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additional information
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N-ethylmaleimide does not affect the catalytic action of RDH1, but interferes with its approach to holo-CRBP1, interrupting retinol transfer. The membrane context of RDH affects function
evolution
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RDH1, RDH10 and DHRS9 are microsomal members of the SDR gene family
evolution
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RDHs that catalyze the interconversion of retinal and retinol involved in rhodopsin turnover are members of the family of short chain dehydrogenase/reductases
evolution
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RDHs that catalyze the interconversion of retinal and retinol involved in rhodopsin turnover are members of the family of short chain dehydrogenase/reductases
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malfunction
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deleting the positive charges from the C-terminal end of the leader, and inserting two arginine residues near the N-terminus of the signaling sequence causes 95% inversion from cytoplasmic to luminal: i.e. the mutant L3R/L5R/R16Q/R19Q/R21Q faces the lumen
malfunction
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outer segments of rods deficient in Rdh8 fail to reduce all-trans-retinal. Following exposure to light, a leak of retinoids from outer to inner segments is detected in rods from both wild-type and knock-out mice. In cells lacking Rdh8 or Rdh12, EC 1.1.1.300, this leak is mainly all-trans-retinal, overview. Retinal reductase activity is lost in RDH12-deficient mutants
malfunction
mice lacking both the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands. The upregulation of hair-follicle stem cell genes is consistent with reduced retinoic acid signaling in the skin of the double-knockout mice
malfunction
mice with targeted knockout of the more catalytically active SDR16C6 enzyme have no obvious phenotype, possibly due to functional redundancy, because Sdr16c5 and Sdr16c6 exhibit an overlapping expression pattern during later developmental stages and in adulthood. Mice lacking both epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands
malfunction
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outer segments of rods deficient in Rdh8 fail to reduce all-trans-retinal. Following exposure to light, a leak of retinoids from outer to inner segments is detected in rods from both wild-type and knock-out mice. In cells lacking Rdh8 or Rdh12, EC 1.1.1.300, this leak is mainly all-trans-retinal, overview. Retinal reductase activity is lost in RDH12-deficient mutants
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malfunction
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mice with targeted knockout of the more catalytically active SDR16C6 enzyme have no obvious phenotype, possibly due to functional redundancy, because Sdr16c5 and Sdr16c6 exhibit an overlapping expression pattern during later developmental stages and in adulthood. Mice lacking both epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands
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malfunction
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mice lacking both the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands. The upregulation of hair-follicle stem cell genes is consistent with reduced retinoic acid signaling in the skin of the double-knockout mice
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metabolism
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the enzyme catalyzes the first step in all-trans-retinal biosynthesis, modeling of all-trans-retinal homeostasis, overview
metabolism
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the enzyme catalyzes the first step in all-trans-retinal biosynthesis, modeling of all-trans-retinal homeostasis, overview
metabolism
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the enzyme catalyzes the first step in all-trans-retinal biosynthesis, modeling of all-trans-retinal homeostasis, overview
metabolism
two murine epidermal retinol dehydrogenases, short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) and SDR16C6 (RDHE2S), contribute to retinoic acid biosynthesis in living cells and are also essential for the oxidation of retinol to retinaldehyde in vivo
metabolism
two murine epidermal retinol dehydrogenases, short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) and SDR16C6 (RDHE2S), contribute to retinoic acid biosynthesis in living cells and are also essential for the oxidation of retinol to retinaldehyde in vivo. RDHE2S is a more active enzyme than RDHE2
metabolism
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two murine epidermal retinol dehydrogenases, short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) and SDR16C6 (RDHE2S), contribute to retinoic acid biosynthesis in living cells and are also essential for the oxidation of retinol to retinaldehyde in vivo
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metabolism
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two murine epidermal retinol dehydrogenases, short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) and SDR16C6 (RDHE2S), contribute to retinoic acid biosynthesis in living cells and are also essential for the oxidation of retinol to retinaldehyde in vivo. RDHE2S is a more active enzyme than RDHE2
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physiological function
