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Volumn 80, Issue 6, 2006, Pages 1320-1327

A high-affinity, tryptophan-selective amino acid transport system in human macrophages

Author keywords

Antigen presenting cells; Indoleamine 2,3 dioxygenase; Tolerance

Indexed keywords

INDOLEAMINE 2,3 DIOXYGENASE; TRYPTOPHAN;

EID: 33845402200     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.1205727     Document Type: Article
Times cited : (65)

References (42)
  • 2
    • 0025320803 scopus 로고
    • Molecular cloning, sequencing and expression of human interferon-γ-inducible indoleamine 2,3-dioxygenase cDNA
    • Dai, W., Gupta, S. L. (1990) Molecular cloning, sequencing and expression of human interferon-γ-inducible indoleamine 2,3-dioxygenase cDNA. Biochem. Biophys. Res. Commun. 168, 1-8.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 1-8
    • Dai, W.1    Gupta, S.L.2
  • 3
    • 0025944659 scopus 로고
    • Relationship between interferon-γ, indoleamine 2,3-dioxygenase, and tryptophan catabolism
    • Taylor, M. W., 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
  • 4
    • 0030608057 scopus 로고    scopus 로고
    • Convergent evolution. The gene structure of Sulculus 41 kDa myoglobin is homologous with that of human indoleamine dioxygenase
    • Suzuki, T., Yuasa, H., Imai, K. (1996) Convergent evolution. The gene structure of Sulculus 41 kDa myoglobin is homologous with that of human indoleamine dioxygenase. Biochim. Biophys. Acta 1308, 41-48.
    • (1996) Biochim. Biophys. Acta , vol.1308 , pp. 41-48
    • Suzuki, T.1    Yuasa, H.2    Imai, K.3
  • 5
    • 0028365389 scopus 로고
    • Antiparasitic and antiproliferative effects of indoleamine 2,3-dioxygenase enzyme expression in human fibroblasts
    • Gupta, S. L., Carlin, J. M., Pyati, P., Dai, W., Pfefferkorn, E. R., Murphy, M. J. (1994) Antiparasitic and antiproliferative effects of indoleamine 2,3-dioxygenase enzyme expression in human fibroblasts. Infect. Immun. 62, 2277-2284.
    • (1994) Infect. Immun. , vol.62 , pp. 2277-2284
    • Gupta, S.L.1    Carlin, J.M.2    Pyati, P.3    Dai, W.4    Pfefferkorn, E.R.5    Murphy, M.J.6
  • 6
    • 0027324876 scopus 로고
    • IFN-γ-mediated antimicrobial response: Indoleamine 2,3-dioxygenase-deficient mutant host cells no longer inhibit intracellular Chlamydia spp. or Toxoplama growth
    • Thomas, S. M., Garrity, L. F., Brandt, C. R., Schobert, C. S., Feng, G-S., Taylor, M. W., Carlin, J. M., Byrne, G. I. (1993) IFN-γ-mediated antimicrobial response: indoleamine 2,3-dioxygenase-deficient mutant host cells no longer inhibit intracellular Chlamydia spp. or Toxoplama growth. J. Immunol. 150, 5529-5534.
    • (1993) J. Immunol. , vol.150 , pp. 5529-5534
    • Thomas, S.M.1    Garrity, L.F.2    Brandt, C.R.3    Schobert, C.S.4    Feng, G.-S.5    Taylor, M.W.6    Carlin, J.M.7    Byrne, G.I.8
  • 7
    • 0000056144 scopus 로고
    • Interferon γ blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan
    • Pfefferkorn, E. R. (1984) Interferon γ blocks the growth of Toxoplasma gondii in human fibroblasts by inducing the host cells to degrade tryptophan. Proc. Natl. Acad. Sci. USA 81, 908-912.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 908-912
    • Pfefferkorn, E.R.1
  • 8
    • 0033555723 scopus 로고    scopus 로고
    • Role of IFN-γ-induced indoleamine 2,3 dioxygenase and inducible nitric oxide synthase in the replication of human cytomegalovirus in retinal pigment epithelial cells
    • Bodaghi, B., Goureau, O., Zipeto, D., Laurent, L., Virelizier, J. L., Michelson, S. (1999) Role of IFN-γ-induced indoleamine 2,3 dioxygenase and inducible nitric oxide synthase in the replication of human cytomegalovirus in retinal pigment epithelial cells. J. Immunol. 162, 957-964.
