title: Widespread occurrence of argyrophilic glial inclusions in Parkinson's disease.
abstract: Argyrophilic glial inclusions, which are immunohistochemically positive for alpha-synuclein but negative for tau protein, were examined in the brain of Parkinson's disease (PD) patients. Autopsied brains of 10 individuals who died from PD, of two incidental Lewy body disease cases and of five age-matched individuals whose deaths were caused by non-neurological diseases were studied, histopathologically, by Gallyas-Braak staining and, immunohistochemically, with anti-alpha-synuclein antibody, anti-ubiquitin, and anti-tyrosine hydroxylase. All postmortem PD brains showed a significant number of argyrophilic glial inclusions, but no glial inclusions were found in control brains. The inclusions were found not only in the regions showing neuronal loss and gliosis, such as the substantia nigra, locus ceruleus and dorsal vagal nucleus, but also in regions without neuronal loss and gliosis, such as the cerebral cortex, cerebral white matter, striatum, globus pallidus, thalamus, cerebellum and spinal cord. The distribution and density of glial inclusions in PD brains varied from case to case but, in the cerebral cortex, the number of glial inclusions were fairly well correlated with the number of Lewy bodies. The distribution pattern of glial inclusions also showed a striking resemblance to that of catecholaminergic neurones and fibres. The abnormal accumulation of alpha-synuclein in glial cells was more widespread than neurone loss, and appears to be an important pathological feature of PD.
authors.affiliation: Department of Neurology, Nagoya University School of Medicine, Showa-ku, Nagoya, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Hishikawa
authors.forename: Y
authors.initials: Y
authors.lastname: Hashizume
authors.forename: M
authors.initials: M
authors.lastname: Yoshida
authors.forename: G
authors.initials: G
authors.lastname: Sobue
mesh_terms: D000368:Aged; D000369:Aged, 80 and over; D002490:Central Nervous System / Q000473:pathology; D005260:Female; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry / Q000473:pathology* / Q000648:ultrastructure; D016631:Lewy Bodies / Q000737:chemistry / Q000473:pathology / Q000648:ultrastructure; D020961:Lewy Body Disease / Q000473:pathology; D008297:Male; D016253:Microscopy, Immunoelectron; D008875:Middle Aged; D009419:Nerve Tissue Proteins / Q000032:analysis; D016501:Neurites / Q000737:chemistry / Q000201:enzymology / Q000473:pathology; D009457:Neuroglia / Q000473:pathology* / Q000648:ultrastructure; D009474:Neurons / Q000201:enzymology / Q000473:pathology / Q000648:ultrastructure; D010300:Parkinson Disease / Q000473:pathology*; D016622:Silver Staining; D051843:Synucleins; D014446:Tyrosine 3-Monooxygenase / Q000032:analysis; D025801:Ubiquitin / Q000032:analysis; D051844:alpha-Synuclein
chemical_list: D009419:Nerve Tissue Proteins; C497604:SNCA protein, human; D051843:Synucleins; D025801:Ubiquitin; D051844:alpha-Synuclein; D014446:Tyrosine 3-Monooxygenase