Distribution of alcohol and sorbitol dehydrogenases

Estonius, Mats; Danielsson, Olle; Karlsson, Christina; Persson, Håkan; Jörnvall, Hans; Höög, Jan‐Olov

doi:10.1111/j.1432-1033.1993.tb18059.x

Cited by 81 publications

(38 citation statements)

References 55 publications

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“…The high levels of SDH mRNA detected in testes, liver and kidney are in agreement with the previous reports on the expression profiles of rat (8) or mouse (9) SDH mRNA by Northern blot analysis. SDH, in conjunction with AR, is thought to be involved in osmoregulation in kidney (5) and fructose synthesis in testis (6).…”

supporting

confidence: 81%

Gene Expression of Enzymes Comprising the Polyol Pathway in Various Rat Tissues Determined by the Competitive RT-PCR Method

Maekawa

Tanimoto

Okada

2002

Japanese Journal of Pharmacology

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ABSTRACT-The quantitative measurements of aldose reductase (AR) and sorbitol dehydrogenase (SDH) gene expression in various rat tissues were performed by the competitive reverse transcription-polymerase chain reaction (RT-PCR). AR mRNA was detectable in all tissues analyzed with pronounced differences in the amounts. SDH mRNA was most abundant in testes and liver, but was absent from lens. The estimation of the AR cDNA / SDH cDNA ratio showed that the relative abundance of SDH to AR differs among tissues. These results indicate that different tissues contain varying amounts of AR mRNA and SDH mRNA; that is, each tissue has its own polyol pathway activity.

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supporting

confidence: 81%

Gene Expression of Enzymes Comprising the Polyol Pathway in Various Rat Tissues Determined by the Competitive RT-PCR Method

Maekawa

Tanimoto

Okada

2002

Japanese Journal of Pharmacology

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“…High levels of class I ADH mRNA were found in the kidney, stomach, duodenum, colon and uterus of rats (Estonius et al 1993), with lower levels in many organs, including the lung, small intestine and hepatic Ito cells (Yamauchi et al 1988). Very low levels were found in the brain, thymus, muscle or heart (Estonius et al 1993).…”

Section: Alcohol Dehydrogenasesmentioning

confidence: 99%

Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology

et al. 2004

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Alcohol dehydrogenase (ADH) and mitochondrial aldehyde dehydrogenase (ALDH2) are responsible for metabolizing the bulk of ethanol consumed as part of the diet and their activities contribute to the rate of ethanol elimination from the blood. They are expressed at highest levels in liver, but at lower levels in many tissues. This pathway probably evolved as a detoxification mechanism for environmental alcohols. However, with the consumption of large amounts of ethanol, the oxidation of ethanol can become a major energy source and, particularly in the liver, interferes with the metabolism of other nutrients. Polymorphic variants of the genes for these enzymes encode enzymes with altered kinetic properties. The pathophysiological effects of these variants may be mediated by accumulation of acetaldehyde; high-activity ADH variants are predicted to increase the rate of acetaldehyde generation, while the low-activity ALDH2 variant is associated with an inability to metabolize this compound. The effects of acetaldehyde may be expressed either in the cells generating it, or by delivery of acetaldehyde to various tissues by the bloodstream or even saliva. Inheritance of the high-activity ADH β2, encoded by the ADH2*2 gene, and the inactive ALDH2*2 gene product have been conclusively associated with reduced risk of alcoholism. This association is influenced by gene–environment interactions, such as religion and national origin. The variants have also been studied for association with alcoholic liver disease, cancer, fetal alcohol syndrome, CVD, gout, asthma and clearance of xenobiotics. The strongest correlations found to date have been those between the ALDH2*2 allele and cancers of the oro-pharynx and oesophagus. It will be important to replicate other interesting associations between these variants and other cancers and heart disease, and to determine the biochemical mechanisms underlying the associations.

