• Journal of Life Science
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• v.21 no.2
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• pp.194-201
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• 2011

Caudal-related homeodomain proteins play critical roles in intestine development and maintenance from Drosophila to humans. The loss or reduction of CDX1 and CDX2 are known to be associated with colon cancers. It has been well known that colorectal carcinogenesis is associated with serious oxidative stress and that catalase is decreased in colon carcinomas. However, the underlying molecular mechanisms remain elusive. Here, we report that Caudal-related homeodomain proteins positively regulate catalase expression in both Drosophila and humans. We found that Drosophila caudal heterozygotes have a decreased catalase expression and increased ROS generation in the hindgut, and that the overexpression of Caudal increases catalase promoter activity and catalase mRNA levels. We also found that CDX1 and CDX2 up-regulate catalase promoter activity and protein levels in HCT116 cells - human colorectal carcinoma cell lines. The level of catalase protein in several colorectal carcinoma cell lines was associated with CDX1 expression. These results suggest that CDX1 and CDX2 may be involved in intestinal homeostasis and tumorigenesis via regulation of catalase expression.

• Proceedings of the Zoological Society Korea Conference
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• 1996.10a
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• pp.182.2-182
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• 1996

• 대한치주과학회:학술대회논문집
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• 1994.12a
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• pp.33-33
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• 1994

• Journal of Preventive Medicine and Public Health
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• v.23 no.4 s.32
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• pp.371-390
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• 1990

Production of free radicals of superoxide anion in tissues by cadmium, activities of superoxide dismutase and catalase to protect tissue damages caused by the free radicals and ATPase that plays an important role in energy metabolism at cellular level were investigated. Experiments in vivo were conducted with liver, kidney and testicle tissue homogenates of rats adding $0.05{\sim}0.50mM$ cadmium chloride, and in vivo experiments administering single dose of 5 mg of cadmium/kg of body weight in 0.1% cadmium chloride solution intraperitoneally 48 hours prior to evisceration. Production of superoxide radicals in liver and testicle increased with addition of cadmium in vitro, but not in kidney. In vivo experiments, however, superoxide radicals slightly increased in liver and kidney but not in testicle. Superoxide dismutase (Cu, Zn-SOD and Mn-SOD), catalase and ATPase (total, $Mg^{++}-\;&\;Na^+,\;K^+-$) activity decreased in the presence of cadimium in dose dependent manner. Reduction of these enzyme activities varied not only with dosage of cadmium but also with type of tissue and between in vitro and in vivo experiment.

• Applied Biological Chemistry
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• v.38 no.3
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• pp.202-206
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• 1995

In order to obtain the basic data for clarifing the mechanism of cold tolerance in crops, we analyzed various biochemical changes according to the Uniconazole treatment in Brassica seedling. Peroxidase activity in the root fraction of Brassica seedling was about 3 to 4 times higher than that in hypocotyl fraction, while catalase activity in those fractions showed opposite trend to the peroxidase activity. The content of hydrogen peroxide in root fraction was higher than that of hypocotyl fraction as being a reciprocal proportion with catalase activity. Especially in all fractions, peroxidase· activity of 'Sandongchae' (B. campestris) seedling, known as cold tolerant, was two-fold higher than that of cold sensitive rape(B. napus). The elongation rate of hypocotyl after germination was faster in B. napus than in B. campestris. The application of Uniconazole at 0.3 to 1.0 ppm to B. napus suppressed 43 to 46% of hypocotyl elongation and increased 65 to 73% of peroxidase activity in hypocotyl fraction. The shortening rate of hypocotyl length due to Uniconazole treatment was positively correlated with the increasing rate of peroxidase activity in hypocotyl fraction. Superoxide dismutase was not induced upon Uniconazole treatment and has only 3 isozymes in any fractions. Its activity was observed in the order of cotyledon>root>hypocotyl fraction.

• Parasites, Hosts and Diseases
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• v.31 no.3
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• pp.259-268
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• 1993

When activity of peroxidase in auld Pnrqfonimn westermqni was monitored using o-dianisidine and $H_2O_2$ as substrates, its specific activity was 1.5 times higher In excretory-secretory product (ESP) than in crude extract. The one was purified by two purification steps of Sephacryl S-300 Superfine gel permeation and DEAE-Trisacryl M anion exchange chromatographies. Its activity increased 16.9 fold with 32.3% recovery. The enzyme was inhibited totally by 1 millimoles of dithiothreitol (DTT), 2-mercaptoethanol and azide. Molecular mass was 16 kDa in reducing SDS-polyacrylamide gel electrophoresis (PAGE) or 19 kDa in TSK-Blue gel filtration high performance liquid chromatography (HPLC). respectively. Special staining for peroxidase by diaminobenzidine on SDS-PAGE confirmed the activity. The peroxidase was less reactive to a paragonimiasis serum when observed by SDS-PAGE/immunoblot. In addition, specific activities of superoxide dismutase (SOD) and catalase were also identified in the ESP. High activities of these antioxidant enzymes in ESP indicate that they are parts of defense mechanisms against reactive oxygen intermediates from host.