    • (1999) J. Immunol. , vol.162 , pp. 957-964
    • Bodaghi, B.1    Goureau, O.2    Zipeto, D.3    Laurent, L.4    Virelizier, J.L.5    Michelson, S.6
  • 9
    • 5044220930 scopus 로고    scopus 로고
    • IDO expression by dendritic cells: Tolerance and tryptophan catabolism
    • Mellor, A. L., Munn, D. H. (2004) IDO expression by dendritic cells: tolerance and tryptophan catabolism. Nat. Rev. Immunol. 4, 762-774.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 762-774
    • Mellor, A.L.1    Munn, D.H.2
  • 11
    • 0035221101 scopus 로고    scopus 로고
    • Prevention of T cell-driven complement activation and inflammation by tryptophan catabolism during pregnancy
    • Mellor, A. L., Sivakumar, J., Chandler, P., Smith, K., Molina, H., Mao, D., Munn, D. H. (2001) Prevention of T cell-driven complement activation and inflammation by tryptophan catabolism during pregnancy. Nat. Immunol. 2, 64-68.
    • (2001) Nat. Immunol. , vol.2 , pp. 64-68
    • Mellor, A.L.1    Sivakumar, J.2    Chandler, P.3    Smith, K.4    Molina, H.5    Mao, D.6    Munn, D.H.7
  • 13
    • 0345490963 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase augments trinitrobenzene sulfonic acid colitis in mice
    • Gurtner, G. J., Newberry, R. D., Schloemann, S. R., McDonald, K. G., Stenson, W. F. (2003) Inhibition of indoleamine 2,3-dioxygenase augments trinitrobenzene sulfonic acid colitis in mice. Gastroenterology 125, 1762-1773.
    • (2003) Gastroenterology , vol.125 , pp. 1762-1773
    • Gurtner, G.J.1    Newberry, R.D.2    Schloemann, S.R.3    McDonald, K.G.4    Stenson, W.F.5
  • 14
    • 27144552597 scopus 로고    scopus 로고
    • Cutting edge: CpG oligonucleotides induce splenic CD19+ dendritic cells to acquire potent indoleamine 2,3-dioxygenase-dependent T cell regulatory functions via IFN type 1 signaling
    • Mellor, A. L., Baban, B., Chandler, P. R., Manlapat, A., Kahler, D. J., Munn, D. H. (2005) Cutting edge: CpG oligonucleotides induce splenic CD19+ dendritic cells to acquire potent indoleamine 2,3-dioxygenase-dependent T cell regulatory functions via IFN type 1 signaling. J. Immunol. 175, 5601-5605.
    • (2005) J. Immunol. , vol.175 , pp. 5601-5605
    • Mellor, A.L.1    Baban, B.2    Chandler, P.R.3    Manlapat, A.4    Kahler, D.J.5    Munn, D.H.6
  • 15
    • 19344377474 scopus 로고    scopus 로고
    • GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase
    • Munn, D. H., Sharma, M. D., Baban, B., Harding, H. P., Zhang, Y., Ron, D., Mellor, A. L. (2005) GCN2 kinase in T cells mediates proliferative arrest and anergy induction in response to indoleamine 2,3-dioxygenase. Immunity 22, 633-642.
    • (2005) Immunity , vol.22 , pp. 633-642
    • Munn, D.H.1    Sharma, M.D.2    Baban, B.3    Harding, H.P.4    Zhang, Y.5    Ron, D.6    Mellor, A.L.7
  • 16
  • 18
    • 16244408626 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy
    • Muller, A. J., Duhadaway, J. B., Donover, P. S., Sutanto-Ward, E., Prendergast, G. C. (2005) Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy. Nat. Med. 11, 312-319.
    • (2005) Nat. Med. , vol.11 , pp. 312-319
    • Muller, A.J.1    Duhadaway, J.B.2    Donover, P.S.3    Sutanto-Ward, E.4    Prendergast, G.C.5
  • 19
    • 0037090313 scopus 로고    scopus 로고
    • Cells expressing indoleamine 2,3 dioxygenase inhibit T cell responses
    • Mellor, A. L., Keskin, D. B., Johnson, T., Chandler, P., Munn, D. H. (2002) Cells expressing indoleamine 2,3 dioxygenase inhibit T cell responses. J. Immunol. 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
  • 20
    • 0035995944 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase expression in transplanted NOD islets prolongs graft survival after adoptive transfer of diabetogenic splenocytes
