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Volumn 146, Issue 6, 2005, Pages 2531-2538

Minireview: Cellular redox state regulates hydroxysteroid dehydrogenase activity and intracellular hormone potency

Author keywords

[No Author keywords available]

Indexed keywords

11BETA HYDROXYSTEROID DEHYDROGENASE; 3ALPHA(OR 20BETA) HYDROXYSTEROID DEHYDROGENASE; HYDROXYSTEROID DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STEROID HORMONE; TESTOSTERONE 17BETA DEHYDROGENASE; TRANSCRIPTION FACTOR;

EID: 18844381164     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/en.2005-0061     Document Type: Short Survey
Times cited : (89)

References (48)
  • 1
    • 0014621744 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver
    • Veech RL, Eggleston LV, Krebs HA 1969 The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem J 115:609-619
    • (1969) Biochem J , vol.115 , pp. 609-619
    • Veech, R.L.1    Eggleston, L.V.2    Krebs, H.A.3
  • 2
    • 0141737064 scopus 로고    scopus 로고
    • + redox poise in Streptomyces coelicolor A3(2)
    • + redox poise in Streptomyces coelicolor A3(2). EMBO J 22:4856-4865
    • (2003) EMBO J , vol.22 , pp. 4856-4865
    • Brekasis, D.1    Paget, M.S.2
  • 6
    • 0344736867 scopus 로고    scopus 로고
    • Cortisol metabolism and visceral obesity: Role of 11β-hydroxysteroid dehydrogenase type I enzyme and reduced co-factor NADPH
    • Agarwal AK 2003 Cortisol metabolism and visceral obesity: role of 11β-hydroxysteroid dehydrogenase type I enzyme and reduced co-factor NADPH. Endocr Res 29:411-418
    • (2003) Endocr Res , vol.29 , pp. 411-418
    • Agarwal, A.K.1
  • 8
    • 0018385653 scopus 로고
    • A possible role for microsomal hexose-6-phosphate dehydrogenase in microsomal electron transport and mixed-function oxygenase activity
    • Stegeman JJ, Klotz AV 1979 A possible role for microsomal hexose-6-phosphate dehydrogenase in microsomal electron transport and mixed-function oxygenase activity. Biochem Biophys Res Commun 87:410-425
    • (1979) Biochem Biophys Res Commun , vol.87 , pp. 410-425
    • Stegeman, J.J.1    Klotz, A.V.2
  • 9
    • 0014082605 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver
    • Williamson DH, Lund P, Krebs HA 1967 The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 103:514-527
    • (1967) Biochem J , vol.103 , pp. 514-527
    • Williamson, D.H.1    Lund, P.2    Krebs, H.A.3
  • 11
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • Zhang Q, Piston DW, Goodman RH 2002 Regulation of corepressor function by nuclear NADH. Science 295:1895-1897
    • (2002) Science , vol.295 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 12
    • 0035997367 scopus 로고    scopus 로고
    • Metabolism and the control of circadian rhythms
    • Rutter J, Reick M, McKnight SL 2002 Metabolism and the control of circadian rhythms. Annu Rev Biochem 71:307-331
    • (2002) Annu Rev Biochem , vol.71 , pp. 307-331
    • Rutter, J.1    Reick, M.2    McKnight, S.L.3
  • 13
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • Rutter J, Reick M, Wu LC, McKnight SL 2001 Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 293:510-514
    • (2001) Science , vol.293 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 14
    • 18844367746 scopus 로고    scopus 로고
    • Minireview: Regulation of steroidogenesis by electron transfer
    • Miller WL 2005 Minireview: regulation of steroidogenesis by electron transfer. Endocrinology, 146:2544-2550
    • (2005) Endocrinology , vol.146 , pp. 2544-2550
    • Miller, W.L.1
  • 15
    • 0001772359 scopus 로고    scopus 로고
    • The principles, pathways, and enzymes of human steroidogenesis
    • DeGroot LJ, Jameson LJ, eds. Philadelphia: WB Saunders
    • Auchus RJ, Miller WL 2001 The principles, pathways, and enzymes of human steroidogenesis. In: DeGroot LJ, Jameson LJ, eds. Endocrinology. 4th ed. Philadelphia: WB Saunders; 1616-1631
    • (2001) Endocrinology. 4th Ed. , pp. 1616-1631
    • Auchus, R.J.1    Miller, W.L.2
  • 17
