• Journal of Nutrition and Health
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• v.40 no.7
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• pp.606-615
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• 2007

This study was performed to investigate anti-thrombogenic, anti-inflammatory effects of n-BuOH (B) and $CH_2Cl_2$ (MC) fractions extracted from Sancho (Zanthoxylum. schinifolium) leaves in rats fed high fat diets. The experimental animal groups were consisted of eight including one 5% fat (N) and one 20% fat (H) without the test materials in diets and six H groups of feeding three levels (50, 100 and 150 mg/day) of the B and the MC fractions from Z. schinifolium, respectively. Plasma activated partial thromboplastin times and thrombin times of H group were decreased compared to the N group, but they were increased by feeding the MC fraction of 50 mg and over. Polymorphonuclear leukocyte 5#-lipo-xygenase activities and leukotriene $B_4$ contents of the H group were significantly increased compared to the N group, but they were decreased in the 100 mg and 150 mg of B fraction or the 150 mg of MC fraction fed groups. Liver cytochrome $P_{450}$, $O_2^-$, $H_2O_2$ and GSSG contents were increased by the high fat diet but decreased by feeding the B fraction or the MC fraction, while GSH content and glutathione S-transferase activity lowered by high fat diet were increased by feeding the two solvent fractions. The effects of the solvent fractions were evident at the level of 100 mg/day and over. The present results confirmed that two solvent fractions from the leaves of Z, schinifolium have enhancing effects on anti-thrombosis and anti-inflammation partly by antioxidant action and partly by direct modulation of the respective processeds. In conclusion, the n-BuOH and $CH_2Cl_2$ fractions from leaves of Z, schinifolium can be utilized as the proper ingredients of functional foods for preventing chronic degenerative disease.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.2
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• pp.278-286
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• 2003

Alcohol is well known agent which can damage the human tissues such as liver via stimulating lipid peroxidation. On the other hand, carotenoids in addition to vitamins A, C and I play important roles in protecting these oxidative damages as well as preventing the production of free radicals. This study was carried out to investigate the effect of dietary vitamin A on lipid peroxidation and antioxidants status in ethanol-treated rats. In the experiment, male Sprague-Dawley rats weighing 160~180 g were given a liquid diet containing 36% of total calories as ethanol for 7 weeks. The pair-fed control rats received an isocaloric amount of diet containing sucrose instead of ethanol on the following day Additionally, the liquid diet contained adequate amount of $\beta$-carotene, retinyl acetate or 13-sis-reinoic acid except vitamin A-deficient diet. The results obtained are as follows. The levels of plasma and hepatic lipid peroxide were increased after chronic ethanol feeding in rats. Retinyl acetate supplementation significantly reduced lipid peroxidation induced by ethanol feeding Glucose 6-phosphatase activity was significantly reduced in rats fed vitamin A-deficient diet with ethanol and alkaline phosphatase activity was significantly induced in rats fed 13-cis-reinoic acid diet with ethanol. Catalase and alcohol dehydrogenase activities did not show a consistent tendency in experiment groups. The hepatic antioxidant enzyme activities did not significantly changed by chronic ethanol feeding groups. The striking decrease in conversion of $\beta$-carotene to retinol was observed in rats fed a $\beta$-carotene diet with ethanol feeding The level of retinol and retinoic acid in plasma and liver was decreased after chronic ethanol administration Based on this result, these data suggest that ethanol feeding enhances oxidative stress especially in those fed a vitamin A-deficient diet, and vitamin A supplementation, especially, retinyl acetate intake can prevent enhanced lipid peroxidation and related damage to some extent.