    • Alexander, A. M., Crawford, M., Bertera, S., Rudert, W. A., Takikawa, O., Robbins, P. D., Trucco, M. (2002) Indoleamine 2,3-dioxygenase expression in transplanted NOD islets prolongs graft survival after adoptive transfer of diabetogenic splenocytes. Diabetes 51, 356-365.
    • (2002) Diabetes , vol.51 , pp. 356-365
    • Alexander, A.M.1    Crawford, M.2    Bertera, S.3    Rudert, W.A.4    Takikawa, O.5    Robbins, P.D.6    Trucco, M.7
  • 23
    • 0034176031 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase production by human dendritic cells results in the inhibition of T cell proliferation
    • Hwu, P., Du, M. X., Lapointe, R., Do, M., Taylor, M. W., Young, H. A. (2000) Indoleamine 2,3-dioxygenase production by human dendritic cells results in the inhibition of T cell proliferation. J. Immunol. 164, 3596-3599.
    • (2000) J. Immunol. , vol.164 , pp. 3596-3599
    • Hwu, P.1    Du, M.X.2    Lapointe, R.3    Do, M.4    Taylor, M.W.5    Young, H.A.6
  • 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, D. H., Sharma, M. D., Mellor, A. L. (2004) Ligation of B7-1/B7-2 by human CD4+ T cells triggers indoleamine 2,3-dioxygenase activity in dendritic cells. J. Immunol. 172, 4100-4110.
    • (2004) J. Immunol. , vol.172 , pp. 4100-4110
    • Munn, D.H.1    Sharma, M.D.2    Mellor, A.L.3
  • 26
    • 0035281651 scopus 로고    scopus 로고
    • The role of L-tryptophan transport in L-tryptophan degradation by indoleamine 2,3-dioxygenase in human placental explants
    • Kudo, Y., Boyd, C. A. (2001) The role of L-tryptophan transport in L-tryptophan degradation by indoleamine 2,3-dioxygenase in human placental explants. J. Physiol. 531, 417-423.
    • (2001) J. Physiol. , vol.531 , pp. 417-423
    • Kudo, Y.1    Boyd, C.A.2
  • 28
    • 0031751209 scopus 로고    scopus 로고
    • Molecular biology of mammalian plasma membrane amino acid transporters
    • Palacin, M., Estevez, R., Bertran, J., Zorzano, A. (1998) Molecular biology of mammalian plasma membrane amino acid transporters. Physiol. Rev. 78, 969-1054.
    • (1998) Physiol. Rev. , vol.78 , pp. 969-1054
    • Palacin, M.1    Estevez, R.2    Bertran, J.3    Zorzano, A.4
  • 29
    • 0027316304 scopus 로고
    • Cytokine regulation of human monocyte differentiation in vitro: The tumor-cytotoxic phenotype induced by macrophage colony-stimulating factor is developmentally regulated by interferon-γ
    • Munn, D. H., Armstrong, E. (1993) Cytokine regulation of human monocyte differentiation in vitro: the tumor-cytotoxic phenotype induced by macrophage colony-stimulating factor is developmentally regulated by interferon-γ. Cancer Res. 53, 2603-2613.
    • (1993) Cancer Res. , vol.53 , pp. 2603-2613
    • Munn, D.H.1    Armstrong, E.2
  • 30
    • 0031916983 scopus 로고    scopus 로고
    • Transporters for cationic amino acids in animal cells: Discovery, structure, and function
    • Deves, R., Boyd, C. A. R. (1998) Transporters for cationic amino acids in animal cells: discovery, structure, and function. Physiol. Rev. 78, 487-545.
    • (1998) Physiol. Rev. , vol.78 , pp. 487-545
    • Deves, R.1    Boyd, C.A.R.2
  • 31
    • 0015861774 scopus 로고
    • Relationship between the inhibtion constant (Ki) and the concentration of inhibitor which causes 50 percent inhibition (I50) of an enzymatic reaction
    • Cheng, Y., Prusoff, W. H. (1973) Relationship between the inhibtion constant (Ki) and the concentration of inhibitor which causes 50 percent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol. 22, 3099-3108.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 32
    • 0022497872 scopus 로고
    • Characterization of tryptophan transport in human placental brush border membrane vesicles
