메뉴 건너뛰기




Volumn 105, Issue 4, 2005, Pages 1574-1581

Regulation of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA-synthetase by CTLA-4-Fc in human CD4+ T cells

Author keywords

[No Author keywords available]

Indexed keywords

CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; INDOLEAMINE 2,3 DIOXYGENASE; PHYTOHEMAGGLUTININ; TRYPTOPHAN; TRYPTOPHAN TRANSFER RNA LIGASE;

EID: 13544271675     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2004-06-2089     Document Type: Article
Times cited : (161)

References (53)
  • 1
    • 0000273861 scopus 로고
    • Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: Its possible occurrence in cancer patients
    • Yasui H, Takai K, Yoshida R, Hayaishi O. Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients. Proc Natl Acad Sci USA. 1986;83:6622-6626.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6622-6626
    • Yasui, H.1    Takai, K.2    Yoshida, R.3    Hayaishi, O.4
  • 3
    • 0022512370 scopus 로고
    • Interferon: A mediator of indoleamine 2,3-dioxygenase induction by lipopolysaccharide, poly(l) X poly(C), and pokeweed mitogen in mouse lung
    • Yoshida R, Oku T, Imanishi J, Kishida T, Hayaishi O. Interferon: a mediator of indoleamine 2,3-dioxygenase induction by lipopolysaccharide, poly(l) X poly(C), and pokeweed mitogen in mouse lung. Arch Biochem Biophys. 1986;249:596-604.
    • (1986) Arch Biochem Biophys , vol.249 , pp. 596-604
    • Yoshida, R.1    Oku, T.2    Imanishi, J.3    Kishida, T.4    Hayaishi, O.5
  • 4
    • 0028951169 scopus 로고
    • Differential regulation of the human, interferon inducible tryptophanyl-tRNA synthetase by various cytokines in cell lines
    • Fleckner J, Martensen PM, Tolstrup AB, Kjeldgaard NO, Justesen J. Differential regulation of the human, interferon inducible tryptophanyl-tRNA synthetase by various cytokines in cell lines. Cytokine. 1995;7:70-77.
    • (1995) Cytokine , vol.7 , pp. 70-77
    • Fleckner, J.1    Martensen, P.M.2    Tolstrup, A.B.3    Kjeldgaard, N.O.4    Justesen, J.5
  • 5
    • 0027289072 scopus 로고
    • The human gene encoding tryptophanyl-tRNA synthetase: Interferon-response elements and exon-intron organization
    • Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL. The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. Gene. 1993;128:237-245.
    • (1993) Gene , vol.128 , pp. 237-245
    • Frolova, L.Y.1    Grigorieva, A.Y.2    Sudomoina, M.A.3    Kisselev, L.L.4
  • 6
    • 0026343599 scopus 로고
    • Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts
    • Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP. Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. J Biol Chem. 1991;266:24245-24248.
    • (1991) J Biol Chem , vol.266 , pp. 24245-24248
    • Rubin, B.Y.1    Anderson, S.L.2    Xing, L.3    Powell, R.J.4    Tate, W.P.5
  • 7
    • 0027228185 scopus 로고
    • The gene encoding IFP 53/tryptophanyl-tRN A synthetase is regulated by the gamma-interferon activation factor
    • Strehlow I, Seegert D, Frick C, et al. The gene encoding IFP 53/tryptophanyl-tRN A synthetase is regulated by the gamma-interferon activation factor. J Biol Chem. 1993;268:16590-16595.
    • (1993) J Biol Chem , vol.268 , pp. 16590-16595
    • Strehlow, I.1    Seegert, D.2    Frick, C.3
  • 8
    • 0028985260 scopus 로고
    • Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-tRNA synthetase includes alternative splicing
    • Tolstrup AB, Bejder A, Fleckner J, Justesen J. Transcriptional regulation of the interferon-gamma-inducible tryptophanyl-tRNA synthetase includes alternative splicing. J Biol Chem. 1995;270:397-403.
    • (1995) J Biol Chem , vol.270 , pp. 397-403
    • Tolstrup, A.B.1    Bejder, A.2    Fleckner, J.3    Justesen, J.4
  • 10
    • 18544364477 scopus 로고    scopus 로고
    • Potential regulatory function of human dendritic cells expressing indoleamine 2,3-dioxygenase
    • Munn DH, Sharma MD, Lee JR, et al. Potential regulatory function of human dendritic cells expressing indoleamine 2,3-dioxygenase. Science. 2002;297:1867-1870.
