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Volumn 67, Issue 3, 2017, Pages 361-372

Effect of water-immersion restraint stress on tryptophan catabolism through the kynurenine pathway in rat tissues

Author keywords

Glucocorticoid; Indoleamine 2,3 Dioxygenase 1; Interferon ; Liver tryptophan catabolism; Tryptophan 2,3 Dioxygenase; Water immersion restraint stress (rats)

Indexed keywords

INDOLEAMINE 2,3 DIOXYGENASE; KYNURENINE; TRYPTOPHAN; TRYPTOPHAN 2,3 DIOXYGENASE;

EID: 84976489030     PISSN: 18806546     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12576-016-0467-y     Document Type: Article
Times cited : (18)

References (51)
  • 1
    • 84855225524 scopus 로고    scopus 로고
    • Kynurenine metabolism in health and disease
    • COI: 1:CAS:528:DC%2BC3MXhtlyqtbbP, PID: 20972599
    • Kolodziej LZ, Paleolog EM, Williams RO (2011) Kynurenine metabolism in health and disease. Amino Acids 41:1173–1183
    • (2011) Amino Acids , vol.41 , pp. 1173-1183
    • Kolodziej, L.Z.1    Paleolog, E.M.2    Williams, R.O.3
  • 2
    • 80155201282 scopus 로고    scopus 로고
    • Changes in kynurenine pathway metabolism in the brain, liver and kidney of aged female Wistar rats
    • COI: 1:CAS:528:DC%2BC3MXhsFaksrfP, PID: 22032336
    • Braidy N, Guilemin GJ, Mansour H, Chan-Ling T, Grant R (2011) Changes in kynurenine pathway metabolism in the brain, liver and kidney of aged female Wistar rats. FEBS J 278:4425–4434
    • (2011) FEBS J , vol.278 , pp. 4425-4434
    • Braidy, N.1    Guilemin, G.J.2    Mansour, H.3    Chan-Ling, T.4    Grant, R.5
  • 3
    • 84862789890 scopus 로고    scopus 로고
    • Effects of indoleamine 2,3-dioxygenases in carbon tetrachloride-induced hepatitis model of rats
    • COI: 1:CAS:528:DC%2BC38XotVOmu7s%3D, PID: 22249930
    • Li D, Cai H, Hou M, Fu D, Ma Y, Luo Q, Yuan X, Lv M, Zhang X, Cong X, Lv Z (2012) Effects of indoleamine 2,3-dioxygenases in carbon tetrachloride-induced hepatitis model of rats. Cell Biochem Funct 30:309–314
    • (2012) Cell Biochem Funct , vol.30 , pp. 309-314
    • Li, D.1    Cai, H.2    Hou, M.3    Fu, D.4    Ma, Y.5    Luo, Q.6    Yuan, X.7    Lv, M.8    Zhang, X.9    Cong, X.10    Lv, Z.11
  • 4
    • 84899682630 scopus 로고    scopus 로고
    • Effect of gold nanoparticles on superoxide dismutase and indoleamine 2,3-dioxygenase in various rat tissues
    • COI: 1:CAS:528:DC%2BC2cXhvFGnur7L, PID: 24980020
    • Siddiqi NJ (2014) Effect of gold nanoparticles on superoxide dismutase and indoleamine 2,3-dioxygenase in various rat tissues. Indian J Biochem Biophys 51:156–159
    • (2014) Indian J Biochem Biophys , vol.51 , pp. 156-159
    • Siddiqi, N.J.1
  • 5
    • 74049090874 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase tissue distribution and cellular localization in mice: implications for its biological functions
    • COI: 1:CAS:528:DC%2BD1MXhs1WhurzK, PID: 19741271
    • Dai X, Zhu BT (2010) Indoleamine 2,3-dioxygenase tissue distribution and cellular localization in mice: implications for its biological functions. J Histochem Cytochem 58:17–28
    • (2010) J Histochem Cytochem , vol.58 , pp. 17-28
    • Dai, X.1    Zhu, B.T.2
  • 6
    • 0016230011 scopus 로고
    • Cellular tryptophan 2,3-dioxygenase (pyrrolase) and its induction in rat brain
    • PID: 4407106
    • Gál E (1974) Cellular tryptophan 2,3-dioxygenase (pyrrolase) and its induction in rat brain. J Neurochem 22:861–863
