• Journal of Ginseng Research
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• 제21권1호
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• pp.53-60
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• 1997

The changes in aldehyde dehydrogenase(ALDH, E.C. 1.2.1.3.) activity in neurons and astrocytes isolated from rat brains were investigated after administration of ethanol and Korean red ginseng(Panax ginseng C.A. Meyer) saponln. The cerebral ALDH activity with acetaldehyde and Propionaldehyde was higher in the white matter than in the gray matter. However, using indole-3-a-cetaldehyde and 3,4-dihydroxyphenylacetaldehyde as substrates, there was no significant difference in activity between two regions in cerebrum. In ethanol treated group, ALDH activity with all the substrates in the gray and white matter was lower than in normal group. In ethanol-saponin treated group, the enzyme activity in the white matter remarkably Increased. The ALDH activity in neurons isolated from cerebral cortex in ethanol-treated group was lower than in normal group. In ethanol-saponin treated group, neuronal ALDH activity with propionaldehyde was significantly recovered but not with Indole-3-acetaldehyde. In astrocytes, although the ALDH activity with propionaldehyde in the ethanol-treated group was not changed as compared with normal group, considerable increase in activity was found in ethanol-saponin treated group. These results suggest that Korean red ginseng saponin may protect the neuronal functions from the toxic effects of acetaldehyde derived from ethanol by stimulation of ALDH activity in astrocytes surrounding nerve cells.

• Journal of Ginseng Research
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• 제18권1호
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• pp.1-9
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• 1994

Sprague-Dawley rats were given freely with 15% ethanol (control) and 15% ethanol containing (1) 0.1% ginseng saponin, (2) 0.02% ginsenoside $Rb_1$, and (3) $Rg_1$ (tests) instead of water for 7 days and aldehyde dehydrogenase (ALDH) and monoamine oxidase (MAO) activity in different regions of brain were examined. In control group, total ALDH activity with indoleacetaldehyde and acetaldehyde as substrate in all different regions was lower than that of normal group except in the hippocampus. The inhibitory effect on the activity was prominent in the corpus striatum and was not in the hippocampus. However, low-$K_m$ ALDH activity in all different regions was much lower than that of normal group. A considerable decrease in mitochondria ALDH activity in cerebellum and striatum was also observed in control group. In test groups total, low-$K_m$, and mitochondria AkDH activities in all different regions were higher than those in control group. Although ALDH activity in the striatum of test group was higher than control group, it was relatively depressed as compared with normal. There was not found a remarkable difference in extent of stimulating effect on the AkDH activity according to the ginseng saponin components. When biogenic aldehydes were used as substrate, ALDH activity with 3,4-dihydroxy-phenylacetaldehyde (DOPAL) in all brain regions of control group was lower than that using 5-hydroxy-indoleacetaldehyde (HIAL) and 3,4-dihydroxyphenylglycolaldehyde (NORAL) as substrate. In control group, ALDH activity with biogenic aldehydes above mentioned was markedly inhibited in the striatum contrary to other regions. The higher ALDH activity with biogenic aldehydes in test group than in control was found in the striatum, cerebrum, and cerebellum. MAO activity in the cerebellum was inhibited in control group and slightly increased in test group. The results of present study suggest that the corpus striatum is significantly affected by ethanol exposure while the hippocampus is not and that ginseng saponin fraction and ginsenosid es might have a preventive effect against depression of brain ALDH activity by chronic administration of ethanol.

• Toxicological Research
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• 제14권2호
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• pp.157-161
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• 1998

The mechanism of active aldehyde-induced liver disease and the enzymatic basis of detoxification were investigated using normal rat liver cell, Ac2F. Aliphatic alcohols including l-decyl alcohol, l-nonanol, l-heptanol, l-hexanol, l-propanol and allyl alcohol exerted a dose- and time-de-pendent toxicity to Ac2F cells. The extent of their toxicities in buthionine sulfoximine (inhibitor of glutathione synthesis) pretreated cells was greater than in pargyline (inhibitor of aldehyde dehydrogenase, ALDH). On the other hand, the toxicity of these alcohols were not affected by 4-methylpyrazole (inhibitor of alcohol dehydrogenase, ADH). These results suggest that the contents of glutathione (GSH) seems to be very important in protecting the cells from toxicants such as aliphatic alcohols.

