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retinol dehydrogenase 8 (all-trans)
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关键词:'retinol dehydrogenase 8 (all-trans)'
显示 1-30 共 131 条结果 关于 "retinol dehydrogenase 8 (all-trans)" 范围 论文
Hajrah Sarkar et al.
International journal of molecular sciences, 22(16) (2021-08-28)
Retinol dehydrogenase 12 (RDH12) is expressed in photoreceptor inner segments and catalyses the reduction of all-trans retinal (atRAL) to all-trans retinol (atROL), as part of the visual cycle. Mutations in RDH12 are primarily associated with autosomal recessive Leber congenital amaurosis.
A Rattner et al.
The Journal of biological chemistry, 275(15), 11034-11043 (2001-02-07)
Retinol dehydrogenase (RDH), the enzyme that catalyzes the reduction of all-trans-retinal to all-trans-retinol within the photoreceptor outer segment, was the first visual cycle enzymatic activity to be identified. Previous work has shown that this enzyme utilizes NADPH, shows a marked
Bill X Wu et al.
Investigative ophthalmology & visual science, 45(11), 3857-3862 (2004-10-27)
To investigate the expression of RDH10, an all-trans retinol dehydrogenase identified in the retinal pigment epithelium (RPE), in retinal Muller cells. The RDH10 protein levels in mouse eyecups and bovine tissues were examined by Western blot analysis using a polyclonal
Bill X Wu et al.
Investigative ophthalmology & visual science, 43(11), 3365-3372 (2002-10-31)
In the photic visual cycle, retinal G protein-coupled receptor (RGR) isomerizes all-trans retinal to 11-cis retinal in the retinal pigment epithelium (RPE) after illumination. It is unclear, however, how all-trans retinal, the substrate for RGR, is generated in the RPE
Kristin M Obrochta et al.
The Journal of biological chemistry, 290(11), 7259-7268 (2015-01-30)
All-trans-retinoic acid (atRA), an autacoid derived from retinol (vitamin A), regulates energy balance and reduces adiposity. We show that energy status regulates atRA biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases (RDH). Six h after re-feeding, Rdh1 expression decreased
Yan-shu Yu et al.
Journal of Zhejiang University. Science. B, 11(11), 836-841 (2010-11-03)
Retinoic acid level in the retina/choroid is altered in induced myopia models. All-trans-retinol dehydrogenase (RDH8) is an important enzyme of retinoic acid metabolism. This study aimed to investigate the association of the RDH8 gene with high myopia. Three single nucleotide
M Zhang et al.
The Journal of biological chemistry, 276(47), 44083-44090 (2001-09-20)
Metabolic activation of retinol (vitamin A) via sequential actions of retinol and retinal dehydrogenases produces the active metabolite all-trans-retinoic acid. This work reports cDNA cloning, enzymatic characterization, function in a reconstituted path of all-trans-retinoic acid biosynthesis in cell culture, and
Chao Wang et al.
The Journal of biological chemistry, 286(8), 6542-6553 (2010-12-09)
All-trans-retinoic acid (atRA) stimulates neurogenesis, dendritic growth of hippocampal neurons, and higher cognitive functions, such as spatial learning and memory formation. Although astrocyte-derived atRA has been considered a key factor in neurogenesis, little direct evidence identifies hippocampus cell types and
W H Gough et al.
The Journal of biological chemistry, 273(31), 19778-19785 (1998-07-25)
We report the cDNA sequence and catalytic properties of a new member of the short chain dehydrogenase/reductase superfamily. The 1134-base pair cDNA isolated from the human liver cDNA library encodes a 317-amino acid protein, retinol dehydrogenase 4 (RoDH-4), which exhibits
Insulin regulates retinol dehydrogenase expression and all-trans-retinoic acid biosynthesis through FoxO1.
Obrochta KM et al.
The Journal of Biological Chemistry, 290, 7259-7259 (2015)
J R Mertz et al.
