Alpha-Synuclein Toxicity on Protein Quality Control, Mitochondria and Endoplasmic Reticulum

Thaiany Quevedo Melo, Sjef J. C. V. M. Copray, Merari F. R. Ferrari*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

11 Citations (Scopus)

Abstract

Parkinson's disease (PD) is characterized by the presence of insoluble protein clusters containing -synuclein. Impairment of mitochondria, endoplasmic reticulum, autophagy and intracellular trafficking proper function has been suggested to be caused by -synuclein toxicity, which is also associated with the higher levels of ROS found in the aged brain and in PD. Oxidative stress leads to protein oligomerization and aggregation that impair autophagy and mitochondrial dynamics leading to a vicious cycle of organelles damage and neurodegeneration. In this review we focused on the role of -synuclein dysfunction as a cellular stressor that impairs mitochondria, endoplasmic reticulum, autophagy and cellular dynamics culminating with dopaminergic depletion and the pathogenesis of PD.

Original languageEnglish
Pages (from-to)2212-2223
Number of pages12
JournalNEUROCHEMICAL RESEARCH
Volume43
Issue number12
DOIs
Publication statusPublished - Dec-2018

Keywords

  • Aging
  • Parkinson's disease
  • Oxidative stress
  • PARKINSONS-DISEASE
  • DOPAMINE NEURONS
  • OXIDATIVE STRESS
  • DNA DELETIONS
  • A53T MUTANT
  • CELL-DEATH
  • IN-VITRO
  • TRANSPORT
  • DYNAMICS
  • CALCIUM

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