• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.3
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• pp.448-452
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• 2000

실험동물에서 곰피로부터 분리한 phlorglucinol은 acetaminophen의 투여로 현저히 증가된 간조직에 있어서 지질과선화의 함량을 억제하였다. Acetaminophen 투여에 따른 간 cytochrome P-450, aminopyrine N-deme-thylase 및 aniline hydroxylase 활성변동은 관찰할 수 없었다. 곰피 성분 투여군은 glutathione S-transferase의 활성에서는 대조군의 수준에는 미치지 않으나 효소의 활성이 acetaminophen 단독 투여군보다 현저히 증가되었다. 그리고 간조직중 glutathione의 함량은 phlorglucionl을 전처리군에서 acetaminophen 단독 투여군보다 증가되었다. Glutathione reductase 활성에서는 acetaminophen 투여군은 대조군보다 활성이 감소되었으며, 성분으로 전처리한 군은 acetaminophen 단독 투여군보다 증가 되었다. 따라서 곰피에서 분리한 페놀성화합물인 phloroglucinol은 acetaminophen 투여로 증가되던 지질과 산화함량을 감소시키며, acetaminophen 대사효소활성에서는 glutathione S-transferase의 활성이 증가되어 acetaminophen 의 대사를 촉진시키는 것으로 추정된다.

• Microbiology and Biotechnology Letters
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• v.25 no.4
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• pp.374-378
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• 1997

Glutathione S-transferase (GST) was purified from Pseudomonas sp. DJ77, and its N-terminal sequence was determined to be MKLFISPGACSL. A specific tyrosyl residue in the vicinity of the N terminus is conserved in all the known cytosolic GSTs and has been shown to function as a catalytic residue in $\alpha$, $\mu$, $\pi$ class GSTs from mammals. However, Pseudomonas sp. DJ77 GST has the Phe-4 and Ile-5 instead of Tyr in N-terminus. Its replacement with tyrosine did not significantly affect the enzyme activity. Results from in vitro biochemical analyses were confirmed by the in vivo activity-based CDNB growth inhibition analyses. Our results clearly indicate that GST of Pseudomonas sp. DJ77 has a novel reaction mechanism different from that of mammalian GSTs.

• The Journal of Internal Korean Medicine
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• v.21 no.3
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• pp.399-407
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• 2000

This study was carried out to examine if Haejohwan (HJ) inhibits oxidant-induced lipid peroxidation and therby produces protective effect against thyroxine-induced hyperthyroid rats. Triiodothyronine $(T_3)$, thyroxine $(T_4)$, lipid peroxidation, xathine oxidase activities and type conversion ratio were increased in thyroxine treated group. However, they were decreased in HJ extract's pre-applied group. Glutathione level, activities of glutathione peroxidase, glutathione Stransferase and glutathione reductase were decreased in thyroxine treated group. But, they were increased in HJ extract's pre-applied group. These results suggest that in thyroxine-induced hyperthyroid rats HJhas an increase in the activities of oxygen free radical scavenging enzymes and inhibition of xanthine oxidase activities, and prevents lipid peroxidation.

• Proceedings of the Korean Society of Toxicology Conference
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• 2003.05a
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• pp.72-72
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• 2003

Induction of glutathione S-transferases is associated with cancer chemoprevention. We reported that PD98059, an MKK1 inhibitor, induces glutathione Stransferase A2 (rGSTA2). This report comparatively examines the role of CCAAT/enhancer binding protein (C/EBP) and Nrf-2 in the induction of rGSTA2 by PD98059. PD98059 at the concentrations effective for the inhibition of MKKI increased the rGSTA2 protein and mRNA levels in H4IIE cells. (omitted)

• Analytical Science and Technology
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• v.23 no.2
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• pp.172-178
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• 2010

Glutathione S-transferase is known to play a crucial role in detoxification in many cases. To develop a herbicide detection biosensor, we in this study attempted to immobilize glutathione S-transferase enzyme on solid supports, polystyrene and agarose, and Na-alginate. These matrixes were attractive materials for the construction of biosensors and might also have utility for the production of immobilized enzyme bioreactors. We also compared the activities of glutathione-S-transferase immobilized OsGSTF3 and free OsGSTF3. The specific activity of the free enzyme in solution was 3.3 higher than the immobilized enzyme. These results suggest that 50% of the enzyme was bound with the catalytic site in polystyrene-alkylamine bead and immobilized enzymes showed 80% remaining activity until 3 times reuse.

• Asian Pacific Journal of Cancer Prevention
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• v.14 no.9
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• pp.5331-5339
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• 2013

Colorectal cancer is one of the leading causes of cancer death, both in men and women. This study investigated the effects of Amorphophallus campanulatus tuber methanolic extract (ACME) on aberrant crypt foci (ACF) formation, colonic cell proliferation, lipid peroxidative damage and the antioxidant status in a long term preclinical model of 1, 2-dimethylhydrazine (DMH) induced colon carcinogenesis in rats. Male Wistar rats were divided into six groups, viz., group I rats served as controls; group II rats treated as drug controls receiving 250 mg/kg body weight of ACME orally; group III rats received DMH (20 mg/kg body weight) subcutaneously once a week for the first 15 weeks; groups IV, V and VI rats received ACME along with DMH during the initiation, post-initiation stages and the entire period of the study, respectively. All the rats were sacrificed at the end of 30 weeks and the intestinal and colonic tissues from different groups were subjected to biochemical and histological studies. Administration of DMH resulted in significant ($p{\leq}0.05$) intestinal and colonic lipid peroxidation (MDA) and reduction of antioxidants such as catalase, glutathione peroxidase, glutathione reductase, glutathione-Stransferase and reduced glutathione. Whereas the supplementation of ACME significantly ($p{\leq}0.05$) improved the intestinal and colonic MDA and reduced glutathione levels and the activities of antioxidant enzymes in DMH intoxicated rats. ACME administration also significantly suppressed the formation and multiplicity of ACF. In addition, the DMH administered rats showed amplified expression of PCNA in the colon and decreased expression of this proliferative marker was clearly noted with initiation, post-initiation and entire period of ACME treatment regimens. These results indicate that ACME could exert a significant chemopreventive effect on colon carcinogenesis induced by DMH.

