• Title/Summary/Keyword: "The cat"

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Effect of Exercise on Antioxidant Enzyme Activities of Skeletal Muscle and Liver in STZ-diabetic Rats (STZ-당뇨쥐에서 운동부하가 골격근 및 간의 항산화효소 활성도에 미치는 영향)

  • Seok, Kwang-Ho;Lee, Suck-Kang
    • Journal of Yeungnam Medical Science
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    • v.17 no.1
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    • pp.21-30
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    • 2000
  • Background: The purpose of the present study was to investigate the effect of exercise on the activities of antioxidant enzymes, super oxide dismutase(SOD), glutathione peroxidase(GPX) and catalase(CAT) of skeletal muscle(gastrocnemius) and liver in streptozotocin(STZ) induced diabetic rats. The malondialdehyde(MDA) concentration was also measured as an index of lipid poroxidation of tho tissues by exercise-induced oxidative stresses in diabetic rats. Material and Methods: Male Sprague-Dawley rats were randomly divided into control and STZ-induced diabetic rats. The STZ in citrate buffer solution was injected twice at S days intervals intraperitoneally(50, 70 mg/kg respectively). On the 28th day after the first STZ injection, the diabetic animals were randomly divided into pre- and post-exercise groups, The exercise was introduced to the rats of post-exercise group by treadmill running until exhaution with moderate intensity ($V_{O2max}$: 50-70%) of exercise. The duration of average running time was 2 hours and 19 minutes. Results: The blood glucose concentration was increased(p<0.001) and plasma insulin concentration was decreased(p<0.001) in the diabetic rats. The glycogen concentration in the muscle and liver was decreased by exhaustive exercise in the diabetic rats(p<0.001), In the skeletal muscle, the activities of GPX was increased(p<0.05) and the activities of SOD and CAT were not changed in the diabetic rats compare to those of the control rats. The activities of GPX was not changed by exercise but the activities of SOD(p<0.01) and CAT(p<0.01) were decreased by exercise in the diabetic rats, The concentration of MDA was not changed by exercise in diabetic rats, and the values of pre-exercise and post-exercise diabetic rats were not different from the value those of control rats, In the liver, the activities of SOD was decreased(p<0.01), and the activities of GPX and CAT were not changed in diabetic rats compared to the values of control rats, The activities of SOD, GPX and CAT were not changed by exercise in diabetic rats but the activity of SOD seemed to decrease slightly, The MDA concentration was increased in the diabetic rats compared to the values of control rats(p<0.001), but there was no change of MDA concentration by exercise in diabetic rats, Conclusions: In summary, exhaustive physical exercise did not seem to impose oxidative stress on the skeletal muscle because of due to oxygen free radicals, regardless of the decrease in SOD and CAT in the diabetic rats, In liver tissue, the tissue damage by oxidative stress was observed in diabetic rats but the additional tissue damage by exhaustive physical exercise was not observed.

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Enhancement of the solubility of human tissue inhibitor of matrix metallocroteinase-2 (TIMP-2) in E. coli using a modified in vitro mutagenesis (새로운 유전자 재조합 방법을 이용한 대장균에서의 인간 tissue inhibitor of mtrix metalloproteinase-2 (TIMP-2) 유전자의 가용성 발현)

