Fluoride and aluminium disturb neuronal morphology, transport functions, cholinesterase, lysosomal and cell cycle activities
Document Type
Article
Publication Date
6-1-2015
Abstract
UNLABELLED: Fluoride and aluminium have been reported to cause severe alterations in the brain. However, their exact mechanisms of neurotoxic activities remain unknown. AIM: This study was designed to investigate the role of fluoride and aluminium in neuronal transport, lysosomal, cell cycle protein and acetylcholinesterase activities. METHOD: Adult Wistar rats were given low and high doses of fluoride, aluminium and a combination of both with the control group receiving distilled water for 30 days. Blood sera and brain homogenates were quantified for alkaline phosphatase (biomarker for neuronal transport) activities. Brain sections were stained with cresyl fast violet to detect neuronal cell damage. Histochemical demonstration of acetylcholinesterase (AChE) activity and the immunohistochemical detection of cell cycle protein (anti-cyclin D) and lysosomal protein (anti-cathepsin D) were done using the antigen retrieval method. RESULT: Results showed severe histomorphologic alterations, dysregulation of membrane transport activities, inhibition of AChE activities and increased expression of lysosomal and cell cycle proteins. CONCLUSION: These findings confirm that excessive fluoride and aluminium intake induces the progression of cell death which inhibit AChE activities and trigger the release of lysosomal and cell cycle proteins.
Publication Source (Journal or Book title)
Pathophysiology : the official journal of the International Society for Pathophysiology
First Page
105
Last Page
15
Recommended Citation
Akinrinade, I. D., Memudu, A. E., & Ogundele, O. M. (2015). Fluoride and aluminium disturb neuronal morphology, transport functions, cholinesterase, lysosomal and cell cycle activities. Pathophysiology : the official journal of the International Society for Pathophysiology, 22 (2), 105-15. https://doi.org/10.1016/j.pathophys.2015.03.001