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Volumn 1661, Issue , 2018, Pages 301-309

Selective evaluation of thioredoxin reductase enzymatic activities

Author keywords

Activity; Assay; Enzyme; Insulin; NADPH; Spectrophotometry; Thioredoxin; Thioredoxin reductase

Indexed keywords

THIOREDOXIN REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOREDOXIN;

EID: 85029582417     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-7258-6_21     Document Type: Chapter
Times cited : (12)

References (32)
  • 2
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases
    • Boca Raton, FL
    • Williams CH Jr (1992) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases. In: M€uller F (ed) Chemistry and biochemistry of flavoen-zymes, vol 3. CRC Press, Boca Raton, FL, pp 121–211
    • (1992) M€uller F (Ed) Chemistry and Biochemistry of Flavoen-Zymes, Vol 3. CRC Press , pp. 121-211
    • Williams, C.H.1
  • 3
    • 0030887844 scopus 로고    scopus 로고
    • The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli
    • Arscott LD, Gromer S, Schirmer RH, Becker K, Williams CH Jr (1997) The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. Proc Natl Acad Sci U S A 94:3621–3626
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 3621-3626
    • Arscott, L.D.1    Gromer, S.2    Schirmer, R.H.3    Becker, K.4    Williams, C.H.5
  • 6
    • 0032502720 scopus 로고    scopus 로고
    • Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue
    • Zhong L, Arnér ESJ, Ljung J, Åslund F, Holmgren A (1998) Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J Biol Chem 273:8581–8591
    • (1998) J Biol Chem , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arnér, E.S.J.2    Ljung, J.3    Åslund, F.4    Holmgren, A.5
  • 7
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arner ES, Holmgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267:6102–6109
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 8
    • 0034705133 scopus 로고    scopus 로고
    • Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
    • Zhong L, Arnér ESJ, Holmgren A (2000) Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proc Natl Acad Sci U S A 97:5854–5859
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5854-5859
    • Zhong, L.1    Arnér, E.S.J.2    Holmgren, A.3
  • 9
    • 0031773474 scopus 로고    scopus 로고
    • Preparation and assay of mammalian thioredoxin and thioredoxin reductase
    • Arnér ESJ, Zhong L, Holmgren A (1999) Preparation and assay of mammalian thioredoxin and thioredoxin reductase. Methods Enzymol 300:226–239
    • (1999) Methods Enzymol , vol.300 , pp. 226-239
    • Arnér, E.S.J.1    Zhong, L.2    Holmgren, A.3
  • 10
    • 0006895581 scopus 로고    scopus 로고
    • Measurement of thioredoxin and thioredoxin reductase
    • Maines M, Costa L, Reed D, Sassa S, Wiley, New York
    • Arnér ESJ, Holmgren A (2000) Measurement of thioredoxin and thioredoxin reductase. In: Maines M, Costa L, Reed D, Sassa S (eds) Current protocols in toxicology. Wiley, New York, pp 7.4.1–7.4.14
    • (2000) Current Protocols in Toxicology , pp. 1-7
    • Arnér, E.S.J.1    Holmgren, A.2
  • 11
    • 67349120863 scopus 로고    scopus 로고
    • Focus on mammalian thioredoxin reductases – important selenoproteins with versatile functions
    • Arnér ESJ (2009) Focus on mammalian thioredoxin reductases – important selenoproteins with versatile functions. Biochim Biophys Acta 1790:495–526
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 495-526
    • Arnér, E.S.J.1
  • 12
    • 0017653811 scopus 로고
    • Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction
    • Holmgren A (1977) Bovine thioredoxin system. Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction. J Biol Chem 252:4600–4606
