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Volumn 311, Issue 2, 2005, Pages 205-217

The C-terminal region of cis-retinol/androgen dehydrogenase 1 (CRAD1) confers ER localization and in vivo enzymatic function

Author keywords

ER; Metabolism; Retention; Retinol; Retinol dehydrogenase

Indexed keywords

RETINOIC ACID; RETINOID; RETINOL ANDROGEN DEHYDROGENASE 1; RETINOL DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 27744496116     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.07.032     Document Type: Article
Times cited : (6)

References (44)
  • 1
    • 0003634325 scopus 로고
    • Elsevier New York
    • T. Moore Vitamin A 1957 Elsevier New York
    • (1957) Vitamin a
    • Moore, T.1
  • 2
    • 0021258853 scopus 로고
    • Multiple functions of vitamin a
    • G. Wolf Multiple functions of vitamin A Physiol. Rev. 64 1984 873 937
    • (1984) Physiol. Rev. , vol.64 , pp. 873-937
    • Wolf, G.1
  • 4
    • 0033911401 scopus 로고    scopus 로고
    • Families of retinoid dehydrogenases regulating vitamin a function: Production of visual pigment and retinoic acid
    • G. Duester Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid Eur. J. Biochem. 267 2000 4315 4324
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4315-4324
    • Duester, G.1
  • 5
    • 0032831815 scopus 로고    scopus 로고
    • Interactions of retinoid binding proteins and enzymes in retinoid metabolism
    • J.L. Napoli Interactions of retinoid binding proteins and enzymes in retinoid metabolism Biochim. Biophys. Acta 1440 1999 139 162
    • (1999) Biochim. Biophys. Acta , vol.1440 , pp. 139-162
    • Napoli, J.L.1
  • 6
    • 0028816843 scopus 로고
    • The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases
    • A. Simon, U. Hellman, C. Wernstedt, and U. Eriksson The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases J. Biol. Chem. 270 1995 1107 1112
    • (1995) J. Biol. Chem. , vol.270 , pp. 1107-1112
    • Simon, A.1    Hellman, U.2    Wernstedt, C.3    Eriksson, U.4
  • 7
    • 0033033364 scopus 로고    scopus 로고
    • Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus
    • H. Yamamoto, A. Simon, U. Eriksson, E. Harris, E.L. Berson, and T.P. Dryja Mutations in the gene encoding 11-cis retinol dehydrogenase cause delayed dark adaptation and fundus albipunctatus Nat. Genet. 22 1999 188 191
    • (1999) Nat. Genet. , vol.22 , pp. 188-191
    • Yamamoto, H.1    Simon, A.2    Eriksson, U.3    Harris, E.4    Berson, E.L.5    Dryja, T.P.6
  • 8
    • 0032958632 scopus 로고    scopus 로고
    • Embryonic retinoic acid synthesis is essential for early mouse post-implantation development
    • K. Niederreither, V. Subbarayan, P. Dolle, and P. Chambon Embryonic retinoic acid synthesis is essential for early mouse post-implantation development Nat. Genet. 21 1999 444 448
    • (1999) Nat. Genet. , vol.21 , pp. 444-448
    • Niederreither, K.1    Subbarayan, V.2    Dolle, P.3    Chambon, P.4
  • 9
    • 0344630320 scopus 로고    scopus 로고
    • A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3 is prevented by maternal retinoic acid treatment
    • V. Dupe, N. Matt, J.M. Garnier, P. Chambon, M. Mark, and N.B. Ghyselinck A newborn lethal defect due to inactivation of retinaldehyde dehydrogenase type 3 is prevented by maternal retinoic acid treatment Proc. Natl. Acad. Sci. 100 2003 14036 14041
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 14036-14041
    • Dupe, V.1    Matt, N.2    Garnier, J.M.3    Chambon, P.4    Mark, M.5    Ghyselinck, N.B.6
  • 10
    • 0031435106 scopus 로고    scopus 로고
    • CDNA cloning and characterization of a cis-retinol/3-alpha-hydroxysterol short-chain dehydrogenase
    • X.Y. Chai, Y. Zhai, and J.L. Napoli cDNA cloning and characterization of a cis-retinol/3-alpha-hydroxysterol short-chain dehydrogenase J. Biol. Chem. 272 1997 33125 33131
