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Disturbance of antioxidant capacity produced by beauvericin in CHO-K1 cells

Toxicol Lett. 2014 May 2;226(3):337-42. doi: 10.1016/j.toxlet.2014.02.023. Epub 2014 Mar 5.

Abstract

Glutathione (GSH) levels, glutathione peroxidase (GPx), glutathione reductase (GR) and glutathione-S-transferase (GST) as antioxidant defense system were evaluated in CHO-K1 cells after beauvericin (BEA) exposure. The effect of N-acetyl-cysteine (NAC) pre-treatment was assessed. GSH levels significantly decrease 18% and 29% after 5 μM of BEA in fresh medium and NAC pre-treatment, respectively compared to their controls. The GPx activity increased significantly from 35% to 66% in fresh medium and 20% in NAC pre-treatment. GR activity decreased after 5 μM of BEA up to 43% and 53% in fresh medium and NAC pre-treatment, respectively. The GST activity increased in fresh medium (from 61% to 89%) and decreased (from 22% to 35%) after NAC pre-treatment. Comparing BEA exposure in fresh medium and NAC pre-treatment, GSH levels, GPx activity and GST activity increased 716%, 458% and 206%, respectively respect to fresh medium; conversely no changes were observed in GR activity. In addition, NAC is an effective scavenger of BEA. GSH and related enzymes play an antioxidant role in the defense system of CHO-K1 cells exposed to BEA.

Keywords: Beauvericin; CHO-K1 cells; Cytotoxicity; Enzymes; GSH; Oxidative stress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcysteine / pharmacology
  • Animals
  • Antioxidants / metabolism*
  • CHO Cells
  • Cell Proliferation / drug effects
  • Cricetulus
  • Depsipeptides / toxicity*
  • Glutathione / analysis
  • Glutathione Peroxidase / metabolism
  • Glutathione Reductase / metabolism

Substances

  • Antioxidants
  • Depsipeptides
  • beauvericin
  • Glutathione Peroxidase
  • Glutathione Reductase
  • Glutathione
  • Acetylcysteine