Targeting α-synuclein aggregation and its role in mitochondrial dysfunction in Parkinson's disease

Br J Pharmacol. 2022 Jan;179(1):23-45. doi: 10.1111/bph.15684. Epub 2021 Nov 24.

Abstract

Lewy bodies that contain aggregated α-synuclein in dopamine neurons are the main culprit for neurodegeneration in Parkinson's disease. However, mitochondrial dysfunction has a well-established and prominent role in the pathogenesis of Parkinson's disease. The exact mechanism by which α-synuclein causes dopamine neuronal loss is unclear. Recent evidence suggests that aggregated α-synuclein localises in the mitochondria contributes to oxidative stress-mediated apoptosis in neurons. Therefore, the involvement of aggregated α-synuclein in mitochondrial dysfunction-mediated neuronal loss has made it an emerging drug target for the treatment of Parkinson's disease. However, the exact mechanism by which α-synuclein permeabilises through the mitochondrial membrane and affects the electron transport chain remains under investigation. In the present study, we describe mitochondria-α-synuclein interactions and how α-synuclein aggregation modulates mitochondrial homeostasis in Parkinson's disease pathogenesis. We also discuss recent therapeutic interventions targeting α-synuclein aggregation that may help researchers to design novel therapeutic treatments for Parkinson's disease.

Keywords: Parkinson's disease; immunotherapy; mitochondria; neurodegeneration; α-synuclein; α-synuclein aggregation inhibitors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Apoptosis
  • Dopaminergic Neurons* / metabolism
  • Dopaminergic Neurons* / pathology
  • Humans
  • Lewy Bodies / metabolism
  • Lewy Bodies / pathology
  • Mitochondria* / metabolism
  • Mitochondria* / pathology
  • Mitochondrial Diseases / metabolism
  • Mitochondrial Diseases / pathology
  • Oxidative Stress
  • Parkinson Disease* / drug therapy
  • Parkinson Disease* / metabolism
  • Protein Aggregation, Pathological* / metabolism
  • Protein Aggregation, Pathological* / pathology
  • alpha-Synuclein* / metabolism

Substances

  • alpha-Synuclein