    • (1974) J Neurochem , vol.22 , pp. 861-863
    • Gál, E.1
  • 7
    • 0027467907 scopus 로고
    • Identification of tryptophan 2,3-dioxygenase RNA in rodent brain
    • COI: 1:CAS:528:DyaK3sXhvVygs7k%3D, PID: 7679723
    • Haber R, Besstte D, Hulihan-Giblin B, Durcan MJ, Goldman D (1993) Identification of tryptophan 2,3-dioxygenase RNA in rodent brain. J Neurochem 60:1159–1162
    • (1993) J Neurochem , vol.60 , pp. 1159-1162
    • Haber, R.1    Besstte, D.2    Hulihan-Giblin, B.3    Durcan, M.J.4    Goldman, D.5
  • 8
    • 64249089979 scopus 로고    scopus 로고
    • Identification and characterization of novel variants of tryptophan 2.3-dioxygenase gene: differential regulation in the mouse nervous system during development
    • COI: 1:CAS:528:DC%2BD1MXkslOqtr0%3D, PID: 19428689
    • Kanai M, Nakamura T, Funakoshi H (2009) Identification and characterization of novel variants of tryptophan 2.3-dioxygenase gene: differential regulation in the mouse nervous system during development. Neurosci Res 64:111–117
    • (2009) Neurosci Res , vol.64 , pp. 111-117
    • Kanai, M.1    Nakamura, T.2    Funakoshi, H.3
  • 9
    • 28044461358 scopus 로고
    • Effect of stress and psychotropic drugs on rat liver tryptophan dioxygenase
    • COI: 1:CAS:528:DyaF2MXktVGqsr4%3D, PID: 14301527
    • Nomura J (1965) Effect of stress and psychotropic drugs on rat liver tryptophan dioxygenase. Endocrinology 76:1190–1194
    • (1965) Endocrinology , vol.76 , pp. 1190-1194
    • Nomura, J.1
  • 10
    • 0016687294 scopus 로고
    • Adrenal hormones and increase of liver tyrosine aminotransferase and tryptophan pyrrolase activity after immobilization in rats
    • PID: 236170
    • Németh Š, Vigaš M (1975) Adrenal hormones and increase of liver tyrosine aminotransferase and tryptophan pyrrolase activity after immobilization in rats. Endocrinol Exp 9:100–104
    • (1975) Endocrinol Exp , vol.9 , pp. 100-104
    • Németh, Š.1    Vigaš, M.2
  • 11
    • 0016652144 scopus 로고
    • Nature of induction of tryptophan pyrrolase in cold exposure
    • Sitaraman V, Ramasarma T (1975) Nature of induction of tryptophan pyrrolase in cold exposure. J Appl Physiol 58:245–249
    • (1975) J Appl Physiol , vol.58 , pp. 245-249
    • Sitaraman, V.1    Ramasarma, T.2
  • 12
    • 0017610004 scopus 로고
    • The effect of stress on the activity of hepatic tryptophan pyrrolase, of tyrosine aminotransferase in various organs and on the level of tryptophan in the liver and plasma of rats
    • Németh Š (1977) The effect of stress on the activity of hepatic tryptophan pyrrolase, of tyrosine aminotransferase in various organs and on the level of tryptophan in the liver and plasma of rats. Physiol Biochem 26:557–563
    • (1977) Physiol Biochem , vol.26 , pp. 557-563
    • Németh, Š.1
  • 13
    • 84899995144 scopus 로고    scopus 로고
    • Inhibition of stress-induced hepatic tryptophan 2,3-dioxygenase exhibits anti-depressant activity in an animal model of depressive behavior
    • COI: 1:CAS:528:DC%2BC2cXntFOnsLw%3D, PID: 24472498
    • Gibney SM, Fagan EM, Waldron A-M, O’Byrne J, Connor TJ, Harkin A (2014) Inhibition of stress-induced hepatic tryptophan 2,3-dioxygenase exhibits anti-depressant activity in an animal model of depressive behavior. Int J Neuropsychopharmacol 17:917–928
    • (2014) Int J Neuropsychopharmacol , vol.17 , pp. 917-928
