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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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Journal ArticleDOI
TL;DR: The in vitro interactions of DSF, as well as a principal metabolite S-methyl-N,N-diethylthiocarbamoyl sulfoxide (MeDTC-SO), with both recombinant rat liver mitochondrial monomeric ALDH (rmALDH) and homotetrameric rmALDH are described.

58 citations

Journal ArticleDOI
TL;DR: Rat colonic mucosa was found to possess detectable amounts of ALDH activity with both micromolar and millimolar acetaldehyde concentrations and in all subcellular fractions, and ALDH isoenzymes found in the small intestine and stomach were not detectable in colonic samples, generally low when compared with the liver and stomach, and they also tended to be lower than in small intestine.
Abstract: Intracolonic bacteria have previously been shown to produce substantial amounts of acetaldehyde during ethanol oxidation, and it has been suggested that this acetaldehyde might be associated with alcohol-related colonic disorders, as well as other alcohol-induced organ injuries. The capacity of colonic mucosa to remove this bacterial acetaldehyde by aldehyde dehydrogenase (ALDH) is, however, poorly known. We therefore measured ALDH activities and determined ALDH isoenzyme profiles from different subcellular fractions of rat colonic mucosa. For comparison, hepatic, gastric, and small intestinal samples were studied similarly. Alcohol dehydrogenase (ADH) activities were also measured from all of these tissues. Rat colonic mucosa was found to possess detectable amounts of ALDH activity with both micromolar and millimolar acetaldehyde concentrations and in all subcellular fractions. The ALDH activities of colonic mucosa were, however, generally low when compared with the liver and stomach, and they also tended to be lower than in small intestine. Mitochondrial low K(m) ALDH2 and cytosolic ALDH with low K(m) for acetaldehyde were expressed in the colonic mucosa, whereas some cytosolic high K(m) isoenzymes found in the small intestine and stomach were not detectable in colonic samples. Cytosolic ADH activity corresponded well to ALDH activity in different tissues: in colonic mucosa, it was approximately 6 times lower than in the liver and about one-half of gastric ADH activity. ALDH activity of the colonic mucosa should, thus, be sufficient for the removal of acetaldehyde produced by colonic mucosal ADH during ethanol oxidation. It may, however, be insufficient for the removal of the acetaldehyde produced by intracolonic bacteria. This may lead to the accumulation of acetaldehyde in the colon and colonic mucosa after ingestion of ethanol that might, at least after chronic heavy alcohol consumption, contribute to the development of alcohol-related colonic morbidity, diarrhea, and cancer.

58 citations

Journal ArticleDOI
TL;DR: Porcine livers and hepatocytes from pigs can detoxify a large spectrum of exogenous and endogenous compounds, which makes them a convenient substitute for allogeneic transplants for patients with liver failure.
Abstract: Background Both livers and hepatocytes from pigs have been proposed for the treatment of end-stage liver diseases, as an alternative to allogeneic liver transplants. However, little is known of the capability of porcine hepatocytes to fulfill the biotransformation pathways of toxic compounds, including those released from livers in acute failure. We have studied the activity and expression of detoxifying enzymes in porcine livers and in cultured hepatocytes and their induction by phenobarbital. Methods Cytochromes P450 (CYP) 1A, 2B, and 3A and GST-like activities were tested with the following specific substrates: 7-ethoxyresorufin, 7-pentoxyresorufin, nifedipine, testosterone, 1-chloro-2,4-dinitrobenzene, 1,2-dichloro-4-nitrobenzene, and ethacrinic acid. CYP 1A1/2-, 2B1/2-, 2E1- and 3A4-related and GSTalpha proteins were analyzed by Western blotting and CYP 1A1/2, 2B1/2, 2C6, 2E1, and 3A4, aldehyde dehydrogenase, epoxide hydrolase, and GSTalpha-like RNA by Northern blotting. Results Enzymatic activities reflecting the expression of CYP 1A-, CYP 2B-, CYP 2E1-, and CYP 3A-like genes, that is, ethoxyresorufin-O-deethylase, pentoxyresorufin-O-deethylase, nifedipine oxidase and testosterone 6beta-hydroxylase, and chlorzoxazone 6-hydroxylase, were identified in pig livers. CYP 1A and CYP 2E1, GSTalpha-like proteins, CYP 1A, 2C, and 2E, epoxide hydrolase, aldehyde dehydrogenase, and GST like RNA were expressed in vivo and in vitro. CYP 2B and CYP 3A RNA and proteins, and their associated activities were induced by phenobarbital. Conclusions Porcine hepatocytes express the most important biotransformation enzymes and their corresponding activities and RNA. Thus, livers and hepatocytes from pigs can detoxify a large spectrum of exogenous and endogenous compounds, which makes them a convenient substitute for allogeneic transplants for patients with liver failure.

58 citations

Journal ArticleDOI
01 Jul 1993-Cornea
TL;DR: Analysis of several studies tends to support the proposed structural function of ALDH in human cornea, and indicates that there is a correlation between the activity of GR and GST in the normal and a separate group of corneal disorders.
Abstract: Previously we have reported that various pathologic corneas exhibited a "diseased" two-band corneal aldehyde dehydrogenase (ALDH) zymogram after native polyacrylamide gel electrophoresis as compared with the three bands in the normal human cornea. Experimentally, such a "diseased" zymogram pattern could be induced by addition of reduced glutathione (GSH) to the normal corneal epithelial extract. This finding suggests that in vivo the conformation of corneal ALDH may be related to changes in the GSH redox system during the process of corneal diseases. To investigate this hypothesis in keratoconus corneal epithelial extracts and a separate group comprising other corneal disorders, mainly herpes keratitis, we indirectly measured the GSH turnover by assaying the activity of glutathione reductase (GR) which is responsible in producing GSH and glutathione s-transferase (GST), which converts GSH into mercapturic acid. Our results indicate that there is a correlation between the activity of GR and GST in the normal and the separate group of corneal disorders. Because GST is the first enzyme in the mercapturic acid pathway, which detoxifies xenobiotic substrates including aldehydes, as by-products of membrane lipid peroxidation, an elevated GSH turnover might be necessary to counteract oxidative threats. However, no correlation was found between corneal ALDH level with either GR or GST. On the other hand, keratoconus samples demonstrated a distinct enzymatic behavior that was in concordance with our earlier result in the corneal ALDH zymogram after isoelectric focusing. Furthermore, analysis of our several studies tends to support the proposed structural function of ALDH in human cornea.

58 citations

Journal ArticleDOI
TL;DR: It is demonstrated that ALDH3A1 can reduce protein inactivation and/or aggregation not only by detoxification of reactive aldehydes but also by directly absorbing UV energy.

58 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023260
2022192
202170
202081
201980
201895