Biochemical changes in primary culture of skeletal muscle cells following dimethoate exposure

In order to investigate the cellular mechanism of muscular weakness in the Intermediate Myasthenia Syndrome (IMS) following acute organophosphate poisoning, we studied the cytotoxicity of dimethoate and its effects on the activity of acetylcholine esterase (AChE), Na +–K +-ATPase, succinate dehydrog...

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Bibliographic Details
Published in:Toxicology (Amsterdam) 2002-05, Vol.174 (2), p.79-85
Main Authors: Yang, Dongren, Lu, Xinfang, Zhang, Weiguo, He, Fengsheng
Format: Article
Language:English
Subjects:
Acetylcholine esterase
Acetylcholinesterase - blood
Animals
Biological and medical sciences
Blotting, Western
Calcium-Transporting ATPases - metabolism
Cell Survival - drug effects
Cells, Cultured
Cholinesterase Inhibitors - toxicity
Cytotoxicity
Dimethoate
Dimethoate - toxicity
Drug Screening Assays, Antitumor
Heat-shock protein
HSP70 Heat-Shock Proteins - metabolism
Insecticides - toxicity
Medical sciences
Muscle, Skeletal - cytology
Muscle, Skeletal - drug effects
Muscle, Skeletal - metabolism
Pesticides, fertilizers and other agrochemicals toxicology
Rats
Rats, Wistar
Skeletal muscle
Sodium-Potassium-Exchanging ATPase - metabolism
Succinate Dehydrogenase - metabolism
Toxicology
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Summary:In order to investigate the cellular mechanism of muscular weakness in the Intermediate Myasthenia Syndrome (IMS) following acute organophosphate poisoning, we studied the cytotoxicity of dimethoate and its effects on the activity of acetylcholine esterase (AChE), Na +–K +-ATPase, succinate dehydrogenase (SDH), and Ca 2+-ATPase in primary cultured skeletal muscle cells. The results showed that the activity of AChE was significantly inhibited in a dose and time-dependent manner when cells were exposed to dimethoate for 2 h, but the expression of heat-shock protein (HSP70) in muscle cells was significantly increased in a time-dependent manner following dimethoate exposure. Dimethoate can significantly increase the activity of Na +–K +-ATPase in the mitochondrial and cytoplasm fraction of muscle cells, and inhibit the activity of Ca 2+-ATPase. This study suggests that the disruption of intracellular homeostasis and energy metabolism of the muscle cells may play a role in the etiology of IMS.
ISSN:0300-483X
1879-3185
DOI:10.1016/S0300-483X(02)00038-0