메뉴 건너뛰기




Volumn 26, Issue 13, 2007, Pages 3086-3097

Selective redox regulation of cytokine receptor signaling by extracellular thioredoxin-1

Author keywords

CD30; Redox regulation; Thiol disulfide exchange; Thioredoxin; TNF receptor superfamily

Indexed keywords

CD30 ANTIGEN; THIOREDOXIN; THIOREDOXIN 1; TUMOR NECROSIS FACTOR RECEPTOR; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 8; UNCLASSIFIED DRUG;

EID: 34447309788     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601746     Document Type: Article
Times cited : (114)

References (42)
  • 4
    • 0027433497 scopus 로고
    • Functional effects of CD30 on a large granular lymphoma cell line, YT. Inhibition of cytotoxicity, regulation of CD28 and IL-2R, and induction of homotypic aggregation
    • Bowen MA, Olsen KJ, Cheng L, Avila D, Podack ER (1993) Functional effects of CD30 on a large granular lymphoma cell line, YT. Inhibition of cytotoxicity, regulation of CD28 and IL-2R, and induction of homotypic aggregation. J Immunol 151: 5896-5906
    • (1993) J Immunol , vol.151 , pp. 5896-5906
    • Bowen, M.A.1    Olsen, K.J.2    Cheng, L.3    Avila, D.4    Podack, E.R.5
  • 9
    • 0141609073 scopus 로고    scopus 로고
    • Co-stimulatory members of the TNFR family: Keys to effective T-cell immunity?
    • Croft M (2003) Co-stimulatory members of the TNFR family: keys to effective T-cell immunity? Nat Rev Immunol 3: 609-620
    • (2003) Nat Rev Immunol , vol.3 , pp. 609-620
    • Croft, M.1
  • 10
    • 0027442858 scopus 로고
    • A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly
    • de Paiva A, Poulain B, Lawrence GW, Shone CC, Tauc L, Dolly JO (1993) A role for the interchain disulfide or its participating thiols in the internalization of botulinum neurotoxin A revealed by a toxin derivative that binds to ecto-acceptors and inhibits transmitter release intracellularly. J Biol Chem 268: 20838-20844
    • (1993) J Biol Chem , vol.268 , pp. 20838-20844
    • de Paiva, A.1    Poulain, B.2    Lawrence, G.W.3    Shone, C.C.4    Tauc, L.5    Dolly, J.O.6
  • 11
    • 0036371484 scopus 로고    scopus 로고
    • Thiol oxidation and reduction in major histocompatibility complex class I-restricted antigen processing and presentation
    • Dick TP, Cresswell P (2002) Thiol oxidation and reduction in major histocompatibility complex class I-restricted antigen processing and presentation. Methods Enzymol 348: 49-54
    • (2002) Methods Enzymol , vol.348 , pp. 49-54
    • Dick, T.P.1    Cresswell, P.2
  • 12
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick TP, Bangia N, Peaper DR, Cresswell P (2002) Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16: 87-98
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 13
    • 3042824871 scopus 로고    scopus 로고
    • The role of thiols and disulfides in platelet function
    • Essex DW (2004) The role of thiols and disulfides in platelet function. Antioxid Redox Signal 6: 736-746
    • (2004) Antioxid Redox Signal , vol.6 , pp. 736-746
    • Essex, D.W.1
  • 14
    • 0019861187 scopus 로고
    • Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells
    • Gill GN, Lazar CS (1981) Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells. Nature 293: 305-307
    • (1981) Nature , vol.293 , pp. 305-307
    • Gill, G.N.1    Lazar, C.S.2
  • 15
    • 0029914089 scopus 로고    scopus 로고
    • Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions
    • Greene JL, Leytze GM, Emswiler J, Peach R, Bajorath J, Cosand W, Linsley PS (1996) Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions. J Biol Chem 271: 26762-26771
    • (1996) J Biol Chem , vol.271 , pp. 26762-26771
    • Greene, J.L.1    Leytze, G.M.2    Emswiler, J.3    Peach, R.4    Bajorath, J.5    Cosand, W.6    Linsley, P.S.7
  • 16
    • 0242277285 scopus 로고    scopus 로고
    • The thioredoxin system - from science to clinic
