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- Title
Immunocytochemical localization of synphilin-1, an α-synuclein-associated protein, in neurodegenerative disorders.
- Authors
Wakabayashi, Koichi; Engelender, Simone; Tanaka, Yuji; Yoshimoto, Makoto; Mori, Fumiaki; Tsuji, Shoji; Ross, Christopher A.; Takahashi, Hitoshi
- Abstract
α-Synuclein is a major component of Lewy bodies (LB) in Parkinson's disease (PD) and dementia with LB (DLB), as well as of glial cytoplasmic inclusions (GCI) in multiple system atrophy (MSA). Recently, a novel protein called synphilin-1 has been identified that associates with α-synuclein, and it has been reported that co-transfection of both α-synuclein and synphilin-1 in mammalian cells yielded eosinophilic cytoplasmic inclusions resembling LB. Immunocytochemical and ultrastructural investigations have now been performed on the brain of patients with various neurodegenerative disorders using anti-synphilin-1 antibodies. These antibodies immunostained the neuropil in a punctate pattern throughout the brain of control subjects. In PD, most LB observed in the brain stem were positive for synphilin-1. These LB showed intense staining in their central cores, but their peripheral portions were only weakly stained or unstained. Pale bodies and Lewy neurites, which were positive for α-synuclein, were synphilin-1 negative. In DLB, a small fraction of cortical LB were immunolabeled by anti-synphilin-1. In MSA, numerous GCI were positive for synphilin-1. Immunoelectron microscopy revealed that the reaction product was localized within filamentous and circular structures in LB. Various neuronal and glial inclusions in neurodegenerative disorders other than LB disease and MSA were synphilin-1 negative. These findings suggest that abnormal accumulation of synphilin-1 is specific for brain lesions in which α-synuclein is a major component.
- Subjects
IMMUNOCYTOCHEMISTRY; CYTOCHEMISTRY; PROTEINS; BIOMOLECULES; NEURODEGENERATION; PARKINSON'S disease; BRAIN stem
- Publication
Acta Neuropathologica, 2002, Vol 103, Issue 3, p209
- ISSN
0001-6322
- Publication type
Article
- DOI
10.1007/s004010100451