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Volumn 52, Issue 6, 2008, Pages 1297-1303

Alterations in kynurenine precursor and product levels in schizophrenia and bipolar disorder

Author keywords

3 Hydroxy anthranilic acid; 3 OH anthranilate; HPLC; Metabolites; Nicotinamide; Psychosis; Suicide; Tryptophan

Indexed keywords

3 HYDROXYANTHRANILIC ACID; KYNURENINE; NICOTINAMIDE; TRYPTOPHAN; TRYPTOPHAN 2,3 DIOXYGENASE;

EID: 40949098991     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2008.01.013     Document Type: Article
Times cited : (74)

References (50)
  • 2
    • 33845206650 scopus 로고    scopus 로고
    • Acute psychotic symptoms in HIV-1 infected patients are associated with increased levels of kynurenic acid in cerebrospinal fluid. 1
    • Atlas A., Gisslen M., Nordin C., Lindstrom L., and Schwieler L. Acute psychotic symptoms in HIV-1 infected patients are associated with increased levels of kynurenic acid in cerebrospinal fluid. 1. Brain Behav. Immun. 21 1 (2007) 86-91
    • (2007) Brain Behav. Immun. , vol.21 , Issue.1 , pp. 86-91
    • Atlas, A.1    Gisslen, M.2    Nordin, C.3    Lindstrom, L.4    Schwieler, L.5
  • 3
    • 0017126084 scopus 로고
    • The regulation of rat liver tryptophan pyrrolase activity by reduced nicotinamide-adenine dinucleotide (phosphate)
    • Badawy A.A., and Evans M. The regulation of rat liver tryptophan pyrrolase activity by reduced nicotinamide-adenine dinucleotide (phosphate). Biochem. J. 156 2 (1976) 381-390
    • (1976) Biochem. J. , vol.156 , Issue.2 , pp. 381-390
    • Badawy, A.A.1    Evans, M.2
  • 5
    • 0033555723 scopus 로고    scopus 로고
    • Role of IFN-gamma-induced indoleamine 2,3-dioxygenase and inducible nitric oxide synthase in the replication of human cytomegalovirus in retinal pigment epithelial cells
    • Bodaghi B., Boureau O., Zipeto D., Laurent L., Virelizier J.L., and Michelson S. Role of IFN-gamma-induced indoleamine 2,3-dioxygenase and inducible nitric oxide synthase in the replication of human cytomegalovirus in retinal pigment epithelial cells. J. Immunol. 162 2 (1999) 957-964
    • (1999) J. Immunol. , vol.162 , Issue.2 , pp. 957-964
    • Bodaghi, B.1    Boureau, O.2    Zipeto, D.3    Laurent, L.4    Virelizier, J.L.5    Michelson, S.6
  • 6
    • 0025949160 scopus 로고
    • Implications of interferon-induced tryptophan catabolism in cancer, auto-immune diseases and AIDs
    • Brown R.R., Ozaki Y., Datta S.P., Borden E.C., Sondel P.M., and Malone D.G. Implications of interferon-induced tryptophan catabolism in cancer, auto-immune diseases and AIDs. Adv. Exp. Med. Biol. 294 (1991) 425-435
    • (1991) Adv. Exp. Med. Biol. , vol.294 , pp. 425-435
    • Brown, R.R.1    Ozaki, Y.2    Datta, S.P.3    Borden, E.C.4    Sondel, P.M.5    Malone, D.G.6
  • 7
    • 0014216321 scopus 로고
    • Feedback control of rat liver tryptophan pyrrolase
    • Cho-chung Y.S., and Pitot H.C. Feedback control of rat liver tryptophan pyrrolase. J. Biol. Chem. 242 6 (1967) 1192-1198
    • (1967) J. Biol. Chem. , vol.242 , Issue.6 , pp. 1192-1198
    • Cho-chung, Y.S.1    Pitot, H.C.2
  • 8
    • 0014253381 scopus 로고
    • Regulatory effects of nicotinamide on tryptophan pyrrolase synthesis in rat liver in vivo
    • Cho-chung Y.S., and Pitot H.C. Regulatory effects of nicotinamide on tryptophan pyrrolase synthesis in rat liver in vivo. Eur. J. Biochem. 3 4 (1968) 401-406