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“…The solution was stirred for 10 min and centrifuged at of Medical Biochemistry and Biophysics, Karolinska Institute 10 000 g for 15 min. The concentration of poly(ethylene glycol) [15]. Northern blot was accomplished according to a standard in the supernatant was brought up to 15% and the solution was procedure [16] using a 32 P-labeled probe generated by PCR (a centrifuged under the same conditions.…”

mentioning

confidence: 99%

A stress‐inducible rat liver endoplasmic reticulum protein, ERp29

Mkrtchian

Fang

Hellman

et al. 1998

European Journal of Biochemistry

103

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We have isolated, cDNA cloned and characterised a 29-kDa protein (ERp29), containing a C-terminal endoplasmic reticulum(ER)-retrieval signal, from the rat liver ER. ERp29 was induced to high levels in the rat hepatoma cells under metabolic stress conditions known to cause an aberrant accumulation of proteins in the ER [(e.g. culture in presence of the Ca 2ϩ ionophore A23187, inhibitors of Ca 2ϩ -ATPase (thapsigargin), intracellular protein transport (brefeldin A), or protein N-glycosylation (tunicamycin)]. Experimental evidence of its localisation in the luminal compartment of the ER was obtained by topology studies including immunofluorescence microscopy, in vitro translation and proteinase protection assay. ERp29 constitutes about 0.1% of the rat hepatic microsomal proteins and is constitutively expressed in all rat tissues examined, as evident from northern blot analysis. In rat hepatoma cells ERp29 was found to be associated with the abundant molecular chaperone/stress protein BiP/GRP78 and this interaction was significantly enhanced after treatment with tunicamycin and A23187. Taken together, these results suggest that ERp29 is a member of the stress-response machinery of the ER.Keywords : ERp29; endoplasmic reticulum; stress protein; retrieval signal; BiP/GRP78.The luminal compartment of the endoplasmic reticulum (ER) of the export of secretory proteins from the ER by brefeldin A, an inhibitor of intracellular transport, may also result in excesin eukaryotic cells is a site where nascent polypeptides, destined for transport to Golgi, lysosomes or cell exterior attain their sive accumulation of malfolded proteins in ER and hence cause induction of stress proteins [7]. native three-dimensional configuration, undergo several posttranslational modifications and are assembled. Molecular chap-ER stress-inducible proteins belong to structurally diverse protein families including glucose-regulated proteins GRP78/ erones facilitate these processes assisting in folding and preventing aggregation of nascent chains by binding to the interactive BiP and GRP94 which are similar to the cytosolic heat-shock proteins (Hsp70 and Hsp90, respectively), calnexin, calreticulin protein surface [1]. Other luminal enzymes, which are involved in protein maturation, catalyze disulphide bond formation and and protein disulfide isomerase (PDI and other thioredoxin-containing proteins such as ERp72 and ERp61). The importance of rearrangement, N-linked glycosylation, participate in maintaining calcium homeostasis and in protein trafficking (reviewed in these proteins for the luminal compartment is accentuated by their ER-retrieval signal, the C-terminal tetrapeptide KDEL [2Ϫ3]).The biosynthesis of chaperones and some folding enzymes [8Ϫ9]. A protein (ERp29) with a similar C-terminal sequence is increased in stressed ER, i.e. under a variety of adverse physiologic or metabolic conditions, whose common denominator is (KEEL) was isolated in our laboratory from rat liver ER and the corresponding cDNA was cloned [10]. An analogous clone was ...

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Distribution of alcohol and sorbitol dehydrogenases

Cited by 81 publications

References 55 publications

Gene Expression of Enzymes Comprising the Polyol Pathway in Various Rat Tissues Determined by the Competitive RT-PCR Method

Gene Expression of Enzymes Comprising the Polyol Pathway in Various Rat Tissues Determined by the Competitive RT-PCR Method

Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology

A stress‐inducible rat liver endoplasmic reticulum protein, ERp29

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