    • Gibney, S.M.1    Fagan, E.M.2    Waldron, A.-M.3    O’Byrne, J.4    Connor, T.J.5    Harkin, A.6
  • 14
    • 0016767545 scopus 로고
    • Control of the mRNA for hepatic tryptophan oxygenase during hormonal and substrate induction
    • COI: 1:CAS:528:DyaE2MXktVWjsLg%3D, PID: 1055360
    • Schutz G, Killewich L, Chen G, Feigelson P (1975) Control of the mRNA for hepatic tryptophan oxygenase during hormonal and substrate induction. Proc Natl Acad Sci USA 72:1017–1020
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1017-1020
    • Schutz, G.1    Killewich, L.2    Chen, G.3    Feigelson, P.4
  • 15
    • 0020641702 scopus 로고
    • Transcriptional regulation of the tryptophan oxygenase gene in rat liver by glucocorticoids
    • COI: 1:CAS:528:DyaL3sXktVSks78%3D, PID: 6187742
    • Danesch U, Hashimoto S, Renkawitz R, Schütz G (1983) Transcriptional regulation of the tryptophan oxygenase gene in rat liver by glucocorticoids. J Biol Chem 258:4750–4753
    • (1983) J Biol Chem , vol.258 , pp. 4750-4753
    • Danesch, U.1    Hashimoto, S.2    Renkawitz, R.3    Schütz, G.4
  • 16
    • 0348141449 scopus 로고
    • Glucocorticoid induction of the rat tryptophan oxygenase gene us mediated by two widely separated glucocorticoid-responsive elements
    • Danesch U, Gloss B, Schmid W, Schütz G, Schüle R, Renkawitz R (1991) Glucocorticoid induction of the rat tryptophan oxygenase gene us mediated by two widely separated glucocorticoid-responsive elements. EMBO J 6:625–630
    • (1991) EMBO J , vol.6 , pp. 625-630
    • Danesch, U.1    Gloss, B.2    Schmid, W.3    Schütz, G.4    Schüle, R.5    Renkawitz, R.6
  • 17
    • 0025944659 scopus 로고
    • Relationship between interferon-γ, indoleamine 2,3-dioxygenase, and tryptophan catabolism
    • COI: 1:CAS:528:DyaK3MXltlentbs%3D, PID: 1907934
    • Taylor MW, Feng G (1991) Relationship between interferon-γ, indoleamine 2,3-dioxygenase, and tryptophan catabolism. FASEB J 5:2516–2522
    • (1991) FASEB J , vol.5 , pp. 2516-2522
    • Taylor, M.W.1    Feng, G.2
  • 18
    • 34748911754 scopus 로고    scopus 로고
    • Molecules in focus: indoleamine 2,3-dioxygenase
    • COI: 1:CAS:528:DC%2BD2sXhtFWgsL%2FL, PID: 17320464
    • King NJC, Thomas SR (2007) Molecules in focus: indoleamine 2,3-dioxygenase. Int J Biochem Cell Biol 39:2167–2172
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 2167-2172
    • King, N.J.C.1    Thomas, S.R.2
  • 19
    • 84882633181 scopus 로고    scopus 로고
    • Species and cell type differences in tryptophan metabolism
    • COI: 1:CAS:528:DC%2BC3sXhsV2gs7zJ, PID: 23922502
    • Murakami Y, Saito K (2013) Species and cell type differences in tryptophan metabolism. Int J Tryptophan Res 6[Suppl 1]:47–54
    • (2013) Int J Tryptophan Res , vol.6 , pp. 47-54
    • Murakami, Y.1    Saito, K.2
  • 20
    • 84942852484 scopus 로고    scopus 로고
    • Role of indoleamine 2,3-dioxygenase in health and disease
    • COI: 1:CAS:528:DC%2BC2MXhslKqtLnN, PID: 26186743
    • Yeung AW, Terentis AC, King NJ, Thomas SR (2015) Role of indoleamine 2,3-dioxygenase in health and disease. Clin Sci 129:601–672
    • (2015) Clin Sci , vol.129 , pp. 601-672
    • Yeung, A.W.1    Terentis, A.C.2    King, N.J.3    Thomas, S.R.4
  • 21
    • 77955648350 scopus 로고    scopus 로고
    • Psychological stress-induced, IDO1-dependent tryptophan catabolism: implications on immunosuppression in mice and humans
