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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: High ALDH3A1 expression and activity have been correlated with cell proliferation, resistance against aldehydes derived from lipid peroxidation, and resistance against drug toxicity, such as oxazaphosphorines.
213 citations
TL;DR: Results indicate that this enzyme may have a physiological function by protecting the cell against the toxic effect of aldehydes derived from lipid oxidation, and speculate that in Escherichia coli YqhD is part of a glutathione-independent, NADPH-dependent response mechanism to lipid peroxidation.
210 citations
TL;DR: Apoptosis of alveolar epithelial cells may be one of the mechanisms of lung injury induced by cigarette smoking, and this cytotoxic effect might be due to an interaction between aldehydes and oxidants present in CSE or formed in C SE-exposed cells.
Abstract: Injury of the alveolar epithelium by cigarette smoke is presumed to be an important process in the pathogenesis of smoking-related pulmonary diseases We investigated the cytotoxic effects of cigarette smoke extract (CSE) on an alveolar type II cell-derived cell line (A549) CSE caused apoptosis at concentrations of 5% or less and necrosis at 10% or more When CSE was exposed to air before application to A549 cells, the cytotoxic effects were attenuated CSE caused cell death without direct contact with the cells Acrolein and hydrogen peroxide, two major volatile factors in cigarette smoke, caused cell death in a similar manner Aldehyde dehydrogenase, a scavenger of aldehydes, and N-acetylcysteine, a scavenger of oxidants and aldehydes, completely inhibited CSE-induced apoptosis CSE and acrolein increased intracellular oxidant activity In conclusion, apoptosis of alveolar epithelial cells may be one of the mechanisms of lung injury induced by cigarette smoking This cytotoxic effect might be due to an interaction between aldehydes and oxidants present in CSE or formed in CSE-exposed cells
208 citations
TL;DR: The model proposed has been confirmed by cloning and by characterization of cDNAs and genes and it was proposed that three non-allelic loci are involved in the synthesis of three types of subunits, α, β , and γ, respectively.
Abstract: Publisher Summary This chapter explains the molecular genetics of human alcohol dehydrogenase and aldehyde dehydrogenase. Relationships between the genetic variations and alcohol-related physiological problems have become apparent. More than 80% of ethanol administered is oxidized by alcohol dehydrogenase and most of the acetaldehyde thus formed is further oxidized to acetate by aldehyde dehydrogenase in the liver. Alcohol dehydrogenases are enzymes catalyzing the conversion of various alcohols to the corresponding aldehydes by means of an NAD+-dependent oxidation. The human ADH isozyme system is extremely complex and varied among individuals. Based on the analyses of electrophoretic variations and the mode of inheritance of isozyme patterns, it was proposed that: three non-allelic loci are involved in the synthesis of three types of subunits, α, β, and γ, respectively. The ADH2 and ADH3 loci are dimorphic— that is, there are two common alleles, ADH12 and ADH22, and ADH31 and ADH23 respectively, in each locus; and the catalytically active ADH isozymes are homo- and heterodimers of these wild-type and variant-type subunits. Later, an additional common variant allele in the ADH2 locus was found in American blacks. The model proposed has been confirmed by cloning and by characterization of cDNAs and genes.
204 citations
TL;DR: Mounting evidence suggests that ALDH not only may be used as a marker for stem cells but also may well regulate cellular functions related to self-renewal, expansion, differentiation, and resistance to drugs and radiation.
Abstract: Aldehyde dehydrogenase (ALDH) is a superfamily of enzymes that detoxify a variety of endogenous and exogenous aldehydes and are required for the biosynthesis of retinoic acid (RA) and other molecular regulators of cellular function. Over the past decade, high ALDH activity has been increasingly used as a selectable marker for normal cell populations enriched in stem and progenitor cells, as well as for cell populations from cancer tissues enriched in tumor-initiating stem-like cells. Mounting evidence suggests that ALDH not only may be used as a marker for stem cells but also may well regulate cellular functions related to self-renewal, expansion, differentiation, and resistance to drugs and radiation. ALDH exerts its functional actions partly through RA biosynthesis, as all-trans RA reverses the functional effects of pharmacological inhibition or genetic suppression of ALDH activity in many cell types in vitro. There is substantial evidence to suggest that the role of ALDH as a stem cell marker comes down to the specific isoform(s) expressed in a particular tissue. Much emphasis has been placed on the ALDH1A1 and ALDH1A3 members of the ALDH1 family of cytosolic enzymes required for RA biosynthesis. ALDH1A1 and ALDH1A3 regulate cellular function in both normal stem cells and tumor-initiating stem-like cells, promoting tumor growth and resistance to drugs and radiation. An improved understanding of the molecular mechanisms by which ALDH regulates cellular function will likely open new avenues in many fields, especially in tissue regeneration and oncology.
204 citations