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Acute Toxicity of Insecticide Thiamethoxam to Crayfish (Astacus leptodactylus): Alterations in Oxidative Stress Markers, ATPases and Cholinesterase
Author(s) -
Miraç Uçkun,
Ertan Yoloğlu,
Aysel Alkan Uçkun,
Özden Barım Öz
Publication year - 2021
Publication title -
acta chimica slovenica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.289
H-Index - 46
eISSN - 1580-3155
pISSN - 1318-0207
DOI - 10.17344/acsi.2021.6823
Subject(s) - superoxide dismutase , astacus leptodactylus , glutathione reductase , glutathione , oxidative stress , crayfish , arsenobetaine , glutathione peroxidase , carboxylesterase , antioxidant , acetylcholinesterase , thiamethoxam , toxicology , biology , catalase , chemistry , pesticide , biochemistry , enzyme , ecology , imidacloprid , mass spectrometry , chromatography , inductively coupled plasma mass spectrometry
Thiamethoxam (Thmx) is a globally used neonicotinoid pesticide contaminated in freshwater ecosystems with residues detected in fishery products. Astacus leptodactylus is a popular freshwater crustacean that is cultivated and exported in many countries. In this study, we investigated the acute toxic effects of Thmx on A. leptodactylus using various biomarkers (acetylcholinesterase, carboxylesterase, glutathione S-transferase, glutathione, superoxide dismutase, glutathione peroxidase, glutathione reductase, and adenosinetriphosphatases). The 96-h LC50 value of Thmx was calculated as 8.95 mg active ingredient L–1. As the dose of Thmx increased, oxidative stress was induced by the inhibition/activation of antioxidant enzymes, while the activities of acetylcholinesterase, carboxylesterase and adenosinetriphosphatases were inhibited. As a result, it can be said that Thmx has highly toxic effects on crayfish, therefore they are under threat in the areas where this pesticide is used.

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