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11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
11-cis-retinol + NAD+
?
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
3,4-didehydroretinol + NAD+
3,4-didehydroretinal + NADH
-
60% of the efficiency against all-trans-retinol
-
-
?
5alpha-androstan-3alpha-ol-17-one + NAD+
? + NADH
-
-
-
-
?
9-cis-retinol + NAD+
9-cis-retinal + NADH + H+
higher activity with all-trans-retinol versus 9-cis-retinol
-
-
?
all-trans retinal + NADH + H+
all-trans retinol + NAD+
26.8% of the activity with butan-1-ol
-
-
?
all-trans retinal + NADH + H+
all-trans-retinol + NAD+
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
-
-
-
?
all-trans-retinaldehyde + NADH + H+
?
-
-
-
?
all-trans-retinaldehyde + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
all-trans-retinaldehyde + NADH + H+
-
-
-
r
all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NADP+
all-trans-retinal-[cellular-retinol-binding-protein] + NADPH + H+
-
-
-
r
androsterone + NAD+
? + NADH
-
-
-
-
?
butyl alcohol + NAD+
butanal + NADH + H+
retinal + NAD(P)H
retinol + NAD(P)+
-
-
-
ir
retinal + NADH
retinol + NAD+
retinal + NADH + H+
retinol + NAD+
-
-
-
r
retinal + NADPH + H+
retinol + NADP+
retinol + NAD+
retinal + NADH
retinol + NADP+
retinal + NADPH
-
-
-
-
?
retinol bound to cellular retinol binding protein + NAD+
retinal bound to cellular retinol binding protein + NADH
-
-
-
-
?
additional information
?
-
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
-
-
-
r
11-cis-retinol + NAD+
11-cis-retinal + NADH + H+
-
-
-
r
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
-
-
-
?
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans retinal + NADH + H+
all-trans-retinol + NAD+
-
oxidative activity is below the detection limit
-
-
r
all-trans retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
-
-
-
?
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
RDH5 has only a minor in vivo all-trans RDH activity
-
-
?
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinal + NAD+
all-trans-retinol + NADH + H+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
wild type RDH10 catalyzes both oxidation of all-trans retinol and reduction of all-trans retinal in vitro. On cultured cells, however, oxidation is the favored reaction catalyzed by RDH10.
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
26% activity compared to butyl alcohol
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
26% activity compared to butyl alcohol
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
catalytic efficiency in the reductive direction is lower than in the oxidative direction
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH
in intact cells, the enzyme functions as retinol dehydrogenase, and contributes to the oxidation of retinol, but not to the reduction of retinaldehyde
-
-
ir
all-trans-retinol + NAD+
all-trans-retinal + NADH
-
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
RoDH-4 is capable of contributing to the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in the cellular context
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH
in intact cells, the enzyme functions as retinol dehydrogenase, and contributes to the oxidation of retinol, but not to the reduction of retinaldehyde
-
-
ir
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity with NAD+ is about 10fold higher than activity in presence of NADP+. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
30.2% activity compared to butyl alcohol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
30.2% activity compared to butyl alcohol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 functions in a path of all-trans-retinoic acid biosynthesis starting early during embryogenesis
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 has 811fold higher activity with NAD+ versus NADP+. Higher activity with all-trans-retinol versus 9-cis-retinol. Multifunctional enzyme. In addition to retinol dehydrogenase activity, RDH1 has strong 3alpha-hydroxy and weak 17beta-hydroxy steroid dehydrogenase activities
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1, except for RDH10 that does not access holo-CRBP1 as substrate
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
RDH interact with/or recognize holo-CRBP1
-
-
ir
butyl alcohol + NAD+
butanal + NADH + H+
100% activity
-
-
?
butyl alcohol + NAD+
butanal + NADH + H+
-
100% activity
-
-
?
retinal + NADH
retinol + NAD+
-
-
-
?
retinal + NADH
retinol + NAD+
-
-
-
-
r
retinal + NADH
retinol + NAD+
-
-
-
-
r
retinal + NADPH + H+
retinol + NADP+
-
-
-
-
?
retinal + NADPH + H+
retinol + NADP+
-
activity is lower than with NADH
-
-
?
retinol + NAD+
retinal + NADH
-
-
-
?
retinol + NAD+
retinal + NADH
-
-
-
-
?
retinol + NAD+
retinal + NADH
-
-
-
?
retinol + NAD+
retinal + NADH
-
-
-
r
additional information
?
