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α-Synuclein in Lewy bodies

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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.

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Figure 1: Substantia nigra from patients with Parkinson's disease (from the MRC Cambridge Brain Bank) immunostained for α-synuclein.
Figure 2: Tissue from patients with DLB (from the tissue collection of the Department of Pathology and Laboratory Medicine, University of Pennsylvania) immunostained for α-synuclein.

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Authors and Affiliations

  1. Medical Research Council Centre for Brain Repair and Department of Neurology, University of Cambridge, Robinson Way, CB2 2PY, Cambridge, UK

    Maria Grazia Spillantini

  2. Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, 19104-4283, Pennsylvania, USA

    Marie Luise Schmidt, Virginia M.-Y. Lee & John Q. Trojanowski

  3. Medical Research Council Laboratory of Molecular Biology, Hills Road, CB2 2QH, Cambridge, UK

    Ross Jakes & Michel Goedert

Authors
  1. Maria Grazia Spillantini
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  2. Marie Luise Schmidt
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  3. Virginia M.-Y. Lee
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  4. John Q. Trojanowski
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  5. Ross Jakes
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  6. Michel Goedert
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Spillantini, M., Schmidt, M., Lee, VY. et al. α-Synuclein in Lewy bodies. Nature 388, 839–840 (1997). https://doi.org/10.1038/42166

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