NDLI: Proteasome inhibitor-induced autophagy in PC12 cells overexpressing A53T mutant α-synuclein

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Proteasome inhibitor-induced autophagy in PC12 cells overexpressing A53T mutant α-synuclein

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Proteasome inhibitor-induced autophagy in PC12 cells overexpressing A53T mutant α-synuclein

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lan, Danmei Wang, Wenzhao Zhuang, Jianhua Zhao, Zhongxin
Description	Author Affiliation: Lan D ( Department of Neurology, Shanghai Changzheng Hospital, Second Military Medical University, Shanghai 200003, P.R. China.); Wang W ( Department of Neurology, Shanghai Changzheng Hospital, Second Military Medical University, Shanghai 200003, P.R. China.); Zhuang J ( Department of Neurology, Shanghai Changzheng Hospital, Second Military Medical University, Shanghai 200003, P.R. China.); Zhao Z ( Department of Neurology, Shanghai Changzheng Hospital, Second Military Medical University, Shanghai 200003, P.R. China.)
Abstract	The aim of the present study was to examine the effects of proteasome inhibitor (PI)induced autophagy on PC12 cells overexpressing A53T mutant synuclein ( syn) by detecting alterations in the levels of microtubuleassociated protein 1A/1B light chain (LC3)+ autophagosomes and the lysotrackerpositive autolysosomes using immunofluorescence, the expression of LC3II using western blot analysis and the morphology of PC12 cells using transmission electron microscopy. It was found that the addition of MG132 (500 nmol/l) significantly increased the number of autophagosomes and autolysosomes and upregulated the expression of LC3II. The autophagy inhibitor 3methyladenine (3MA) completely inhibited the autophagy induced by MG132 (500 nmol/l). The autophagy enhancer trehalose significantly increased the number of autophagosomes and autolysosomes and improved the protein level of LC3II induced by MG132. To examine the effect of PIinduced autophagy on the degradation of A53T mutant syn, the expression of syn was detected by western blot analysis. It was revealed that MG132 increased the expression of A53T syn and trehalose counteracted the increase of A53T syn induced by MG132. Combined inhibition of 3MA and PI significantly increased the accumulation of A53T syn as compared with treatment using either single agent. In addition, combination of MG132 (500 nmol/l) with trehalose (50 mmol/l) or 3MA (2 mmol/l) markedly decreased the cell viability as compared with treatment using either single agent individually as demonstrated using a 3(4,5dimethylthiazol2yl)2,5diphenyltetrazolium bromide assay. These results suggest that the PI, MG132, could induce autophagy in PC12 cells overexpressing A53T mutant syn and this autophagy could be completely inhibited by 3MA, indicating that PIinduced autophagy is mediated by the upregulation of the macroautophagy class III PI3K pathway. PIinduced autophagy may act as a compensatory degradation system for degradation of A53T syn when the ubiquitinproteasome system is impaired. Autophagy activation may directly contribute to the survival of PC12 cells treated with proteasome inhibitors. The present study may assist in illuminating the association between PI and autophagy in the pathogenesis of Parkinson's disease.
ISSN	17912997
e-ISSN	17913004
DOI	10.3892/mmr.2014.3011
Journal	Molecular Medicine Reports
Issue Number	3
Volume Number	11
Language	English
Publisher	Spandidos Publications
Publisher Date	2015-03-01
Publisher Place	Greece
Access Restriction	Open
Subject Keyword	Autophagy Drug Effects Genetics Gene Expression Mutation Proteasome Inhibitors Pharmacology Alpha-synuclein Adenine Analogs & Derivatives Animals Cell Death Leupeptins Pc12 Cells Tor Serine-threonine Kinases Metabolism Research Support, Non-u.s. Gov't Discipline Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Genetics Biochemistry Molecular Biology Cancer Research Molecular Medicine Oncology

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