    • (2002) Science , vol.297 , pp. 1867-1870
    • Munn, D.H.1    Sharma, M.D.2    Lee, J.R.3
  • 11
    • 0042591467 scopus 로고    scopus 로고
    • Cutting edge: Induced indoleamine 2,3 dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion
    • Mellor AL, Baban B, Chandler P, et al. Cutting edge: induced indoleamine 2,3 dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion. J Immunol. 2003;171:1652-1655.
    • (2003) J Immunol , vol.171 , pp. 1652-1655
    • Mellor, A.L.1    Baban, B.2    Chandler, P.3
  • 12
    • 0038215374 scopus 로고    scopus 로고
    • Tolerance, DCs and tryptophan: Much ado about IDO
    • Grohmann U, Fallarino F, Puccetti P. Tolerance, DCs and tryptophan: much ado about IDO. Trends Immunol. 2003;24:242-248.
    • (2003) Trends Immunol , vol.24 , pp. 242-248
    • Grohmann, U.1    Fallarino, F.2    Puccetti, P.3
  • 13
    • 0033215041 scopus 로고    scopus 로고
    • Tryptophan catabolism and T-cell tolerance: Immunosuppression by starvation?
    • Mellor AL, Munn DH. Tryptophan catabolism and T-cell tolerance: immunosuppression by starvation? Immunol Today. 1999;20:469-473.
    • (1999) Immunol Today , vol.20 , pp. 469-473
    • Mellor, A.L.1    Munn, D.H.2
  • 14
    • 0037090313 scopus 로고    scopus 로고
    • Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses
    • Mellor AL, Keskin DB, Johnson T, Chandler P, Munn DH. Cells expressing indoleamine 2,3-dioxygenase inhibit T cell responses. J Immunol. 2002;168:3771-3776.
    • (2002) J Immunol , vol.168 , pp. 3771-3776
    • Mellor, A.L.1    Keskin, D.B.2    Johnson, T.3    Chandler, P.4    Munn, D.H.5
  • 15
    • 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 TM, Rose L, et al. Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites. J Exp Med. 2002;196:447-457.
    • (2002) J Exp Med , vol.196 , pp. 447-457
    • Terness, P.1    Bauer, T.M.2    Rose, L.3
  • 16
    • 0036884130 scopus 로고    scopus 로고
    • Tryptophan deprivation sensitizes activated T cells to apoptosis prior to cell division
    • Lee GK, Park HJ, Macleod M, Chandler P, Munn DH, Mellor AL. Tryptophan deprivation sensitizes activated T cells to apoptosis prior to cell division. Immunology. 2002;107:452-460.
    • (2002) Immunology , vol.107 , pp. 452-460
    • Lee, G.K.1    Park, H.J.2    Macleod, M.3    Chandler, P.4    Munn, D.H.5    Mellor, A.L.6
  • 17
    • 0036790338 scopus 로고    scopus 로고
    • T cell apoptosis by tryptophan catabolism
    • Fallarino F, Grohmann U, Vacca C, et al. T cell apoptosis by tryptophan catabolism. Cell Death Differ, 2002;9:1069-1077.
    • (2002) Cell Death Differ , vol.9 , pp. 1069-1077
    • Fallarino, F.1    Grohmann, U.2    Vacca, C.3
  • 18
    • 0141533178 scopus 로고    scopus 로고
    • Tryptophan depletion and HIV infection: A metabolic link to pathogenesis
    • Murray MF. Tryptophan depletion and HIV infection: a metabolic link to pathogenesis. Lancet Infect Dis. 2003;3:644-652.
    • (2003) Lancet Infect Dis , vol.3 , pp. 644-652
    • Murray, M.F.1
  • 19
    • 0034117681 scopus 로고    scopus 로고
    • The B7/CD28/CTLA4 T-cell activation pathway: Implications for inflammatory lung disease
    • Green JM. The B7/CD28/CTLA4 T-cell activation pathway: implications for inflammatory lung disease. Am J Respir Cell Mol Biol. 2000;22:261-264.
    • (2000) Am J Respir Cell Mol Biol , vol.22 , pp. 261-264
    • Green, J.M.1
  • 22
    • 0032545452 scopus 로고    scopus 로고
    • Molecular basis of T cell inactivation by CTLA-4
    • Lee KM, Chuang E, Griffin M, et al. Molecular basis of T cell inactivation by CTLA-4. Science. 1998;282:2263-2266.
    • (1998) Science , vol.282 , pp. 2263-2266
    • Lee, K.M.1    Chuang, E.2    Griffin, M.3
  • 23
    • 0036852170 scopus 로고    scopus 로고
    • CTLA-4-Ig regulates tryptophan catabolism in vivo
    • Grohmann U, Orabona C, Fallarino F, et al. CTLA-4-Ig regulates tryptophan catabolism in vivo. Nat Immunol. 2002;3:1097-1101.