    • (1997) J. Biol. Chem. , vol.272 , pp. 33125-33131
    • Chai, X.Y.1    Zhai, Y.2    Napoli, J.L.3
  • 11
    • 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
    • A. Simon, A. Romert, A.-L. Gustafsson, J.M. McCaffrey, and U. Eriksson 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 1999 549 558
    • (1999) J. Cell Sci. , vol.112 , pp. 549-558
    • Simon, A.1    Romert, A.2    Gustafsson, A.-L.3    McCaffrey, J.M.4    Eriksson, U.5
  • 12
    • 0035377196 scopus 로고    scopus 로고
    • Biosynthesis of 9-cis retinoic acid; The roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases
    • K. Tryggvason, A. Romert, and U. Eriksson Biosynthesis of 9-cis retinoic acid; the roles of different retinol dehydrogenases and a structure-activity analysis of microsomal retinol dehydrogenases J. Biol. Chem. 276 2001 19253 19258
    • (2001) J. Biol. Chem. , vol.276 , pp. 19253-19258
    • Tryggvason, K.1    Romert, A.2    Eriksson, U.3
  • 14
    • 0032504149 scopus 로고    scopus 로고
    • CDNA cloning, tissue distribution, and substrate characteristics of a cis-retinol/3 hydroxysterol short-chain dehydrogenase isozyme
    • J. Su, X. Chai, B. Kahn, and J.L. Napoli cDNA cloning, tissue distribution, and substrate characteristics of a cis-retinol/3 hydroxysterol short-chain dehydrogenase isozyme J. Biol. Chem. 273 1998 17910 17916
    • (1998) J. Biol. Chem. , vol.273 , pp. 17910-17916
    • Su, J.1    Chai, X.2    Kahn, B.3    Napoli, J.L.4
  • 15
    • 0032584601 scopus 로고    scopus 로고
    • CDNA cloning and characterization of a new human microsomal NAD(+)-dependent dehydrogenase that oxidizes all-trans-retinol and 3 alpha-hydroxysteroids
    • W.H. Gough, S. VanOoteghem, T. Sint, and N.Y. Kedishvili cDNA cloning and characterization of a new human microsomal NAD(+)-dependent dehydrogenase that oxidizes all-trans-retinol and 3 alpha-hydroxysteroids J. Biol. Chem. 273 1998 19778 19785
    • (1998) J. Biol. Chem. , vol.273 , pp. 19778-19785
    • Gough, W.H.1    Vanooteghem, S.2    Sint, T.3    Kedishvili, N.Y.4
  • 16
    • 0035966021 scopus 로고    scopus 로고
    • Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus
    • M. Lidén, A. Romert, K. Tryggvason, B. Persson, and U. Eriksson Biochemical defects in 11-cis-retinol dehydrogenase mutants associated with fundus albipunctatus J. Biol. Chem. 276 2001 49251 49257
    • (2001) J. Biol. Chem. , vol.276 , pp. 49251-49257
    • Lidén, M.1    Romert, A.2    Tryggvason, K.3    Persson, B.4    Eriksson, U.5
  • 17
    • 0032744250 scopus 로고    scopus 로고
    • A soluble NH(2)-terminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria(1)
    • E.P. Neve, and M. Ingelman-Sundberg A soluble NH(2)-terminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria(1) FEBS Lett. 460 1999 309 314
    • (1999) FEBS Lett. , vol.460 , pp. 309-314
    • Neve, E.P.1    Ingelman-Sundberg, M.2
  • 19
    • 0021796923 scopus 로고
    • Complement activation and attack on autologous cell membranes induced by streptolysin-O
    • S. Bhakdi, and J. Tranum-Jensen Complement activation and attack on autologous cell membranes induced by streptolysin-O Infect. Immun. 48 1985 713 719
    • (1985) Infect. Immun. , vol.48 , pp. 713-719
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 20
    • 0028037571 scopus 로고
    • The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum
    • J.C. Otto, and W.L. Smith The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum J. Biol. Chem. 269 1994 19868 19875
    • (1994) J. Biol. Chem. , vol.269 , pp. 19868-19875
    • Otto, J.C.1    Smith, W.L.2
  • 21
    • 0024720325 scopus 로고
    • The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity
