Редактирование: RDH11

Retinol dehydrogenase 11 (EC 1.1.1.300) (Androgen-regulated short-chain dehydrogenase/reductase 1) (HCV core-binding protein HCBP12) (Prostate short-chain dehydrogenase/reductase 1) (Retinal reductase 1) (RalR1) (Short chain dehydrogenase/reductase family 7C member 1) [ARSDR1] [PSDR1] [SDR7C1] [CGI-82]

==Publications==

{{medline-entry
|title=Retinol dehydrogenases [[RDH11]] and [[RDH12]] in the mouse retina: expression levels during development and regulation by oxidative stress.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/18326732
|abstract=[[RDH11]] and [[RDH12]] are closely related retinol dehydrogenases expressed in the retina. [[RDH12]] has been linked to the early-onset retinal dystrophy Leber congenital amaurosis, whereas [[RDH11]] has not been associated with human disease. To understand their physiological roles, the authors investigated their expression during development and their regulation by light-induced oxidative stress in mouse retina. Quantitative RT-PCR and immunoblot analysis were used for quantification of [[RDH11]] and [[RDH12]] during development and oxidative stress. Expression during development was measured between embryonic day (E) 12 and postnatal day (P) 210 (7 months) in C57BL/6 mouse eyes. Expression during light-induced oxidative stress was measured between 2 and 24 hours of exposure to light in BALB/c mouse retina. The [[RDH11]] level was low and remarkably constant during development and oxidative stress. [[RDH12]] expression started at P7 and increased until P30 to approximately sevenfold higher than [[RDH11]]. Oxidative stress induced by exposure to constant bright light led to a rapid and significant decrease of [[RDH12]] protein. The low and constant expression of [[RDH11]] suggested a housekeeping function for this enzyme. The onset of [[RDH12]] expression during the maturation of photoreceptor cells suggested a function related to the visual process. The light-induced rapid decrease of [[RDH12]] protein, preceding the decrease of the mRNA, suggested a specific degradation of the protein rather than a regulation of gene expression.
|mesh-terms=* Aging
* Alcohol Oxidoreductases
* Animals
* Gene Expression Regulation, Developmental
* Immunoblotting
* In Situ Hybridization
* Light
* Mice
* Mice, Inbred BALB C
* Mice, Inbred C57BL
* Mice, Knockout
* Oxidative Stress
* Oxidoreductases
* RNA, Messenger
* Radiation Injuries, Experimental
* Retina
* Retinal Degeneration
* Retinal Dehydrogenase
* Reverse Transcriptase Polymerase Chain Reaction
* Transcription, Genetic

|full-text-url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2366097
}}
{{medline-entry
|title=Functional characterization of mouse [[RDH11]] as a retinol dehydrogenase involved in dark adaptation in vivo.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/15790565
|abstract=We previously cloned mouse [[RDH11]] (m[[RDH11]]) as a gene regulated by the transcription factor sterol regulatory element-binding proteins and showed that it is a retinol dehydrogenase expressed in non-ocular tissues such as the liver and testis and in the retina (Kasus-Jacobi, A., Ou, J., Bashmakov, Y. K., Shelton, J. M., Richardson, J. A., Goldstein, J. L., and Brown, M. S. (2003) J. Biol. Chem. 278, 32380-32389). It was proposed to function in the recycling of the visual chromophore 11-cis-retinal after photoisomerization by a bleaching light, a pathway referred to as the visual cycle. In this work, we describe our studies on the ocular function of m[[RDH11]]. We created a knockout mouse by replacing the mrdh11 coding sequence with the lacZ reporter gene for expression profiling. 5-Bromo-4-chloro-3-indolyl-beta-D-galactopyranoside (X-Gal) staining demonstrated active transcription of this gene in photoreceptor cells. We show by immunoblot analysis that m[[RDH11]] is associated with retinal membranes purified from a non-outer segment fraction of the retina. No obvious retinal defect was found during development and aging of [[RDH11]]-deficient mice. The functional consequences of m[[RDH11]] disruption were investigated by electroretinography. Dark adaptation was delayed by a factor of 2.5-3 compared with wild-type mice. However, the kinetics of 11-cis-retinal recycling during dark adaptation was not affected, suggesting that m[[RDH11]] is not involved in the visual cycle. We propose that m[[RDH11]] disruption affects retinoid metabolism in photoreceptor inner segments and delays the kinetics of dark adaptation through modulation of calcium homeostasis.
|mesh-terms=* Aging
* Animals
* Calcium
* Chromatography, High Pressure Liquid
* DNA
* Dark Adaptation
* Drug Resistance
* Electroretinography
* Female
* Gene Expression
* Gene Expression Profiling
* Homeostasis
* Immunoblotting
* Kinetics
* Liver
* Male
* Mice
* Mice, Knockout
* Neomycin
* Oxidoreductases
* RNA, Messenger
* Retina
* Retinal Rod Photoreceptor Cells
* Retinoids
* Testis
* Transcription, Genetic
* beta-Galactosidase

|full-text-url=https://sci-hub.do/10.1074/jbc.M413789200
}}