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3α, 20β- hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases
    • Ghosh D, Wawrzak Z, Weeks CM, Duax WL, Erman M 1994 The refined three-dimensional structure of 3α, 20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure 2:629-640
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 19
    • 13644269232 scopus 로고    scopus 로고
    • The crystal structure of guinea pig 11β-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions
    • Ogg D, Elleby B, Norstrom C, Stefansson K, Abrahmsen L, Oppermann U, Svensson S 2004 The crystal structure of guinea pig 11β-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions. J Biol Chem 280:3789-3794
    • (2004) J Biol Chem , vol.280 , pp. 3789-3794
    • Ogg, D.1    Elleby, B.2    Norstrom, C.3    Stefansson, K.4    Abrahmsen, L.5    Oppermann, U.6    Svensson, S.7
  • 20
    • 0035969891 scopus 로고    scopus 로고
    • The aldo-keto reductase (AKR) superfamily: An update
    • Jez JM, Penning TM 2001 The aldo-keto reductase (AKR) superfamily: an update. Chem Biol Interact 130-132:499-525
    • (2001) Chem Biol Interact , vol.130-132 , pp. 499-525
    • Jez, J.M.1    Penning, T.M.2
  • 21
    • 0028274855 scopus 로고
    • Three-dimensional structure of rat liver 3α-hydroxysteroid/ dihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily
    • Hoog SS, Pawlowski JE, Alzari PM, Penning TM, Lewis M 1994 Three-dimensional structure of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc Natl Acad Sci USA 91:2517-2521
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2517-2521
    • Hoog, S.S.1    Pawlowski, J.E.2    Alzari, P.M.3    Penning, T.M.4    Lewis, M.5
  • 23
    • 3042829462 scopus 로고    scopus 로고
    • Crystal structures of the multispecific 17β-hydroxysteroid dehydrogenase type 5: Critical androgen regulation in human peripheral tissues
    • Qiu W, Zhou M, Labrie F, Lin SX 2004 Crystal structures of the multispecific 17β-hydroxysteroid dehydrogenase type 5: critical androgen regulation in human peripheral tissues. Mol Endocrinol 18:1798-1807
    • (2004) Mol Endocrinol , vol.18 , pp. 1798-1807
    • Qiu, W.1    Zhou, M.2    Labrie, F.3    Lin, S.X.4
  • 24
    • 0029593494 scopus 로고
    • Characteristics of human types 1, 2 and 3 17β;-hydroxysteroid dehydrogenase activities: Oxidation/reduction and inhibition
    • Luu-The V, Zhang Y, Poirier D, Labrie F 1995 Characteristics of human types 1, 2 and 3 17β;-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition. J Steroid Biochem Mol Biol 55:581-587
    • (1995) J Steroid Biochem Mol Biol , vol.55 , pp. 581-587
    • Luu-The, V.1    Zhang, Y.2    Poirier, D.3    Labrie, F.4
  • 25
    • 0027225486 scopus 로고
    • Expression cloning and characterization of human 17β-hydrosteroid dehydrogenase type 2, a microsomal enzyme possessing 20α-hydroxysteroid dehydrogenase activity
    • Wu L, Einstein M, Geissler WM, Chan HK, Ellison KO, Andersson S 1993 Expression cloning and characterization of human 17β-hydrosteroid dehydrogenase type 2, a microsomal enzyme possessing 20α-hydroxysteroid dehydrogenase activity. J Biol Chem 268:12964-12969
    • (1993) J Biol Chem , vol.268 , pp. 12964-12969
    • Wu, L.1    Einstein, M.2    Geissler, W.M.3    Chan, H.K.4    Ellison, K.O.5    Andersson, S.6
  • 26
    • 0022845066 scopus 로고
    • Mechanism-based inactivation of 17β,20α-hydroxysteroid dehydrogenase by an acetylenic secoestradiol
    • Auchus RJ, Covey DF 1986 Mechanism-based inactivation of 17β,20α-hydroxysteroid dehydrogenase by an acetylenic secoestradiol. Biochemistry 25:7295-7300
    • (1986) Biochemistry , vol.25 , pp. 7295-7300
    • Auchus, R.J.1    Covey, D.F.2
  • 27
    • 3543068881 scopus 로고    scopus 로고
    • Human 17β-hydroxysteroid dehydrogenases types 1, 2, and 3 catalyze bi-directional equilibrium reactions, rather than unidirectional metabolism, in HEK-293 cells