    • Gromer S, Urig S, Becker K (2004) The thioredoxin system - from science to clinic. Med Res Rev 24: 40-89
    • (2004) Med Res Rev , vol.24 , pp. 40-89
    • Gromer, S.1    Urig, S.2    Becker, K.3
  • 18
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg PJ (2003) Disulfide bonds as switches for protein function. Trends Biochem Sci 28: 210-214
    • (2003) Trends Biochem Sci , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 19
    • 0032387839 scopus 로고    scopus 로고
    • CD30: Expression and function in health and disease
    • Horie R, Watanabe T (1998) CD30: expression and function in health and disease. Semin Immunol 10: 457-470
    • (1998) Semin Immunol , vol.10 , pp. 457-470
    • Horie, R.1    Watanabe, T.2
  • 20
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • Jordan PA, Gibbins JM (2006) Extracellular disulfide exchange and the regulation of cellular function. Antioxid Redox Signal 8: 312-324
    • (2006) Antioxid Redox Signal , vol.8 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 24
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi K, Kondoh A, Stumpp MT, Hisabori T (2001) Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc Natl Acad Sci USA 98: 11224-11229
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 25
    • 0034327179 scopus 로고    scopus 로고
    • CD30 signals integrate expression of cytotoxic effector molecules, lymphocyte trafficking signals, and signals for proliferation and apoptosis
    • Muta H, Boise LH, Fang L, Podack ER (2000) CD30 signals integrate expression of cytotoxic effector molecules, lymphocyte trafficking signals, and signals for proliferation and apoptosis. J Immunol 165: 5105-5111
    • (2000) J Immunol , vol.165 , pp. 5105-5111
    • Muta, H.1    Boise, L.H.2    Fang, L.3    Podack, E.R.4
  • 26
    • 0035956987 scopus 로고    scopus 로고
    • Chronic elevation of plasma thioredoxin: Inhibition of chemotaxis and curtailment of life expectancy in AIDS
    • Nakamura H, De Rosa SC, Yodoi J, Holmgren A, Ghezzi P, Herzenberg LA (2001a) Chronic elevation of plasma thioredoxin: inhibition of chemotaxis and curtailment of life expectancy in AIDS. Proc Natl Acad Sci USA 98: 2688-2693
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2688-2693
    • Nakamura, H.1    De Rosa, S.C.2    Yodoi, J.3    Holmgren, A.4    Ghezzi, P.5    Herzenberg, L.A.6
  • 30
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J, Arner ES (2001) Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31: 1287-1312
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 31
    • 33750621913 scopus 로고    scopus 로고
    • Insights into deglutathionylation reactions: Different intermediates in the glutaredoxin and protein disulphide isomerase catalysed reactions are defined by the gamma-linkage present in glutathione
    • Peltoniemi MJ, Karala AR, Jurvansuu JK, Kinnula VL, Ruddock LW (2006) Insights into deglutathionylation reactions: Different intermediates in the glutaredoxin and protein disulphide isomerase catalysed reactions are defined by the gamma-linkage present in glutathione. J Biol Chem 281: 33107-33114
    • (2006) J Biol Chem , vol.281 , pp. 33107-33114
    • Peltoniemi, M.J.1    Karala, A.R.2    Jurvansuu, J.K.3    Kinnula, V.L.4    Ruddock, L.W.5
  • 32
    • 0034990527 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • Powis G, Montfort WR (2001) Properties and biological activities of thioredoxins. Annu Rev Biophys Biomol Struct 30: 421-455
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 421-455
    • Powis, G.1    Montfort, W.R.2
  • 33
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • Rubartelli A, Bajetto A, Allavena G, Wollman E, Sitia R (1992) Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway. J Biol Chem 267: 24161-24164
    • (1992) J Biol Chem , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 34
