α-synuclein and the pathogenesis of Parkinson's disease

Francis L. Martin, Sally J M Williamson, Katerina E. Paleologou, David Allsop, Omar Ali El-Agnaf

Research output: Contribution to journalReview article

23 Citations (Scopus)

Abstract

Lesions known as Lewy bodies (LBs) and Lewy neurites (LNs) characterise brains of Parkinson's disease (PD) patients. Intracellular aggregation of α-synuclein (α-syn) appears to play a key role in the generation of LBs and LNs. Such aggregation in the presence of redox metals may initiate Fenton reaction-mediated generation of reactive oxygen species (ROS). ROS thus generated may result in cytotoxic mechanisms such as the induction of DNA single-strand breaks.

Original languageEnglish
Pages (from-to)229-237
Number of pages9
JournalProtein and Peptide Letters
Volume11
Issue number3
DOIs
Publication statusPublished - Jun 2004
Externally publishedYes

Fingerprint

Synucleins
Lewy Bodies
Neurites
Parkinson Disease
Reactive Oxygen Species
Agglomeration
Single-Stranded DNA Breaks
Brain Diseases
Oxidation-Reduction
Brain
Metals
DNA

Keywords

  • α-synuclein
  • Comet assay
  • Comet tail length
  • DNA single-strand breaks
  • Environmental causation
  • Fe(II)
  • Parkinson's disease
  • Reactive oxygen species

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

α-synuclein and the pathogenesis of Parkinson's disease. / Martin, Francis L.; Williamson, Sally J M; Paleologou, Katerina E.; Allsop, David; Ali El-Agnaf, Omar.

In: Protein and Peptide Letters, Vol. 11, No. 3, 06.2004, p. 229-237.

Research output: Contribution to journalReview article

Martin, FL, Williamson, SJM, Paleologou, KE, Allsop, D & Ali El-Agnaf, O 2004, 'α-synuclein and the pathogenesis of Parkinson's disease', Protein and Peptide Letters, vol. 11, no. 3, pp. 229-237. https://doi.org/10.2174/0929866043407138
Martin, Francis L. ; Williamson, Sally J M ; Paleologou, Katerina E. ; Allsop, David ; Ali El-Agnaf, Omar. / α-synuclein and the pathogenesis of Parkinson's disease. In: Protein and Peptide Letters. 2004 ; Vol. 11, No. 3. pp. 229-237.
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