    • PID: 20689575
    • Kiank C, Zeden J-P, Drude S, Domanska G, Fusch G, Otten W, Schuett C (2010) Psychological stress-induced, IDO1-dependent tryptophan catabolism: implications on immunosuppression in mice and humans. PLoS One 5(7):e11825. doi:10.1371/journal.pone.001185
    • (2010) PLoS One , vol.5 , Issue.7
    • Kiank, C.1    Zeden, J.-P.2    Drude, S.3    Domanska, G.4    Fusch, G.5    Otten, W.6    Schuett, C.7
  • 22
    • 0035211318 scopus 로고    scopus 로고
    • Mechanisms and roles of neutrophil infiltration in stress-induced gastric injury in rats
    • COI: 1:CAS:528:DC%2BD38XltVKmug%3D%3D, PID: 11768264
    • Hamaguchi M, Watanabe T, Higuchi H, Tominaga K, Fujiwara Y, Arakawa T (2001) Mechanisms and roles of neutrophil infiltration in stress-induced gastric injury in rats. Dig Dis Sci 46:2708–2715
    • (2001) Dig Dis Sci , vol.46 , pp. 2708-2715
    • Hamaguchi, M.1    Watanabe, T.2    Higuchi, H.3    Tominaga, K.4    Fujiwara, Y.5    Arakawa, T.6
  • 23
    • 0038150572 scopus 로고    scopus 로고
    • Implication of reactive oxygen species and cytokines in gastroprotection against stress-induced gastric damage by nitric oxide releasing aspirin
    • PID: 12774247
    • Brzozowski T, Konturek PC, Konturek SJ, Kwiecień S, Sliwowski Z, Pajdo R, Duda A, Ptak A (2003) Implication of reactive oxygen species and cytokines in gastroprotection against stress-induced gastric damage by nitric oxide releasing aspirin. Int J Colorectal Dis 18:320–329
    • (2003) Int J Colorectal Dis , vol.18 , pp. 320-329
    • Brzozowski, T.1    Konturek, P.C.2    Konturek, S.J.3    Kwiecień, S.4    Sliwowski, Z.5    Pajdo, R.6    Duda, A.7    Ptak, A.8
  • 24
    • 34249302795 scopus 로고    scopus 로고
    • Sustained activation of nuclear factor-κB by reactive oxygen species is involved in the pathogenesis of stress-induced gastric damage in rats
    • COI: 1:CAS:528:DC%2BD2sXls1GqsbY%3D, PID: 17452936
    • Jia Y-T, Ma B, Wei W, Xu Y, Wang Y, Tang H-T, Xia Z-F (2007) Sustained activation of nuclear factor-κB by reactive oxygen species is involved in the pathogenesis of stress-induced gastric damage in rats. Crit Care Med 35:1582–1591
    • (2007) Crit Care Med , vol.35 , pp. 1582-1591
    • Jia, Y.-T.1    Ma, B.2    Wei, W.3    Xu, Y.4    Wang, Y.5    Tang, H.-T.6    Xia, Z.-F.7
  • 25
    • 38849184654 scopus 로고    scopus 로고
    • Activation of p38 MARK by reactive oxygen species is essential in a rat model of stress-induced gastric mucosal injury
    • COI: 1:CAS:528:DC%2BD2sXhtlajt7jE, PID: 18025227
    • Jia Y-T, Wei W, Ma B, Xu Y, Liu W-J, Wang Y, Lv K-Y, Tang H-T, Wei D, Xia Z-F (2007) Activation of p38 MARK by reactive oxygen species is essential in a rat model of stress-induced gastric mucosal injury. J Immunol 179:7808–7819
    • (2007) J Immunol , vol.179 , pp. 7808-7819
    • Jia, Y.-T.1    Wei, W.2    Ma, B.3    Xu, Y.4    Liu, W.-J.5    Wang, Y.6    Lv, K.-Y.7    Tang, H.-T.8    Wei, D.9    Xia, Z.-F.10
  • 26
    • 0028889379 scopus 로고
    • Changes in the central and peripheral serotonergic system in rats exposed to water-immersion restraint stress and nicotine administration
    • COI: 1:CAS:528:DyaK28XitV2ruw%3D%3D, PID: 8545079
    • Takada Y, Urano T, Ihara H, Takada A (1995) Changes in the central and peripheral serotonergic system in rats exposed to water-immersion restraint stress and nicotine administration. Neurosci Res 23:305–311