    • (2002) Nat Immunol , vol.3 , pp. 1097-1101
    • Grohmann, U.1    Orabona, C.2    Fallarino, F.3
  • 24
    • 0036852242 scopus 로고    scopus 로고
    • When ligand becomes receptor-tolerance via B7 signaling on DCs
    • Finger EB, Bluestone JA. When ligand becomes receptor-tolerance via B7 signaling on DCs. Nat Immunol. 2002;3:1056-1057.
    • (2002) Nat Immunol , vol.3 , pp. 1056-1057
    • Finger, E.B.1    Bluestone, J.A.2
  • 25
    • 1642396607 scopus 로고    scopus 로고
    • Ligation of B7-1/B7-2 by human CD4(+) T cells triggers indoleamine 2,3-dioxygenase activity in dendritic cells
    • Munn DH, Sharma MD, Mellor AL. Ligation of B7-1/B7-2 by human CD4(+) T cells triggers indoleamine 2,3-dioxygenase activity in dendritic cells. J Immunol. 2004;172:4100-4110.
    • (2004) J Immunol , vol.172 , pp. 4100-4110
    • Munn, D.H.1    Sharma, M.D.2    Mellor, A.L.3
  • 26
    • 0036341332 scopus 로고    scopus 로고
    • Effect of indoleamine 2,3-dioxygenase on induction of experimental autoimmune encephalomyelitis
    • Sakurai K, Zou JP, Tschetter JR, Ward JM, Shearer GM. Effect of indoleamine 2,3-dioxygenase on induction of experimental autoimmune encephalomyelitis. J Neuroimmunol. 2002;129:186-196.
    • (2002) J Neuroimmunol , vol.129 , pp. 186-196
    • Sakurai, K.1    Zou, J.P.2    Tschetter, J.R.3    Ward, J.M.4    Shearer, G.M.5
  • 27
    • 0037815119 scopus 로고    scopus 로고
    • A defect in tryptophan catabolism impairs tolerance in nonobese diabetic mice
    • Grohmann U, Fallarino F, Bianchi R, et al. A defect in tryptophan catabolism impairs tolerance in nonobese diabetic mice. J Exp Med. 2003;198:153-160.
    • (2003) J Exp Med , vol.198 , pp. 153-160
    • Grohmann, U.1    Fallarino, F.2    Bianchi, R.3
  • 28
    • 0037056234 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase contributes to tumor cell evasion of T cell-mediated rejection
    • Friberg M, Jennings R, Alsarraj M, et al. Indoleamine 2,3-dioxygenase contributes to tumor cell evasion of T cell-mediated rejection. Int J Cancer. 2002;101:151-155.
    • (2002) Int J Cancer , vol.101 , pp. 151-155
    • Friberg, M.1    Jennings, R.2    Alsarraj, M.3
  • 29
    • 0026177095 scopus 로고
    • Localization and developmental change of indoleamine 2,3-dioxygenase activity in the human placenta
    • Kamimura S, Eguchi K, Yonezawa M, Sekiba K. Localization and developmental change of indoleamine 2,3-dioxygenase activity in the human placenta. Acta Med Okayama. 1991;45:135-139.
    • (1991) Acta Med Okayama , vol.45 , pp. 135-139
    • Kamimura, S.1    Eguchi, K.2    Yonezawa, M.3    Sekiba, K.4
  • 30
    • 0033990826 scopus 로고    scopus 로고
    • Human placental indoleamine 2,3-dioxygenase: Cellular localization and characterization of an enzyme preventing fetal rejection
    • Kudo Y, Boyd CA. Human placental indoleamine 2,3-dioxygenase: cellular localization and characterization of an enzyme preventing fetal rejection. Biochim Biophys Acta. 2000;1500:119-124.
    • (2000) Biochim Biophys Acta , vol.1500 , pp. 119-124
    • Kudo, Y.1    Boyd, C.A.2
  • 31
    • 0034809511 scopus 로고    scopus 로고
    • Tryptophan catabolism prevents maternal T cells from activating lethal anti-fetal immune responses
    • Mellor AL, Munn DH. Tryptophan catabolism prevents maternal T cells from activating lethal anti-fetal immune responses. J Reprod Immunol. 2001;52:5-13.