    • (1968) Eur. J. Biochem. , vol.3 , Issue.4 , pp. 401-406
    • Cho-chung, Y.S.1    Pitot, H.C.2
  • 9
    • 0023095424 scopus 로고
    • Oxidative reactivity of the tryptophan metabolites 3-hydroxyanthranilate, cinnabarinate, quinolinate and picolinate
    • Dykens J.A., Sullivan S.G., and Stern A. Oxidative reactivity of the tryptophan metabolites 3-hydroxyanthranilate, cinnabarinate, quinolinate and picolinate. Biochem. Pharmacol. 36 2 (1987) 211-217
    • (1987) Biochem. Pharmacol. , vol.36 , Issue.2 , pp. 211-217
    • Dykens, J.A.1    Sullivan, S.G.2    Stern, A.3
  • 10
    • 40949103238 scopus 로고
    • Oxidation of 3-hydroxy-anthranilic acid by human serum
    • Ehrensvard G., Liljekvist J., and Heath R.G. Oxidation of 3-hydroxy-anthranilic acid by human serum. Acta Chem. Scand. 14 (1960) 2081-2088
    • (1960) Acta Chem. Scand. , vol.14 , pp. 2081-2088
    • Ehrensvard, G.1    Liljekvist, J.2    Heath, R.G.3
  • 12
    • 0021042967 scopus 로고
    • On the excitotoxic properties of quinolinic acid, 2,3-piperidine dicarboxylic acids and structurally related compounds
    • Foster A.C., Collins J.F., and Schwarcz R. On the excitotoxic properties of quinolinic acid, 2,3-piperidine dicarboxylic acids and structurally related compounds. Neuropharmacology 22 12A (1983) 1331-1342
    • (1983) Neuropharmacology , vol.22 , Issue.12 A , pp. 1331-1342
    • Foster, A.C.1    Collins, J.F.2    Schwarcz, R.3
  • 13
    • 0033045078 scopus 로고    scopus 로고
    • Pigments of fungi (Macromycetes)
    • Gill M. Pigments of fungi (Macromycetes). Nat. Prod. Rep. 16 (1999) 301-317
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 301-317
    • Gill, M.1
  • 16
    • 0015074837 scopus 로고
    • Tryptophan metabolism in patients with pellagra: the problem of vitamin B6 activity and feedback control of tryptophan pyrrolase enzyme
    • Hankes L.V., Leklem J.E., Brown R.R., and Mekel R.C. Tryptophan metabolism in patients with pellagra: the problem of vitamin B6 activity and feedback control of tryptophan pyrrolase enzyme. Am. J. Clin. Nutr. 24 6 (1971) 730-739
    • (1971) Am. J. Clin. Nutr. , vol.24 , Issue.6 , pp. 730-739
    • Hankes, L.V.1    Leklem, J.E.2    Brown, R.R.3    Mekel, R.C.4
  • 17
    • 0017086970 scopus 로고
    • Properties and function of indoleamine 2,3-dioxygenase
    • Hayaishi O. Properties and function of indoleamine 2,3-dioxygenase. J. Biochem. 79 (1976) 13-21
    • (1976) J. Biochem. , vol.79 , pp. 13-21
    • Hayaishi, O.1
  • 18
    • 0028291455 scopus 로고
    • A multidimensional approach to analysis of cerebrospinal fluid biogenic amines in schizophrenia. I. Comparisons with healthy control subjects and neuroleptic-treated/unmedicated pairs analyses
    • Issa F., Gerhardt G.A., Bartko J.J., Suddath R.L., Lynch M., Gamache P.H., Freedman R., Wyatt R.J., and Kirch D.G. A multidimensional approach to analysis of cerebrospinal fluid biogenic amines in schizophrenia. I. Comparisons with healthy control subjects and neuroleptic-treated/unmedicated pairs analyses. Psychiatry Res. 52 3 (1994) 237-249
    • (1994) Psychiatry Res. , vol.52 , Issue.3 , pp. 237-249
    • Issa, F.1    Gerhardt, G.A.2    Bartko, J.J.3    Suddath, R.L.4    Lynch, M.5    Gamache, P.H.6    Freedman, R.7    Wyatt, R.J.8    Kirch, D.G.9