-
-
negligible activity with 9-cis-retinol
-
-
?
additional information
?
-
-
the enzyme is expressed predominantly in the differentiating spinous layers and is under positive, feed-forward regulation by retinoic acid
-
-
?
additional information
?
-
-
substrate bound to cellular retinol binding protein is preferred
-
-
?
additional information
?
-
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
no activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
-
-
?
additional information
?
-
-
RoDH-4 belongs to the group of short-chain dehydrogenase/reductases that are active toward two types of substrates, retinoids and 3alpha-hydroxysteroids
-
-
?
additional information
?
-
the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol
-
-
?
additional information
?
-
-
the enzymes utilizes retinol bound to cellular retinol binding protein type I at a much lower rate than free retinol
-
-
?
additional information
?
-
the multifunctional enzyme oxidizes the 3alpha-hydroxysteroids androstane-diol and androsterone to dihydrotestosterone and androstanedione, respectively
-
-
?
additional information
?
-
-
the multifunctional enzyme oxidizes the 3alpha-hydroxysteroids androstane-diol and androsterone to dihydrotestosterone and androstanedione, respectively
-
-
?
additional information
?
-
-
NAD+-dependent retinoid-active SDRs have higher catalytic efficiencies for the oxidation of 3alpha-hydroxysterols than of retinols
-
-
?
additional information
?
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
no activity is detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD+/NADH or NADP+/NADPH
-
-
?
additional information
?
-
-
the enzyme is not active with NADP+ or NADPH as cofactors
-
-
?
additional information
?
-
the enzyme is not active with NADP+ or NADPH as cofactors
-
-
?
additional information
?
-
-
enzyme is an alcohol dehydrogenase, EC 1.1.1.1, with activity for all-trans-retinol using NAD+ as a cofactor
-
-
?
additional information
?
-
enzyme is an alcohol dehydrogenase, EC 1.1.1.1, with activity for all-trans-retinol using NAD+ as a cofactor
-
-
?
additional information
?
-
-
no activity with decanal
-
-
?
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
-
no activity with decanal
-
-
?
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
in addition to all-trans-retinol, RDHE2S recognizes 11-cis-retinol as substrate
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
no activity toward all-trans-retinol is detected using the microsomal and mitochondrial preparations of recombinant murine RDHE2 protein expressed in Spodoptera frugiperda Sf9 cells. But although inactive toward retinol in isolated microsomes, RDHE2 is able to function as a retinol dehydrogenase in intact cells
-
-
-
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
additional information
?
-
RDH10 is required for proper retinoic acid signalling in the early embryo, RDH10 cooperates with retinal dehydrogenase 2 during axis development and central nervous system patterning
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
13-cis-retinol + NAD+
13-cis-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinal + NAD(P)H + H+
all-trans-retinol + NAD(P)+
RDH5 has only a minor in vivo all-trans RDH activity
-
-
?
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
all-trans-retinol + NAD+
all-trans-retinal + NADH
RoDH-4 is capable of contributing to the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in the cellular context
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
retinal + NAD(P)H
retinol + NAD(P)+
-
-
-
ir
retinal + NADH
retinol + NAD+
-
-
-
?
additional information
?
-
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinal + NADH + H+
all-trans-retinol + NAD+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
exhibits a strong preference for NAD+/NADH as cofactors. Activity toward all-trans-retinal in the presence of NADH is 2fold lower than activity with all-trans-retinol and NAD+. The preference for NAD+ suggests that RDH-E2 is likely to function in the oxidative direction in vivo, further supporting its potential role in the oxidation of retinol to retinaldehyde for retinoic acid biosynthesis in human keratinocytes
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RoDH-4 can potentially contribute to the biosynthesis of two powerful modulators of gene expression: retinoic acid from retinol and dihydrotestosterone from 3alpha-androstane-diol
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
RDH1 functions in a path of all-trans-retinoic acid biosynthesis starting early during embryogenesis
-
-
?
all-trans-retinol + NAD+
all-trans-retinal + NADH + H+
-
-
-
r
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
?
all-trans-retinol-[cellular-retinol-binding-protein] + NAD+
all-trans-retinal-[cellular-retinol-binding-protein] + NADH + H+
-
-
-
-
ir
additional information
?
