Cytoskeletal proteins have been reported as constituents of cytoplasmic inclusions typical of degenerated neurones in Parkinson's disease and, in addition, the involvement of cytoskeleton in the mechanism of action of the parkinsonism-producing neurotoxin MPP+ is emerging. Here we investigate the in
Involvement of tubulin in MPP+ neurotoxicity on NGF-differentiated PC12 cells.
✍ Scribed by Graziella Cappelletti; Cristina Incani; Rosalba Maci
- Book ID
- 102564868
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 453 KB
- Volume
- 19
- Category
- Article
- ISSN
- 1065-6995
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✦ Synopsis
Abstract
In vivo, the neurotoxin MPTP is oxidated to MPP^+^, which is toxic to dopaminergic neurons. In this paper, we have used MPP^+^ as a tool to evoke neurotoxicity in the PC12 cell line and investigate the intracellular events that are involved. A cytotoxicity test, performed on undifferentiated and NGF‐differentiated PC12 cells, showed that MPP^+^ is much more toxic on differentiated cells and indicated the suitable range of concentrations for studying the starting events evoked by the neurotoxin. By indirect immunofluorescence we have shown that the localisation of α ‐ and β ‐tubulin in NGF‐differentiated cells was modified by a 24 h treatment with 15 μmol/l MPP^+^. A biochemical analysis was performed on cell extracts and the results showed that MPP^+^ treatment induced an increase in α ‐tubulin levels and a decrease in β ‐tubulin levels. These results suggest the involvement of the two microtubule proteins in MPP^+^ neurotoxicity on NGF‐differentiated PC12 cells.
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