Systemic activation of Nrf2 pathway in Parkinson's disease

Mov Disord. 2020 Jan;35(1):180-184. doi: 10.1002/mds.27878. Epub 2019 Nov 4.

Abstract

Background: Preclinical studies underlined the relevance of Nuclear factor erythroid 2-related factor 2 (Nrf2) transcription factor pathway in the pathogenesis of Parkinson's disease (PD).

Objective: The objective of this study was to explore Nrf2 pathway in vivo in PD, looking for novel disease biomarkers and therapeutic targets.

Methods: The levels of Nrf2, the downstream effectors (NAD(P)H dehydrogenase [quinone] 1 (Nqo1) enzyme, glutathione metabolism enzymes Glutamate-cysteine ligase (GCL) and Glutathione Reductase (GR)), the upstream activators (redox state and mitochondrial dysfunction), and α-synuclein oligomers were assessed in the blood leukocytes of PD patients comparatively to controls. Biochemical data were correlated to clinical parameters.

Results: In PD, Nrf2 was highly transcribed and expressed as well as its target effectors. The mitochondrial complex I activity was reduced and the oxidized form of glutathione prevailed, disclosing the presence of pathway's activators. Also, α-synuclein oligomers levels were increased. Nrf2 transcript and oligomers levels correlated with PD duration.

Conclusions: Blood leukocytes mirror pathogenic mechanisms of PD, showing the systemic activation of the Nrf2 pathway and its link with synucleinopathy and clinical events. © 2019 International Parkinson and Movement Disorder Society.

Keywords: Nrf2; Parkinson's disease; biomarkers; oxidative stress; synuclein.

MeSH terms

  • Adult
  • Aged
  • Animals
  • Glutathione / metabolism
  • Humans
  • Male
  • Middle Aged
  • NF-E2-Related Factor 2 / metabolism*
  • Oxidative Stress / physiology
  • Parkinson Disease / metabolism*
  • Parkinson Disease / physiopathology
  • Parkinsonian Disorders / metabolism*
  • Reactive Oxygen Species / metabolism
  • Signal Transduction / physiology*
  • alpha-Synuclein / metabolism

Substances

  • NF-E2-Related Factor 2
  • NFE2L2 protein, human
  • Reactive Oxygen Species
  • alpha-Synuclein
  • Glutathione