Effects of Diallyl Disulfide on the Hepatic Glutathione Peroxidase Activity in Rat

허근,이상일,박종민,Huh, Keun,Lee, Sang-Il,Park, Jong-Min The Korean Society of Pharmacology 1986 대한약리학잡지 Vol.22 No.2

Glutathione peroxidase might play an important role in the protection of cellular structures against oxidative challange by hydrogen peroxide and several organic hydroperoxides. It is widely accepted that allicin is biological active component of garlic, and allicin is easily degraded to diallyl disulfide and other components. This study was attempted to elucidate the effect of diallyl disulfide on some biological activities. It was observed that the activity of serum transaminase and glutathione level in liver were not changed by the treatment of diallyl disulfide. The liver cytosolic glutathione peroxidase activity was significantly enhanced. Whereas, mitochondrial enzyme activity was slightly increased. In the presence of diallyl disulfide in vitro, $V_{max}$ value of glutathione peroxidase for hydrogen peroxide was increased. On the other hand, Km value was not changed. 마늘성분중의 하나인 diallyl disulfide가 간 glutathione peroxidase 활성에 어떠한 영향을 주는가를 관찰하여 다음과 같은 성적을 얻었다. 여러 농도의 diallyl disulfide를 흰쥐에 투여 하였을때 혈청 transaminase의 활성은 변동이 없었으며 또한 간 glutathione의 함량도 변화되지 않았다. 그러나 간 가용성분획의 glutathion peroxidase 활성은 현저히 증가되었다. 시험관 내에서 간 가용성분획의 glutathione peroxidase의 활성은 $15{\mu}g/m{\ell}$ 이상의 diallyl disulfide를 첨가 하였을때 현저히 증가되었으며, 동력학적인 측면에서 관찰하였을때 diallyl disulfide$(20{\mu}g/m{\ell})$에 의해 Km치는 별 변화가 없었으나 Vmax치는 현저히 증가되었다. 이상의 실험결과에서 마늘 성분 중에 glutathione peroxidase 활성을 증가시키는 성분은 allicin의 분해산물인 diallyl disulfide에 기인된 것으로 사료되며 또한 이 성분은 효소의 기질결합 부위가 아닌 다른 부위에서 효소의 활성을 조절해 줄 것으로 생각되어진다.

흰쥐 담즙울체간의 Glutathione S-Transferase, Glutathione Reductase 및 Glutathione Peroxidase의 활성도

권용철,곽춘식,문교철 啓明大學校 醫科大學 1990 계명의대학술지 Vol.9 No.2

Changes in the activities of the following enzymes have been studied over a period of forty two days after the ligation of common bile duct in rats: cytosolic, mitochondrial and microsomal glutathione S-transferase, cytosolic glutathione reductase and cytosolic glutathione peroxidase of cholestatic liver. The activity of cytosolic glutathione S-transferase in the cholestatic rat liver strikingly diminished between the third and the forty-second days after the ligation of common bile duct and of mitochondrial glutathione S-transferase also showed significant decrease between the fourteenth and the forty-second days after operation. However, the microsomal glutathione S-transferase activity in the cholestatic rat liver showed a substantial increase between the seventh and twenty-eight days after operation. The cytosolic glutathione reductase activity in the cholstatic rat liver elevated considerably between the second and the forty-second days after operation, but the cytosolic glutathione peroxidase activity in the cholestatic rat liver had a significant diminution between the fourteenth and the forty-second days after the ligation of common bile duct.

노화와 간경변이 인체의 적혈구, 혈장 및 위 점막의 Glutathione 농도와 Glutathione Peroxidase 활성도에 대해 미치는 영향