    • (1977) J Biol Chem , vol.252 , pp. 4600-4606
    • Holmgren, A.1
  • 13
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action
    • Holmgren A (1979) Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J Biol Chem 254:9113–9119
    • (1979) J Biol Chem , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 14
    • 0018723651 scopus 로고
    • Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide
    • Holmgren A (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254:9627–9632
    • (1979) J Biol Chem , vol.254 , pp. 9627-9632
    • Holmgren, A.1
  • 15
    • 0036119837 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase: Preparation and inhibitor studies
    • Gromer S, Merkle H, Schirmer RH, Becker K (2002) Human placenta thioredoxin reductase: preparation and inhibitor studies. Methods Enzymol 347:382–394
    • (2002) Methods Enzymol , vol.347 , pp. 382-394
    • Gromer, S.1    Merkle, H.2    Schirmer, R.H.3    Becker, K.4
  • 16
    • 0032493647 scopus 로고    scopus 로고
    • Human placenta thioredoxin reductase: Isolation of the selenoen-zyme, steady state kinetics, and inhibition by therapeutic gold compounds
    • Gromer S, Arscott LD, Williams CH, Schirmer RH, Becker K (1998) Human placenta thioredoxin reductase: isolation of the selenoen-zyme, steady state kinetics, and inhibition by therapeutic gold compounds. J Biol Chem 273:20096–20101
    • (1998) J Biol Chem , vol.273 , pp. 20096-20101
    • Gromer, S.1    Arscott, L.D.2    Williams, C.H.3    Schirmer, R.H.4    Becker, K.5
  • 17
    • 0036119737 scopus 로고    scopus 로고
    • High-throughput 96-well microplate assays for determining specific activities of glutathione peroxidase and thioredoxin reductase
    • Smith AD, Levander OA (2002) High-throughput 96-well microplate assays for determining specific activities of glutathione peroxidase and thioredoxin reductase. Methods Enzymol 347:113–121
    • (2002) Methods Enzymol , vol.347 , pp. 113-121
    • Smith, A.D.1    Levander, O.A.2
  • 20
    • 84892924777 scopus 로고    scopus 로고
    • Activity assays of mammalian thioredoxin and thioredoxin reductase: Fluorescent disulfide substrates, mechanisms, and use with tissue samples
    • Montano SJ, Lu J, Gustafsson TN, Holmgren A (2014) Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples. Anal Biochem 449:139–146
    • (2014) Anal Biochem , vol.449 , pp. 139-146
    • Montano, S.J.1    Lu, J.2    Gustafsson, T.N.3    Holmgren, A.4
  • 21
    • 84990020613 scopus 로고    scopus 로고
    • A fast response and red emission probe for mammalian thioredoxin reductase
    • Ma H, Zhang J, Zhang Z, Liu Y, Fang J (2016) A fast response and red emission probe for mammalian thioredoxin reductase. Chem Commun (Camb) 52:12060–12063
    • (2016) Chem Commun (Camb) , vol.52 , pp. 12060-12063
    • Ma, H.1    Zhang, J.2    Zhang, Z.3    Liu, Y.4    Fang, J.5
  • 22
    • 84957580289 scopus 로고    scopus 로고
    • A small molecule probe reveals declined mitochondrial thioredoxin reductase activity in a Parkinson’s disease model
    • Liu Y, Ma H, Zhang L, Cui Y, Liu X, Fang J (2016) A small molecule probe reveals declined mitochondrial thioredoxin reductase activity in a Parkinson’s disease model. Chem Commun (Camb) 52:2296–2299
    • (2016) Chem Commun (Camb) , vol.52 , pp. 2296-2299
    • Liu, Y.1    Ma, H.2    Zhang, L.3    Cui, Y.4    Liu, X.5    Fang, J.6
  • 23
    • 84921523909 scopus 로고    scopus 로고
    • Selective selenol fluorescent probes: Design, synthesis, structural determinants, and biological applications
    • Zhang B, Ge C, Yao J, Liu Y, Xie H, Fang J (2015) Selective selenol fluorescent probes: design, synthesis, structural determinants, and biological applications. J Am Chem Soc 137:757–769
