La maladie de Parkinson en France (serveur d'exploration)

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Extracellular toxicity of 6-hydroxydopamine on PC12 cells

Identifieur interne : 003B91 ( Main/Exploration ); précédent : 003B90; suivant : 003B92

Extracellular toxicity of 6-hydroxydopamine on PC12 cells

Auteurs : D. Blum [Belgique, France] ; S. Torch [France] ; M.-F. Nissou [France] ; A.-L. Benabid [France] ; J.-M. Verna [France]

Source :

RBID : Pascal:00-0242455

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English descriptors

Abstract

6-hydroxydopamine (6-OHDA) is usually thought to cross cell membrane through dopamine uptake transporters, to inhibit mitochondrial respiration and to generate intracellular reactive oxygen species. In this study, we show that the anti-oxidants catalase, glutathion and N-acetyl-cystein are able to reverse the toxic effects of 6-OHDA. These two latter compounds considerably slow down 6-OHDA oxidation in a cell free system suggesting a direct chemical interaction with the neurotoxin. Moreover, desipramine does not protect PC12 cells and 6-OHDA is also strongly toxic towards non-catecholaminergic C6 and NIH3T3 cells. These results thus suggest that 6-OHDA toxicity on PC12 cells mainly involves an extracellular process.


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Le document en format XML

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<div type="abstract" xml:lang="en">6-hydroxydopamine (6-OHDA) is usually thought to cross cell membrane through dopamine uptake transporters, to inhibit mitochondrial respiration and to generate intracellular reactive oxygen species. In this study, we show that the anti-oxidants catalase, glutathion and N-acetyl-cystein are able to reverse the toxic effects of 6-OHDA. These two latter compounds considerably slow down 6-OHDA oxidation in a cell free system suggesting a direct chemical interaction with the neurotoxin. Moreover, desipramine does not protect PC12 cells and 6-OHDA is also strongly toxic towards non-catecholaminergic C6 and NIH3T3 cells. These results thus suggest that 6-OHDA toxicity on PC12 cells mainly involves an extracellular process.</div>
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