Effects of short-term exposure to fluoxetine and carbamazepine to the collembolan Folsomia candida

Chemosphere. 2015 Feb:120:86-91. doi: 10.1016/j.chemosphere.2014.06.038. Epub 2014 Jul 8.

Abstract

Pharmaceuticals, emerging environmental contaminants, have their ecotoxicological effects to non-target organisms in soil largely unknown. This study assessed short-term effects of two human pharmaceuticals, carbamazepine and fluoxetine, to Folsomia candida. Avoidance to spiked soils was assessed after 48 and 96 h exposure and biochemical changes (acetylcholinesterase and glutathione S-transferase activities, and lipid peroxidation levels) after 96 h. F. candida avoided soils spiked with 0.04, 0.4 and 4 mg carbamazepine kg(-1) after 48 h. However, higher number of organisms were found in soils with 40 mg carbamazepine kg(-1), a behavior also displayed for 40 mg fluoxetine kg(-1) spiked soils. After 96 h, F. candida showed avoidance behavior to soils with 4 and 40 mg carbamazepine kg(-1). Acetylcholinesterase activity decreased in 0.4 mg fluoxetine kg(-1) exposed organisms. Peroxidative damages were detected in organisms exposed to 4 and 40 mg kg(-1) carbamazepine and glutathione S-transferase inhibition was observed at 40 mg kg(-1). Data suggests that carbamazepine and fluoxetine may pose risk to soil collembolan.

Keywords: Avoidance; Biomarkers; Human pharmaceuticals; Soil; Springtail.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arthropods / drug effects*
  • Arthropods / enzymology
  • Carbamazepine / analysis
  • Carbamazepine / toxicity*
  • Cholinesterases / metabolism
  • Ecotoxicology
  • Environmental Monitoring / methods*
  • Escape Reaction / drug effects
  • Fluoxetine / analysis
  • Fluoxetine / toxicity*
  • Glutathione Transferase / metabolism
  • Lipid Peroxidation / drug effects
  • Soil Pollutants / analysis
  • Soil Pollutants / toxicity*
  • Time Factors

Substances

  • Soil Pollutants
  • Fluoxetine
  • Carbamazepine
  • Glutathione Transferase
  • Cholinesterases