ParkinsonFranceV1, Ncbi, Checkpoint, bibRecord, 001632

New Roles of Glycosaminoglycans in α-Synuclein Aggregation in a Cellular Model of Parkinson Disease

Identifieur interne : 001632 ( Ncbi/Checkpoint ); précédent : 001631; suivant : 001633

New Roles of Glycosaminoglycans in α-Synuclein Aggregation in a Cellular Model of Parkinson Disease

Auteurs : Sonia Lehri-Boufala [France] ; Mohand-Ouidir Ouidja [France] ; Véronique Barbier-Chassefière [France] ; Emilie Hénault [France] ; Rita Raisman-Vozari [France] ; Laure Garrigue-Antar [France] ; Dulce Papy-Garcia [France] ; Christophe Morin [France]

Source :

PLoS ONE [ 1932-6203 ] ; 2015.

RBID : PMC:4305359

English descriptors

KwdEn :
- 1-Methyl-4-phenylpyridinium (pharmacology), Amino Acid Sequence, Apoptosis (drug effects), Cathepsin D (metabolism), Cell Line, Tumor, Glycosaminoglycans (biosynthesis), Glycosaminoglycans (metabolism), Humans, Intracellular Space (drug effects), Intracellular Space (metabolism), Parkinson Disease (metabolism), Parkinson Disease (pathology), Protein Aggregates (drug effects), Protein Transport (drug effects), Proteolysis (drug effects), alpha-Synuclein (chemistry), alpha-Synuclein (metabolism).
MESH :
- chemical , biosynthesis : Glycosaminoglycans.
- chemical , chemistry : alpha-Synuclein.
- chemical , drug effects : Protein Aggregates.
- chemical , metabolism : Cathepsin D, Glycosaminoglycans, alpha-Synuclein.
- chemical , pharmacology : 1-Methyl-4-phenylpyridinium.
- drug effects : Apoptosis, Intracellular Space, Protein Transport, Proteolysis.
- metabolism : Intracellular Space, Parkinson Disease.
- pathology : Parkinson Disease.
- Amino Acid Sequence, Cell Line, Tumor, Humans.

Abstract

The causes of Parkinson disease (PD) remain mysterious, although some evidence supports mitochondrial dysfunctions and α-synuclein accumulation in Lewy bodies as major events. The abnormal accumulation of α-synuclein has been associated with a deficiency in the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Cathepsin D (cathD), the major lysosomal protease responsible of α-synuclein degradation was described to be up-regulated in PD model. As glycosaminoglycans (GAGs) regulate cathD activity, and have been recently suggested to participate in PD physiopathology, we investigated their role in α-synuclein accumulation by their intracellular regulation of cathD activity. In a classical neuroblastoma cell model of PD induced by MPP⁺, the genetic expression of GAGs-biosynthetic enzymes was modified, leading to an increase of GAGs amounts whereas intracellular level of α-synuclein increased. The absence of sulfated GAGs increased intracellular cathD activity and limited α-synuclein accumulation. GAGs effects on cathD further suggested that specific sequences or sulfation patterns could be responsible for this regulation. The present study identifies, for the first time, GAGs as new regulators of the lysosome degradation pathway, regulating cathD activity and affecting two main biological processes, α-synuclein aggregation and apoptosis. Finally, this opens new insights into intracellular GAGs functions and new fields of investigation for glycobiological approaches in PD and neurobiology.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4305359

DOI: 10.1371/journal.pone.0116641
PubMed: 25617759
PubMed Central: 4305359

Affiliations:

Links to Exploration step

PMC:4305359

Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>The causes of Parkinson disease (PD) remain mysterious, although some evidence supports mitochondrial dysfunctions and α-synuclein accumulation in Lewy bodies as major events. The abnormal accumulation of α-synuclein has been associated with a deficiency in the ubiquitin-proteasome system and the autophagy-lysosomal pathway. Cathepsin D (cathD), the major lysosomal protease responsible of α-synuclein degradation was described to be up-regulated in PD model. As glycosaminoglycans (GAGs) regulate cathD activity, and have been recently suggested to participate in PD physiopathology, we investigated their role in α-synuclein accumulation by their intracellular regulation of cathD activity. In a classical neuroblastoma cell model of PD induced by MPP<sup>+</sup>
, the genetic expression of GAGs-biosynthetic enzymes was modified, leading to an increase of GAGs amounts whereas intracellular level of α-synuclein increased. The absence of sulfated GAGs increased intracellular cathD activity and limited α-synuclein accumulation. GAGs effects on cathD further suggested that specific sequences or sulfation patterns could be responsible for this regulation. The present study identifies, for the first time, GAGs as new regulators of the lysosome degradation pathway, regulating cathD activity and affecting two main biological processes, α-synuclein aggregation and apoptosis. Finally, this opens new insights into intracellular GAGs functions and new fields of investigation for glycobiological approaches in PD and neurobiology.</p>
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La maladie de Parkinson en France (serveur d'exploration)

New Roles of Glycosaminoglycans in α-Synuclein Aggregation in a Cellular Model of Parkinson Disease

New Roles of Glycosaminoglycans in α-Synuclein Aggregation in a Cellular Model of Parkinson Disease

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