• 약학회지
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• 제39권5호
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• pp.521-527
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• 1995

This study was done to determine the effect of lead acetate on the activities of the hepatic cytosofic xanthine oxidase and aldehyde oxidase which were well known as oxygen free radical generating enzyme in vitro. Lead ion accelerated the formation of lipid peroxide and the increment of xanthine oxidase(type O) activity and the type conversion ratio from xanthine dehydrogenase to xanthine oxidase dose-dependently. But xanthine dehydrogenase(type D) activity was decreased. Aldehyde oxidase activity was not changed by lead ion. These data suggested that lead-induced cellular to)dcity may be concerned partially with xanthine oxidase mediated lipid peroxidation.

• Journal of Microbiology and Biotechnology
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• 제32권2호
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• pp.170-175
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• 2022

3-Hydroxypropionic acid (3HP) is a platform chemical and can be converted into other valuable C3-based chemicals. Because a large amount of glycerol is produced as a by-product in the biodiesel industry, glycerol is an attractive carbon source in the biological production of 3HP. Although eight 3HP-producing aldehyde dehydrogenases (ALDHs) have been reported so far, the low conversion rate from 3-hydroxypropionaldehyde (3HPA) to 3HP using these enzymes is still a bottleneck for the production of 3HP. In this study, we elucidated the substrate binding modes of the eight 3HP-producing ALDHs through bioinformatic and structural analysis of these enzymes and selected protein engineering targets for developing enzymes with enhanced enzymatic activity against 3HPA. Among ten AbKGSADH variants we tested, three variants with replacement at the Arg281 site of AbKGSADH showed enhanced enzymatic activities. In particular, the AbKGSADH^R281Y variant exhibited improved catalytic efficiency by 2.5-fold compared with the wild type.

• BMB Reports
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• 제28권2호
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• pp.177-183
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• 1995

The activity of aldehyde dehydrogenase (ALDH) in the cerebrum, cerebellum, striatum, and medulla oblongata was examined and mitochondrial matrix ALDH was purified prior to immunohistochemical study on the localization of ALDH isozymes in pig brain. Relatively high enzyme activity was found in the striatum and medulla oblongata when using indole-3-acetaldehyde as substrate, and in the striatum when using 3,4-dihydroxyphenylacetaldehyde (DOPAL). The main part of mitochondrial ALDH activities with both acetaldehyde and DOPAL existed in the matrix fraction. The ratio of activity of the matrix to the membrane fraction in the cerebrum was higher than in the cerebellum, suggesting that the distribution pattern of ALDH isozymes was different according to the brain regions. The 276-fold purified mitochondrial matrix ALDH from pig brain was identified to be homologous tetramers with 53 KD subunits. The enzyme showed maximal activity at pH 9.0 and was stable in the temperature range from $25^{\circ}C$ to $37^{\circ}C$. The mitochondrial matrix ALDH activity was considerably inhibited by acetaldehyde in vitro. The $K_m$ values of the enzyme for acetaldehyde and propionaldehyde were 5.8 mM and 4.9 mM, respectively, whereas $K_m$ values for indole-3-acetaldehyde and DOPAL were 44 ${\mu}M$ and 1.6 ${\mu}M$, respectively. The $V_{max}/K_{m}$ ratio was the highest with DOPAL as compared with other substrates. These results suggested that mitochondrial matrix ALDH in the present work might be a low Km isozyme involved in biogenic aldehyde oxidation in pig brain.

