Scientific
Retinol Dehydrogenases Editor’s

Recent update from: 25.04.2005
RDH,
Notes

  • Membrane associated
  • Utilizes NADP and NAD
  • Catalyses the limiting step in the visual cycle: atRAl to atRol due to accumulation of atRAl in mice exposed to constant light
Species:
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (8)


RDH,
Notes

  • All-trans-RDH in ROS completes Rho quenching
  • Starts regeneration of visual pigments
  • atRAl -> at Rol
  • Diffuses across the ROS-membrane -> IPS and binds to IRBP
  • Reaction rate is very slow, takes minutes
Species: Bos taurus
See also: RDH
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (7)


RDH,
Notes

  • Expressed in bovine retinal pigment epithelium
  • Membrane-bound stereospecific 11-cis-RDH
  • NADH+ as cofactor
  • Integral membrane protein
  • Short chain alcohol DH catalyses the final step in 11cRoldehyde biosynthesis
Species: Bos taurus
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (11)


RDH,
Notes

  • Membrane bound enzyme abundant in RPE
  • 91% identity to bovine
  • Catalyses 11cRol to 11cRAl oxidation
  • Spans 4,1 kb of genome
Species: Homo sapiens
See also:
Chromosomal localisation in man: 12q13-14

in mouse:
Gene Data
mRNA: 1348 bp
Exons: 5
Primers:
Protein Data
Amino acids: 318 AA
Molecular weight on SDS-PAGE: 32 kDa

calculated:
Reference: (12)


RDH, all-trans-RDH Notes

  • NADPH as cofactor
  • Expression in retina (PIS, INL, COS!, no ROS), kidney, liver, lung, placenta
  • Prefers atRal as substrate
  • Belongs to SDR family
  • RDH : RHO very low
  • Cone specific
Species: Homo sapiens
See also:
Chromosomal localisation in man: 1p36.1

in mouse:
Gene Data
mRNA: 1.8 kb
Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (2)


Rdh10, all-trans-RDH Notes

  • Restricted to bovine RPE
Species: Bos taurus
See also:
Chromosomal localisation in man:

in mouse:
Gene Data
mRNA: 3 kb
Exons:
Primers:
Protein Data
Amino acids: 341 AA
Molecular weight on SDS-PAGE:

calculated:
Reference: (15)


RDH10,
Notes

Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (9)


RDH10, all-trans-RDH Notes

  • 100% and 98% identity to bovine and mouse RDH10
  • Predominantly expressed in the microsomal fraction of RPE
  • Oxidizes atRol to atRAl
  • NADP is preferred
  • IP: 7.35
  • No IR in cytosol
  • Membrane-bound activity
Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids: 341 AA
Molecular weight on SDS-PAGE: 38 kDa

calculated:
Reference: (15)


Rdh10, all-trans-RDH Notes

Species: Mus musculus
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids: 341 AA
Molecular weight on SDS-PAGE:

calculated:
Reference: (15)


rdh11, all-trans/11-cis RDH Notes

  • Immunolocalization in RPE and Müller cells
Species: Bos taurus
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (3)


RDH11, all-trans/11-cis RDH Notes

  • In RPE cells
  • Equal to PSDR1
  • Expressed abundantly in prostate tissue but also in eye, kidney, pancreas, liver, testis, heart, and brain
  • ~30 kb from rdh12
  • Reaction catalyzed in both directions
Species: Homo sapiens
See also:
Chromosomal localisation in man: 14q23.3

in mouse:
Gene Data
gDNA: 13-18 kb
Exons: 7
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (3)


RDH11,
Notes

Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (9)


RDH12, all-trans/11-cis RDH Notes

  • In photoreceptors
  • SDR-specific motifs
    • Cofactor-binding site (GXXXGXG)
    • catalytic residues (YXXXK)
  • Preference for NADP/NADPH indicated
  • ESTs mostly in eye, but also in kidney, brain, skeletal muscle, and stomach
  • Reaction catalyzed in both directions
Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data
gDNA: 13-18 kb
Exons: 7
Primers:
Protein Data
Amino acids: 316
Molecular weight on SDS-PAGE: 35 kDa

calculated:
Reference: (3)


RDH12,
Notes

  • Photorezeptor-specific
Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (9)


RDH12,
Notes

  • NADPH is cofactor
  • Conversion of 11-cis and all-trans retinal to retinol and vice versa
Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (5)


rdh12, all-trans/11-cis RDH Notes

  • mRNA in-situ hybridization revealed localization in PIS
Species: Monkey
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (3)


rdh12, all-trans/11-cis RDH Notes

  • BALB/c: no signal on in-situ mRNA Hybrifization in RPE
Species: Mus musculus
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (3)


RDH13,
Notes

  • Photorezeptor-specific
Species: Homo sapiens
See also:
Chromosomal localisation in man:

in mouse:
Gene Data

Exons:
Primers:
Protein Data
Amino acids:
Molecular weight on SDS-PAGE:

calculated:
Reference: (9)