• Journal of Life Science
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• v.16 no.7 s.80
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• pp.1133-1140
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• 2006

Human HtrA1 (High temperature requirement protein A1) is a homologue of the E. coli periplasmic serine protease HtrA. A recent study has demonstrated that HtrA1 is a serine protease involved in processing of insulin like growth factor binding protein (ICFBP), indicating that it serves as an important regulator of IGF activity. Additionally, several lines of evidence suggest a striking correlation between proteolytic activity of HtrA1 serine protease and the pathogenesis of several diseases; however, physiological roles of HtrA1 remain to be elucidated. We used the pGEX bacterial expression system to develop a simple and rapid method for purifying HtrA1, and the recombinant HtrA1 protein was utilized to investigate the optimal conditions in executing its proteolytic activity. The proteolytically active HtrA1 was purified to approximately 85% purity, although the yield of the recombinant HtrA1 protein was slightly low $460{\mu}g$ for 1 liter E. coli culture). Using in vitro endoproteolytic cleavage assay, we identified that the HtrA1 serine protease activity was dependent on the enzyme concentration and the incubation time and that the best reaction temperature was $42^{\circ}C$ instead of $37^{\circ}C$. We arbitrary defined one unit of proteolytic activity of the HtrA1 serine protease as 200nM of HtrA1 that cleaves half of $5{\mu}M\;of\;{\beta}-casein$ during 3 hr incubation at $37^{\circ}C$. Our study provides a method for generating useful reagents to investigate the molecular mechanisms by which HtrA1 serine protease activity contributes in regulating its physiological function and to identify natural substrates of HtrA1.

• Journal of Life Science
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• v.17 no.4 s.84
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• pp.462-469
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• 2007

In this study, we isolated, characterized, and compared the vasa homologous genes of diploid and triploid Paragonimus westermani and localized VASA homologous proteins in both lung fluke types. Open reading frames of Pw-vasa-2n and Pw-vasa-3n were of 1812 bp, and encoded deduced proteins of 622 amino acids with calculated molecular weights of 69.0 kDa and 68.9 kDa and pI's of 9.11 and 9.03, respectively. A comparison of these two VASA deduced protein sequences showed that only 6 of the 622 amino acids differed. The deduced sequences of Pw-VASA-2n and Pw-VASA-3n contained eight consensus sequences characteristic of the DEAD-box protein family and their N-terminal regions contained four arginine-glycine-glycine (RGG) motifs. These two lung fluke VASA-like proteins were more similar to those of other VASA proteins than to those of other DEAD-family proteins isolated from several organisms (planarian, zebra fish, mouse, and human). vasa homologous gene transcription and VASA protein expressions in triploid type lung flukes was slightly stronger than in the diploid type. Immunostaining showed that testes and a portion of the ovaries of both diploid and triploid lung flukes reacted strongly to anti-Pw-VASA antibody.

• Journal of Marine Bioscience and Biotechnology
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• v.1 no.3
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• pp.178-185
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• 2006

This study was to investigate the effect of 0.1% chitosan-ascorbate (CA) prepared with different molecular weight (223, 746, 1,110 and 2,025 kDa) of chitosan on the changes in antioxidant activity of mul-kimchi during storage at $10^{\circ}C$ for 20 days. Animal experiments were divided to 5 groups; normal control group (NC), high cholesterol diet group (HC), high cholesterol diet mul-kimchi diet group (HCKC), high cholesterol diet and CA2025 containing mul-kimchi administrated group (HCCA), and high cholesterol diet and 1/2 concentrated CA containing mul-kimchi administrated group (HC2CA). Mul-kimchi juice was administered 0.5 mL per 100 g body weight once a day and fed for 5 weeks. Electron donating activity of the 20 days-stored mul-kimchi with 0.1% CA showed higher activity (84.74~89.13%) than those of control and ascorbic acid mul-kimchi (35.04 and 75.04%). Superoxide dismutase activities of the kimchijuice with CA were higher in the higher molecular of chitosan. In the animal experiments, the average body weight of the HCCA and HC2CA group were lower 6.9% and 8.4% than that of HC control group, respectively. Hepatic glutathione content in HCCA and HC2CA group was increased 22.5% and 9.1% as compared to HC group. Hepatic glutathione S-transferase activities were significantly increased in the HCCA (219.9%) and HC2CA group (153.8%) compared to NC group. Hepatic superoxide dismutase activity was highest in the HCCA group, and the activities in CA groups were higher than those of NC and HC group.