A close association of torsinA and α-synuclein in lewy bodies: A fluorescence resonance energy transfer study

Nutan Sharma, Jeffrey Hewett, Laurie J. Ozelius, Vijaya Ramesh, Pamela J. McLean, Xandra O. Breakefield, Bradley T. Hyman

Research output: Contribution to journalArticle

92 Scopus citations

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 α-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 α-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 α-synuclein in Lewy bodies.

Original languageEnglish (US)
Pages (from-to)339-344
Number of pages6
JournalAmerican Journal of Pathology
Volume159
Issue number1
DOIs
StatePublished - Jul 2001

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

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