-
-
the enzyme is expressed predominantly in the differentiating spinous layers and is under positive, feed-forward regulation by retinoic acid
-
-
?
additional information
?
-
-
NAD+-dependent retinoid-active SDRs have higher catalytic efficiencies for the oxidation of 3alpha-hydroxysterols than of retinols
-
-
?
additional information
?
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
-
RDH-E2 may be involved in the pathogenesis of psoriasis through its potential role in retinoic acid biosynthesis and stimulation of keratinocyte proliferation
-
-
?
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
additional information
?
-
-
chronic ethanol consumption results in an increased activity of the microsomal retinol dehydrogenase which may contribute to hepatic retinol depletion, especially in the view of the insensitivity of the enzyme to ethanol inhibition
-
-
?
additional information
?
-
RDH10 is required for proper retinoic acid signalling in the early embryo, RDH10 cooperates with retinal dehydrogenase 2 during axis development and central nervous system patterning
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
mRNA expression
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strong mRNA expression
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mRNA expression
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mRNA expression
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strong mRNA expression
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mRNA expression
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strong mRNA expression
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mRNA expression
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mRNA expression
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mRNA expression
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strong mRNA expression
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the mouse embryo expresses RDH1 as early as 7.0 days post-coitus, and expression is especially intense within the neural tube, gut, and neural crest at embryo day 10.5
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Rdhe2 is observed starting at E12.5, increasing in abundance through E14.5. Both Rdhe2 and Rdhe2s are expressed from middle to late gestation
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Rdhe2s is detected earlier in development at E10.5 and persisted through E14.5. Both Rdhe2 and Rdhe2s are expressed from middle to late gestation
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Rdhe2s is detected earlier in development at E10.5 and persisted through E14.5. Both Rdhe2 and Rdhe2s are expressed from middle to late gestation
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Rdhe2 is observed starting at E12.5, increasing in abundance through E14.5. Both Rdhe2 and Rdhe2s are expressed from middle to late gestation
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dorsal blastopore lip
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epidermal keratinocytes, gene is expressed predominantly in the differentiating spinous layers
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retinal dehydrogenase 2 is significantly elevated in psoriatic skin
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mRNA expression
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RDH8 localizes to photoreceptor outer segments
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RDH8 localizes to photoreceptor outer segments
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strong mRNA expression
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mRNA for RoDH-4 is abundant in adult liver, where it is translated into RoDH-4 protein. Significant amounts of RoDH-4 message is detected in fetal liver
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strong mRNA expression
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significant amounts of RoDH-4 message is detected in fetal lung
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mRNA expression
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strong mRNA expression
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the highest level of RDH12 expression is in the retina where it is localised to the inner segments and cell bodies of rod and cone photoreceptors
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strong mRNA expression
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additional information
RDH1 has widespread and intense mRNA expression in tissues of embryonic and adult mice
brenda
additional information
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RDH1 has widespread and intense mRNA expression in tissues of embryonic and adult mice
brenda
additional information
analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
brenda
additional information
analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
brenda
additional information
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analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
brenda
additional information
analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
brenda
additional information
analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
brenda
additional information
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analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
brenda
additional information
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analysis of the expression patterns of RDHE2S, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis
-
brenda
additional information
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analysis of the expression patterns of RDHE2, quantitative RT-PCR enzyme expression analysis. The two transcripts of Rdhe2 and Rdhe2s exhibit a largely overlapping expression pattern with the highest expression levels in skin, followed by tongue, intestine, and esophagus, trace amounts of transcripts are detected in adipose tissue, colon, and possibly testis. Rdhe2 transcripts are detected in sebaceous glands and epidermis of adult wild-type C57BL/J6 mice by in situ hybridization