    • Ganapathy, M. E., Leibach, F. H., Mahesh, V. B., Howard, J. C., Devoe, L. D., Ganapathy, V. (1986) Characterization of tryptophan transport in human placental brush border membrane vesicles. Biochem. J. 238, 201-208.
    • (1986) Biochem. J. , vol.238 , pp. 201-208
    • Ganapathy, M.E.1    Leibach, F.H.2    Mahesh, V.B.3    Howard, J.C.4    Devoe, L.D.5    Ganapathy, V.6
  • 33
    • 0027317233 scopus 로고
    • + amino acid transport activity in cultured vascular smooth muscle cells
    • + amino acid transport activity in cultured vascular smooth muscle cells. J. Cell. Physiol. 156, 626-634.
    • (1993) J. Cell. Physiol. , vol.156 , pp. 626-634
    • Low, B.C.1    Ross, I.K.2    Grigor, M.R.3
  • 34
    • 0028147406 scopus 로고
    • Relationship between thyroid hormone transport and neutral amino acid transport in JAR human choriocarcinoma cells
    • Prasad, P. D., Leibach, F. H., Mahesh, V. B., Ganapathy, V. (1994) Relationship between thyroid hormone transport and neutral amino acid transport in JAR human choriocarcinoma cells. Endocrinology 134, 574-581.
    • (1994) Endocrinology , vol.134 , pp. 574-581
    • Prasad, P.D.1    Leibach, F.H.2    Mahesh, V.B.3    Ganapathy, V.4
  • 37
    • 0037291723 scopus 로고    scopus 로고
    • System L: Heteromeric exchangers of large, neutral amino acids involved in directional transport
    • Verrey, F. (2003) System L: heteromeric exchangers of large, neutral amino acids involved in directional transport. Pflugers Arch. 445, 529-533.
    • (2003) Pflugers Arch. , vol.445 , pp. 529-533
    • Verrey, F.1
  • 38
    • 0028967644 scopus 로고
    • The role of indoleamine 2,3-dioxygenase in the anti-tumor activity of human interferon-γ in vivo
    • Burke, F., Knowles, R. G., East, N., Balkwill, F. R. (1995) The role of indoleamine 2,3-dioxygenase in the anti-tumor activity of human interferon-γ in vivo. Int. J. Cancer 60, 115-122.
    • (1995) Int. J. Cancer , vol.60 , pp. 115-122
    • Burke, F.1    Knowles, R.G.2    East, N.3    Balkwill, F.R.4
  • 39
    • 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., Rose, L., Dufter, C., Watzlik, A., Simon, H., Opelz, G. (2002) Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites. J. Exp. Med. 196, 447-457.
    • (2002) J. Exp. Med. , vol.196 , pp. 447-457
    • Terness, P.1    Bauer, T.M.2    Rose, L.3    Dufter, C.4    Watzlik, A.5    Simon, H.6    Opelz, G.7
  • 40
    • 0037136328 scopus 로고    scopus 로고
    • Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase
    • Frumento, G., Rotondo, R., Tonetti, M., Damonte, G., Benatti, U., Ferrara, G. B. (2002) Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase. J. Exp. Med. 196, 459-468.
    • (2002) J. Exp. Med. , vol.196 , pp. 459-468
    • Frumento, G.1    Rotondo, R.2    Tonetti, M.3    Damonte, G.4    Benatti, U.5    Ferrara, G.B.6
  • 41
    • 0035880924 scopus 로고    scopus 로고
    • Tryptophan degradation by human placental indoleamine 2,3-dioxygenase regulates lymphocyte proliferation
    • Kudo, Y., Boyd, C. A., Sargent, I. L., Redman, C. W. (2001) Tryptophan degradation by human placental indoleamine 2,3-dioxygenase regulates lymphocyte proliferation. J. Physiol. 535, 207-215.
    • (2001) J. Physiol. , vol.535 , pp. 207-215
    • Kudo, Y.1    Boyd, C.A.2    Sargent, I.L.3    Redman, C.W.4
  • 42
    • 1042264014 scopus 로고    scopus 로고
    • Indoleamine 2,3-dioxygenase activity and L-tryptophan transport in human breast cancer cells
    • Travers, M. T., Gow, I. F., Barber, M. C., Thomson, J., Shennan, D. B. (2004) Indoleamine 2,3-dioxygenase activity and L-tryptophan transport in human breast cancer cells. Biochim. Biophys. Acta 1661, 106-112.
    • (2004) Biochim. Biophys. Acta , vol.1661 , pp. 106-112
    • Travers, M.T.1    Gow, I.F.2    Barber, M.C.3    Thomson, J.4    Shennan, D.B.5


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