RDH13, all-trans/11-cis RDH Notes

  • Preference for NADP/NADPH indicated
  • SDR-specific motifs<(UL>
  • Cofactor-binding site (GXXXGXG)
  • catalytic residues (YXXXK)
  • ESTs mostly in eye, pancreas, placenta, and lung
  • Immunolocalization in PIS
  • Reaction catalyzed in both directions
  • Species: Homo sapiens
    See also:
    Chromosomal localisation in man: 19q13.42

    in mouse:
    Gene Data
    gDNA: 13-18 kb
    Exons: 7
    Primers:
    Protein Data
    Amino acids: 316
    Molecular weight on SDS-PAGE: 36 kDa

    calculated:
    Reference: (3)


    rdh14, all-trans/11-cis RDH Notes

    • Immunolaclization in PNL, COS, and ROS, Müller cells
    Species: Bos taurus
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids: 336
    Molecular weight on SDS-PAGE: 37 kDa

    calculated:
    Reference: (3)


    RDH14,
    Notes

    • Photorezeptor-specific
    Species: Homo sapiens
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE:

    calculated:
    Reference: (9)


    RDH14, all-trans/11-cis RDH Notes

    • Preference for NADP/NADPH indicated
    • SDR-specific motifs<(UL>
    • Cofactor-binding site (GXXXGXG)
    • catalytic residues (YXXXK)
  • Many ESTs in brain, kidney, pancreas, and placenta
  • Minor component of retinal retinoid metabolism
  • Reaction catalyzed in both directions
  • Species: Homo sapiens
    See also:
    Chromosomal localisation in man: 2p24.1

    in mouse:
    Gene Data
    gDNA: 6 kb
    Exons: 2
    Primers:
    Protein Data
    Amino acids: 336
    Molecular weight on SDS-PAGE: 37 kDa

    calculated:
    Reference: (3)


    RDH5,
    Notes

    • Abundantly expressed in RPE
    • N-terminal hydrophobic putative signal sequence mediating cotranslational translocation of parts into ER lumen
    • Major part of RDH is confined to the lumenal aspect of microsomal membranes
    • Membrane topology is intrinsic
    • Lumenal orientation of catalytic domain
    Species: Bos taurus
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE:

    calculated:
    Reference: (13)


    RDH5, 11-cis-RDH Notes

    • Identical expression in RPE and IPE
    Species: Bos taurus
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE:

    calculated:
    Reference: (14)


    RDH5, 11-cis-RDH Notes

    • Pronounced activity with ER and PM preparations
    • Activity depends on the interaction with other RAl-binding proteins
    Species: Bos taurus
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE:

    calculated:
    Reference: (6)


    RDH5,
    Notes

    • Copurifies with RGR from RPE microsomes
    • Prefers NADH as ion source
    • Does not react with atRAl but with RGR product 11cRAl
    • Reduction of 11cRAl to 11cRol enhances net photoisomerization of RGR
    • Catalytic domain is oriented towards the lumen of RPE smooth ER
    Species: Bos taurus
    See also: RGR
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE: 32 kDa

    calculated:
    Reference: (1)


    RDH8, all-trans RDH Notes

    • Visual cycle enzyme
    • Identification of flanlking SNPs
    Species: Homo sapiens
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids: 318 AA
    Molecular weight on SDS-PAGE: 32 kDa

    calculated:
    Reference: (4)


    RDH8, all-trans RDH Notes

    • Visual cycle enzyme
    • In POS tightly associated with plasmamembrane
    • Utilizes NADPH
    • all-trans-preference
    • In rods and cones
    • Includes invariant YXXXK motif containing the catalytic residue (TYR155)
    • Highly conserved nucleotide-binding factor motif GXXXGXG at AA12-18
    • single copy gene
    Species: Homo sapiens
    See also:
    Chromosomal localisation in man: 19p13

    in mouse:
    Gene Data
    mRNA: 1.8-2.1-3.4 kb
    Exons: 6
    Primers:
    Protein Data
    Amino acids: 318 AA
    Molecular weight on SDS-PAGE: 32 kDa

    calculated:
    Reference: (10)


    RDH8, all-trans RDH Notes

    • SDR
    • Catalyzes rate-limiting step
    Species: Homo sapiens
    See also:
    Chromosomal localisation in man: 19p13

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE:

    calculated:
    Reference: (4)


    RDH8,
    Notes

    • Photorezeptor-specific
    Species: Homo sapiens
    See also:
    Chromosomal localisation in man:

    in mouse:
    Gene Data

    Exons:
    Primers:
    Protein Data
    Amino acids:
    Molecular weight on SDS-PAGE:

    calculated:
    Reference: (9)


