine 2,3-dioxygenase. Biochem Biophys Res Commun 137:1106–1111 Papadopoulou ND, Mewies M, McLean KJ, Seward HE, Svistunenko DA, Munro AW, Raven EL (2005) Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis. Biochemistry 44:14318–14328 Pereira A, Vottero E, Roberge M, Mauk AG, Andersen RJ (2006) Indoleamine 2,3-dioxygenase inhibitors from the Northeastern Pacific Marine Hydroid Garveia annulata. J Nat Prod 69:1496–1499 Peters JC (1991) Tryptophan nutrition and metabolism: an overview. Adv Exp Med Biol 294:345–358 Peterson AC, La Loggia AJ, Hamaker LK et al (1993) Evaluation of substituted beta-carbolines as noncompetitive indoleamine 2,3-dioxygenase inhibitors. Med Chem Res 4:473–482 Peterson AC, Migawa MT, Martin MM et al (1994) Evaluation of functionalized tryptophan derivatives and related compounds as competitive inhibitors of Indoleamine 2,3-dioxygenase. Med Chem Res 3:531–544 Prendergast GC (2008) Immune escape as a fundamental trait of cancer: focus on IDO. Oncogene. Puccetti P, Grohmann U (2007) IDO and regulatory T cells: a role for reverse signalling and non-canonical NF-kappaB activation. Nat Rev Immunol 7:817–823 Romani L, Fallarino F, De Luca A, Montagnoli C, D’Angelo C, Zelante T, Vacca C, Bistoni F, Fioretti MC, Grohmann U, Segal BH, Puccetti P (2008) Defective tryptophan catabolism underlies inflammation in mouse chronic granulomatous disease. Nature 451:211–215 Ruddick JP, Evans AK, Nutt DJ, Lightman SL, Rook GA, Lowry CA (2006) Tryptophan metabolism in the central nervous system: medical implications. Expert Rev Mol Med 8:1–27 Samelson-Jones BJ, Yeh SR (2006) Interactions between nitric oxide and indoleamine 2,3-dioxygenase. Biochemistry 45:8527–8538 Sono M (1989) Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 2. Evidence for the existence of another binding site in the enzyme for indole derivative effectors. Biochemistry 28:5400–5407 Sono M, Cady SG (1989) 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 28:5392–5399 Sono M, Roach MP, Coulter ED, Dawson JH (1996) Heme-containing oxygenases. Chem Rev 96:2841–2888 Sono M, Taniguchi T, Watanabe Y, Hayaishi O (1980) Indoleamine 2,3-dioxygenase. Equilibrium studies of the tryptophan binding to the ferric, ferrous, and CO-bound enzymes. J Biol Chem 255:1339–1345 Southan MD, Truscott RJW, Jamie JF, Pelosi L, Walker MJ, Maeda H, Iwamoto Y, Tone S (1996) Structural requirements of the competitive binding site of recombinant human indoleamine 2,3-dioxygenase. Med Chem Res 6:343–352 Stone TW, Darlington LG (2002) Endogenous kynurenines as targets for drug discovery and development. Nat Rev Drug Discov 1:609–620 Sugimoto H, Oda S, Otsuki T, Hino T, Yoshida T, Shiro Y (2006) Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase. Proc Natl Acad Sci USA 103:2611–2616 Taniguchi T, Hirata F, Hayaishi O (1977) Intracellular utilization of superoxide anion by indoleamine 2,3-dioxygenase of rabbit enterocytes. J Biol Chem 252:2774–2776 Taylor MW, Feng GS (1991) Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism. FASEB J 5:2516–2522 Uchida K, Bandow H, Makino R, Sakaguchi K, Iizuka T, Ishimura Y (1985) Infrared spectra of carbon monoxide complexes of indoleamine 2,3-dioxygenase and l-tryptophan 2,3-dioxygenases. Effects of substrates on the CO-stretching frequencies. J Biol Chem 260:1400–1406 Uyttenhove C, Pilotte L, Theate I, Stroobant V, Colau D, Parmentier N, Boon T, Van den Eynde BJ (2003) Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase. Nat Med 9:1269–1274 Vottero E, Balgi A, Woods K, Tugendreich S, Melese T, Andersen RJ, Mauk AG, Roberge M (2006a) Inhibitors of human indoleamine 2,3-dioxygenase identified with a target-based screen in yeast. Biotechnol J 1:282–288 Vottero E, Mitchell DA, Page MJ, MacGillivray RT, Sadowski IJ, Roberge M, Mauk AG (2006b) Cytochrome b(5) is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast. FEBS Lett 580:2265–2268 Watanabe Y, Fujiwara M, O H, Takeuchi T, Hamao U (1978) 2,5-dihydro-l-phemilalanine: a competitive inhibitor of indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase. Biochem Biophys Res Commun 85:273–279 Wheeler KE, Nocek JM, Cull DA, Yatsunyk LA, Rosenzweig AC, Hoffman BM (2007) Dynamic docking of cytochrome b5 with myoglobin and alpha-hemoglobin: heme-neutralization “squares” and the binding of electron-transfer-reactive configurations. J Am Chem Soc 129:3906–3917 Zhang Y, Kang SA, Mukherjee T, Bale S, Crane BR, Begley TP, Ealick SE (2007) Crystal structure and mechanism of tryptophan 2,3-dioxygenase, a heme enzyme involved in tryptophan catabolism and in quinolinate biosynthesis. Biochemistry 46:145–155