کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2583775 | 1130702 | 2007 | 5 صفحه PDF | دانلود رایگان |
To explore the changes of the endogenous phosphorylation of brainstem mitochondrial and synaptosomal proteins in adult hens dosed with tri-o-cresyl phosphate (TOCP) following the development of organophosphate-induced delayed neurotoxicity (OPIDN). Verapamil (7 mg/(kg day), i.m.) was given for 4 days. A dose of TOCP (750 mg/kg, p.o.) was administrated in second day after verapamil. Phosphorylation of the proteins from brainstem mitochondria and synaptosomes was assayed in vitro by using [γ-32P]ATP as phosphate donor. Radiolabeled proteins were separated by SDS-PAGE and visualized by autoradiography. The results showed that TOCP administration enhanced the phosphorylation of the cell organelle proteins (mitochondria: 60, 55, 45, and 20 kDa; synaptosomes: 65, 60, and 20 kDa), while verapamil abolished the enhancement induced by TOCP. Additionally, the reaction for the phosphorylation is catalyzed by the calcium/calmodulin protein kinase. Therefore, TOCP can enhance the phosphorylation of the brainstem mitochondrial and synaptosomal proteins from the hens with OPIDN; however, protection from the enhancement of the phosphorylation should be involved in the mechanisms of the amelioration of TOCP-induced delayed neurotoxicity by verapamil.
Journal: Environmental Toxicology and Pharmacology - Volume 24, Issue 1, July 2007, Pages 67–71