백광호,김종혁,백일현,한태호,박현주,박상훈,서중산,박충기,유재영 대한노인병학회 2001 대한노인병학회지 Vol.5 No.3

흰쥐 간 Glutathione peroxidase 활성에 미치는 Diallyl disulfide의 영향

허근(Keun Huh),이상일(Sang Il Lee),박종민(Jong Min Park) 대한약리학회 1986 대한약리학잡지 Vol.22 No.2

마늘성분중의 하나인 diallyl disulfide가 간 glutathione peroxidase 활성에 어떠한 영향을 주는가를 관찰하여 다음과 같은 성적을 얻었다. 여러 농도의 diallyl disulfide를 흰쥐에 투여 하였을때 혈청 transaminase의 활성은 변동이 없었으며 또한 간 glutathione의 함량도 변화되지 않았다. 그러나 간 가용성분획의 glutathion peroxidase 활성은 현저히 증가되었다. 시험관 내에서 간 가용성분획의 glutathione peroxidase의 활성은 15μg/㎖ 이상의 diallyl disulfide를 첨가 하였을때 현저히 증가되었으며, 동력학적인 측면에서 관찰하였을때 diallyl disulfide(20μg/㎖)에 의해 Km치는 별 변화가 없었으나 Vmax치는 현저히 증가되었다. 이상의 실험결과에서 마늘 성분 중에 glutathione peroxidase 활성을 증가시키는 성분은 allicin의 분해산물인 diallyl disulfide에 기인된 것으로 사료되며 또한 이 성분은 효소의 기질결합 부위가 아닌 다른 부위에서 효소의 활성을 조절해 줄 것으로 생각되어진다. Glutathione peroxidase might play an important role in the protection of cellular structures against oxidative challange by hydrogen peroxide and several organic hydroperoxides. It is widely accepted that allicin is biological active component of garlic, and allicin is easily degraded to diallyl disulfide and other components. This study was attempted to elucidate the effect of diallyl disulfide on some biological activities. It was observed that the activity of serum transaminase and glutathione level in liver were not changed by the treatment of diallyl disulfide. The liver cytosolic glutathione peroxidase activity was significantly enhanced. Whereas, mitochondrial enzyme activity was slightly increased. In the presence of diallyl disulfide in vitro, V_max value of glutathione peroxidase for hydrogen peroxide was increased. On the other hand, Km value was not changed.

Activities of Antioxidant and Redox Enzymes in Human Normal Hepatic and Hepatoma Cell Lines

Yuk-Young Lee,Hong-Gyum Kim,Haeng-Im Jung,Youn Hee Shin,Sung Min Hong,박은희,Jae Hoon Sa,Chang Jin Lim 한국분자세포생물학회 2002 Molecules and cells Vol.14 No.2

The cellular defense system (including glutathione, glutathione-related enzymes, antioxidant and redox enzymes) plays a crucial role in cell survival and growth in aerobic organisms. To understand its physiological role in tumor cells, the glutathione con-tent and related enzyme activities in the human nor-mal hepatic cell line, Chang and human hepatoma cell line, HepG2, were systematically measured and com-pared. Superoxide dismutase, catalase, and glutathione peroxidase activities are 2.8-, 4.3-, and 2.9-fold higher in HepG2 cells than in Chang cells. Total glutathione content is also about 1.4-fold higher in HepG2, which is supported by significant increases in γ-glutamylcy-steine synthetase and glutathione synthetase activities. Two other glutathione-related enzymes, glutathione reductase and γ-glutamyltranspeptidase, are up-regulated in HepG2 cells. However, thioredoxin reduc-tase and glutathione S-transferase activities are sig-nificantly lower in HepG2 cells. These results propose that defense-related enzymes are largely modulated in tumor cells, which might be linked to their growth and maintenance.

