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Volumn 419, Issue 1, 2009, Pages 113-122

Characterization of key residues and membrane association domains in retinol dehydrogenase 10

Author keywords

All trans retinol (atROL); Retinoic acid; Retinol dehydrogenase 10 (RDH10); Retinol pigment epithelium (RPE); Visual cycle; Vitamin A

Indexed keywords

ALL-TRANS RETINOL (ATROL); RETINOIC ACID; RETINOL DEHYDROGENASE 10 (RDH10); RETINOL PIGMENT EPITHELIUM (RPE); VISUAL CYCLE; VITAMIN A;

EID: 62749091619     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080812     Document Type: Article
Times cited : (21)

References (57)
  • 1
    • 0032605231 scopus 로고    scopus 로고
    • Retinoids and mammalian development
    • Morriss-Kay, G. M. and Ward, S. J. (1999) Retinoids and mammalian development. Int. Rev. Cytol. 188, 73-131
    • (1999) Int. Rev. Cytol , vol.188 , pp. 73-131
    • Morriss-Kay, G.M.1    Ward, S.J.2
  • 2
    • 33745387612 scopus 로고    scopus 로고
    • Overview of retinoid metabolism and function
    • Blomhoff, R. and Blomhoff, H. K. (2006) Overview of retinoid metabolism and function. J. Neurobiol. 66, 606-630
    • (2006) J. Neurobiol , vol.66 , pp. 606-630
    • Blomhoff, R.1    Blomhoff, H.K.2
  • 3
    • 0027995188 scopus 로고
    • Retinoic acid receptors and cellular retinoid binding proteins: Complex interplay in retinoid signaling
    • Giguere, V. (1994) Retinoic acid receptors and cellular retinoid binding proteins: complex interplay in retinoid signaling. Endocr. Rev. 15, 61-79
    • (1994) Endocr. Rev , vol.15 , pp. 61-79
    • Giguere, V.1
  • 5
    • 0000430527 scopus 로고
    • Bridges, C. D. B, ed, Springer, Berlin
    • Bridges, C. D. B. (ed.) (1972) The Rhodopsin-Porphyropsin System, Springer, Berlin
    • (1972) The Rhodopsin-Porphyropsin System
  • 6
    • 0034982559 scopus 로고    scopus 로고
    • Confronting complexity: The interlink of phototransduction and retinoid metabolism in the vertebrate retina
    • McBee, J. K., Palczewski, K., Baehr, W. and Pepperberg, D. R. (2001) Confronting complexity: the interlink of phototransduction and retinoid metabolism in the vertebrate retina. Prog. Retin. Eye Res. 20, 469-529
    • (2001) Prog. Retin. Eye Res , vol.20 , pp. 469-529
    • McBee, J.K.1    Palczewski, K.2    Baehr, W.3    Pepperberg, D.R.4
  • 7
    • 0035385140 scopus 로고    scopus 로고
    • The biochemistry of the visual cycle
    • Rando, R. R. (2001) The biochemistry of the visual cycle. Chem. Rev. 101, 1881-1896
    • (2001) Chem. Rev , vol.101 , pp. 1881-1896
    • Rando, R.R.1
  • 8
    • 0043201078 scopus 로고    scopus 로고
    • Vitamin A metabolism in the retinal pigment epithelium: Genes, mutations, and diseases
    • Thompson, D. A. and Gal, A. (2003) Vitamin A metabolism in the retinal pigment epithelium: genes, mutations, and diseases. Prog. Retin. Eye Res. 22, 683-703
    • (2003) Prog. Retin. Eye Res , vol.22 , pp. 683-703
    • Thompson, D.A.1    Gal, A.2
  • 11
    • 33744950570 scopus 로고    scopus 로고
    • Understanding retinol metabolism: Structure and function of retinol dehydrogenases
    • Liden, M. and Eriksson, U. (2006) Understanding retinol metabolism: structure and function of retinol dehydrogenases. J. Biol. Chem. 281, 13001-13004
    • (2006) J. Biol. Chem , vol.281 , pp. 13001-13004
    • Liden, M.1    Eriksson, U.2
  • 12
    • 0033911401 scopus 로고    scopus 로고
    • Families of retinoid dehydrogenases regulating vitamin A function: Production of visual pigment and retinoic acid
    • Duester, G. (2000) Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid. Eur. J. Biochem. 267, 4315-4324
