Ask about this productRelated genes to: RDH14 antibody
- Gene:
- RDH14 NIH gene
- Name:
- retinol dehydrogenase 14
- Previous symbol:
- -
- Synonyms:
- PAN2, SDR7C4
- Chromosome:
- 2p24.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-12-11
- Date modifiied:
- 2017-12-15
Related products to: RDH14 antibody
Related articles to: RDH14 antibody
- This study provides a comprehensive tissue-specific transcriptomic analysis of mitochondrial genes associated with vitamin metabolism in buffalo. Using RNA-seq data from four post-pubertal female buffalo tissues (kidney, heart, brain, and ovary), we profiled 41 nuclear-encoded mitochondrial genes involved in the metabolism of B-complex vitamins, vitamins A, C, D, folate, choline, and one-carbon pathways. The kidney exhibited the highest expression of biotin-related genes (ACACB, PC, PCCA), supporting roles in fatty acid oxidation and gluconeogenesis, while the heart showed moderate expression, and the brain and ovary lower expression, consistent with their metabolic functions. In vitamin A metabolism, the kidney showed elevated transcription of AKR1B10 and BCO2 (retinoid detoxification), whereas the heart exhibited moderate RDH14 expression, and the brain and ovary showed minimal transcriptional activity. Vitamin D-related genes were highly expressed in the kidney (FDX1) and ovary (FDXR), with lower expression in heart and brain. Vitamin B6-associated genes were prominently expressed in the ovary (PLPBP) and kidney/brain (PNPO), with low expression in the heart. B12-processing genes (MMAA, MMAB, MMADHC) showed the highest expression in the kidney, followed by the heart. The thiamine transporter SLC25A19 was transcriptionally enriched in the ovary, with moderate expression in kidney and brain. Riboflavin metabolism genes (RFK, FLAD1, SLC25A32) were more highly expressed in the kidney and heart, while choline and betaine metabolism genes (DMGDH, CHDH, SARDH) and one-carbon metabolism genes (ALDH1L1, AMT, SFXN1) were predominantly expressed in the kidney. Overall, this transcriptomic evidence reveals organ-specific expression patterns of vitamin-dependent mitochondrial pathways in buffalo, offering insights for nutritional strategies to enhance livestock metabolic efficiency and contributing to the broader understanding of mammalian mitochondrial physiology. - Source: PubMed
Publication date: 2025/12/29
Sadeesh E MLahamge Madhuri SSingh PratikshaMohiddin Roshan - Preterm birth affects approximately 5% to 7% of live births worldwide and is the leading cause of neonatal morbidity and mortality. Amniotic fluid supernatant (AFS) contains abundant cell-free nucleic acids (cfNAs) that can provide genetic information associated with pregnancy complications. In the current study, cfNAs of AFS in the early second-trimester before the onset of symptoms of preterm birth were analyzed, and we compared gene expression levels between spontaneous preterm birth (n = 5) and term birth (n = 5) groups using sequencing analysis. Differential expression analyses detected 24 genes with increased and 6 genes with decreased expression in the preterm birth group compared to term birth. Upregulated expressions of RDH14, ZNF572, VOPP1, SERPINA12, and TCF15 were validated in an extended AFS sample by quantitative PCR (preterm birth group, n = 21; term birth group, n = 40). Five candidate genes displayed a significant increase in mRNA expression in immortalized trophoblast HTR-8/SVneo cell with HO treatment. Moreover, the expression of five candidate genes was increased to more than twofold by pretreatment with lipopolysaccharide in HTR-8/SVneo cells. Changes in gene expression between preterm birth and term birth is strongly correlated with oxidative stress and infection during pregnancy. Specific expression patterns of genes could be used as potential markers for the early identification of women at risk of having a spontaneous preterm birth. - Source: PubMed
Publication date: 2022/03/31