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brenda
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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
-
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
-
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
-
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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C201R
the loss of function mutant is associated with severe loss of retinal functionand early onset severe retinal dystrophy
DELTAM1-Y13
truncated RoDH-4 that lacks the first thirteen amino acids of the N-terminal segment is partially active and exhibits the apparent Km value for androsterone similar to that of the wild-type enzyme, truncated mutant behaves as an integral membrane protein
DELTAS295-L317
removal of 23 N-terminal hydrophobic amino acids results in significant loss of activity and a 14fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein
DELTAY291-L317
removal of the C-terminal 27 amino acid segment results in about 600fold increase in the apparent Km value, truncated mutant behaves as an integral membrane protein
G43A/G47A/G49A
the triple mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
K214A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
K214R
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
N169A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
N169D
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197A
mutant retains significant enzymatic activities, although lower than that of wild type enzyme
S197C
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197G
mutant retains significant enzymatic activities, although lower than that of wild type enzyme
S197T
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
S197V
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
Y210A
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
Y210F
the mutation completely abolishes the enzymatic activity of RDH10 without affecting its protein level
L3R/L5R/R16Q/R19Q/R21Q
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RDH1 mutant, 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, the mutant faces the lumen
additional information
protein that lacked all four hydrophobic segments remains associated with the membrane. Thus, the N-terminal and the C-terminal ends are both important for RoDH-4 activity and the removal of the putative transmembrane segments does not convert RoDH-4 into a soluble protein, suggesting additional sites of membrane interaction
additional information
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protein that lacked all four hydrophobic segments remains associated with the membrane. Thus, the N-terminal and the C-terminal ends are both important for RoDH-4 activity and the removal of the putative transmembrane segments does not convert RoDH-4 into a soluble protein, suggesting additional sites of membrane interaction
additional information
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RDH8 genotping and phenotyping in Han Chinese population, identification of single nucleotide polymorphisms in RDH8 gene: RDH855b (-1715G/A; rs3760753), RDH851 (-472C/T; rs2233789), and RDH8E5a (7826T/C; rs1644731), overview
additional information
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mutants lacking amino-terminal 18 or 30 amino acids do not localize to endoplasmic reticulum but to mitochondria instead. Deletion mutant lacking 28 C-terminal amino acids localizes both to microsomal and mitochondrial fractions. Deletion of both 18 N-terminal and 28 C-terminal amino acids leeds to overwhelming detection in mitochondria. Fusion of N-terminal 22 amino acids of enzyme with green fluorescent protein localizes in endoplasmic reticulum. Fusion of N-terminal 18 amino acids of enzyme with green fluorescent protein shows diffuse localization. Fusion of green fluorescent protein with C-terminal 29 amino acids of enzyme shows diffuse cytoplasmic and nuclear localization.
additional information
generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
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generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
-
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
additional information
-
generation of single knockout Rdhe2s-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
-
additional information
-
generation of single knockout Rdhe2-/- and Rdhe2-/-,Rdhe2s-/- double-knockout mice (DKO) lacking both RDHE2 and RDHE2S using CRISPR-mediated gene editing. Phenotypes of femal DKO mice compared to male wild-type mice, overview. Elevated expression of hair-follicle growth and differentiation marker genes in DKO skin relative to littermate wild-type skin. The lack of expression of RDHE2 and RDHE2S results in enlargement of meibomian glands of DKO animals
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Koen, A.L.; Shaw, C.R.
Retinol and alcohol dehydrogenases in retina and liver
Biochim. Biophys. Acta
128
48-54
1966
Rattus norvegicus
brenda
Leo, M.A.; Lieber, C.S.
NAD+-dependent retinol dehydrogenase in liver microsomes
Methods Enzymol.
189
520-524
1990
Rattus norvegicus
brenda
Leo, M.A.; Kim., C.I.; Lieber, C.S.
NAD+-dependent retinol dehydrogenase in liver microsomes
Arch. Biochem. Biophys.
259
241-249
1987
Peromyscus maniculatus, Rattus norvegicus
brenda
Kishore, G.S.; Boutwell, R.K.
Enzymatic oxidation and reduction of retinal by mouse epidermis
Biochem. Biophys. Res. Commun.
94
1381-1386
1980
Mus musculus
brenda
Gough, W.H.; VanOoteghem, S.; Sint, T.; Kedishvili, N.Y.
cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids
J. Biol. Chem.
273
19778-19785
1998
Homo sapiens (O75452), Homo sapiens
brenda
Jurukovski, V.; Markova, N.G.; Karaman-Jurukovska, N.; Randolph, R.K.; Su, J.; Napoli, J.L.; Simon, M.