    • (2000) Eur. J. Biochem , vol.267 , pp. 4315-4324
    • Duester, G.1
  • 13
    • 33751030498 scopus 로고    scopus 로고
    • Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity
    • Belyaeva, O. V. and Kedishvili, N. Y. (2006) Comparative genomic and phylogenetic analysis of short-chain dehydrogenases/reductases with dual retinol/sterol substrate specificity. Genomics 88, 820-830
    • (2006) Genomics , vol.88 , pp. 820-830
    • Belyaeva, O.V.1    Kedishvili, N.Y.2
  • 14
    • 0029778148 scopus 로고    scopus 로고
    • Involvement of alcohol dehydrogenase, short-chain dehydrogenase/reductase, aldehyde dehydrogenase, and cytochrome P450 in the control of retinoid signaling by activation of retinoic acid synthesis
    • Duester, G. (1996) Involvement of alcohol dehydrogenase, short-chain dehydrogenase/reductase, aldehyde dehydrogenase, and cytochrome P450 in the control of retinoid signaling by activation of retinoic acid synthesis. Biochemistry 35, 12221-12227
    • (1996) Biochemistry , vol.35 , pp. 12221-12227
    • Duester, G.1
  • 15
    • 58149133711 scopus 로고    scopus 로고
    • The SDR superfamily: Functional and structural diversity within a family of metabolic and regulatory enzymes
    • Kavanagh, K. L., Jornvall, H., Persson, B. and Oppermann, U. (2008) The SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes. Cell. Mol. Life Sci. 65, 3895-3906
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 3895-3906
    • Kavanagh, K.L.1    Jornvall, H.2    Persson, B.3    Oppermann, U.4
  • 16
    • 0030878052 scopus 로고    scopus 로고
    • Drosophila alcohol dehydrogenase: Evaluation of Ser139 site-directed mutants
    • Cols, N., Atrian, S., Benach, J., Ladenstein, R. and Gonzalez-Duarte, R. (1997) Drosophila alcohol dehydrogenase: evaluation of Ser139 site-directed mutants. FEBS Lett. 413, 191-193
    • (1997) FEBS Lett , vol.413 , pp. 191-193
    • Cols, N.1    Atrian, S.2    Benach, J.3    Ladenstein, R.4    Gonzalez-Duarte, R.5
  • 18
    • 0031021249 scopus 로고    scopus 로고
    • Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions
    • Oppermann, U. C., Filling, C., Berndt, K. D., Persson, B., Benach, J., Ladenstein, R. and Jornvall, H. (1997) Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions. Biochemistry 36, 34-40
    • (1997) Biochemistry , vol.36 , pp. 34-40
    • Oppermann, U.C.1    Filling, C.2    Berndt, K.D.3    Persson, B.4    Benach, J.5    Ladenstein, R.6    Jornvall, H.7
  • 19
    • 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, Y. W., Pineau, I., Chang, H. J., Azzi, A., Bellemare, V., Laberge, S. and Lin, S. X. (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
  • 20
    • 0027309435 scopus 로고
    • Site-specific mutagenesis of Drosophila alcohol dehydrogenase: Evidence for involvement of tyrosine-152 and lysine-156 in catalysis
    • Chen, Z., Jiang, J. C., Lin, Z. G., Lee, W. R., Baker, M. E. and Chang, S. H. (1993) Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Biochemistry 32, 3342-3346
    • (1993) Biochemistry , vol.32 , pp. 3342-3346
    • Chen, Z.1    Jiang, J.C.2    Lin, Z.G.3    Lee, W.R.4    Baker, M.E.5    Chang, S.H.6
  • 21
    • 0027959919 scopus 로고
    • Site-directed mutagenesis of the putative active site of human 17β-hydroxysteroid dehydrogenase type 1
    • Puranen, T. J., Poutanen, M. H., Peltoketo, H. E., Vihko, P. T. and Vihko, R. K. (1994) Site-directed mutagenesis of the putative active site of human 17β-hydroxysteroid dehydrogenase type 1. Biochem. J. 304, 289-293
    • (1994) Biochem. J , vol.304 , pp. 289-293
    • Puranen, T.J.1    Poutanen, M.H.2    Peltoketo, H.E.3    Vihko, P.T.4    Vihko, R.K.5