The Journal of biological chemistry, 272(18), 11744-11749 (1997-05-02)
All-trans- and 9-cis-retinoic acid are active retinoids for regulating expression of retinoid responsive genes, serving as ligands for two classes of ligand-dependent transcription factors, the retinoic acid receptors and retinoid X receptors. Little is known, however, regarding 9-cis-retinoic acid formation.
Mao Yang et al.
The Journal of biological chemistry, 277(5), 3318-3324 (2001-11-28)
Light-dependent production of 11-cis-retinal by the retinal pigment epithelium (RPE) and normal regeneration of rhodopsin under photic conditions involve the RPE retinal G protein-coupled receptor (RGR) opsin. This microsomal opsin is bound to all-trans-retinal which, upon illumination, isomerizes stereospecifically to
Olga V Belyaeva et al.
The Journal of biological chemistry, 283(29), 20299-20308 (2008-05-27)
Human retinol dehydrogenase 10 (RDH10) was implicated in the oxidation of all-trans-retinol for biosynthesis of all-trans-retinoic acid, however, initial assays suggested that RDH10 prefers NADP(+) as a cofactor, undermining its role as an oxidative enzyme. Here, we present evidence that
J Labrecque et al.
The Biochemical journal, 305 ( Pt 2), 681-684 (1995-01-15)
The pleiotropic effects of retinoids are mediated by two families of nuclear receptors: RAR (retinoic acid receptors) and RXR (retinoid X receptors). 9-cis-Retinoic acid is a specific ligand for RXR receptors, whereas either 9-cis- or all-trans-retinoic acid activates the RAR
Mark K Adams et al.
The Journal of biological chemistry, 289(21), 14868-14880 (2014-04-16)
The retinoic acid-inducible dehydrogenase reductase 3 (DHRS3) is thought to function as a retinaldehyde reductase that controls the levels of all-trans-retinaldehyde, the immediate precursor for bioactive all-trans-retinoic acid. However, the weak catalytic activity of DHRS3 and the lack of changes
Gennaro Taibi et al.
Journal of enzyme inhibition and medicinal chemistry, 23(3), 317-327 (2008-06-24)
Retinoic acid is considered to be the active metabolite of retinol, able to control differentiation and proliferation of epithelia. Retinoic acid biosynthesis has been widely described with the implication of multiple enzymatic activities. However, our understanding of the cell biological
Akiko Maeda et al.
The Journal of biological chemistry, 280(19), 18822-18832 (2005-03-10)
The retinoid cycle is a recycling system that replenishes the 11-cis-retinal chromophore of rhodopsin and cone pigments. Photoreceptor-specific retinol dehydrogenase (prRDH) catalyzes reduction of all-trans-retinal to all-trans-retinol and is thought to be a key enzyme in the retinoid cycle. We
M H Foglio et al.
Biochimica et biophysica acta, 1432(2), 239-250 (1999-07-17)
Some members of the human alcohol dehydrogenase (ADH) family possess retinol dehydrogenase activity and may thus function in production of the active nuclear receptor ligand retinoic acid. Many diverse natural forms of retinol exist including all-trans-retinol (vitamin A(1)), 9-cis-retinol, 3,4-didehydroretinol
Françoise Haeseleer et al.
The Journal of biological chemistry, 277(47), 45537-45546 (2002-09-13)
Retinoids are chromophores involved in vision, transcriptional regulation, and cellular differentiation. Members of the short chain alcohol dehydrogenase/reductase superfamily catalyze the transformation of retinol to retinal. Here, we describe the identification and properties of three enzymes from a novel subfamily
Ryan O Parker et al.
Experimental eye research, 91(6), 788-792 (2010-08-31)
The isomerization of 11-cis retinal to all-trans retinal in photoreceptors is the first step in vision. For photoreceptors to function in constant light, the all-trans retinal must be converted back to 11-cis retinal via the enzymatic steps of the visual
Min Zhang et al.
