Disease relevance of RDH10

• A cDNA clone up-regulated in hydraulic lung edema in rabbit showed high similarity with human RDH10 mRNA, which encodes a protein involved in retinoic acid metabolism [1].

High impact information on RDH10

• Identification of RDH10, an All-trans Retinol Dehydrogenase, in Retinal Muller Cells [2].
• Expression of RDH10 in rMC-1, a cell line derived from rat Muller cells, was determined by RT-PCR and Western blot analysis [2].
• NADP was shown to be the preferred cofactor, which is identical with the cofactor preference of the recombinant RDH10 [2].
• CONCLUSIONS: RDH10 is a novel retinol oxidase expressed in the RPE [3].
• Human RDH10 expressed in COS cells oxidized all-trans retinol to all-trans retinal [3].

Biological context of RDH10

• METHODS: The full-length cDNA encoding a novel atRDH, RDH10, was cloned by PCR based on an expressed sequence tag (EST) [3].
• The human RDH10 shares 100% and 98.6% amino acid sequence identity with the bovine and mouse proteins, respectively, suggesting a highly conserved sequence during evolution [3].
• RDH10 displayed substrate specificity for all-trans retinol and preferred nicotinamide adenine dinucleotide phosphate (NADP) as the cofactor [3].
• METHODS: We screened by denaturing-high performance liquid chromatography (D-HPLC) and direct sequencing all coding exons of LRAT and RDH10 in 216 patients, including 134 with simplex or multiplex retinitis pigmentosa and 82 with various types of flecked retinal dystrophies [4].

Anatomical context of RDH10

• The activity was measured by an RDH activity assay with recombinant RDH10 expressed in COS cells [3].
• PURPOSE: To investigate the expression of RDH10, an all-trans retinol dehydrogenase identified in the retinal pigment epithelium (RPE), in retinal Muller cells [2].

Associations of RDH10 with chemical compounds

• The group A is blank control group, the group B positive control group (Captopril), the group C (1.0 mg/kg), the group D (RDHP 10 mg/kg) and group E (RDHP 50 mg/kg) [5].
• Due to its high affinity for all-trans-retinol, RDH10 exhibits a greater rate of retinol oxidation in the presence of cellular retinol-binding protein type I (CRBPI) than human microsomal RoDH4, but like RoDH4, RDH10 does not recognize retinol bound to CRBPI as a substrate [6].

Analytical, diagnostic and therapeutic context of RDH10

• Immunohistochemistry showed that RDH10 was localized in Muller cells in retinal sections [2].
• Cellular localization was determined at the mRNA level by Northern blot analysis, RT-PCR, and in situ hybridization and at the protein level by immunohistochemistry with an antibody specific to RDH10 [3].

References