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in vertebrate rod cells, retinoid dehydrogenases/reductases are critical for reducing the reactive aldehyde all-trans-retinal that is released by photoactivated rhodopsin, to all-trans-retinol. Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12. RDH8 in the outer segment provides most of the activity needed to reduce all-trans-retinal generated by the light response, overview
physiological function
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RDH1 contributes to a reconstituted pathway of all-trans-retinal biosynthesis, when expressed in intact cells with each of the three retinal dehydrogenases
physiological function
energy status regulates all-trans-retinoic acid biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases. Removing serum from the medium of the human hepatoma cell line HepG2 increases isoforms Rdh10 and Rdh16 mRNA expression 2-3-fold by 4 h, by increasing transcription and stabilizing mRNA. Insulin decreases Rdh10 and Rdh16 mRNA in HepG2 cells incubated in serum-free medium by inhibiting transcription and destabilizing mRNA. Insulin action requires PI3K and Akt, which suppress FoxO1
physiological function
energy status regulates all-trans-retinoic acid biosynthesis at the rate-limiting step, catalyzed by retinol dehydrogenases. Six hours after re-feeding, isoform Rdh1 expression decreases 80-90% in liver and brown adipose tissue, relative to mice fasted 16 h. All-trans-retinoic acid in the liver is decreased 44% 3 h after reduced Rdh expression. Oral gavage with glucose or injection with insulin decreases Rdh1 mRNA 50% or greater in mouse liver
physiological function
RDHE2 does not partner with dehydrogenase/reductase DHRS3/SDR16C1 or cellular retinol binding protein type CRBP1
physiological function
the retinol dehydrogenase activity of RDH10 is activated by retinaldehyde reductase DHRS3. In turn, DHRS3 requires the presence of retinol dehydrogenase RDH10 to display its full catalytic activity. Neither RDH10 nor DHRS3 has to be itself catalytically active to activate each other
physiological function
the epidermal retinol dehydrogenase short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) contributes to retinoic acid biosynthesis in living cells and is also essential for the oxidation of retinol to retinaldehyde in vivo. The retinol dehydrogenase activities of murine SDR16C5 and SDR16C6 enzymes are not critical for survival but are responsible for most of the retinol dehydrogenase activity in skin, essential for the regulation of the hair-follicle cycle, and required for the maintenance of both sebaceous and meibomian glands
physiological function
the epidermal retinol dehydrogenase short-chain dehydrogenase/reductase family 16C member 6 (SDR16C6 or RDHE2S) contributes to retinoic acid biosynthesis in living cells and is also essential for the oxidation of retinol to retinaldehyde in vivo. RDHE2S is a more active enzyme than RDHE2. The upregulation of hair-follicle stem cell genes is consistent with reduced retinoic acid signaling in the skin of the double-knockout mice. The retinol dehydrogenase activities of murine SDR16C5 and SDR16C6 enzymes are not critical for survival but are responsible for most of the retinol dehydrogenase activity in skin, essential for the regulation of the hair-follicle cycle, and required for the maintenance of both sebaceous and meibomian glands
physiological function
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in vertebrate rod cells, retinoid dehydrogenases/reductases are critical for reducing the reactive aldehyde all-trans-retinal that is released by photoactivated rhodopsin, to all-trans-retinol. Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12. RDH8 in the outer segment provides most of the activity needed to reduce all-trans-retinal generated by the light response, overview
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physiological function
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the epidermal retinol dehydrogenase short-chain dehydrogenase/reductase family 16C member 6 (SDR16C6 or RDHE2S) contributes to retinoic acid biosynthesis in living cells and is also essential for the oxidation of retinol to retinaldehyde in vivo. RDHE2S is a more active enzyme than RDHE2. The upregulation of hair-follicle stem cell genes is consistent with reduced retinoic acid signaling in the skin of the double-knockout mice. The retinol dehydrogenase activities of murine SDR16C5 and SDR16C6 enzymes are not critical for survival but are responsible for most of the retinol dehydrogenase activity in skin, essential for the regulation of the hair-follicle cycle, and required for the maintenance of both sebaceous and meibomian glands
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physiological function
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the epidermal retinol dehydrogenase short-chain dehydrogenase/reductase family 16C member 5 (SDR16C5 or RDHE2) contributes to retinoic acid biosynthesis in living cells and is also essential for the oxidation of retinol to retinaldehyde in vivo. The retinol dehydrogenase activities of murine SDR16C5 and SDR16C6 enzymes are not critical for survival but are responsible for most of the retinol dehydrogenase activity in skin, essential for the regulation of the hair-follicle cycle, and required for the maintenance of both sebaceous and meibomian glands
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