Premium
Alterations in xenobiotic metabolizing enzymes in brain and liver of rats coexposed to endosulfan and malathion
Author(s) -
Srikanth Nadadur S.,
Seth Prahlad K.
Publication year - 1990
Publication title -
journal of applied toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.784
H-Index - 87
eISSN - 1099-1263
pISSN - 0260-437X
DOI - 10.1002/jat.2550100303
Subject(s) - malathion , carboxylesterase , endosulfan , glutathione , chemistry , toxicity , pharmacology , xenobiotic , biochemistry , endocrinology , medicine , toxicology , enzyme , biology , pesticide , organic chemistry , agronomy
The effects of endosulfan (3 mg kg −1 body wt., i.p.) and malathion (30 mg kg −1 body wt.) and their coexposure on rat hepatic and brain xenobiotic metabolizing enzymes were investigated. Endosulfan was found to induce aminopyrine‐ n ‐demethylase (81%) and aniline hydroxylase (59%) activities significantly in liver and to a lesser extent in brain. Malathion treatment induced malathion carboxylesterase activity in both liver (50%) and brain (22%), significantly depleted liver glutathione (35%) content with stimulation of glutathione‐ S ‐transferase (50%) and inhibited the activity of mixed‐function oxidases. In the coexposed animals, malathion's inhibitory influence on mixed‐function oxidases and endosulfan's inhibitory effect on malathion carboxylesterase were found to dominate, while endosulfan potentiated the activity of glutathione‐ S ‐transferase significantly in liver (69%) and brain. A similar trend of alteration in coexposed brain was found, but to a lesser extent. A significant inhibition in brain acetylcholine esterase activity (42%) in the coexposed animals suggests that endosulfan may potentiate the toxicity of malathion by interfering with glutathione and carboxylesterase routes of malathion detoxification.