    • M. Pinkney, E. Beachey, and M. Kehoe The thiol-activated toxin streptolysin O does not require a thiol group for cytolytic activity Infect. Immun. 57 1989 2553 2558
    • (1989) Infect. Immun. , vol.57 , pp. 2553-2558
    • Pinkney, M.1    Beachey, E.2    Kehoe, M.3
  • 22
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • K.J. Livak, and T.D. Schmittgen Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method Methods 25 2001 402 408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 23
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • T.A. Kunkel, J.D. Roberts, and R.A. Zakour Rapid and efficient site-specific mutagenesis without phenotypic selection Methods Enzymol. 154 1987 367 382
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 24
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • J. Vieira, and J. Messing Production of single-stranded plasmid DNA Meth. Enzymol. 153 1987 3 11
    • (1987) Meth. Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 26
    • 0023770976 scopus 로고
    • Signals for the incorporation and orientation of cytochrome P450 in the endoplasmic reticulum membrane
    • S. Monier, P. Van Luc, G. Kreibich, D.D. Sabatini, and M. Adesnik Signals for the incorporation and orientation of cytochrome P450 in the endoplasmic reticulum membrane J. Cell Biol. 107 1988 457 470
    • (1988) J. Cell Biol. , vol.107 , pp. 457-470
    • Monier, S.1    Van Luc, P.2    Kreibich, G.3    Sabatini, D.D.4    Adesnik, M.5
  • 27
    • 0022356559 scopus 로고
    • The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: A new member of the immunoglobulin gene family
    • P.J. Maddon, D.R. Littman, M. Godfrey, D.E. Maddon, L. Chess, and R. Axel The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family Cell 42 1985 93 104
    • (1985) Cell , vol.42 , pp. 93-104
    • Maddon, P.J.1    Littman, D.R.2    Godfrey, M.3    Maddon, D.E.4    Chess, L.5    Axel, R.6
  • 28
    • 0035934296 scopus 로고    scopus 로고
    • Structure, promoter and chromosomal localization of rdh6
    • X. Chai, W. Chen, and J.L. Napoli Structure, promoter and chromosomal localization of rdh6 Gene 274 2001 27 33
    • (2001) Gene , vol.274 , pp. 27-33
    • Chai, X.1    Chen, W.2    Napoli, J.L.3
  • 29
    • 3242878193 scopus 로고    scopus 로고
    • ECR Browser: A tool for visualizing and accessing data from comparisons of multiple vertebrate genomes
    • I. Ovcharenko, M.A. Nobrega, G.G. Loots, and L. Stubbs ECR Browser: a tool for visualizing and accessing data from comparisons of multiple vertebrate genomes Nucleic Acids Res. 32 2004 W280 W286
    • (2004) Nucleic Acids Res. , vol.32
    • Ovcharenko, I.1    Nobrega, M.A.2    Loots, G.G.3    Stubbs, L.4
  • 30
    • 4444232905 scopus 로고    scopus 로고
    • The unfolded protein response-A stress signaling pathway of the endoplasmic reticulum
    • X. Shen, K. Zhang, and R.J. Kaufman The unfolded protein response-A stress signaling pathway of the endoplasmic reticulum J. Chem. Neuroanat. 28 2004 79 92
    • (2004) J. Chem. Neuroanat. , vol.28 , pp. 79-92
    • Shen, X.1    Zhang, K.2    Kaufman, R.J.3
  • 31
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • T. Nilsson, M. Jackson, and P. Peterson Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum Cell 58 1989 707 718
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.3
  • 32
    • 0025808061 scopus 로고
    • Identification and partial characterization of a retinal pigment epithelial membrane receptor for plasma retinol-binding protein
    • C.-O. Båvik, U. Eriksson, R.A. Allen, and P.A. Peterson Identification and partial characterization of a retinal pigment epithelial membrane receptor for plasma retinol-binding protein J. Biol. Chem. 266 1991 14978 14985
    • (1991) J. Biol. Chem. , vol.266 , pp. 14978-14985
    • Båvik, C.-O.1    Eriksson, U.2    Allen, R.A.3    Peterson, P.A.4