    • (1995) Neurosci Res , vol.23 , pp. 305-311
    • Takada, Y.1    Urano, T.2    Ihara, H.3    Takada, A.4
  • 27
    • 0030768072 scopus 로고    scopus 로고
    • Involvement of the xanthine-xanthine oxidase system and neutrophils in the development of acute gastric mucosal lesions in rats water immersion restraint stress
    • COI: 1:CAS:528:DyaK2sXmtFSisLs%3D, PID: 9324161
    • Nishida K, Ohta Y, Kobayashi T, Ishiguro I (1997) Involvement of the xanthine-xanthine oxidase system and neutrophils in the development of acute gastric mucosal lesions in rats water immersion restraint stress. Digestion 58:340–351
    • (1997) Digestion , vol.58 , pp. 340-351
    • Nishida, K.1    Ohta, Y.2    Kobayashi, T.3    Ishiguro, I.4
  • 28
    • 70649114677 scopus 로고    scopus 로고
    • Involvement of oxidative stress in increases in serum levels of various enzymes and components in rats with water-immersion restraint stress
    • PID: 19902027
    • Ohta Y, Kaida S, Chiba S, Tada M, Teruya A, Imai Y, Kawanishi M (2009) Involvement of oxidative stress in increases in serum levels of various enzymes and components in rats with water-immersion restraint stress. J Clin Biochem Nutr 45:347–354
    • (2009) J Clin Biochem Nutr , vol.45 , pp. 347-354
    • Ohta, Y.1    Kaida, S.2    Chiba, S.3    Tada, M.4    Teruya, A.5    Imai, Y.6    Kawanishi, M.7
  • 29
    • 84865959869 scopus 로고    scopus 로고
    • Disruption of non-enzymatic antioxidant defense systems in the brain of rats with water-immersion restraint stress
    • Ohta Y, Yashiro K, Ohashi K, Imai Y (2012) Disruption of non-enzymatic antioxidant defense systems in the brain of rats with water-immersion restraint stress. J Clin Biochem Nutr 51:36–42
    • (2012) J Clin Biochem Nutr , vol.51 , pp. 36-42
    • Ohta, Y.1    Yashiro, K.2    Ohashi, K.3    Imai, Y.4
  • 30
    • 84876078902 scopus 로고    scopus 로고
    • Water-immersion restraint stress disrupts nonenzymatic antioxidant defense systems through rapid and continuous ascorbic acid depletion in the adrenal gland
    • COI: 1:CAS:528:DC%2BC3sXhtVGiurfJ, PID: 22987339
    • Ohta Y, Yashiro K, Kiada S, Imai Y, Ohashi K, Kitagawa A (2013) Water-immersion restraint stress disrupts nonenzymatic antioxidant defense systems through rapid and continuous ascorbic acid depletion in the adrenal gland. Cell Biochem Funct 31:254–262
    • (2013) Cell Biochem Funct , vol.31 , pp. 254-262
    • Ohta, Y.1    Yashiro, K.2    Kiada, S.3    Imai, Y.4    Ohashi, K.5    Kitagawa, A.6
  • 31
    • 43749097853 scopus 로고    scopus 로고
    • Protection of stress-induced impairment of hippocampal/prefrontal LTP through blockade of glucocorticoid receptors. Implication of MEK signaling
    • Mailliet F, Qi H, Rocher C, Spending M, Svenningsson P, Jay TM (2008) Protection of stress-induced impairment of hippocampal/prefrontal LTP through blockade of glucocorticoid receptors. Implication of MEK signaling. Exp Neurol 21:593–596
    • (2008) Exp Neurol , vol.21 , pp. 593-596
    • Mailliet, F.1    Qi, H.2    Rocher, C.3    Spending, M.4    Svenningsson, P.5    Jay, T.M.6
  • 32
    • 0000112052 scopus 로고
    • Fluorometric measurement of rat plasma and adrenal corticosterone. A note on technical details
    • COI: 1:CAS:528:DyaG1MXpsFWgtQ%3D%3D, PID: 13654928