  • 22
    • 0031027687 scopus 로고    scopus 로고
    • Characterization of structural and functional properties of human 17β-hydroxysteroid dehydrogenase type 1 using recombinant enzymes and site-directed mutagenesis
    • Puranen, T., Poutanen, M., Ghosh, D., Vihko, P. and Vihko, R. (1997) Characterization of structural and functional properties of human 17β-hydroxysteroid dehydrogenase type 1 using recombinant enzymes and site-directed mutagenesis. Mol. Endocrinol. 11, 77-86
    • (1997) Mol. Endocrinol , vol.11 , pp. 77-86
    • Puranen, T.1    Poutanen, M.2    Ghosh, D.3    Vihko, P.4    Vihko, R.5
  • 23
    • 0026445622 scopus 로고
    • Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase
    • Obeid, J. and White, P. C. (1992) Tyr-179 and Lys-183 are essential for enzymatic activity of 11β-hydroxysteroid dehydrogenase. Biochem. Biophys. Res. Commun. 188, 222-227
    • (1992) Biochem. Biophys. Res. Commun , vol.188 , pp. 222-227
    • Obeid, J.1    White, P.C.2
  • 24
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution
    • Benach, J., Atrian, S., Gonzalez-Duarte, R. and Ladenstein, R. (1998) The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution. J. Mol. Biol. 282, 383-399
    • (1998) J. Mol. Biol , vol.282 , pp. 383-399
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 26
    • 0037126640 scopus 로고    scopus 로고
    • Structure of bacterial 3β/17β-hydroxysteroid dehydrogenase at 1.2 Å resolution: A model for multiple steroid recognition
    • Benach, J., Filling, C., Oppermann, U. C., Roversi, P., Bricogne, G., Berndt, K. D., Jornvall, H. and Ladenstein, R. (2002) Structure of bacterial 3β/17β-hydroxysteroid dehydrogenase at 1.2 Å resolution: a model for multiple steroid recognition. Biochemistry 41, 14659-14668
    • (2002) Biochemistry , vol.41 , pp. 14659-14668
    • Benach, J.1    Filling, C.2    Oppermann, U.C.3    Roversi, P.4    Bricogne, G.5    Berndt, K.D.6    Jornvall, H.7    Ladenstein, R.8
  • 27
    • 33644989471 scopus 로고    scopus 로고
    • Structure and function of human 17β-hydroxysteroid dehydrogenases
    • Lukacik, P., Kavanagh, K. L. and Oppermann, U. (2006) Structure and function of human 17β-hydroxysteroid dehydrogenases. Mol. Cell. Endocrinol. 248, 61-71
    • (2006) Mol. Cell. Endocrinol , vol.248 , pp. 61-71
    • Lukacik, P.1    Kavanagh, K.L.2    Oppermann, U.3
  • 29
    • 0025989616 scopus 로고
    • Role of aspartic acid 38 in the cofactor specificity of Drosophila alcohol dehydrogenase
    • Chen, Z., Lee, W. R. and Chang, S. H. (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
  • 33
    • 0345411950 scopus 로고    scopus 로고
    • Rational proteomics I. Fingerprint identification and cofactor specificity in the short-chain oxidoreductase (SCOR) enzyme family
    • Duax, W. L., Pletnev, V., Addlagatta, A., Bruenn, J. and Weeks, C. M. (2003) Rational proteomics I. Fingerprint identification and cofactor specificity in the short-chain oxidoreductase (SCOR) enzyme family. Proteins 53, 931-943
    • (2003) Proteins , vol.53 , pp. 931-943
    • Duax, W.L.1    Pletnev, V.2    Addlagatta, A.3    Bruenn, J.4    Weeks, C.M.5
  • 35
    • 0033004738 scopus 로고    scopus 로고
    • Intracellular localization and membrane topology of 11-cis-retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis- retinaldehyde
    • Simon, A., Romert, A., Gustafson, A. L., McCaffery, J. M. and Eriksson, U. (1999) Intracellular localization and membrane topology of 11-cis-retinol dehydrogenase in the retinal pigment epithelium suggest a compartmentalized synthesis of 11-cis- retinaldehyde. J. Cell Sci. 112, 549-558