Kim Min-ALee Eun-JuYang WookyeomShin Ha-YeonKim Young-HanKim Jae-Hoon - In a multi-branch family from Pakistan, individuals presenting with palmoplantar keratoderma segregate in autosomal dominant fashion, and individuals with intellectual disability (ID) segregate in apparent autosomal recessive fashion. Initial attempts to identify the ID locus using homozygosity-by-descent (HBD) mapping were unsuccessful. However, following an assumption of locus heterogeneity, a reiterative HBD approach in concert with whole exome sequencing (WES) was employed. We identified a known disease-linked mutation in the polymicrogyria gene, ADGRG1, in two affected members. In the remaining two (living) affected members, HBD mapping cross-referenced with WES data identified a single biallelic frameshifting variant in the gene encoding retinol dehydrogenase 14 (RDH14). Transcription data indicate that RDH14 is expressed in brain, but not in retina. Magnetic resonance imaging for the individuals with this RDH14 mutation show no signs of polymicrogyria, however cerebellar atrophy was a notable feature. RDH14 in HEK293 cells localized mainly in the nucleoplasm. Co-immunoprecipitation studies confirmed binding to the proton-activated chloride channel 1 (PACC1/TMEM206), which is greatly diminished by the mutation. Our studies suggest RDH14 as a candidate for autosomal recessive ID and cerebellar atrophy, implicating either disrupted retinoic acid signaling, or, through PACC1, disrupted chloride ion homeostasis in the brain as a putative disease mechanism. - Source: PubMed
Publication date: 2021/11/30
Pastore Stephen FMuhammad TahirHarripaul RicardoLau RebeccaKhan Muhammad Tariq MasoodKhan Muhammad IsmailIslam OmarKang ChangsooAyub MuhammadJelani MusharrafVincent John B - Cone photoreceptors require effective pigment regeneration mechanisms to maintain their sensitivity in the light. Our previous studies in carp cones suggested the presence of an unconventional and very effective mechanism to produce 11-cis retinal, the necessary component in pigment regeneration. In this reaction (aldehyde-alcohol redox coupling reaction, AL-OL coupling reaction), formation of 11-cis retinal, i.e. oxidation of 11-cis retinol is coupled to reduction of an aldehyde at a 1:1 molar ratio without exogenous NADP(H) which is usually required in this kind of reaction. Here, we identified carp retinol dehydrogenase 13-like (RDH13L) as an enzyme catalyzing the AL-OL coupling reaction. RDH13L was partially purified from purified carp cones, identified as a candidate protein, and its AL-OL coupling activity was confirmed using recombinant RDH13L. We further examined the substrate specificity, subcellular localization, and expression level of RDH13L. Based on these results, we concluded that RDH13L contributes to a significant part, but not all, of the AL-OL coupling activity in carp cones. RDH13L contained tightly bound NADP(+) which presumably functions as a cofactor in the reaction. Mouse RDH14, a mouse homolog of carp RDH13L, also showed the AL-OL coupling activity. Interestingly, although carp cone membranes, carp RDH13L and mouse RDH14 all showed the coupling activity at 15-37 °C, they also showed a conventional NADP(+)-dependent 11-cis retinol oxidation activity above 25 °C without addition of aldehydes. This dual mechanism of 11-cis retinal synthesis attained by carp RDH13L and mouse RDH14 probably contribute to effective pigment regeneration in cones that function in the light. - Source: PubMed
Publication date: 2014/12/22
Sato ShinyaMiyazono SadaharuTachibanaki ShujiKawamura Satoru - Retinol dehydrogenase 13 (RDH13) is a recently identified short-chain dehydrogenase/reductase related to microsomal retinoid oxidoreductase RDH11. In this study, we examined the distribution of RDH13 in human tissues, determined its subcellular localization and characterized the substrate and cofactor specificity of purified RDH13 in order to better understand its properties. The results of this study demonstrate that RDH13 exhibits a wide tissue distribution and, by contrast with other members of the RDH11-like group of short-chain dehydrogenases/reductases, is a mitochondrial rather than a microsomal protein. Protease protection assays suggest that RDH13 is localized on the outer side of the inner mitochondrial membrane. Kinetic analysis of the purified protein shows that RDH13 is catalytically active and recognizes retinoids as substrates. Similar to the microsomal RDHs, RDH11, RDH12 and RDH14, RDH13 exhibits a much lower Km value for NADPH than for NADH and has a greater catalytic efficiency in the reductive than in the oxidative direction. The localization of RDH13 at the entrance to the mitochondrial matrix suggests that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene. - Source: PubMed
Publication date: 2007/11/26
Belyaeva Olga VKorkina Olga VStetsenko Anton VKedishvili Natalia Y