전북지역 한우의 red cell fragility와 glutathione peroxidase활성에 관한 연구

조종후,이성희,Cho, Jong-hoo,Lee, Seong-hee 대한수의학회 1990 大韓獸醫學會誌 Vol.30 No.3

The tests related to red cell fragility were performed. Samples of blood anticoagulated with heparin were obtained from Korean native cattle in Chonbuk region abattoir, and classified by the district(Kun) with reference to breeding location. Hemolysis test for red cell fragility was performed with whole blood and glutathione peroxidase activity was measured spectrophotometrically. Blood concentration of selenium, inorganic component of glutathione peroxidase, was also determined fluorophotometrically. The results obtained were summerized as follows; 1. Percent hemolysis of erythrocytes ranged from 13.53 to 20.74%, and its mean Palue was low as $17.11{\pm}9.91%$. Means in all were not district(Kun) in Chonbuk region significantly different. 2. Glutathione peroxidase activity ranged from 2,881 to 4,000mU/ml, and high mean values, $3,352{\pm}1,872mU/ml$, reflected low percent hemolysis. 3. There was a highly negative correlation between the red cell fragility(Y) and blood glutathione peroxidase activity(X). The linear regression equation for these data was: Y=29.86-3.75X with a correlation coefficient of r=-.6886 (p<0.01) 4. Blood selenium concentration ranged from 0.16 to $0.24{\mu}g/ml$, and mean values was normal level as $0.2{\pm}0.11{\mu}g/ml$. 5. There was a highly positive correlation between blood selenium concentration(X), and blood glutathione peroxidase activity(Y). The linear regression for these data was: Y=230+15,790X, with a correlation coefficient officient of r=0. 8635.

Saccharomyces cerevisiae에서 N acetyl L cysteine 처리와 감마선 조사에 따른 Glutathione Peroxidase 유전자 발현

박지영 ( Ji Young Park ),백동원 ( Dong Won Baek ),모하마드닐리 ( Mohammad Nili ),김진규 ( Jin Kyu Kim ) 한국환경생물학회 2011 환경생물 : 환경생물학회지 Vol.29 No.4

Glutathione (GSH) has important roles in cellular defense against oxidative stress, 1) direct scavenging of reactive oxygen species (ROS), and 2) coenzyme of ROS scavenging enzyme like glutathione peroxidases (GPx). GSH peroxidase reduces free hydrogen peroxide to water using 2GSH. N acetyl L cysteine (NAC), one of the antioxidants, is used as a precursor for intracellular GSH. In this study, relation of GSH, NAC, and GSH peroxidase was investigated through transcriptional expression of GPX1 and GPX2, which are GSH peroxidase encoding genes, in yeast cells treated with 0 mM to 20 mM of NAC or in combination with 100 Gy gamma rays. The transcriptional expression of GPX1 and GPX2 was induced by NAC and 100 Gy gamma rays. The gene expression of both GSH peroxidases was decreased with increasing concentrations of NAC in irradiated yeast cells. These results suggest that elevation of intracellular GSH by NAC and oxidative stress and ROS generated from gamma rays induces expression of GSH peroxidase genes, and that NAC can protect the yeast cells against ROS generated from gamma rays through direct scavenging of ROS and transcriptional activation of GSH peroxidase.

Effect of Selenium on Pulmonary Glutathione Peroxidase and Alveolarization of Neonatal Rats

( Hye Young P. Kim ) 한국환경생물학회 2003 환경생물 : 환경생물학회지 Vol.21 No.3

N/A This study was designed to determine whether selenium (Se) nutrition affects pulmonary glutathione peroxidase and alveolarization in the neonatal rat. Twenty-four female Sprague Dawley rats were bred and fed a semipurified Se-deficient (0.04 ppm, Se-) or a Se-adequate (0.5 ppm, Se+) diet through pregnancy and lactation. Pulmonary DNA synthesis was slightly higher in Se+ pups than in Se- pups on d 6 and d 9 of lactation, but significant difference was not found. As pulmonary alveolarization progressed, mean air space size decreased and internal surface area and lung volume increased. No difference in pulmonary alveolarization was found between Se- and Se+pups by age. Pulmonary Se concentration was higher in Se+ pups than in Se pups at all age. Glutathione peroxidase activity in lung tissue reflected Se status and was lower in Se- pups than in Se+ pups. In conclusion, selenium has no significant effect on alveolarization of neonatal lungs, but it is necessary for adequate supply of pulmonary antioxidant, glutathione peroxidase.