    • Guillemin R, Clayton GW, Lipscomb HS, Smith JD (1959) Fluorometric measurement of rat plasma and adrenal corticosterone. A note on technical details. J Lab Clin Med 53:830–832
    • (1959) J Lab Clin Med , vol.53 , pp. 830-832
    • Guillemin, R.1    Clayton, G.W.2    Lipscomb, H.S.3    Smith, J.D.4
  • 33
    • 0032532675 scopus 로고    scopus 로고
    • Species differences in l-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes
    • COI: 1:CAS:528:DyaK1cXmslyksLo%3D, PID: 9784247
    • Fujigaki S, Saito K, Takemura M, Fujii H, Wasa H, Noma A, Seishima M (1998) Species differences in l-tryptophan-kynurenine pathway metabolism: quantification of anthranilic acid and its related enzymes. Arch Biochem Biophys 358:329–335
    • (1998) Arch Biochem Biophys , vol.358 , pp. 329-335
    • Fujigaki, S.1    Saito, K.2    Takemura, M.3    Fujii, H.4    Wasa, H.5    Noma, A.6    Seishima, M.7
  • 34
    • 0036156098 scopus 로고    scopus 로고
    • l-Tryptophan-l-kynurenine pathway metabolism accelerated by toxoplasma gondii infection is abolished in gamma interferon-gene-deficient mice: cross-regulation between inducible nitric oxide synthase and indoleamine 2,3-dioxygenase
    • COI: 1:CAS:528:DC%2BD38XoslyjtA%3D%3D, PID: 11796611
    • Fujigaki S, Saito K, Takemura M, Maekawa N, Yamada Y, Wasa H, Seishima M (2002) l-Tryptophan-l-kynurenine pathway metabolism accelerated by toxoplasma gondii infection is abolished in gamma interferon-gene-deficient mice: cross-regulation between inducible nitric oxide synthase and indoleamine 2,3-dioxygenase. Infect Immun 70:779–786
    • (2002) Infect Immun , vol.70 , pp. 779-786
    • Fujigaki, S.1    Saito, K.2    Takemura, M.3    Maekawa, N.4    Yamada, Y.5    Wasa, H.6    Seishima, M.7
  • 35
    • 84944887314 scopus 로고    scopus 로고
    • Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable
    • COI: 1:CAS:528:DC%2BC2MXosFOisb0%3D, PID: 25950090
    • Yuasa HJ, Mizuno K, Ball HJ (2015) Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable. FEBS J 282:2735–2745
    • (2015) FEBS J , vol.282 , pp. 2735-2745
    • Yuasa, H.J.1    Mizuno, K.2    Ball, H.J.3
  • 36
    • 58149308592 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase-2: a new enzyme in the kynurenine pathway
    • COI: 1:CAS:528:DC%2BD1MXns1OrsQ%3D%3D
    • Ball HJ, Yuasa HJ, Austin CJD, Weiser S, Hunt NH (2009) Indoleamine 2,3-dioxygenase-2: a new enzyme in the kynurenine pathway. Int J Biochem Cell 41:467–471
    • (2009) Int J Biochem Cell , vol.41 , pp. 467-471
    • Ball, H.J.1    Yuasa, H.J.2    Austin, C.J.D.3    Weiser, S.4    Hunt, N.H.5
  • 37
    • 84872015298 scopus 로고    scopus 로고
    • Studies on tissue and cellular distribution of indoleamine 2,3-dioxygenase 2: the absence of IDO1 upregulates IDO2 expression in the epididymis
    • PID: 22895526
    • Fukunaga M, Yamamoto Y, Kawasoe M, Arioka Y, Murakami Y, Hoshi M, Saito K (2012) Studies on tissue and cellular distribution of indoleamine 2,3-dioxygenase 2: the absence of IDO1 upregulates IDO2 expression in the epididymis. J Histochem Cytochem 60:854–960
    • (2012) J Histochem Cytochem , vol.60 , pp. 854-960
    • Fukunaga, M.1    Yamamoto, Y.2    Kawasoe, M.3    Arioka, Y.4    Murakami, Y.5    Hoshi, M.6    Saito, K.7
  • 38
    • 0015379893 scopus 로고
    • Human tryptophan and tyrosine metabolism: effects of acute exposure to cold stress