    • (1999) J. Cell Sci , vol.112 , pp. 549-558
    • Simon, A.1    Romert, A.2    Gustafson, A.L.3    McCaffery, J.M.4    Eriksson, U.5
  • 36
    • 27744496116 scopus 로고    scopus 로고
    • The C-terminal region of cis-retinol/androgen dehydrogenase 1 (CRAD1) confers ER localization and in vivo enzymatic function
    • Liden, M., Tryggvason, K. and Eriksson, U. (2005) The C-terminal region of cis-retinol/androgen dehydrogenase 1 (CRAD1) confers ER localization and in vivo enzymatic function. Exp. Cell Res. 311, 205-217
    • (2005) Exp. Cell Res , vol.311 , pp. 205-217
    • Liden, M.1    Tryggvason, K.2    Eriksson, U.3
  • 37
    • 11144337677 scopus 로고    scopus 로고
    • Elements in the N-terminal signaling sequence that determine cytosolic topology of short-chain dehydrogenases/reductases. Studies with retinol dehydrogenase type 1 and cis-retinol/androgen dehydrogenase type 1
    • Zhang, M., Hu, P. and Napoli, J. L. (2004) Elements in the N-terminal signaling sequence that determine cytosolic topology of short-chain dehydrogenases/reductases. Studies with retinol dehydrogenase type 1 and cis-retinol/androgen dehydrogenase type 1. J. Biol. Chem. 279, 51482-51489
    • (2004) J. Biol. Chem , vol.279 , pp. 51482-51489
    • Zhang, M.1    Hu, P.2    Napoli, J.L.3
  • 38
    • 37349084165 scopus 로고    scopus 로고
    • Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity
    • Belyaeva, O. V., Korkina, O. V., Stetsenko, A. V. and Kedishvili, N. Y. (2008) Human retinol dehydrogenase 13 (RDH13) is a mitochondrial short-chain dehydrogenase/reductase with a retinaldehyde reductase activity. FEBS J. 275, 138-147
    • (2008) FEBS J , vol.275 , pp. 138-147
    • Belyaeva, O.V.1    Korkina, O.V.2    Stetsenko, A.V.3    Kedishvili, N.Y.4
  • 39
    • 34447340649 scopus 로고    scopus 로고
    • Analysis of the NADH-dependent retinaldehyde reductase activity of amphioxus retinol dehydrogenase enzymes enhances our understanding of the evolution of the retinol dehydrogenase family
    • Dalfo, D., Marques, N. and Albalat, R. (2007) Analysis of the NADH-dependent retinaldehyde reductase activity of amphioxus retinol dehydrogenase enzymes enhances our understanding of the evolution of the retinol dehydrogenase family. FEBS J. 274, 3739-3752
    • (2007) FEBS J , vol.274 , pp. 3739-3752
    • Dalfo, D.1    Marques, N.2    Albalat, R.3
  • 40
    • 0036845581 scopus 로고    scopus 로고
    • Cloning and characterization of a novel all-trans-retinol short-chain dehydrogenase/reductase from the RPE
    • Wu, B. X., Chen, Y., Fan, J., Rohrer, B., Crouch, R. K. and Ma, J. X. (2002) Cloning and characterization of a novel all-trans-retinol short-chain dehydrogenase/reductase from the RPE. Invest. Ophthalmol. Vis. Sci. 43, 3365-3372
    • (2002) Invest. Ophthalmol. Vis. Sci , vol.43 , pp. 3365-3372
    • Wu, B.X.1    Chen, Y.2    Fan, J.3    Rohrer, B.4    Crouch, R.K.5    Ma, J.X.6
  • 41
    • 23944508500 scopus 로고    scopus 로고
    • Transcriptome analysis of the murine forelimb and hindlimb autopod
    • Shou, S., Scott, V., Reed, C., Hitzemann, R. and Stadler, H. S. (2005) Transcriptome analysis of the murine forelimb and hindlimb autopod. Dev. Dyn. 234, 74-89
    • (2005) Dev. Dyn , vol.234 , pp. 74-89
    • Shou, S.1    Scott, V.2    Reed, C.3    Hitzemann, R.4    Stadler, H.S.5
  • 43
    • 35349027768 scopus 로고    scopus 로고
    • Expression of the murine retinol dehydrogenase 10 (Rdh10) gene correlates with many sites of retinoid signalling during embryogenesis and organ differentiation
