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α-Synuclein in Lewy bodies

Author

Listed:
  • Maria Grazia Spillantini

    (University of Cambridge)

  • Marie Luise Schmidt

    (University of Pennsylvania School of Medicine)

  • Virginia M.-Y. Lee

    (University of Pennsylvania School of Medicine)

  • John Q. Trojanowski

    (University of Pennsylvania School of Medicine)

  • Ross Jakes

    (Medical Research Council Laboratory of Molecular Biology)

  • Michel Goedert

    (Medical Research Council Laboratory of Molecular Biology)

Abstract

Lewy bodies, a defining pathological characteristic of Parkinson's disease and dementia with Lewy bodies (DLB)1,2,3,4, constitute the second most common nerve cell pathology, after the neurofibrillary lesions of Alzheimer's disease. Their formation may cause neurodegeneration, but their biochemical composition is unknown. Neurofilaments and ubiquitin are present5,6,7,8, but it is unclear whether they are major components of the filamentous material of the Lewy body9,10. Here we describe strong staining of Lewy bodies from idiopathic Parkinson's disease with antibodies for α-synuclein, a presynaptic protein of unknown function which is mutated in some familial cases of the disease11. α-Synuclein may be the main component of the Lewy body in Parkinson's disease. We also show staining for α-synuclein of Lewy bodies from DLB, indicating that the Lewy bodies from these two diseases may have identical compositions.

Suggested Citation

  • Maria Grazia Spillantini & Marie Luise Schmidt & Virginia M.-Y. Lee & John Q. Trojanowski & Ross Jakes & Michel Goedert, 1997. "α-Synuclein in Lewy bodies," Nature, Nature, vol. 388(6645), pages 839-840, August.
    • Handle: RePEc:nat:nature:v:388:y:1997:i:6645:d:10.1038_42166
    DOI: 10.1038/42166
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    Cited by:

    1. Shoshana Shendelman & Alan Jonason & Cecile Martinat & Thomas Leete & Asa Abeliovich, 2004. "DJ-1 Is a Redox-Dependent Molecular Chaperone That Inhibits α-Synuclein Aggregate Formation," PLOS Biology, Public Library of Science, vol. 2(11), pages 1-1, October.

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