Decrease in catalase activity of Folsomia candida fed a Bt rice diet

Environ Pollut. 2011 Dec;159(12):3714-20. doi: 10.1016/j.envpol.2011.07.015. Epub 2011 Aug 11.

Abstract

Here we report the effects of three Bt-rice varieties and their non-Bt conventional isolines on biological traits including survival, reproduction, and the activities of three antioxidant enzymes superoxide dismutase, catalase and peroxidase, in the Collembolan, Folsomia candida. The reproduction was significantly lower when fed Kemingdao and Huahui1 than those feeding on their non-GM near-isogenic varieties Xiushui and Minghui63 respectively, this can be explained by the differences of plant compositions depended on variety of rice. The catalase activity of F. candida was significantly lower when fed the Bt-rice variety Kemingdao compared to the near-isogenic non-Bt-rice variety Xiushui. This suggests that some Bt-rice varieties may impose environmental stress to collembolans. We emphasize that changes in activity of antioxidant enzymes of non-target organisms are important in understanding the ecological consequences for organisms inhabiting transgenic Bt-rice plantations.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / pharmacology*
  • Catalase / antagonists & inhibitors
  • Catalase / metabolism*
  • Down-Regulation* / drug effects
  • Eating
  • Endotoxins / genetics
  • Endotoxins / metabolism
  • Endotoxins / pharmacology*
  • Hemolysin Proteins / genetics
  • Hemolysin Proteins / metabolism
  • Hemolysin Proteins / pharmacology*
  • Insect Proteins / antagonists & inhibitors
  • Insect Proteins / metabolism*
  • Insecta / drug effects
  • Insecta / enzymology
  • Insecta / physiology*
  • Oryza / genetics*
  • Oryza / metabolism
  • Plants, Genetically Modified / genetics
  • Plants, Genetically Modified / metabolism
  • Reproduction / drug effects

Substances

  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • Insect Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis
  • Catalase