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Aldehyde dehydrogenase
About: Aldehyde dehydrogenase is a research topic. Over the lifetime, 3365 publications have been published within this topic receiving 107683 citations.
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TL;DR: The identification of an aldehyde dehydrogenase in the rat kidney that catalysed the oxidation of 9-cis- and all-trans-retinal to corresponding retinoic acids with high efficiency is reported, with 9-Cis-Retinol being 2-fold more active than all- Trans-Retinoic acid.
Abstract: 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 receptor family The existence of RXRs suggests a new role for isomerization in the biology of retinoic acid We report here the identification of an aldehyde dehydrogenase in the rat kidney that catalysed the oxidation of 9-cis- and all-trans-retinal to corresponding retinoic acids with high efficiency, 9-cis-retinal being 2-fold more active than all-trans-retinal Based on several criteria, such as amino acid sequence, pH optimum, and inhibition by chloral hydrate, this enzyme was found to be a novel isoenzyme of aldehyde dehydrogenase 9-cis-Retinol, the precursor for the biosynthesis of 9-cis-retinal was identified in the rat kidney The occurrence of endogenous 9-cis-retinol and the existence of specific dehydrogenase which participates in the catalysis of 9-cis-retinal suggest that all-trans-retinoi(d) isomerization to 9-cis-retinoi(d) occurs at the retinol level, analogous to all-trans-retinol isomerization to 11-cis-retinol in the visual cycle
105 citations
TL;DR: Arabidopsis thaliana belongs to those plants that do not naturally accumulate glycine betaine, although its genome contains two genes that code for betaine aldehyde dehydrogenases, and it is hypothesized that these genes may serve as detoxification enzymes controlling the level of aminoaldehydes, which are produced in cellular metabolism under stress conditions.
Abstract: Arabidopsis thaliana belongs to those plants that do not naturally accumulate glycine betaine (GB), although its genome contains two genes, ALDH10A8 and ALDH10A9 that code for betaine aldehyde dehydrogenases (BADHs). BADHs were initially known to catalyze the last step of the biosynthesis of GB in plants. But they can also oxidize metabolism-derived aminoaldehydes to their corresponding amino acids in some cases. This study was carried out to investigate the functional properties of Arabidopsis BADH genes. Here, we have shown that ALDH10A8 and ALDH10A9 proteins are targeted to leucoplasts and peroxisomes, respectively. The expression patterns of ALDH10A8 and ALDH10A9 genes have been analysed under abiotic stress conditions. Both genes are expressed in the plant and weakly induced by ABA, salt, chilling (4°C), methyl viologen and dehydration. The role of the ALDH10A8 gene was analysed using T-DNA insertion mutants. There was no phenotypic difference between wild-type and mutant plants in the absence of stress. But ALDH10A8 seedlings and 4-week-old plants were more sensitive to dehydration and salt stress than wild-type plants. The recombinant ALDH10A9 enzyme was shown to oxidize betaine aldehyde, 4-aminobutyraldehyde and 3-aminopropionaldehyde to their corresponding carboxylic acids. We hypothesize that ALDH10A8 or ALDH10A9 may serve as detoxification enzymes controlling the level of aminoaldehydes, which are produced in cellular metabolism under stress conditions.
104 citations
TL;DR: Combined exposure to these aldehydes with the same target organ (nose) and exerting the same type of adverse effect (nasal cytotoxicity), but partly with different target sites (different regions of the nasal mucosa), is not associated with a greater hazard than that associated with exposure to the individual chemicals.
104 citations
TL;DR: It is demonstrated that cervical cancer cells with high ALDH activity fulfill the functional criteria for CSCs, and ALDHhigh cells have enhanced self-renewal and differentiation potentials and are more resistant to cisplatin treatment than ALDHlow cells.
Abstract: // Shu-Yan Liu 1 and Peng-Sheng Zheng 1,2 1 Department of Reproductive Medicine, The First Affiliated Hospital of the Medical College, Xi’an Jiaotong University, Xi’an, The People’s Republic of China 2S ection of Cancer Stem Cell Research, Key Laboratory of Environment and Genes Related to Diseases, Ministry of Education of the People’s Republic of China, Xi’an, The People’s Republic of China Correspondence: Peng-Sheng Zheng, email: // Keywords : aldehyde dehydrogenase, cancer stem cells, cervical cancer, self-renewal, chemoresistance Received : November 5, 2013 Accepted : November 23, 2013 Published : November 25, 2013 Abstract High aldehyde dehydrogenase (ALDH) activity characterizes a subpopulation of cells with cancer stem cell (CSC) properties in several malignancies. To clarify whether ALDH can be used as a marker of cervical cancer stem cells (CCSCs), ALDH high and ALDH low cells were sorted from 4 cervical cancer cell lines and 5 primary tumor xenografts and examined for CSC characteristics. Here, we demonstrate that cervical cancer cells with high ALDH activity fulfill the functional criteria for CSCs: (1) ALDH high cells, unlike ALDH low cells, are highly tumorigenic in vivo ; (2) ALDH high cells can give rise to both ALDH high and ALDH low cells in vitro and i n vivo , thereby establishing a cellular hierarchy; and (3) ALDH high cells have enhanced self-renewal and differentiation potentials. Additionally, ALDH high cervical cancer cells are more resistant to cisplatin treatment than ALDH low cells. Finally, expression of the stem cell self-renewal-associated transcription factors OCT4, NANOG, KLF4 and BMI1 is elevated in ALDH high cervical cancer cells. Taken together, our data indicated that high ALDH activity may represent both a functional marker for CCSCs and a target for novel cervical cancer therapies.
104 citations
TL;DR: Ethanol in the presence of the EtOH-metabolizing enzyme, alcohol dehydrogenase (ADH) leads to the induction of sister-chromatid exchanges (SCEs) in human peripheral lymphocytes in vitro, interpreted to show that not ethanol itself, but its first metabolite acetaldehyde is mutagenic.
103 citations