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 Citations (Scopus)

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
StatePublished - Jul 2001
Externally publishedYes

Fingerprint

Synucleins
Lewy Bodies
Fluorescence Resonance Energy Transfer
Protein Refolding
Mutation
Energy Transfer
Neurites
Substantia Nigra
Proteolysis
Parkinson Disease
Anti-Idiotypic Antibodies
Proteins
Coloring Agents

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

Sharma, N., Hewett, J., Ozelius, L. J., Ramesh, V., McLean, P. J., Breakefield, X. O., & Hyman, B. T. (2001). A close association of torsinA and α-synuclein in lewy bodies: A fluorescence resonance energy transfer study. American Journal of Pathology, 159(1), 339-344.

A close association of torsinA and α-synuclein in lewy bodies : A fluorescence resonance energy transfer study. / Sharma, Nutan; Hewett, Jeffrey; Ozelius, Laurie J.; Ramesh, Vijaya; McLean, Pamela J; Breakefield, Xandra O.; Hyman, Bradley T.

In: American Journal of Pathology, Vol. 159, No. 1, 07.2001, p. 339-344.

Research output: Contribution to journalArticle

Sharma, N, Hewett, J, Ozelius, LJ, Ramesh, V, McLean, PJ, Breakefield, XO & Hyman, BT 2001, 'A close association of torsinA and α-synuclein in lewy bodies: A fluorescence resonance energy transfer study', American Journal of Pathology, vol. 159, no. 1, pp. 339-344.
Sharma, Nutan ; Hewett, Jeffrey ; Ozelius, Laurie J. ; Ramesh, Vijaya ; McLean, Pamela J ; Breakefield, Xandra O. ; Hyman, Bradley T. / A close association of torsinA and α-synuclein in lewy bodies : A fluorescence resonance energy transfer study. In: American Journal of Pathology. 2001 ; Vol. 159, No. 1. pp. 339-344.
@article{e3341c674bce429fbe699ffc4148d0ca,
title = "A close association of torsinA and α-synuclein in lewy bodies: A fluorescence resonance energy transfer study",
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.",
author = "Nutan Sharma and Jeffrey Hewett and Ozelius, {Laurie J.} and Vijaya Ramesh and McLean, {Pamela J} and Breakefield, {Xandra O.} and Hyman, {Bradley T.}",
year = "2001",
month = "7",
language = "English (US)",
volume = "159",
pages = "339--344",
journal = "American Journal of Pathology",
issn = "0002-9440",
publisher = "Elsevier Inc.",
number = "1",

}

TY - JOUR

T1 - A close association of torsinA and α-synuclein in lewy bodies

T2 - A fluorescence resonance energy transfer study

AU - Sharma, Nutan

AU - Hewett, Jeffrey

AU - Ozelius, Laurie J.

AU - Ramesh, Vijaya

AU - McLean, Pamela J

AU - Breakefield, Xandra O.

AU - Hyman, Bradley T.

PY - 2001/7

Y1 - 2001/7

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0035404388&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035404388&partnerID=8YFLogxK

M3 - Article

C2 - 11438481

AN - SCOPUS:0035404388

VL - 159

SP - 339

EP - 344

JO - American Journal of Pathology

JF - American Journal of Pathology

SN - 0002-9440

IS - 1

ER -