• Archives of Pharmacal Research
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• v.29 no.3
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• pp.209-212
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• 2006

We investigated the effect of protein extract of Asterina pectinifera on the activity of 4 enzymes that may playa role in adenocarcinoma of the colon: quinone reductase (QR), glutathione Stransferase (GST), ornithine decarboxylase (ODC), and cyclooxygenase (COX)-2. QR and GST activity increased in HT-29 human colon adenocarcinoma cells increased that had been exposed to 4 concentrations of the protein extract (80, 160, 200, and $240{\mu}g/mL$). Additionally, 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced ODC activity decreased significantly in cells exposed to the extract in concentrations of $160{\mu}g/mL$ (p<0.05), $200{\mu}g/mL$ (p<0.005), and $240{\mu}g/mL$ (p<0.005). TPA-induced COX-2 activity also decreased in cells exposed to extract concentrations of 10, 20, 40, and $60{\mu}g/mL$. COX-2 expression was also inhibited in cells exposed to this extract. These results suggest that this protein extract of A pectinifera has chemopreventive activity in HT-29 human colon adenocarcinoma cells, and therefore, may have the potential to function as a chemopreventive agent in human colorectal cancer.

• Korean Journal of Community Nutrition
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• v.4 no.2
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• pp.239-247
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• 1999

Six-week-old Sprague Dawley rats were fed the diets of 20% casein or soy protein. Two weeks after the feeding, hepatocellular chemical carcinogenesis was initiated by diethylnitrosamine(DEN), and promoted by the diet containing 0.01% 2-acetylamino-fluorene(AAF) and two-thirds partial hepatectomy(PH). The animals were sacrificed at 8 weeks after the DEN injection. The area of placetal glutathione S-trnasferase(GST-P) positive foci, the activities of several enzymes in cellualr antioxidant enzyme systems and glucose 6-phosphatase were determined to investigate the mechanism of the anticarcinogenic effect by the dietary proteins. In another set of experiments, the drinking water of rats fed casein was supplemented with 1.5% inositol hexaphosphate(InsP6) to elucidate whether it has the comparable anticancer action of soy protein. The area and number of GST-P positive foci in the soy protein group were significantly(p<0.05) lower than those inthe casein group. The livers of rats fed casein showed moderate fattydegeneration and larger hyperplastic nodules than those of rats fed soy protein. In another set of experiments, the area and number of GST-P positive foci in the rats fed casein supplemented with InsP6 were not significantly different from those in the rats fed casein or soy protein. The lipid peroxidation of rats fed different protein sources showed no significant difference. Glutathione S-transferase(GST) activities were increased significantly(p<0.05) by carcinogen treatment in all dietary groups. Glucose 6-phosphatase(G6Pase) activities were decreased by carcinogen treatment, and hence showed a reverse relationship(r=-0.695, p<0.01) to the GST-P positive foci. Therefore, the activities in the rats fed casein were lower than those in the rats fed soy protein. These results suggest that the soy protein seems to be more anti-carcinogenic than casein by decreasing the preneoplastic lesion and by increasing the membrane stability but inositol hexaphosphate, a component of soy protein, may not be protective against hepatocarcinogenesis.

• Applied Biological Chemistry
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• v.45 no.2
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• pp.119-123
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• 2002

Antioxidative activities of ethanol extracts of fruits from three cultivars of Prunus mune with different harvest times were determined. Extracts of P. mune cutivar Okyoung showed the strongest activity at 97.5%(compared to BHT) using DPPH or thiocyanate method, although no statistically significant differences were observed among the cultivars. Antioxidative activities of the extracts measured with glutathione-S-transferase method was over 70% of that of BHT. Survival rates of cells in mouse spinal cord culture challenged by superoxide anion were 89, 79, and 62% at 40 mg/ml of Okyoung, Namgo, and Kochunme extracts, respectively, whereas 90% at 6mM glutathion.

• Korean Journal of Medicinal Crop Science
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• v.15 no.1
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• pp.21-25
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• 2007

The root of Rosa rugosa has been used in folkloric medicine as a treatment agent for diabetes. In the present study, we investigated whether (+)-catechin isolated from this plant can change the activities of hepatic drug metabolizing enzymes in rats treated with bromobenzene. Pretreatment with (+)-catechin gave no effects on the activities of aminopyrine N-demethylase and aniline hydroxylase, enzymes forming toxic bromobenzene epoxide intermediates and glutathione Stransferase, an enzyme removing toxic epoxides. However, the activity of epoxide hydrolase, an enzyme detoxifying the bromobenzene toxic intermediates was mildly recovered by (+)-catechin treatment.