The BioGRID | PUBLICATION VIEW

	Am. J. Pathol. Jul (2001); 159(1):339-44
A close association of torsinA and alpha-synuclein in Lewy bodies: a fluorescence resonance energy transfer study.
Sharma N, Hewett J, Ozelius LJ, Ramesh V, McLean PJ, Breakefield XO, Hyman BT
Department 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.
Abstract: 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.
[PUBMED: 11438481]