    • (2015) J am Chem Soc , vol.137 , pp. 757-769
    • Zhang, B.1    Ge, C.2    Yao, J.3    Liu, Y.4    Xie, H.5    Fang, J.6
  • 24
    • 84892164605 scopus 로고    scopus 로고
    • Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells
    • Zhang L, Duan D, Liu Y, Ge C, Cui X, Sun J, Fang J (2014) Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells. J Am Chem Soc 136:226–233
    • (2014) J am Chem Soc , vol.136 , pp. 226-233
    • Zhang, L.1    Duan, D.2    Liu, Y.3    Ge, C.4    Cui, X.5    Sun, J.6    Fang, J.7
  • 26
    • 84959322213 scopus 로고    scopus 로고
    • Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities
    • Xu J, Cheng Q, Arner ES (2016) Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities. Free Radic Biol Med 94:110–120
    • (2016) Free Radic Biol Med , vol.94 , pp. 110-120
    • Xu, J.1    Cheng, Q.2    Arner, E.S.3
  • 27
    • 0035865881 scopus 로고    scopus 로고
    • 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: Synthesis and correlation between redox cycling activities and in vitro cytotoxicity
    • Salmon-Chemin L, Buisine E, Yardley V, Kohler S, Debreu MA, Landry V, Sergheraert C, Croft SL, Krauth-Siegel RL, Davioud-Charvet E (2001) 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity. J Med Chem 44:548–565
    • (2001) J Med Chem , vol.44 , pp. 548-565
    • Salmon-Chemin, L.1    Buisine, E.2    Yardley, V.3    Kohler, S.4    Debreu, M.A.5    Landry, V.6    Sergheraert, C.7    Croft, S.L.8    Krauth-Siegel, R.L.9    Davioud-Charvet, E.10
  • 28
    • 44849125526 scopus 로고    scopus 로고
    • Cell death by SecTRAPs: Thioredoxin reductase as a prooxidant killer of cells
    • Anestal K, Prast-Nielsen S, Cenas N, Arner ES (2008) Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. PLoS One 3:e1846
    • (2008) Plos One , vol.3
    • Anestal, K.1    Prast-Nielsen, S.2    Cenas, N.3    Arner, E.S.4
  • 29
    • 1642535437 scopus 로고    scopus 로고
    • Interactions of quinones with thioredoxin reductase: A challenge to the antioxidant role of the mammalian selenoprotein
    • Cenas N, Nivinskas H, Anusevicius Z, Sarlaus-kas J, Lederer F, Arner ES (2004) Interactions of quinones with thioredoxin reductase: a challenge to the antioxidant role of the mammalian selenoprotein. J Biol Chem 279:2583–2592
    • (2004) J Biol Chem , vol.279 , pp. 2583-2592
    • Cenas, N.1    Nivinskas, H.2    Anusevicius, Z.3    Sarlaus-Kas, J.4    Lederer, F.5    Arner, E.S.6
  • 30
    • 84893484616 scopus 로고    scopus 로고
    • Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium?
    • Lothrop AP, Snider GW, Ruggles EL, Hondal RJ (2014) Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium? Biochemistry 53:554–565
    • (2014) Biochemistry , vol.53 , pp. 554-565
    • Lothrop, A.P.1    Snider, G.W.2    Ruggles, E.L.3    Hondal, R.J.4
  • 31
    • 84976615559 scopus 로고    scopus 로고
    • Thioredoxin reductase 1 suppresses adipocyte differentiation and insulin responsiveness
    • Peng X, Gimenez-Cassina A, Petrus P, Conrad M, Ryden M, Arner ES (2016) Thioredoxin reductase 1 suppresses adipocyte differentiation and insulin responsiveness. Sci Rep 6:28080
    • (2016) Sci Rep , vol.6
    • Peng, X.1    Gimenez-Cassina, A.2    Petrus, P.3    Conrad, M.4    Ryden, M.5    Arner, E.S.6
  • 32
    • 0027443868 scopus 로고
    • Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by seleno-diglutathione
    • Ren X, Bjornstedt M, Shen B, Ericson ML, Holmgren A (1993) Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by seleno-diglutathione. Biochemistry 32:9701–9708
    • (1993) Biochemistry , vol.32 , pp. 9701-9708
    • Ren, X.1    Bjornstedt, M.2    Shen, B.3    Ericson, M.L.4    Holmgren, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.