    References:
    1. Chen,P., Lee,T.D., and Fong,H.K.W. Interaction between 11-cis-retinol dehydrogenase and RGR opsin. 2001; Invest.Ophthalmol.Vis.Sci. 42: S356 Goto Top
    2. Haeseleer,F., Huang,J., Buczylko,J., Possin,D.E., Lebioda,L., Sokal,I., Palczewski,K., and Saari,J.C. Characterization Of A Putative Photoreceptor All-Trans-Retinol Dehydrogenase (RDH). 1998; Invest.Ophthalmol.Vis.Sci. 39: S423 Goto Top
    3. Haeseleer,F., Jang,G.F., Imanishi,Y., Driessen,C.A., Matsumura,M., Nelson,P.S., and Palczewski,K. Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina. 2002; J.Biol.Chem. 277: 45537-45546. Link Goto Top
    4. Han,W., Yip,S.P., Wang,J., and Yap,M.K. Using denaturing HPLC for SNP discovery and genotyping, and establishing the linkage disequilibrium pattern for the all-trans-retinol dehydrogenase (RDH8) gene. 2004; J Hum Genet. 49: 16-23. Link Goto Top
    5. Janecke,A.R., Thompson,D.A., Utermann,G., Becker,C., Hubner,C.A., Schmid,E., McHenry,C.L., Nair,A.R., Ruschendorf,F., Heckenlively,J., Wissinger,B., Nurnberg,P., and Gal,A. Mutations in RDH12 encoding a photoreceptor cell retinol dehydrogenase cause childhood-onset severe retinal dystrophy. 2004; Nat.Genet. 36: 850-854. Link Goto Top
    6. Mata,J.R., Mata,N.L., and Tsin,A.T. Substrate specificity of retinyl ester hydrolase activity in retinal pigment epithelium. 1998; J.Lipid Res. 39: 604-612. Link Goto Top
    7. Palczewski,K., Jager,S., Buczylko,J., Crouch,R.K., Bredberg,D.L., Hofmann,K.P., Asson-Batres,M.A., and Saari,J.C. Rod outer segment retinol dehydrogenase: Substrate specificity and role in phototransduction. 1994; Biochemistry. 33: 13741-13750.
      Link Goto Top
    8. Palczewski,K. and Saari,J.C. Activation And Inactivation Steps In The Visual Transduction Pathway. 1997; Current.Opinion.In Neurobiology. 7: 500-504. Link Goto Top
    9. Perrault,I., Hanein,S., and Kaplan,J. L'amaurose congenitale de Leber: les retinol-deshydrogenases au banc des accuses. 2004; Med.Sci.(Paris). 20: 1066-1068. Link Goto Top
    10. Rattner,A., Smallwood,P.M., and Nathans,J. Identification and characterization of all-trans-retinol dehydrogenase from photoreceptor outer segments, the visual cycle enzyme that reduces all-trans-retinal to all-trans-retinol. 2000; J.Biol.Chem. 275: 11034-11043.
      Link Goto Top
    11. Simon,A., Hellman,U., Wernstedt,C., and Eriksson,U. The retinal pigment epithelial-specific 11-cis retinol dehydrogenase belongs to the family of short chain alcohol dehydrogenases. 1995; J.Biol.Chem. 270: 1107-1112.
      Link Goto Top
    12. Simon,A., Lagercrantz,J., Bajalica Lagercrantz,S., and Eriksson,U. Primary structure of human 11-cis retinol dehydrogenase and organization and chromosomal localization of the corresponding gene. 1996; Genomics. 36: 424-430. Goto Top
    13. Simon,A., Romert,A., and Eriksson,U. Analyzing membrane topology of 11-cis-retinol dehydrogenase. 2000; Methods Enzymol. 316:344-58.: 344-358.
      Link Goto Top
    14. Thumann,G., Kociok,N., Bartz-Schmidt,K.U., Esser,P., Schraermeyer,U., and Heimann,K. Detection of mRNA for proteins involved in retinol metabolism in iris pigment epithelium. 1999; Graefes.Arch.Clin.Exp.Ophthalmol. 237: 1046-1051.
      Link Goto Top
    15. Wu,B.X., Chen,Y., Chen,Y., Fan,J., Rohrer,B., Crouch,R.K., and Ma,J.X. Cloning and characterization of a novel all-trans retinol short-chain dehydrogenase/reductase from the RPE. 2002; Invest.Ophthalmol.Vis.Sci. 43: 3365-3372.
      Link Goto Top

    Return to pagehead

    Return to Retina International‘s
    Scientific Newsletter


    Contact the editor
    This site is maintained and edited by
    Dr. rer. medic. Markus Preising, Dipl.Biol.
    Molecular Genetics Laboratory
    Department of Paediatric Ophthalmology, Strabismology and Ophthalmogenetics
    University of Regensburg
    Head: Prof. Dr. med. Birgit Lorenz