    • (2001) J Reprod Immunol , vol.52 , pp. 5-13
    • Mellor, A.L.1    Munn, D.H.2
  • 32
    • 0037206423 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase, immunosuppression and pregnancy
    • Mellor AL, Chandler P, Lee GK, et al. Indoleamine 2,3-dioxygenase, immunosuppression and pregnancy. J Reprod Immunol. 2002;57:143-150.
    • (2002) J Reprod Immunol , vol.57 , pp. 143-150
    • Mellor, A.L.1    Chandler, P.2    Lee, G.K.3
  • 33
    • 0032555614 scopus 로고    scopus 로고
    • Prevention of allogeneic fetal rejection by tryptophan catabolism
    • Munn DH, Zhou M, Attwood JT, et al. Prevention of allogeneic fetal rejection by tryptophan catabolism. Science. 1998;281:1191-1193.
    • (1998) Science , vol.281 , pp. 1191-1193
    • Munn, D.H.1    Zhou, M.2    Attwood, J.T.3
  • 34
    • 0037414726 scopus 로고    scopus 로고
    • Longitudinal study of tryptophan degradation during and after pregnancy
    • Schrocksnadel K, Widner B, Bergant A, et al. Longitudinal study of tryptophan degradation during and after pregnancy. Life Sci. 2003;72:785-793.
    • (2003) Life Sci , vol.72 , pp. 785-793
    • Schrocksnadel, K.1    Widner, B.2    Bergant, A.3
  • 35
    • 0025291262 scopus 로고
    • AIDS dementia may be linked to metabolite of tryptophan
    • Cotton P. AIDS dementia may be linked to metabolite of tryptophan. JAMA. 1990;264:305-306.
    • (1990) JAMA , vol.264 , pp. 305-306
    • Cotton, P.1
  • 38
    • 0027225504 scopus 로고
    • Quantitation of human immunodeficiency virus, immune activation factors, and quinolinic acid in AIDS brains
    • Achim CL, Heyes MP, Wiley CA. Quantitation of human immunodeficiency virus, immune activation factors, and quinolinic acid in AIDS brains. J Clin Invest. 1993;91:2769-2775.
    • (1993) J Clin Invest , vol.91 , pp. 2769-2775
    • Achim, C.L.1    Heyes, M.P.2    Wiley, C.A.3
  • 39
    • 0033998033 scopus 로고    scopus 로고
    • Induction of indolamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent
    • Grant RS, Naif H, Thuruthyil SJ, et al. Induction of indolamine 2,3-dioxygenase in primary human macrophages by human immunodeficiency virus type 1 is strain dependent. J Virol. 2000;74:4110-4115.
    • (2000) J Virol , vol.74 , pp. 4110-4115
    • Grant, R.S.1    Naif, H.2    Thuruthyil, S.J.3
  • 40
    • 0036370969 scopus 로고    scopus 로고
    • Role of the B7-CD28/CTLA-4 pathway in autoimmune disease
    • Chang TT, Kuchroo VK, Sharpe AH. Role of the B7-CD28/CTLA-4 pathway in autoimmune disease. Curr Dir Autoimmun. 2002;5:113-130.
    • (2002) Curr Dir Autoimmun , vol.5 , pp. 113-130
    • Chang, T.T.1    Kuchroo, V.K.2    Sharpe, A.H.3
  • 41
    • 0042353836 scopus 로고    scopus 로고
    • CTLA-4 and its role in autoimmune thyroid disease
    • Chistiakov DA, Turakulov RI. CTLA-4 and its role in autoimmune thyroid disease. J Mol Endocrinol. 2003;31:21-36.
    • (2003) J Mol Endocrinol , vol.31 , pp. 21-36
    • Chistiakov, D.A.1    Turakulov, R.I.2
  • 42
    • 0037265618 scopus 로고    scopus 로고
    • The CTLA4 region as a general autoimmunity factor: An extended pedigree provides evidence for synergy with the HLA locus in the etiology of type 1 diabetes mellitus, Hashimoto's thyroiditis and Graves' disease
    • Einarsdottir E, Soderstrom I, Lofgren-Burstrom A, et al. The CTLA4 region as a general autoimmunity factor: an extended pedigree provides evidence for synergy with the HLA locus in the etiology of type 1 diabetes mellitus, Hashimoto's thyroiditis and Graves' disease. Eur J Hum Genet. 2003;11:81-84.
    • (2003) Eur J Hum Genet , vol.11 , pp. 81-84
    • Einarsdottir, E.1    Soderstrom, I.2    Lofgren-Burstrom, A.3
  • 43
    • 0034139830 scopus 로고    scopus 로고
    • CTLA-4 in autoimmune diseases-a general susceptibility gene to autoimmunity?