    • 0033658703 scopus 로고    scopus 로고
    • Sulfhydryl involvement in fusion mechanisms
    • Sanders DA (2000) Sulfhydryl involvement in fusion mechanisms. Subcell Biochem 34: 483-514
    • (2000) Subcell Biochem , vol.34 , pp. 483-514
    • Sanders, D.A.1
  • 35
    • 0036302480 scopus 로고    scopus 로고
    • Pleiotropic signal transduction mediated by human CD30: A member of the tumor necrosis factor receptor (TNFR) family
    • Schneider C, Hubinger G (2002) Pleiotropic signal transduction mediated by human CD30: a member of the tumor necrosis factor receptor (TNFR) family. Leuk Lymphoma 43: 1355-1366
    • (2002) Leuk Lymphoma , vol.43 , pp. 1355-1366
    • Schneider, C.1    Hubinger, G.2
  • 36
    • 0242501629 scopus 로고    scopus 로고
    • Thioredoxin reductase, a redox-active selenoprotein, is secreted by normal and neoplastic cells: Presence in human plasma
    • Soderberg A, Sahaf B, Rosen A (2000) Thioredoxin reductase, a redox-active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma. Cancer Res 60: 2281-2289
    • (2000) Cancer Res , vol.60 , pp. 2281-2289
    • Soderberg, A.1    Sahaf, B.2    Rosen, A.3
  • 37
    • 0024461420 scopus 로고
    • ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction
    • Tagaya Y, Maeda Y, Mitsui A, Kondo N, Matsui H, Hamuro J, Brown N, Arai K, Yokota T, Wakasugi H, Yodoi J (1989) ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction. EMBO J 8: 757-764
    • (1989) EMBO J , vol.8 , pp. 757-764
    • Tagaya, Y.1    Maeda, Y.2    Mitsui, A.3    Kondo, N.4    Matsui, H.5    Hamuro, J.6    Brown, N.7    Arai, K.8    Yokota, T.9    Wakasugi, H.10    Yodoi, J.11
  • 39
    • 0025066731 scopus 로고
    • Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotropic virus type I- and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2
    • Wakasugi N, Tagaya Y, Wakasugi H, Mitsui A, Maeda M, Yodoi J, Tursz T (1990) Adult T-cell leukemia-derived factor/thioredoxin, produced by both human T-lymphotropic virus type I- and Epstein-Barr virus-transformed lymphocytes, acts as an autocrine growth factor and synergizes with interleukin 1 and interleukin 2. Proc Natl Acad Sci USA 87: 8282-8286
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8282-8286
    • Wakasugi, N.1    Tagaya, Y.2    Wakasugi, H.3    Mitsui, A.4    Maeda, M.5    Yodoi, J.6    Tursz, T.7
  • 40
    • 0041856170 scopus 로고    scopus 로고
    • Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif
    • Watson WH, Pohl J, Montfort WR, Stuchlik O, Reed MS, Powis G, Jones DP (2003) Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J Biol Chem 278: 33408-33415
    • (2003) J Biol Chem , vol.278 , pp. 33408-33415
    • Watson, W.H.1    Pohl, J.2    Montfort, W.R.3    Stuchlik, O.4    Reed, M.S.5    Powis, G.6    Jones, D.P.7
  • 41
    • 0032497928 scopus 로고    scopus 로고
    • Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity
    • Yang Y, Jao S, Nanduri S, Starke DW, Mieyal JJ, Qin J (1998) Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry 37: 17145-17156
    • (1998) Biochemistry , vol.37 , pp. 17145-17156
    • Yang, Y.1    Jao, S.2    Nanduri, S.3    Starke, D.W.4    Mieyal, J.J.5    Qin, J.6
  • 42
    • 0033168698 scopus 로고    scopus 로고
    • Involvement of thioredoxin in rheumatoid arthritis: Its costimulatory roles in the TNF-alpha-induced production of IL-6 and IL-8 from cultured synovial fibroblasts
    • Yoshida S, Katoh T, Tetsuka T, Uno K, Matsui N, Okamoto T (1999) Involvement of thioredoxin in rheumatoid arthritis: its costimulatory roles in the TNF-alpha-induced production of IL-6 and IL-8 from cultured synovial fibroblasts. J Immunol 163: 351-358
    • (1999) J Immunol , vol.163 , pp. 351-358
    • Yoshida, S.1    Katoh, T.2    Tetsuka, T.3    Uno, K.4    Matsui, N.5    Okamoto, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.