  • 20
    • 78651013065 scopus 로고
    • The conversion of tryptophan to kynurenine in the liver
    • Knox W.E., and Mehler A.H. The conversion of tryptophan to kynurenine in the liver. J. Biol. Chem. 187 (1950) 419-430
    • (1950) J. Biol. Chem. , vol.187 , pp. 419-430
    • Knox, W.E.1    Mehler, A.H.2
  • 21
    • 0023597265 scopus 로고
    • Neurotransmitter amino acids in post-mortem brains of chronic schizophrenic patients
    • Korpi E.R., Kleinman J.E., Goodman S.I., and Wyatt R.J. Neurotransmitter amino acids in post-mortem brains of chronic schizophrenic patients. Psychiatry Res. 22 4 (1987) 291-301
    • (1987) Psychiatry Res. , vol.22 , Issue.4 , pp. 291-301
    • Korpi, E.R.1    Kleinman, J.E.2    Goodman, S.I.3    Wyatt, R.J.4
  • 22
    • 14544282437 scopus 로고    scopus 로고
    • Potential role for nonesterified fatty acids in beta-adrenoceptor-induced increases in brain tryptophan. 1
    • Lenard N.R., and Dunn A.J. Potential role for nonesterified fatty acids in beta-adrenoceptor-induced increases in brain tryptophan. 1. Neurochem. Int. 46 2 (2005) 179-187
    • (2005) Neurochem. Int. , vol.46 , Issue.2 , pp. 179-187
    • Lenard, N.R.1    Dunn, A.J.2
  • 25
    • 0025236783 scopus 로고
    • Mechanism of reaction of 3-hydroxyanthranilic acid with molecular oxygen
    • Manthey M.K., Pyne S.G., and Truscott J.W. Mechanism of reaction of 3-hydroxyanthranilic acid with molecular oxygen. Biochim. Biophys. Acta 1034 (1990) 207-212
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 207-212
    • Manthey, M.K.1    Pyne, S.G.2    Truscott, J.W.3
  • 26
    • 1842419381 scopus 로고    scopus 로고
    • Expression of the kynurenine pathway enzyme tryptophan 2,3-dioxygenase is increased in the frontal cortex of individuals with schizophrenia
    • Miller C.L., Llenos I.C., Dulay J.R., Barillo M.M., Yolken R.H., and Weis S. Expression of the kynurenine pathway enzyme tryptophan 2,3-dioxygenase is increased in the frontal cortex of individuals with schizophrenia. Neurobiol. Dis. 15 3 (2004) 618-629
    • (2004) Neurobiol. Dis. , vol.15 , Issue.3 , pp. 618-629
    • Miller, C.L.1    Llenos, I.C.2    Dulay, J.R.3    Barillo, M.M.4    Yolken, R.H.5    Weis, S.6
  • 27
    • 33644963618 scopus 로고    scopus 로고
    • Upregulation of the initiating step of the kynurenine pathway in postmortem anterior cingulate cortex from individuals with schizophrenia and bipolar disorder
    • Miller C.L., Llenos I.C., Dulay J.R., and Weis S. Upregulation of the initiating step of the kynurenine pathway in postmortem anterior cingulate cortex from individuals with schizophrenia and bipolar disorder. Brain Res. 1073-1074 (2006) 25-37
    • (2006) Brain Res. , vol.1073-1074 , pp. 25-37
    • Miller, C.L.1    Llenos, I.C.2    Dulay, J.R.3    Weis, S.4
  • 28
    • 34548772356 scopus 로고    scopus 로고
    • Schizophrenia as an inflammation-mediated dysbalance of glutamatergic neurotransmission
    • Muller N., and Schwarz M. Schizophrenia as an inflammation-mediated dysbalance of glutamatergic neurotransmission. Neurotox. Res. 10 2 (2006) 131-148
    • (2006) Neurotox. Res. , vol.10 , Issue.2 , pp. 131-148
    • Muller, N.1    Schwarz, M.2
  • 30
    • 0022503270 scopus 로고
    • Characterization of an indoleamine 2,3-dioxygenase induced by gamma-interferon in cultured human fibroblasts