    • Fracesconi RP, Boyd AE III, Mager M (1972) Human tryptophan and tyrosine metabolism: effects of acute exposure to cold stress. J Appl Physiol 33:165–169
    • (1972) J Appl Physiol , vol.33 , pp. 165-169
    • Fracesconi, R.P.1    Boyd, A.E.2    Mager, M.3
  • 39
    • 0036825363 scopus 로고    scopus 로고
    • Effects of stress on the urinary excretory pattern of niacin catabolites, the most reliable index of niacin status, in humans
    • COI: 1:CAS:528:DC%2BD3sXnvFKgsg%3D%3D, PID: 12656218
    • Okamoto H, Ishikawa A, Nishimuta M, Kodama N, Yoshitake Y, Furwatari T, Shibata K (2002) Effects of stress on the urinary excretory pattern of niacin catabolites, the most reliable index of niacin status, in humans. J Nutr Sci Vitaminol 48:417–419
    • (2002) J Nutr Sci Vitaminol , vol.48 , pp. 417-419
    • Okamoto, H.1    Ishikawa, A.2    Nishimuta, M.3    Kodama, N.4    Yoshitake, Y.5    Furwatari, T.6    Shibata, K.7
  • 40
    • 0025117365 scopus 로고
    • Relationship between l-tryptophan uptake and l-tryptophan 2.3-dioxygenase activity in rat hepatocytes
    • COI: 1:CAS:528:DyaK3cXhtFKht7c%3D, PID: 2328025
    • Saito K, Ohta Y, Nagamura Y, Sasaki E, Ishiguro I (1990) Relationship between l-tryptophan uptake and l-tryptophan 2.3-dioxygenase activity in rat hepatocytes. Biochem Int 20:71–80
    • (1990) Biochem Int , vol.20 , pp. 71-80
    • Saito, K.1    Ohta, Y.2    Nagamura, Y.3    Sasaki, E.4    Ishiguro, I.5
  • 41
    • 0034055490 scopus 로고    scopus 로고
    • Serotonegic and kynurenic pathways in rats exposed to foot shock
    • Pawlfak D, Takada Y, Urano T, Takada A (2000) Serotonegic and kynurenic pathways in rats exposed to foot shock. Brain Res Bull 52:197–205
    • (2000) Brain Res Bull , vol.52 , pp. 197-205
    • Pawlfak, D.1    Takada, Y.2    Urano, T.3    Takada, A.4
  • 42
    • 0019845879 scopus 로고
    • Mechanism of decline in rat brain 5-hydrozytryptamine after induction of liver tryptophan pyrrolase by hydrocortisone: roles of tryptophan catabolism and kynurenine synthesis
    • COI: 1:CAS:528:DyaL38XhtFKisLk%3D, PID: 7296169
    • Young SN (1981) Mechanism of decline in rat brain 5-hydrozytryptamine after induction of liver tryptophan pyrrolase by hydrocortisone: roles of tryptophan catabolism and kynurenine synthesis. Br J Pharmacol 74:695–700
    • (1981) Br J Pharmacol , vol.74 , pp. 695-700
    • Young, S.N.1
  • 43
    • 0017911444 scopus 로고
    • Studies on the glucocorticoid receptor and the hormonal modulation of the mRNA for tryptophan oxygenase
    • COI: 1:CAS:528:DyaE1MXhs1agsL4%3D, PID: 205117
    • Ramanarayanan-Murthy L, Colman PD, Feigelson P (1978) Studies on the glucocorticoid receptor and the hormonal modulation of the mRNA for tryptophan oxygenase. Adv Exp Med Biol 96:73–107
    • (1978) Adv Exp Med Biol , vol.96 , pp. 73-107
    • Ramanarayanan-Murthy, L.1    Colman, P.D.2    Feigelson, P.3
  • 44
    • 0022377081 scopus 로고
    • A new glucocorticoid receptor species: relation to induction of tryptophan dioxygenase by glucocorticoid
    • COI: 1:CAS:528:DyaL2MXmtVKru7Y%3D, PID: 2864234
    • Hirota T, Hirota K, Sanno Y, Tanaka T (1985) A new glucocorticoid receptor species: relation to induction of tryptophan dioxygenase by glucocorticoid. Endocrinology 117:1788–1795
    • (1985) Endocrinology , vol.117 , pp. 1788-1795
    • Hirota, T.1    Hirota, K.2    Sanno, Y.3    Tanaka, T.4
  • 45
    • 84953358488 scopus 로고    scopus 로고
