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The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of α‐synuclein aggregates
Author(s) -
Wakabayashi Koichi,
Tanji Kunikazu,
Mori Fumiaki,
Takahashi Hitoshi
Publication year - 2007
Publication title -
neuropathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.701
H-Index - 61
eISSN - 1440-1789
pISSN - 0919-6544
DOI - 10.1111/j.1440-1789.2007.00803.x
Subject(s) - locus ceruleus , alpha synuclein , substantia nigra , lewy body , fibril , parkinson's disease , synuclein , immunohistochemistry , pathology , degeneration (medical) , chemistry , biology , medicine , disease , biochemistry
The histological hallmark of Parkinson's disease (PD) is the presence of fibrillar aggregates called Lewy bodies (LBs). LB formation has been considered to be a marker for neuronal degeneration, because neuronal loss is found in the predilection sites for LBs. To date, more than 70 molecules have been identified in LBs, in which α‐synuclein is a major constituent of LB fibrils. α‐synuclein immunohistochemistry reveals that diffuse cytoplasmic staining develops into pale bodies via compaction, and that LBs arise from the peripheral portion of pale bodies. This α‐synuclein abnormality is found in 10% of pigmented neurons in the substantia nigra and more than 50% of those in the locus ceruleus in PD. Recent studies have suggested that oligomers and protofibrils of α‐synuclein are cytotoxic, and that LBs may represent a cytoprotective mechanism in PD.