Methylglyoxal-Scavenging Enzyme Activities Trigger Erythroascorbate Peroxidase and Cytochrome c Peroxidase in Glutathione-Depleted Candida albicans

( Sa-ouk Kang ),( Min-kyu Kwak ) 한국미생물생명공학회(구 한국산업미생물학회) 2021 Journal of microbiology and biotechnology Vol.31 No.1

γ-Glutamylcysteine synthetase (Gcs1) and glutathione reductase (Glr1) activity maintains minimal levels of cellular methylglyoxal in Candida albicans. In glutathione-depleted Δgcs1, we previously saw that NAD(H)-linked methylglyoxal oxidoreductase (Mgd1) and alcohol dehydrogenase (Adh1) are the most active methylglyoxal scavengers. With methylglyoxal accumulation, disruptants lacking MGD1 or ADH1 exhibit a poor redox state. However, there is little convincing evidence for a reciprocal relationship between methylglyoxal scavenger genes-disrupted mutants and changes in glutathione-(in)dependent redox regulation. Herein, we attempt to demonstrate a functional role for methylglyoxal scavengers, modeled on a triple disruptant (Δmgd1/Δadh1/Δgcs1), to link between antioxidative enzyme activities and their metabolites in glutathione-depleted conditions. Despite seeing elevated methylglyoxal in all of the disruptants, the result saw a decrease in pyruvate content in Δmgd1/Δadh1/Δgcs1 which was not observed in double gene-disrupted strains such as Δmgd1/Δgcs1 and Δadh1/Δgcs1. Interestingly, Δmgd1/Δadh1/Δgcs1 exhibited a significantly decrease in H₂O₂ and superoxide which was also unobserved in Δmgd1/Δgcs1 and Δadh1/Δgcs1. The activities of the antioxidative enzymes erythroascorbate peroxidase and cytochrome c peroxidase were noticeably higher in Δmgd1/Δadh1/Δgcs1 than in the other disruptants. Meanwhile, Glr1 activity severely diminished in Δmgd1/Δadh1/Δgcs1. Monitoring complementary gene transcripts between double gene-disrupted Δmgd1/Δgcs1 and Δadh1/Δgcs1 supported the concept of an unbalanced redox state independent of the Glr1 activity for Δmgd1/Δadh1/Δgcs1. Our data demonstrate the reciprocal use of Eapx1 and Ccp1 in the absence of both methylglyoxal scavengers; that being pivotal for viability in non-filamentous budding yeast.

The Effect of Dimethyl Dimethoxy Biphenyl Dicarboxylate (DDB) against Tamoxifen-induced Liver Injury in Rats: DDB Use Is Curative or Protective

El-Beshbishy, Hesham A. Korean Society for Biochemistry and Molecular Biol 2005 Journal of biochemistry and molecular biology Vol.38 No.3

Tamoxifen citrate is an anti-estrogenic drug used for the treatment of breast cancer. It showed a degree of hepatic carcinogenesis, when it used for long term as it can decrease the hexose monophosphate shunt and thereby increasing the incidence of oxidative stress in liver rat cells leading to liver injury. In this study, a model of liver injury in female rats was done by intraperitoneal injection of tamoxifen in a dose of 45 mg/kg body weight for 7 successive days. This model produced a state of oxidative stress accompanied with liver injury as noticed by significant declines in the antioxidant enzymes (glutathione-S-transferase, glutathione peroxidase and catalase) and reduced glutathione concomitant with significant elevations in TBARS (thiobarbituric acid reactive substance) and liver transaminases; sGPT (serum glutamate pyruvate transaminase) and sGOT (serum glutamate oxaloacetate transaminase) levels. The oral administration of dimethyl dimethoxy biphenyl dicarboxylate (DDB) in a dose of 200 mg/kg body weight daily for 10 successive days, resulted in alleviation of the oxidative stress status of tamoxifen-intoxicated liver injury in rats as observed by significant increments in the antioxidant enzymes (glutathione-S-transferase, glutathione peroxidase and catalase) and reduced glutathione concomitant with significant decrements in TBARS and liver transaminases; sGPT and sGOT levels. The administration of DDB before tamoxifen intoxication (as protection) is more little effective than its curative effect against tamoxifen-induced liver injury. The data obtained from this study speculated that DDB can mediate its biochemical effects through the enhancement of the antioxidant enzyme activities and reduced glutathione level as well as decreasing lipid peroxides.