A close association of torsinA and alpha-synuclein in Lewy bodies: a fluorescence resonance energy transfer study

Am J Pathol. 2001 Jul;159(1):339-44. doi: 10.1016/s0002-9440(10)61700-2.


TorsinA, a novel protein in which a mutation causes dominant, early onset torsion dystonia, may serve as a chaperone for misfolded proteins that require refolding or degradation. It has been hypothesized that misfolded alpha-synuclein, a protein in which two mutations cause autosomal dominantly inherited Parkinson's disease, serves as a nidus for the development of a Lewy body. We hypothesized that torsinA plays a role in the cellular processing of alpha-synuclein. We demonstrate that anti-torsin antibodies stain Lewy bodies and Lewy neurites in the substantia nigra and cortex. Using sensitive fluorescent resonance energy transfer (FRET) techniques, we find evidence of a close association between torsinA and alpha-synuclein in Lewy bodies.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Carrier Proteins*
  • Energy Transfer
  • Hippocampus / metabolism*
  • Humans
  • Immunohistochemistry
  • Lewy Bodies / metabolism*
  • Lewy Body Disease / metabolism
  • Microscopy, Confocal
  • Molecular Chaperones*
  • Nerve Tissue Proteins / metabolism*
  • Reference Values
  • Spectrometry, Fluorescence
  • Substantia Nigra / metabolism*
  • Synucleins
  • alpha-Synuclein


  • Carrier Proteins
  • Molecular Chaperones
  • Nerve Tissue Proteins
  • SNCA protein, human
  • Synucleins
  • TOR1A protein, human
  • alpha-Synuclein