    • Cammas, L., Romand, R., Fraulob, V., Mura, C. and Dolle, P. (2007) Expression of the murine retinol dehydrogenase 10 (Rdh10) gene correlates with many sites of retinoid signalling during embryogenesis and organ differentiation. Dev. Dyn. 236, 2899-2908
    • (2007) Dev. Dyn , vol.236 , pp. 2899-2908
    • Cammas, L.1    Romand, R.2    Fraulob, V.3    Mura, C.4    Dolle, P.5
  • 44
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 45
    • 6944248900 scopus 로고    scopus 로고
    • Identification of RDH10, an all-trans-retinol dehydrogenase, in retinal Muller cells
    • Wu, B. X., Moiseyev, G., Chen, Y., Rohrer, B., Crouch, R. K. and Ma, J. X. (2004) Identification of RDH10, an all-trans-retinol dehydrogenase, in retinal Muller cells. Invest. Ophthalmol. Vis. Sci. 45, 3857-3862
    • (2004) Invest. Ophthalmol. Vis. Sci , vol.45 , pp. 3857-3862
    • Wu, B.X.1    Moiseyev, G.2    Chen, Y.3    Rohrer, B.4    Crouch, R.K.5    Ma, J.X.6
  • 46
    • 0346365098 scopus 로고    scopus 로고
    • Properties of short-chain dehydrogenase/reductase RalR1: Characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines
    • Belyaeva, O. V., Stetsenko, A. V., Nelson, P. and Kedishvili, N. Y. (2003) Properties of short-chain dehydrogenase/reductase RalR1: characterization of purified enzyme, its orientation in the microsomal membrane, and distribution in human tissues and cell lines. Biochemistry 42, 14838-14845
    • (2003) Biochemistry , vol.42 , pp. 14838-14845
    • Belyaeva, O.V.1    Stetsenko, A.V.2    Nelson, P.3    Kedishvili, N.Y.4
  • 47
    • 18244398944 scopus 로고    scopus 로고
    • Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): Catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids
    • Belyaeva, O. V., Korkina, O. V., Stetsenko, A. V., Kim, T., Nelson, P. S. and Kedishvili, N. Y. (2005) Biochemical properties of purified human retinol dehydrogenase 12 (RDH12): catalytic efficiency toward retinoids and C9 aldehydes and effects of cellular retinol-binding protein type I (CRBPI) and cellular retinaldehyde-binding protein (CRALBP) on the oxidation and reduction of retinoids. Biochemistry 44, 7035-7047
    • (2005) Biochemistry , vol.44 , pp. 7035-7047
    • Belyaeva, O.V.1    Korkina, O.V.2    Stetsenko, A.V.3    Kim, T.4    Nelson, P.S.5    Kedishvili, N.Y.6
  • 48
    • 0028917903 scopus 로고
    • Cloning of a cDNA for liver microsomal retinol dehydrogenase. A tissue-specific, short-chain alcohol dehydrogenase
    • Chai, X., Boerman, M. H., Zhai, Y. and Napoli, J. L. (1995) Cloning of a cDNA for liver microsomal retinol dehydrogenase. A tissue-specific, short-chain alcohol dehydrogenase. J. Biol. Chem. 270, 3900-3904
    • (1995) J. Biol. Chem , vol.270 , pp. 3900-3904
    • Chai, X.1    Boerman, M.H.2    Zhai, Y.3    Napoli, J.L.4
  • 49
    • 0028790334 scopus 로고
    • Cloning of a cDNA for a second retinol dehydrogenase type II. Expression of its mRNA relative to type I
    • Chai, X., Zhai, Y., Popescu, G. and Napoli, J. L. (1995) Cloning of a cDNA for a second retinol dehydrogenase type II. Expression of its mRNA relative to type I. J. Biol. Chem. 270, 28408-28412
    • (1995) J. Biol. Chem , vol.270 , pp. 28408-28412
    • Chai, X.1    Zhai, Y.2    Popescu, G.3    Napoli, J.L.4
  • 51
    • 0025166586 scopus 로고
    • Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase
    • Chen, Z., Lu, L., Shirley, M., Lee, W. R. and Chang, S. H. (1990) Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase. Biochemistry 29, 1112-1118
    • (1990) Biochemistry , vol.29 , pp. 1112-1118
    • Chen, Z.1    Lu, L.2    Shirley, M.3    Lee, W.R.4    Chang, S.H.5


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