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Am J Pathol. 2001 Jul;159(1):339-44.

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

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  • 1Department of Neurology, Alzheimer's Disease Research Unit, and the Department of Neurology, Molecular Neurogenetics Unit, Massachusetts General Hospital East, Charlestown, Massachusetts. Albert Einstein College of Medicine, Bronx, New York.


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.

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