  • 33
    • 0026446319 scopus 로고
    • Characterization of a plasma retinol-binding protein membrane receptor expressed in the retinal pigment epithelium
    • C.-O. Båvik, C. Busch, and U. Eriksson Characterization of a plasma retinol-binding protein membrane receptor expressed in the retinal pigment epithelium J. Biol. Chem. 267 1992 23035 23042
    • (1992) J. Biol. Chem. , vol.267 , pp. 23035-23042
    • Båvik, C.-O.1    Busch, C.2    Eriksson, U.3
  • 34
    • 0028900991 scopus 로고
    • Retinol-binding protein mediates uptake of retinol to human keratinocytes
    • C.-O. Båvik, P.A. Peterson, and U. Eriksson Retinol-binding protein mediates uptake of retinol to human keratinocytes Exp. Cell Res. 216 1995 358 362
    • (1995) Exp. Cell Res. , vol.216 , pp. 358-362
    • Båvik, C.-O.1    Peterson, P.A.2    Eriksson, U.3
  • 35
    • 0029081959 scopus 로고
    • Retinoids: Transport, metabolism, and mechanisms of action
    • A.V. Vieira, W.J. Schneider, and P.M. Vieira Retinoids: transport, metabolism, and mechanisms of action J. Endocrinol. 146 1995 201 207
    • (1995) J. Endocrinol. , vol.146 , pp. 201-207
    • Vieira, A.V.1    Schneider, W.J.2    Vieira, P.M.3
  • 36
    • 2942755631 scopus 로고    scopus 로고
    • Organelle identity and the organization of membrane traffic
    • S. Munro Organelle identity and the organization of membrane traffic Nat. Cell Biol. 6 2004 469 472
    • (2004) Nat. Cell Biol. , vol.6 , pp. 469-472
    • Munro, S.1
  • 37
    • 0037683407 scopus 로고    scopus 로고
    • Signals for COPII-dependent export from the ER: What's the ticket out?
    • C. Barlowe Signals for COPII-dependent export from the ER: what's the ticket out? Trends Cell Biol. 13 2003 295 300
    • (2003) Trends Cell Biol. , vol.13 , pp. 295-300
    • Barlowe, C.1
  • 38
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: Lipid rafts and intracellular trafficking
    • J.B. Helms, and C. Zurzolo Lipids as targeting signals: lipid rafts and intracellular trafficking Traffic 5 2004 247 254
    • (2004) Traffic , vol.5 , pp. 247-254
    • Helms, J.B.1    Zurzolo, C.2
  • 39
    • 0037469145 scopus 로고    scopus 로고
    • Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: Characterization of the holo-CRBP dehydrogenase activity of RoDH-4
    • E.A. Lapshina, O.V. Belyaeva, O.V. Chumakova, and N.Y. Kedishvili Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4 Biochemistry 42 2003 776 784
    • (2003) Biochemistry , vol.42 , pp. 776-784
    • Lapshina, E.A.1    Belyaeva, O.V.2    Chumakova, O.V.3    Kedishvili, N.Y.4
  • 40
    • 0035940448 scopus 로고    scopus 로고
    • The N-terminus of retinol dehydrogenase type 1 signals cytosolic orientation in the microsomal membrane
    • J. Wang, J.K. Bongianni, and J.L. Napoli The N-terminus of retinol dehydrogenase type 1 signals cytosolic orientation in the microsomal membrane Biochemistry 40 2001 12533 12540
    • (2001) Biochemistry , vol.40 , pp. 12533-12540
    • Wang, J.1    Bongianni, J.K.2    Napoli, J.L.3
  • 41
    • 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
    • M. Zhang, P. Hu, and J.L. Napoli 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. 2004 51482 51489
    • (2004) J. Biol. Chem. , pp. 51482-51489
    • Zhang, M.1    Hu, P.2    Napoli, J.L.3
  • 43
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • G. von Heijne, and Y. Gavel Topogenic signals in integral membrane proteins Eur. J. Biochem. 174 1988 671 678
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 44
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • M. Higy, T. Junne, and M. Spiess Topogenesis of membrane proteins at the endoplasmic reticulum Biochemistry 43 2004 12716 12722
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3


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