    • Pfefferkorn E.R., Rebhun S., and Eckel M. Characterization of an indoleamine 2,3-dioxygenase induced by gamma-interferon in cultured human fibroblasts. J. Interferon Res. 6 (1986) 267-279
    • (1986) J. Interferon Res. , vol.6 , pp. 267-279
    • Pfefferkorn, E.R.1    Rebhun, S.2    Eckel, M.3
  • 32
    • 0025651921 scopus 로고
    • Serum amino acids, central monoamines, and hormones in drug-naive, drug-free, and neuroleptic-treated schizophrenic patients and healthy subjects. 1
    • Rao M.L., Gross G., Strebel B., Braunig P., Huber G., and Klosterkotter J. Serum amino acids, central monoamines, and hormones in drug-naive, drug-free, and neuroleptic-treated schizophrenic patients and healthy subjects. 1. Psychiatry Res. 34 3 (1990) 243-257
    • (1990) Psychiatry Res. , vol.34 , Issue.3 , pp. 243-257
    • Rao, M.L.1    Gross, G.2    Strebel, B.3    Braunig, P.4    Huber, G.5    Klosterkotter, J.6
  • 33
    • 0033755158 scopus 로고    scopus 로고
    • Tryptophan and tyrosine catabolic pattern in neuropsychiatric disorders
    • Ravikumar A., Deepadevi K.V., Arun P., Manojkumar V., and Kurup P.A. Tryptophan and tyrosine catabolic pattern in neuropsychiatric disorders. Neurol. India 48 3 (2000) 231-238
    • (2000) Neurol. India , vol.48 , Issue.3 , pp. 231-238
    • Ravikumar, A.1    Deepadevi, K.V.2    Arun, P.3    Manojkumar, V.4    Kurup, P.A.5
  • 34
    • 0030249220 scopus 로고    scopus 로고
    • Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme
    • Ren S., Liu H., Licad E., and Correia M.A. Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Arch. Biochem. Biophys. 333 1 (1996) 96-102
    • (1996) Arch. Biochem. Biophys. , vol.333 , Issue.1 , pp. 96-102
    • Ren, S.1    Liu, H.2    Licad, E.3    Correia, M.A.4
  • 35
    • 0037829279 scopus 로고    scopus 로고
    • Reconstructing eukaryotic NAD metabolism. 1
    • Rongvaux A., Andris F., Van Gool F., and Leo O. Reconstructing eukaryotic NAD metabolism. 1. Bioessays 25 7 (2003) 683-690
    • (2003) Bioessays , vol.25 , Issue.7 , pp. 683-690
    • Rongvaux, A.1    Andris, F.2    Van Gool, F.3    Leo, O.4
  • 38
    • 0030733131 scopus 로고    scopus 로고
    • The role of adrenal hormones in the activation of tryptophan 2,3-dioxygenase by nicotinic acid in rat liver
    • Sainio E.L. The role of adrenal hormones in the activation of tryptophan 2,3-dioxygenase by nicotinic acid in rat liver. Methods Find. Exp. Clin. Pharmacol. 19 7 (1997) 465-470
    • (1997) Methods Find. Exp. Clin. Pharmacol. , vol.19 , Issue.7 , pp. 465-470
    • Sainio, E.L.1
  • 39
    • 0015501720 scopus 로고
    • Purification and properties of rat liver tryptophan oxygenase
    • Schutz G., and Feigelson P. Purification and properties of rat liver tryptophan oxygenase. J. Biol. Chem. 247 17 (1972) 5327-5332
    • (1972) J. Biol. Chem. , vol.247 , Issue.17 , pp. 5327-5332
    • Schutz, G.1    Feigelson, P.2
  • 40
    • 0023764653 scopus 로고
    • Cerebrospinal fluid levels of quinolinic acid in Huntington's disease and schizophrenia
    • Schwarcz R., Tamminga C.A., Kurlan R., and Shoulson I. Cerebrospinal fluid levels of quinolinic acid in Huntington's disease and schizophrenia. Ann. Neurol. 24 4 (1988) 580-582
    • (1988) Ann. Neurol. , vol.24 , Issue.4 , pp. 580-582