    • Kristiansen OP, Larsen ZM, Pociot F. CTLA-4 in autoimmune diseases-a general susceptibility gene to autoimmunity? Genes Immun. 2000;1:170-184.
    • (2000) Genes Immun , vol.1 , pp. 170-184
    • Kristiansen, O.P.1    Larsen, Z.M.2    Pociot, F.3
  • 44
    • 0035059417 scopus 로고    scopus 로고
    • Complexities of CD28/B7: CTLA-4 costimulatory pathways in autoimmunity and transplantation
    • Salomon B, Bluestone JA. Complexities of CD28/B7: CTLA-4 costimulatory pathways in autoimmunity and transplantation. Annu Rev Immunol. 2001;19:225-252.
    • (2001) Annu Rev Immunol , vol.19 , pp. 225-252
    • Salomon, B.1    Bluestone, J.A.2
  • 45
    • 0037080929 scopus 로고    scopus 로고
    • Immunomodulation with CTLA4-Ig in islet transplantation
    • Benhamou PY. Immunomodulation with CTLA4-Ig in islet transplantation. Transplantation. 2002;73:S40-S42.
    • (2002) Transplantation , vol.73
    • Benhamou, P.Y.1
  • 46
    • 0038153907 scopus 로고    scopus 로고
    • Cancer regression and autoimmunity induced by cytotoxic T lymphocyte-associated antigen 4 blockade in patients with metastatic melanoma
    • Phan GQ, Yang JC, Sherry RM, et al. Cancer regression and autoimmunity induced by cytotoxic T lymphocyte-associated antigen 4 blockade in patients with metastatic melanoma. Proc Natl Acad Sci USA. 2003;100:8372-8377.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 8372-8377
    • Phan, G.Q.1    Yang, J.C.2    Sherry, R.M.3
  • 47
    • 0031451315 scopus 로고    scopus 로고
    • Simultaneous measurement of serum tryptophan and kynurenine by HPLC
    • Widner B, Werner ER, Schennach H, Wachter H, Fuchs D. Simultaneous measurement of serum tryptophan and kynurenine by HPLC. Clin Chem. 1997;43:2424-2426.
    • (1997) Clin Chem , vol.43 , pp. 2424-2426
    • Widner, B.1    Werner, E.R.2    Schennach, H.3    Wachter, H.4    Fuchs, D.5
  • 48
    • 0027434907 scopus 로고
    • Antigen-presenting human T cells and antigen-presenting B cells induce a similar cytokine profile in specific T cell clones
    • Wyss-Coray T, Gallati H, Pracht I, et al. Antigen-presenting human T cells and antigen-presenting B cells induce a similar cytokine profile in specific T cell clones. Eur J Immunol. 1993;23:3350-3357.
    • (1993) Eur J Immunol , vol.23 , pp. 3350-3357
    • Wyss-Coray, T.1    Gallati, H.2    Pracht, I.3
  • 50
    • 0027473759 scopus 로고
    • B7/BB1, the ligand for CD28, is expressed on repeatedly activated human T cells in vitro
    • Sansom DM, Hall ND. B7/BB1, the ligand for CD28, is expressed on repeatedly activated human T cells in vitro. Eur J Immunol. 1993;23:295-298.
    • (1993) Eur J Immunol , vol.23 , pp. 295-298
    • Sansom, D.M.1    Hall, N.D.2
  • 51
    • 0347994958 scopus 로고    scopus 로고
    • B7 expression on T cells down-regulates immune responses through CTLA-4 ligation via T-T interactions
    • Taylor PA, Lees CJ, Fournier S, Allison JP, Sharpe AH, Blazar BR. B7 expression on T cells down-regulates immune responses through CTLA-4 ligation via T-T interactions [corrections], J Immunol. 2004;172:34-39.
    • (2004) J Immunol , vol.172 , pp. 34-39
    • Taylor, P.A.1    Lees, C.J.2    Fournier, S.3    Allison, J.P.4    Sharpe, A.H.5    Blazar, B.R.6
  • 52
    • 0016424540 scopus 로고
    • The control of protein synthesis during the stimulation of lymphocytes by phytohaemagglutinin: III, poly(U) translation and the rate of polypeptide chain elongation
    • Kay JE, Ahern T, Lindsay VJ, Sampson J. The control of protein synthesis during the stimulation of lymphocytes by phytohaemagglutinin: III, poly(U) translation and the rate of polypeptide chain elongation. Biochim Biophys Acta. 1975;378:241-250.
    • (1975) Biochim Biophys Acta , vol.378 , pp. 241-250
    • Kay, J.E.1    Ahern, T.2    Lindsay, V.J.3    Sampson, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.