Gene, 305(1), 121-131 (2003-02-21)
Mouse rdh1 encodes retinol dehydrogenase type 1 (RDH1), a short-chain dehydrogenase, which recognizes as substrates all-trans-retinol, 9-cis-retinol, 5alpha-androstan-3,17-diol and 5alpha-androstan-3-ol-17-one. RDH1 is the most efficient known mouse short-chain dehydrogenase that catalyzes dehydrogenation of all-trans-retinol, and contributes to a reconstituted path
Olga V Belyaeva et al.
Biochemistry, 42(50), 14838-14845 (2003-12-17)
Recently, we reported the first biochemical characterization of a novel member of the short-chain dehydrogenase/reductase superfamily, retinal reductase 1 (RalR1) (Kedishvili et al. (2002) J. Biol. Chem. 277, 28909-28915). In the present study, we purified the recombinant enzyme from the
J Su et al.
The Journal of biological chemistry, 273(28), 17910-17916 (1998-07-04)
We report here a mouse cDNA that encodes a 316-amino acid short-chain dehydrogenase that prefers NAD+ as its cofactor and recognizes as substrates androgens and retinols, i.e. has steroid 3alpha- and 17beta-dehydrogenase and cis/trans-retinol catalytic activities. This cis-retinol/androgen dehydrogenase type
Olga V Belyaeva et al.
Biochemistry, 44(18), 7035-7047 (2005-05-04)
Retinol dehydrogenase 12 (RDH12) is a novel member of the short-chain dehydrogenase/reductase superfamily of proteins that was recently linked to Leber's congenital amaurosis 3 (LCA). We report the first biochemical characterization of purified human RDH12 and analysis of its expression
Min-Sun Song et al.
The Journal of biological chemistry, 278(41), 40079-40087 (2003-07-12)
We report a mouse short-chain dehydrogenase/reductase (SDR), retinol dehydrogenase-similar (RDH-S), with intense mRNA expression in liver and kidney. The RDH-S gene localizes to chromosome 10D3 with the SDR subfamily that catalyzes metabolism of retinoids and 3 alpha-hydroxysteroids. RDH-S has no
F Haeseleer et al.
The Journal of biological chemistry, 273(34), 21790-21799 (1998-08-15)
The reduction of all-trans-retinal in photoreceptor outer segments is the first step in the regeneration of bleached visual pigments. We report here the cloning of a dehydrogenase, retSDR1, that belongs to the short-chain dehydrogenase/reductase superfamily and localizes predominantly in cone
N Y Kedishvili et al.
The Journal of biological chemistry, 270(8), 3625-3630 (1995-02-24)
A full-length 1966-base pair clone of the human class IV alcohol dehydrogenase (sigma-ADH) was isolated from a human stomach cDNA library. The 373-amino acid sigma-ADH encoded by this cDNA was expressed in Escherichia coli. The specific activity of the recombinant
Richard Kin Ting Kam et al.
The Journal of biological chemistry, 288(44), 31477-31487 (2013-09-21)
All-trans-retinoic acid (atRA) is an important morphogen involved in many developmental processes, including neural differentiation, body axis formation, and organogenesis. During early embryonic development, atRA is synthesized from all-trans-retinal (atRAL) in an irreversible reaction mainly catalyzed by retinal dehydrogenase 2
M Lin et al.
The Journal of biological chemistry, 275(51), 40106-40112 (2000-09-29)
This report describes the isolation of a heretofore uncharacterized aldehyde dehydrogenase (ALDH) with retinal dehydrogenase activity from rat kidney and the cloning and expression of a cDNA that encodes its human ortholog, the previously unknown ALDH12. The human ALDH12 cDNA
Nedialka G Markova et al.
Molecular genetics and metabolism, 78(2), 119-135 (2003-03-06)
The biological functions of vitamin A in the epidermis are mediated by all-trans retinoic acid, which is biosynthesized from retinol in two oxidative reactions. The first step involves enzymatic conversion of retinol to retinaldehyde. The physiological significance and relative contributions
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