  • Kim, Jong-Uk;Choi, Dong-Soon;Joo, Hyun;Min, Churl-K.
    • KSBB Journal
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    • v.23 no.3
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    • pp.231-238
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    • 2008
  • The second family member of tissue inhibitors of matrix metalloproteinases, TIMP-2, is a 21kDa protein which inhibits matrix metalloproteinases 2 (MMP-2). Expression of mammalian proteins in E. coli often forms inclusion bodies that are made up of mis-folded or insoluble protein aggregates. The requirement for the formation of 6 disulfide bonds in the process of the TIMP-2 folding is likely to be incompatible with the reducing environment of E. coli. However, this incompatibility can be often overcome by introducing a mutagenesis that could lead to enhancement of the protein solubility. In this reason, we have attempted to express the soluble TIMP-2 in E. coli by applying a modified staggered extension process (StEP), one of the in vitro PCR-based recombinant mutagenesis methods, and error-prone PCR. C-terminally located CAT fusion protein with respect to mutated TIMP-2 proteins enables us to differentiate the soluble TIMP-2 from the insoluble in E. coli by virtue of chloramphenicol resistance. According to this scheme, E. coli harboring properly-folded CAT fused to TIMP-2 protein was selected, and some of the resulting colonies exhibited an enhanced, soluble expression of TIMP-2 compared to the wild type, implying (i) the StEP technique is successfully employed to enhance the proper folding thereby increasing the solubility of TIMP-2, and (ii) the CAT dependent screening may be a simple and effective method to differentiate the soluble protein expression in E. coli.

Cat is not a small dog!

  • Lee, Mi-Gyeong
    • Proceedings of the Korean Society of Veterinary Clinics Conference
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    • 2009.10a
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    • pp.28-30
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    • 2009
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Effect of Achyranthis Radix and Drynariae Rhizoma Extracts on Antioxidant Activity and Antioxidant Enzymes (우슬과 골쇄보의 추출물이 항산화 활성 및 항산화 효소 대사에 미치는 효과)

  • Kang, Mi Young;Lee, Soo Hyun;Lee, Sang Won;Cha, Sun Woo;Song, Jae Lim;Lee, Sang Chul
    • Korean Journal of Plant Resources
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    • v.28 no.5
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    • pp.600-607
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    • 2015
  • In vitro and in vivo experiments using Achyranthis radix and Drynariae rhizoma extracts were conducted. Antioxidant properties were analyzed and the effects on bone, glucose and lipid metabolism were investigated. Drynariae rhizoma (64.67%) obtained higher DPPH radical scavenging activity compared to Achyranthis radix (19.03%). Similar results were obtained in the reducing power. No differences were observed on the ABTS radical scavenging ability and SOD. In contrast, Achyranthis radix (77.60%) has higher chelating ability compared to Drynariae rhizoma (46.21%). In vivo experiments revealed higher plasma TBARS in OVX-DR than in OVX-AR. Opposite result was seen in erythrocyte TBARS. Hepatic, nephritic and erythrocyte enzymes were considered for the antioxidant enzyme activities. GSH-Px and PON of hepatic enzymes were higher in OVX-AR. While the CAT and GR were higher in OVX-DR. SOD, GSH-Px, GR and PON of nephritic enzymes of OVX-DR were higher compared to OVX-AR. Almost similar values were obtained in CAT using both extracts. The OVX treated rats obtained higher CAT and GR in the erythrocyte enzymes compared to SHAM. The SOD of erythrocyte enzymes in OVX-DR was higher compared to OVX-AR. On the other hand, the GSH-Px was higher in OVX-AR.

HALO EMISSION OF THE CAT’S EYE NEBULA, NGC 6543: SHOCK EXCITATION BY FAST STELLAR WINDS

  • Hyung, Siek;Lee, Seong-Jae
    • Journal of Astronomy and Space Sciences
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    • v.19 no.3
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    • pp.173-180
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    • 2002
  • Images taken with the Chandra X-ray telescope have for the the first time revealed the central, wind-driven, hot bubble (Chu et al. 2001), while Hubble Space Telescope (HST) WFPC2 images of the Cat's Eye nebula, NGC 6543, show that the temperature of the halo region of angular radius ~ 20", is much higher than that of the inner bright H II region. With the coupling of a photoionization calculation to a hydrodynamic simulation, we predict the observed 〔O III〕 line intensities of the halo region with the same O abundance as in the core H II region: oxygen abundance gradient does not appear to exist in the NGC 6543 inner halo. An interaction between a (leaky) fast stellar wind and halo gas may cause the higher excitation temperatures in the halo region and the inner hot bubble region observed with the Chandra X-ray telescope.