期刊文献+

Variations of antioxidant enzyme activity and malondialdehyde content in nemertean Cephalothrix hongkongiensis after exposure to heavy metals 被引量:1

Variations of antioxidant enzyme activity and malondialdehyde content in nemertean Cephalothrix hongkongiensis after exposure to heavy metals
下载PDF
导出
摘要 The antioxidant enzyme activity and malondialdehyde(MDA) content of Cephalothrix hongkongiensis were studied to assess variations in the biochemical/physiological parameters of nemerteans under heavy metal stress.Worms were exposed to copper,zinc and cadmium solutions at different concentrations,and the activity of three antioxidant enzymes,catalase(CAT),superoxide dismutase(SOD),and glutathione peroxidase(GPX),and MDA content were measured.The results show that the activity of each enzyme changed immediately after exposure to heavy metals.CAT was invariably inhibited throughout the experimental period,while the SOD activity was significantly elevated by exposure to Cu^(2+) for 48h,but then decreased.SOD was inhibited by Zn^(2+) during the first 12h of exposure,but activated when exposed for longer periods.Under Cd^(2+) stress,SOD activity decreased within 72h.GPX activity varied greatly,being significantly increased by both Cu^(2+) and Zn^(2+),but significantly inhibited by Cd^(2+) in the first 12-24h after exposure.MDA content increased on Cu^(2+) exposure,but normally decreased on Zn^(2+) exposure.MDA content followed an increase-decrease-increase pattern under Cd^(2+) stress.In conclusion,the antioxidant system of this nemertean is sensitive to heavy metals,and its CAT activity may be a potential biomarker for monitoring heavy metal levels in the environment. The antioxidant enzyme activity and malondialdehyde(MDA) content of Cephalothrix hongkongiensis were studied to assess variations in the biochemical/physiological parameters of nemerteans under heavy metal stress.Worms were exposed to copper,zinc and cadmium solutions at different concentrations,and the activity of three antioxidant enzymes,catalase(CAT),superoxide dismutase(SOD),and glutathione peroxidase(GPX),and MDA content were measured.The results show that the activity of each enzyme changed immediately after exposure to heavy metals.CAT was invariably inhibited throughout the experimental period,while the SOD activity was significantly elevated by exposure to Cu^2+ for 48h,but then decreased.SOD was inhibited by Zn^2+ during the first 12h of exposure,but activated when exposed for longer periods.Under Cd^2+ stress,SOD activity decreased within 72h.GPX activity varied greatly,being significantly increased by both Cu^2+ and Zn^2+,but significantly inhibited by Cd^2+ in the first 12-24h after exposure.MDA content increased on Cu^2+ exposure,but normally decreased on Zn^2+ exposure.MDA content followed an increase-decrease-increase pattern under Cd^2+ stress.In conclusion,the antioxidant system of this nemertean is sensitive to heavy metals,and its CAT activity may be a potential biomarker for monitoring heavy metal levels in the environment.
出处 《Chinese Journal of Oceanology and Limnology》 SCIE CAS CSCD 2010年第4期917-923,共7页 中国海洋湖沼学报(英文版)
基金 Supported by the National Natural Science Foundation of China(No.30270235)
关键词 Cephalothrix hongkongiensis CATALASE superoxide dismutase glutathione peroxidase MALONDIALDEHYDE heavy metal 抗氧化酶活性 重金属胁迫 丙二醛含量 超氧化物歧化酶活性 谷胱甘肽过氧化物酶 GPX活性 MDA含量 CAT活性
  • 相关文献

参考文献39

  • 1Almeida E A, de Miyamoto S, Bainy A C D, de Medeiros M H G, Mascio P D. 2004. Protective effect of phospholipid hydroperoxide glutathione peroxidase (PHGPx) against lipid peroxidation in mussels Perna perna exposed to different metals. Marine Pollution Bulletin, 49: 386-392.
  • 2Bagnyukova T V, Storey K B, Lushchak V I. 2005. Adaptive response of antioxidant enzymes to catalase inhibition by aminotriazole in goldfish liver and kidney. Comparative Biochemistry and Physiology Part B, 142: 335-341.
  • 3Bagnyukova T V, Chahrak O I, Lushchak V I. 2006. Coordinated response of goldfish antioxidant defenses to environmental stress. Aquatic Toxicology, 78:325-331.
  • 4Barja de Quiroga G, Lopez-Torres M, P6rez-Campo R. 1989. Catalase is needed to avoid tissue peroxidation in Rana perezi in normoxia. Comparative Biochemistry and Physiology Part C, 94: 391-398.
  • 5Beuge J A, Aust S D. 1978. Microsomal lipids peroxidation. Methods in Enzymology, 52:302-310.
  • 6Bouzyk E, Iwanenko T, Jaroeewiez N, Kruszewski M, Sochanowicz B, Szumiel I. 1997. Antioxidant defense system in differentially hydrogen peroxide sensitive L5178Y sublines. Free Radical Biology and Medicine, 22: 697-704.
  • 7Bradford M M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry, 72: 248-254.
  • 8Casalino E, Calzaretti G, Sblano C, Landriscina C. 2002. Molecular inhibitory mechanisms of antioxidant enzymes in rat liver and kidney by cadmium. Toxicology, 179: 37-50.
  • 9Chandran R, Sivakuma A A, Mohandas S, Aruchami M. 2005 Effect of cadmium and zinc on antioxidant enzyme activity in the gastropod, Achatina fulica. Comparative Biochemistry and Physiology Part C, 140: 422-426.
  • 10Correia A D, Livingstone D R, Costa M H. 2002. Effects of water-borne copper on metallothionein and lipid peroxidation in the marine amphipod (Gammarus locusta). Marine Environmental Research, 54: 357-360.

同被引文献7

引证文献1

二级引证文献5

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部