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Increase of gluthatione S-transferase, carboxyl esterase and carbonyl reductase in Fasciola hepatica recovered from triclabendazole treated sheep
Enzymatic activities of carboxylesterase (CE), glutathione S-transferase (GST) and carbonyl reductase (CBR) measured in F. hepatica recovered from sheep treated with triclabendazole (10mg/kg). •In vivo assessment of CE, GST and CBR in F. hepatica recovered to TCBZ treated sheep.•Increase of the meta...
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Published in: | Molecular and biochemical parasitology 2013-10, Vol.191 (2), p.63-65 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Enzymatic activities of carboxylesterase (CE), glutathione S-transferase (GST) and carbonyl reductase (CBR) measured in F. hepatica recovered from sheep treated with triclabendazole (10mg/kg).
•In vivo assessment of CE, GST and CBR in F. hepatica recovered to TCBZ treated sheep.•Increase of the metabolite sulfoxide (TCBZSO) and sulfone (TCBZSO2).•Increase in enzymatic activity at 24 and 48h PT of the three enzymes tested.•The highest enzymatic activity was observed after peak of TCBZSO (active metabolite).•Return of enzyme activities to basal values to 60h PT.
Fasciolasis is a zoonotic parasitic disease caused by Fasciola hepatica and its control is mainly based on the use of triclabendazole (TCBZ). Parasite resistance to different anthelmintics is growing worldwide, including the resistance of F. hepatica to TCBZ. In the present work we evaluate “in vivo” the activity of xenobiotic metabolizing enzymes of phase I (carboxyl esterases) and phase II (glutathione S-transferases and carbonyl reductases) recovered of flukes from sheep treated with TCBZ. All three enzymes showed increased activity in TCBZ flukes returning 60h post-treatment at similar to baseline unexposed flukes. TCBZ action may induce secondary oxidative stress, which may explain the observed increment in activities of the analyzed enzymes as a defensive mechanism. The enzymes analyzed are candidates to participate actively in the development of resistance at TCBZ in F. hepatica. |
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ISSN: | 0166-6851 1872-9428 |
DOI: | 10.1016/j.molbiopara.2013.09.002 |