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

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.
Mesh Terms:
Carrier Proteins, Energy Transfer, Hippocampus, Humans, Immunohistochemistry, Lewy Bodies, Lewy Body Disease, Microscopy, Confocal, Molecular Chaperones, Nerve Tissue Proteins, Reference Values, Spectrometry, Fluorescence, Substantia Nigra, Synucleins, alpha-Synuclein
Am. J. Pathol.
Date: Jul. 01, 2001
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