    • Glucocorticoids and stress-induced changes in the expression of PERIOD1 in the rat forebrain
    • PID: 26075608
    • Al-Safadi S, Branchaud M, Rutherford S, Amir S (2015) Glucocorticoids and stress-induced changes in the expression of PERIOD1 in the rat forebrain. PLoS One 10(6):e0130085. doi:10.1371/journal.pone.0130085
    • (2015) PLoS One , vol.10 , Issue.6
    • Al-Safadi, S.1    Branchaud, M.2    Rutherford, S.3    Amir, S.4
  • 46
    • 78449247275 scopus 로고    scopus 로고
    • The regulation of blood glucose level in physical and emotional stress models: possible involvement of adrenergic and glucocorticoid systems
    • COI: 1:CAS:528:DC%2BC3cXhtlOqtr%2FF, PID: 21052944
    • Sim Y-B, Park S-H, Kang Y-J, Kim S-M, Lee J-K, Jung J-S, Suh H-W (2010) The regulation of blood glucose level in physical and emotional stress models: possible involvement of adrenergic and glucocorticoid systems. Arch Pharm Res 33:1679–1683
    • (2010) Arch Pharm Res , vol.33 , pp. 1679-1683
    • Sim, Y.-B.1    Park, S.-H.2    Kang, Y.-J.3    Kim, S.-M.4    Lee, J.-K.5    Jung, J.-S.6    Suh, H.-W.7
  • 47
    • 0032067762 scopus 로고    scopus 로고
    • Mifepristone (RU 486). Current knowledge and future prospects
    • Jeffrey R, Plescia MG, Anastasio GD (1998) Mifepristone (RU 486). Current knowledge and future prospects. Arch Fam Med 7:219–222
    • (1998) Arch Fam Med , vol.7 , pp. 219-222
    • Jeffrey, R.1    Plescia, M.G.2    Anastasio, G.D.3
  • 48
    • 15544368594 scopus 로고    scopus 로고
    • Endocrinology of the stress response
    • COI: 1:CAS:528:DC%2BD2MXjsFelu7c%3D, PID: 15709959
    • Charmandari E, Tsigos C, Chrousos G (2005) Endocrinology of the stress response. Annu Rev Physiol 67:259–284
    • (2005) Annu Rev Physiol , vol.67 , pp. 259-284
    • Charmandari, E.1    Tsigos, C.2    Chrousos, G.3
  • 49
    • 0030906093 scopus 로고    scopus 로고
    • Stress increases plasma enzyme activity in rats: differential effects of adrenergic and cholinergic blockers
    • COI: 1:CAS:528:DyaK2sXhvF2mtLc%3D, PID: 9067316
    • Arakawa H, Kodama H, Matsuoka N, Yamaguchi I (1997) Stress increases plasma enzyme activity in rats: differential effects of adrenergic and cholinergic blockers. J Pharmacol Exp Ther 280:1296–1303
    • (1997) J Pharmacol Exp Ther , vol.280 , pp. 1296-1303
    • Arakawa, H.1    Kodama, H.2    Matsuoka, N.3    Yamaguchi, I.4
  • 50
    • 0027312471 scopus 로고
    • Glucoregulatory hormones in the immobilization stress-induced increase in plasma glucose in fasted and fed rats
    • COI: 1:CAS:528:DyaK3sXkt1WitLg%3D, PID: 8477665
    • Yamada F, Inoue S, Saitoh T, Tanaka K (1993) Glucoregulatory hormones in the immobilization stress-induced increase in plasma glucose in fasted and fed rats. Endocrinology 132:2199–2205
    • (1993) Endocrinology , vol.132 , pp. 2199-2205
    • Yamada, F.1    Inoue, S.2    Saitoh, T.3    Tanaka, K.4
  • 51
    • 0036307544 scopus 로고    scopus 로고
    • Stress hormones, proinflammatory and antiinflammatory cytokines, and autoimmunity
    • COI: 1:CAS:528:DC%2BD38XlvVWmur0%3D, PID: 12114286
    • Elenkov IJ, Chroudsos GF (2002) Stress hormones, proinflammatory and antiinflammatory cytokines, and autoimmunity. Ann NY Acad Sci 966:290–303
    • (2002) Ann NY Acad Sci , vol.966 , pp. 290-303
    • Elenkov, I.J.1    Chroudsos, G.F.2


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