Cloning and characterization of retinol dehydrogenase transcripts expressed in human epidermal keratinocytes
Mol. Genet. Metab.
67
62-73
1999
Homo sapiens
brenda
Tajima, S.; Goda, T.; Takase, S.
Co-ordinated induction of beta-caroten cleavage enzyme and retinal reductase in the duodenum of the developing chicks
Comp. Biochem. Physiol. B
128
425-434
2001
Gallus gallus
brenda
Karlsson, T.; Vahlquist, A.; Kedishvili, N.; Torma, H.
13-cis-retinoic acid competitively inhibits 3alpha-hydroxysteroid oxidation by retinol dehydrogenase RoDH-4: a mechanism for its anti-androgenic effects in sebaceous glands?
Biochem. Biophys. Res. Commun.
303
273-278
2003
Homo sapiens
brenda
Lapshina, E.A.; Belyaeva, O.V.; Chumakova, O.V.; Kedishvili, N.Y.
Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4
Biochemistry
42
776-784
2003
Homo sapiens
brenda
Zhang, M.; Hu, P.; Napoli, J.L.
Elements in the N-terminal signaling sequence that determine cytosolic topology of short-chain dehydrogenases/reductases. Studies with retinol dehydrogenase type 1 and cis-retinol/androgen dehydrogenase type 1
J. Biol. Chem.
279
51482-51489
2004
Mus musculus
brenda
Gallego, O.; Belyaeva, O.V.; Porte, S.; Ruiz, F.X.; Stetsenko, A.V.; Shabrova, E.V.; Kostereva, N.V.; Farres, J.; Pares, X.; Kedishvili, N.Y.
Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids
Biochem. J.
399
101-109
2006
Homo sapiens (O75452), Homo sapiens
brenda
Liden, M.; Eriksson, U.
Understanding retinol metabolism: Structure and function of retinol dehydrogenases
J. Biol. Chem.
281
13001-13004
2006
Bos taurus, Homo sapiens, Mus musculus
brenda
Dalfo, D.; Marques, N.; Albalat, R.
Analysis of the NADH-dependent retinaldehyde reductase activity of amphioxus retinol dehydrogenase enzymes enhances our understanding of the evolution of the retinol dehydrogenase family
FEBS J.
274
3739-3752
2007
Branchiostoma floridae
brenda
Maeda, A.; Maeda, T.; Sun, W.; Zhang, H.; Baehr, W.; Palczewski, K.
Redundant and unique roles of retinol dehydrogenases in the mouse retina
Proc. Natl. Acad. Sci. USA
104
19565-19570
2007
Mus musculus (O55240), Mus musculus
brenda
Takahashi, Y.; Moiseyev, G.; Farjo, K.; Ma, J.X.
Characterization of key residues and membrane association domains in retinol dehydrogenase 10
Biochem. J.
419
113-122
2009
Homo sapiens (Q8IZV5)
brenda
Pares, X.; Farres, J.; Kedishvili, N.; Duester, G.
Medium- and short-chain dehydrogenase/reductase gene and protein families: Medium-chain and short-chain dehydrogenases/reductases in retinoid metabolism
Cell. Mol. Life Sci.
65
3936-3949
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Belyaeva, O.V.; Chetyrkin, S.V.; Kedishvili, N.Y.
Characterization of truncated mutants of human microsomal short-chain dehydrogenase/reductase RoDH-4
Chem. Biol. Interact.
143-144
279-287
2003
Homo sapiens (O75462), Homo sapiens
brenda
Lee, S.A.; Belyaeva, O.V.; Kedishvili, N.Y.
Biochemical characterization of human epidermal retinol dehydrogenase 2
Chem. Biol. Interact.
178
182-187
2009
Homo sapiens (Q8N3Y7), Homo sapiens
brenda
Zhang, M.
Chen, W.; Smith, S.M.; Napoli, J.L.: Molecular characterization of a mouse short chain dehydrogenase/reductase active with all-trans-retinol in intact cells, mRDH1
J. Biol. Chem.
276
44083-44090
2001
Mus musculus (Q8VIJ7), Mus musculus
brenda
Strate, I.; Min, T.H.; Iliev, D.; Pera, E.M.