• Archives of Pharmacal Research
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• 제20권5호
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• pp.432-437
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• 1997

We used a herbal medicine, roots of Rhodiola sachalinensis (RS) to assess whether RS extract can decrease blood ethanol concentrations in rats fed ethanol and if so, to elucidate the mechanism by which RS extract reduces blood ethanol levels. Rats were fed ethanol orally 1 hr after the oral administration of various doses of RS extract. In another experiment, rats were injected intraperitoneally with ethanol following the intake of RS extract via gastric catheter to eliminate possible inhibition of ethanol absorption in the gastrointestine by RS extract. The administration of RS extract remarkably lowered blood ethanol levels in a dose-dependent manner in rats given ethanol orally. However, the intake of RS extract did not reduce ethanol levels in rats injected with ethanol intraperitoneally. The activities of two main hepatic enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), involved in ethanol metabolism, were not affected by the administration of RS extract in rats fed ethanol. In addition, the intake of RS extract reduced serum triglyceride levels elevated by ethanol to the normal level. We conclude that the administration of RS extract lowers blood ethanol concentrations by inhibition of ethanol absorption in the gastrointestinal tracts of ethanol-fed animals.

• Natural Product Sciences
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• 제21권1호
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• pp.54-58
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• 2015

The protective effect of EtOAc fraction of Limonium tetragonum extract (EALT) against alcohol-induced hepatotoxicity was assessed following acute ethanol intoxication in Spraque-Dawley rats. EALT (200 mg/kg p.o.) was administrated once before alcohol intake (8 g/kg, p.o.). Blood ethanol concentration, and the activities of alcohol metabolic enzymes, alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the liver were measured. Also, the formation of malondialdehyde (MDA) and the activities of antioxidant enzymes, superoxide dismutase (SOD), glutathione peroxidase (GSH-px), catalase were determined after acute alcohol exposure. Pretreatment of rats received ethanol with EALT significantly decreased blood ethanol concentration and elevated the activities of ADH and ALDH in liver. The increased MDA level was decreased, and the reduced activities of SOD, GSH-px and catalase were markedly preserved by the treatment with EALT. This study suggests that EALT prevent hepatic injury induced by acute alcohol which is likely related to its modulation on the alcohol metabolism and antioxidant enzymes activities.

• Fisheries and Aquatic Sciences
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• 제14권2호
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• pp.79-88
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• 2011

The sea tangle, Laminaria japonica has long been used in Korea as a folk remedy to promote health. Gamma-amino butyric acid-enriched (5.56% of dry weight) sea tangle was obtained by fermentation with Lactobacillus brevis BJ-20 (FLJ). A suppressive effect of FLJ on carbon tetrachloride-induced hepatotoxicity has been shown previously. Alcohol administration to Sprague-Dawley rats leads to hepatotoxicity, as demonstrated by heightened levels of hepatic marker enzymes as well as increases in both the number and volume of lipid droplets as fatty liver progresses. However, FLJ attenuated alcohol-induced hepatotoxicity and the accumulation of lipid droplets following ethanol administration. Additionally, FLJ increased the activities and transcript levels of major alcoholmetabolizing enzymes, such as alcohol dehydrogenase and aldehyde dehydrogenase, and reduced blood concentrations of alcohol and acetaldehyde. These data suggest that FLJ protects against alcohol-induced hepatotoxicity and that FLJ could be used as an ingredient in functional foods to ameliorate the effects of excessive alcohol consumption.

• 방사선산업학회지
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• 제7권1호
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• pp.75-80
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• 2013

This study was designed to elucidate the effect of fermented blackberry drinks (BD) on alcohol metabolism and hangover in alcohol-treated rats. We showed that the administration of BD increased the activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in alcohol-treated rats. Moreover, the administration of BD reduced the serum alcohol and acetaldehyde concentrations in alcohol-treated rats. Furthermore, the administration of BD attenuated the levels of serum aspartate aminotransferase and alanine aminotransferase in alcohol-treated rats. Taken together, these results suggest that BD plays an important role in alcohol metabolism and liver function by reducing blood alcohol and acetaldehyde through the activation of ADH and ALDH in alcohol-treated rats and could be used as a functional anti-hangover drinks.