    • Khan N, Sharma KK, Andersson S, Auchus RJ 2004 Human 17β- hydroxysteroid dehydrogenases types 1, 2, and 3 catalyze bi-directional equilibrium reactions, rather than unidirectional metabolism, in HEK-293 cells. Arch Biochem Biophys 429:50-59
    • (2004) Arch Biochem Biophys , vol.429 , pp. 50-59
    • Khan, N.1    Sharma, K.K.2    Andersson, S.3    Auchus, R.J.4
  • 28
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrufton NS, Berry A, Perham RN 1990 Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343:38-43
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrufton, N.S.1    Berry, A.2    Perham, R.N.3
  • 29
    • 0025989616 scopus 로고
    • Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase
    • Chen Z, Lee WR, Chang SH 1991 Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase. Eur J Biochem 202:263-267
    • (1991) Eur J Biochem , vol.202 , pp. 263-267
    • Chen, Z.1    Lee, W.R.2    Chang, S.H.3
  • 30
    • 0034749467 scopus 로고    scopus 로고
    • Critical residues for the specificity of cofactors and substrates in human estrogenic 17β-hydroxysteroid dehydrogenase 1: Variants designed from the three-dimensional structure of the enzyme
    • Huang YW, Pineau I, Chang HJ, Azzi A, Bellemare V, Laberge S, Lin SX 2001 Critical residues for the specificity of cofactors and substrates in human estrogenic 17β-hydroxysteroid dehydrogenase 1: variants designed from the three-dimensional structure of the enzyme. Mol Endocrinol 15:2010-2020
    • (2001) Mol Endocrinol , vol.15 , pp. 2010-2020
    • Huang, Y.W.1    Pineau, I.2    Chang, H.J.3    Azzi, A.4    Bellemare, V.5    Laberge, S.6    Lin, S.X.7
  • 32
    • 1242273808 scopus 로고    scopus 로고
    • Amino acid substitution of arginine 80 in 17β-hydroxysteroid dehydrogenase type 3 and its effect on NADPH cofactor binding and oxidation/reduction kinetics
    • McKeever BM, Hawkins BK, Geissler WM, Wu L, Sheridan RP, Mosley RT, Andersson S 2002 Amino acid substitution of arginine 80 in 17β- hydroxysteroid dehydrogenase type 3 and its effect on NADPH cofactor binding and oxidation/reduction kinetics. Biochim Biophys Acta 1601:29-37
    • (2002) Biochim Biophys Acta , vol.1601 , pp. 29-37
    • McKeever, B.M.1    Hawkins, B.K.2    Geissler, W.M.3    Wu, L.4    Sheridan, R.P.5    Mosley, R.T.6    Andersson, S.7
  • 33
    • 0041816090 scopus 로고    scopus 로고
    • Structure/function relationships responsible for coenzyme specificity and the isomerase activity of human type 1 3β-hydroxysteroid dehydrogenase/isomerase
    • Thomas JL, Duax WL, Addlagatta A, Brandt S, Fuller RR, Norris W 2003 Structure/function relationships responsible for coenzyme specificity and the isomerase activity of human type 1 3β-hydroxysteroid dehydrogenase/ isomerase. J Biol Chem 278:35483-35490
    • (2003) J Biol Chem , vol.278 , pp. 35483-35490
    • Thomas, J.L.1    Duax, W.L.2    Addlagatta, A.3    Brandt, S.4    Fuller, R.R.5    Norris, W.6
  • 34
    • 0030991226 scopus 로고    scopus 로고
    • Expression cloning and characterization of oxidative 17β- and 3α-hydroxysteroid dehydrogenases from rat and human prostate
    • Biswas MG, Russell DW 1997 Expression cloning and characterization of oxidative 17β- and 3α-hydroxysteroid dehydrogenases from rat and human prostate. J Biol Chem 272:15959-15966
    • (1997) J Biol Chem , vol.272 , pp. 15959-15966
    • Biswas, M.G.1    Russell, D.W.2
  • 35
    • 0035931118 scopus 로고    scopus 로고
    • 17β-Hydroxysteroid dehydrogenase type 9 and other short-chain dehydrogenases/reductases that catalyze retinoid, 17β- and 3α-hydroxysteroid metabolism
    • Napoli JL 2001 17β-Hydroxysteroid dehydrogenase type 9 and other short-chain dehydrogenases/reductases that catalyze retinoid, 17β- and 3α-hydroxysteroid metabolism. Mol Cell Endocrinol 171:103-109
    • (2001) Mol Cell Endocrinol , vol.171 , pp. 103-109
    • Napoli, J.L.1
  • 36
    • 0034703043 scopus 로고    scopus 로고
    • Molecular characterization of a first human 3(α→β)- hydroxysteroid epimerase
    • Huang XF, Luu-The V 2000 Molecular characterization of a first human 3(α→β)-hydroxysteroid epimerase. J Biol Chem 275:29452-29457