    • Schwarcz, R.1    Tamminga, C.A.2    Kurlan, R.3    Shoulson, I.4
  • 42
    • 0042887022 scopus 로고    scopus 로고
    • Micromolar brain levels of kynurenic acid are associated with a disruption of auditory sensory gating in the rat
    • Shepard P.D., Joy B., Clerkin L., and Schwarcz R. Micromolar brain levels of kynurenic acid are associated with a disruption of auditory sensory gating in the rat. Neuropsychopharmacology 28 8 (2003) 1454-1462
    • (2003) Neuropsychopharmacology , vol.28 , Issue.8 , pp. 1454-1462
    • Shepard, P.D.1    Joy, B.2    Clerkin, L.3    Schwarcz, R.4
  • 43
    • 0025954814 scopus 로고
    • Fenton chemistry. Amino acid oxidation
    • Stadtman E.R., and Berlett B.S. Fenton chemistry. Amino acid oxidation. J. Biol. Chem. 266 26 (1991) 17201-17211
    • (1991) J. Biol. Chem. , vol.266 , Issue.26 , pp. 17201-17211
    • Stadtman, E.R.1    Berlett, B.S.2
  • 44
    • 0000773632 scopus 로고
    • Beef liver 3-hydroxyanthranilic acid oxidase
    • Stevens C.O., and Henderson L.M. Beef liver 3-hydroxyanthranilic acid oxidase. J. Biol. Chem. 234 (1959) 1188-1190
    • (1959) J. Biol. Chem. , vol.234 , pp. 1188-1190
    • Stevens, C.O.1    Henderson, L.M.2
  • 45
    • 0027486072 scopus 로고
    • Neuropharmacology of quinolinic and kynurenic acids
    • Stone T.W. Neuropharmacology of quinolinic and kynurenic acids. Pharmacol. Rev. 45 3 (1993) 309-379
    • (1993) Pharmacol. Rev. , vol.45 , Issue.3 , pp. 309-379
    • Stone, T.W.1
  • 46
    • 0037136266 scopus 로고    scopus 로고
    • Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites
    • Terness P., Bauer T.M., Röse L., Dufter C., Watzlik A., Simon H., and Opelz G. Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites. J. Exp. Med. 196 4 (2002) 447-457
    • (2002) J. Exp. Med. , vol.196 , Issue.4 , pp. 447-457
    • Terness, P.1    Bauer, T.M.2    Röse, L.3    Dufter, C.4    Watzlik, A.5    Simon, H.6    Opelz, G.7
  • 47
    • 0034601620 scopus 로고    scopus 로고
    • The Stanley Foundation brain collection and neuropathology consortium
    • Torrey E.F., Webster M., Knable M., Johnston N., and Yolken R. The Stanley Foundation brain collection and neuropathology consortium. Schizophr. Res. 44 2 (2000) 151-155
    • (2000) Schizophr. Res. , vol.44 , Issue.2 , pp. 151-155
    • Torrey, E.F.1    Webster, M.2    Knable, M.3    Johnston, N.4    Yolken, R.5
  • 49
    • 0026623270 scopus 로고
    • Characteristics of substrates and inhibitors in binding to rat liver l-tryptophan 2,3-dioxygenase: a Fourier transform infrared and kinetic study
    • Uchida K., Usami M., Bandow H., and Harada I. Characteristics of substrates and inhibitors in binding to rat liver l-tryptophan 2,3-dioxygenase: a Fourier transform infrared and kinetic study. Biochim. Biophys. Acta 1121 (1992) 153-159
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 153-159
    • Uchida, K.1    Usami, M.2    Bandow, H.3    Harada, I.4
  • 50
    • 29244464827 scopus 로고    scopus 로고
    • Altered glutathione redox state in schizophrenia
    • Yao J., Leonard S., and Reddy R. Altered glutathione redox state in schizophrenia. Dis. Markers 22 1-2 (2006) 83-93
    • (2006) Dis. Markers , vol.22 , Issue.1-2 , pp. 83-93
    • Yao, J.1    Leonard, S.2    Reddy, R.3


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