Retinol dehydrogenase 10 is a feedback regulator of retinoic acid signalling during axis formation and patterning of the central nervous system
Development
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461-472
2009
Xenopus laevis (C3TWL9)
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Moradi, P.; Mackay, D.; Hunt, D.; Moore, A.
Focus on molecules: Retinol dehydrogenase 12 (RDH12)
Exp. Eye Res.
87
160-161
2008
Homo sapiens (Q96NR8)
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Napoli, J.L.
Physiological insights into all-trans-retinoic acid biosynthesis
Biochim. Biophys. Acta
1821
152-167
2012
Homo sapiens, Mus musculus, Rattus norvegicus
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Chen, C.; Thompson, D.A.; Koutalos, Y.
Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12
J. Biol. Chem.
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2012
Mus musculus, Mus musculus C57BL/6 x 129/Sv
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Yu, Y.S.; Wang, L.L.; Shen, Y.; Yap, M.K.; Yip, S.P.; Han, W.
Investigation of the association between all-trans-retinol dehydrogenase (RDH8) polymorphisms and high myopia in Chinese
J. Zhejiang Univ. Sci. B
11
836-841
2010
Homo sapiens
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Hong, S.H.; Ngo, H.P.; Kang, L.W.; Oh, D.K.
Characterization of alcohol dehydrogenase from Kangiella koreensis and its application to production of all-trans-retinol
Biotechnol. Lett.
37
849-856
2015
Kangiella koreensis, Kangiella koreensis (C7R702), Kangiella koreensis SW-125
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Belyaeva, O.V.; Chang, C.; Berlett, M.C.; Kedishvili, N.Y.
Evolutionary origins of retinoid active short-chain dehydrogenases/reductases of SDR16C family
Chem. Biol. Interact.
234
135-143
2015
Ciona intestinalis, Ciona intestinalis (F6WB20), Lytechinus variegatus (A0A0A7HFB2), Lytechinus variegatus (A0A0A7HFH3), Lytechinus variegatus (A0A0A7HGC7), Lytechinus variegatus
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Adams, M.K.; Lee, S.A.; Belyaeva, O.V.; Wu, L.; Kedishvili, N.Y.
Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10
Chem. Biol. Interact.
276
88-94
2017
Homo sapiens, Homo sapiens (Q8N3Y7)
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Adams, M.K.; Belyaeva, O.V.; Wu, L.; Kedishvili, N.Y.
The retinaldehyde reductase activity of DHRS3 is reciprocally activated by retinol dehydrogenase 10 to control retinoid homeostasis
J. Biol. Chem.
289
14868-14880
2014
Homo sapiens, Homo sapiens (Q8IZV5)
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Obrochta, K.M.; Krois, C.R.; Campos, B.; Napoli, J.L.
Insulin regulates retinol dehydrogenase expression and all-trans-retinoic acid biosynthesis through FoxO1
J. Biol. Chem.
290
7259-7268
2015
Homo sapiens (O75452), Homo sapiens (Q8IZV5), Homo sapiens, Mus musculus (Q8VIJ7), Mus musculus
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Hofmann, L.; Tsybovsky, Y.; Alexander, N.S.; Babino, D.; Leung, N.Y.; Montell, C.; Banerjee, S.; von Lintig, J.; Palczewski, K.
Structural insights into the Drosophila melanogaster retinol dehydrogenase, a member of the short-chain dehydrogenase/reductase family
Biochemistry
55
6545-6557
2016
Drosophila melanogaster (Q7KNR7), Drosophila melanogaster
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Wu, L.; Belyaeva, O.V.; Adams, M.K.; Klyuyeva, A.V.; Lee, S.A.; Goggans, K.R.; Kesterson, R.A.; Popov, K.M.; Kedishvili, N.Y.
Mice lacking the epidermal retinol dehydrogenases SDR16C5 and SDR16C6 display accelerated hair growth and enlarged meibomian glands
J. Biol. Chem.
294
17060-17074
2019
Mus musculus (Q05A13), Mus musculus (Q7TQA3), Mus musculus, Mus musculus C57BL/6J (Q05A13), Mus musculus C57BL/6J (Q7TQA3)
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