    • (2000) J Biol Chem , vol.275 , pp. 29452-29457
    • Huang, X.F.1    Luu-The, V.2
  • 37
    • 0033564742 scopus 로고    scopus 로고
    • The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase
    • Ratnam K, Ma H, Penning TM 1999 The arginine 276 anchor for NADP(H) dictates fluorescence kinetic transients in 3α-hydroxysteroid dehydrogenase, a representative aldo-keto reductase. Biochemistry 38:7856-7864
    • (1999) Biochemistry , vol.38 , pp. 7856-7864
    • Ratnam, K.1    Ma, H.2    Penning, T.M.3
  • 38
    • 4644346337 scopus 로고    scopus 로고
    • Dissection of the physiological interconversion of 5α-DHT and 3α-diol by rat 3α-HSD via transient kinetics shows that the chemical step is rate-determining: Effect of mutating cofactor and substrate-binding pocket residues on catalysis
    • Heredia VV, Penning TM 2004 Dissection of the physiological interconversion of 5α-DHT and 3α-diol by rat 3α-HSD via transient kinetics shows that the chemical step is rate-determining: effect of mutating cofactor and substrate-binding pocket residues on catalysis. Biochemistry 43:12028-12037
    • (2004) Biochemistry , vol.43 , pp. 12028-12037
    • Heredia, V.V.1    Penning, T.M.2
  • 39
    • 0031046241 scopus 로고    scopus 로고
    • 11β-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess
    • White PC, Mune T, Agarwal AK 1997 11β-Hydroxysteroid dehydrogenase and the syndrome of apparent mineralocorticoid excess. Endocr Rev 18:135-156
    • (1997) Endocr Rev , vol.18 , pp. 135-156
    • White, P.C.1    Mune, T.2    Agarwal, A.K.3
  • 40
    • 0025611952 scopus 로고
    • Expression of 11β-hydroxysteroid dehydrogenase using recombinant vaccinia virus
    • Agarwal AK, Tusie-Luna M-T, Monder C, White PC 1990 Expression of 11β-hydroxysteroid dehydrogenase using recombinant vaccinia virus. Mol Endocrinol 4:1827-1832
    • (1990) Mol Endocrinol , vol.4 , pp. 1827-1832
    • Agarwal, A.K.1    Tusie-Luna, M.-T.2    Monder, C.3    White, P.C.4
  • 41
    • 0035877598 scopus 로고    scopus 로고
    • Functional expression, characterization, and purification of the catalytic domain of human 11β-hydroxysteroid dehydrogenase type 1
    • Walker EA, Clark AM, Hewison M, Ride JP, Stewart PM 2001 Functional expression, characterization, and purification of the catalytic domain of human 11β-hydroxysteroid dehydrogenase type 1. J Biol Chem 276:21343-21350
    • (2001) J Biol Chem , vol.276 , pp. 21343-21350
    • Walker, E.A.1    Clark, A.M.2    Hewison, M.3    Ride, J.P.4    Stewart, P.M.5
  • 43
    • 2642663375 scopus 로고
    • Mechanism of inhibition of growth of 3T3-L1 fibroblasts and their differentiation to adipocytes by dehydroepiandrosterone and related steroids: Role of glucose-6-phosphate dehydrogenase
    • Shantz LM, Talalay P, Gordon GB 1989 Mechanism of inhibition of growth of 3T3-L1 fibroblasts and their differentiation to adipocytes by dehydroepiandrosterone and related steroids: role of glucose-6-phosphate dehydrogenase. Proc Natl Acad Sci USA 86:3852-3856
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3852-3856
    • Shantz, L.M.1    Talalay, P.2    Gordon, G.B.3
  • 46
    • 3042595899 scopus 로고    scopus 로고
    • Cooperativity between 11β-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase in the lumen of the endoplasmic reticulum
    • Banhegyi G, Benedetti A, Fulceri R, Senesi S 2004 Cooperativity between 11β-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase in the lumen of the endoplasmic reticulum. J Biol Chem 279:27017-27021
    • (2004) J Biol Chem , vol.279 , pp. 27017-27021
    • Banhegyi, G.1    Benedetti, A.2    Fulceri, R.3    Senesi, S.4
  • 47
    • 5344232041 scopus 로고    scopus 로고
    • Fluorescent proteins as sensors for cellular functions
    • Griesbeck O 2004 Fluorescent proteins as sensors for cellular functions. Curr Opin Neurobiol 14:636-641
    • (2004) Curr Opin Neurobiol , vol.14 , pp. 636-641
    • Griesbeck, O.1
  • 48


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