• Korean Journal of Plant Tissue Culture
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• v.28 no.2
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• pp.69-74
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• 2001

Calli were induced on MS medium supplemented with 0.5 mg/L 2,4-D by using the leaf explants of haploid which were derived from the diploid and haploid of Nicotiana tabacum cv BY4. These calli were subcultured on MS medium with the combination of 2.0 mg/L 2,4-D, 1.0 mg/L kinetin and 0.1 mg/L BAP. Cell propagation of diploid plants were good in a combination of 2.0 mg/L 2,4-D, 0.1mg/L BAP in vitro conditions, suspension cultures were conducted in equal condition. Homogenized suspension cultured cells were smeared 2.0 mL each on MS medium with 0~100 $\mu$M PFP, to select the resistant colony to PFP, and were examined after 10d, 20d and 30d. Measurment of fresh weight of cells after 30d of culture shows that with more concentration of PFP in medium the fresh weight of the cells decreased. In case of diploid, selected callus was the highest in vitro treated with 5 $\mu$M PFP. It was higher than control until 100 $\mu$M PFP. The active degree of catalase was the highest in vitro with 5 $\mu$M PFP but the lowest in vitro with 10 $\mu$M PFP on the other hand, in case of haploid plant, the active degree of peroxidase and catalase was the highest in vitro treated with 50 $\mu$M PFP. It's sure that enzyme active degree of between diploid and haploid had big differences.

• Korean Journal of Microbiology
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• v.32 no.2
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• pp.155-162
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• 1994

Cells of Acinetobacter sp. strain JC1 DSM 3803, an aerobic monoxide-oxidizing bacterium, growing on glucose exhibited high catalase activity at the mid-exponential growth phase. The enzyme activity decreased gradually after then until the early stationary phase, increased again at the mid-stationary phase, and then decreased again thereafter. Cells growing on glucose was found to contain three kinds of catalses. Cat1, Cat2 and Cat3. The activities of Cat1 and Cat3 did change significantly during growth, but that of Cat2 exhibited significant variation. Cat3 was found to present only in cells growing on glucose, but not in cells growing on carbon monoxide of methanol. The activities of call and Cat3 in cell-free extracts were stable upon treatment with ethanol and chloroform, but decreased to some extent when the enzymewere treated with 2mM $H_2O_2$ and/or 3-amino-1,2,4-triazole (AT). Cat2 was found to be extremely sensitive to the ethanol-chloroform and $H_2O_2$ treatments, but was insensitive to the AT treatment. Cat1 exhibited enzyme activity after incubation for 1 min at 80$^{\circ}C$. Cat2 and Cat3 did not show enzyme activity after incubation for 1 min at 60$^{\circ}C$ and 70$^{\circ}C$, respectively. Cat2 was found to have peroxidase activity. Cat3 was purified to homogenity in seven steps. The molecular weight of the native enzyme was estimated to be 150,000. Sodium dodecyl sulfate-gel electrophoresis revealed two identical subunits of molecular weight 65,000. The enzyme was found to show two $K_m$ values of 39 mM and 58mM. The optimal pH for the enzyme activity was 7.0, but the activities at pH 6.0, 8.0, and 9.0, were found to be comparable to that at the optimal pH. The optimal temperature for the enzyme activity was found to be 40$^{\circ}C$. The enzyme also exhibited strong activity at 20$^{\circ}C$, 30$^{\circ}C$, and 50$^{\circ}C$. The purified enzyme was not affected by the ethanol-chloroform treatment. The enzyme, howerver, showed less than 10% of the original activity when it was treated with 12 mN AT, 0.1 mM $NaN_3$ of 1mM KCN.

• Current Research on Agriculture and Life Sciences
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• v.16
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• pp.24-30
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• 1998

This experiment was carried out to elucidate and study about plant defense mechanism subjected to water stress(drought, flooding). We measured water content, total soluble protein content as stress marker and superoxide dismutase(SOD), catalase (CAT) as antioxidant enzymes subjected to water stress(drought, flooding) and recovery in soybean leaves. The results obtained were as follows; Two soybean lines(keonolkong, euhakong)leaves exposed to water stress (drought, flooding) showed premature senescence as evidence by the decrease in water content, and total soluble protein content, but those of soybean leaves subject to water stress recovery for 3 days were recovered. Visual damage was much worse at drought stress than flooding stress and was worse keunolkong than enhakong. The activity of superoxide dismutase, catalase subjected to water stress(drought, flooding)was on the decrease, but degree of decrease was different from a sort of soybean lines, drought and flooding stress.

• Journal of the Korean Society of Tobacco Science
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• v.15 no.1
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• pp.3-14
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• 1993

Oxidants in environment or cigarette smoke are known to be implicated in the oxidative damages of pulmonary system. Such cellular damages are prevented by the presence of adequate levels of antioxidants in the tissue. In the present study, we investigated the influences of smoking duration and concentration of smoke on lung antioxidant defense in rats. Subchronic exposure of rats to smoke generated from 6 cigarettes per day for 90 days caused the activities of catalase and superoxide dismutase (SOD) to increase. However, glutathione peroxidase (GP-Xase) was not significantly changed. Total sulfhydryl compounds (Total-SH) in the lung homogenates from the rats inhaled with cigarette smoke for 15 days was decreased by 44% , thereafter it was returned to the level of normal rats. On the contrary, when rats were daily exposed to a different concentration of smoke generated from 1 to 20 cigarettes per day for 15 days, the activity of catalase was increased gradually with dose, but total SOD activity was increased only in the rats of low dose groups less than 5 cigarettes. Three types of SOD (one Cu, Zn-SOD with pI 4.9, and two Zn-SOD with pI 4.7 and 7.9)were detected in the lung homogenates and Zn-SOD with pI 4.7 was the major and cigarette-smoke inducible form. These results indicate that the protection of lung against oxidants from cigarette smoke seems to be accomplished by the induction of catalase and SOD, especially a cyanide resistant Zn-SOD with pI 4.f, following the consumption of antioxidants such as GSH in the beginning of inhalation period.