Accumulation of human alpha-synuclein in different cytoskeletons in Lewy bodies in brains of dementia with Lewy bodies.
We investigated the origin of alpha-synuclein-immunoreactive components in Lewy bodies (LB) in brains of dementia with Lewy bodies (DLB) using immunohistochemistry and immunoelectron microscopy with anti-alpha-synuclein antibodies and anti-cytoskeleton antibodies. alpha-Synuclein-positive LB light microscopically consisted of phosphorylated neurofilament (PN)-positive LB, tubulin-positive LB and LB that were negative for both stains. Immunoelectron microscopically, PN-positive LB were composed of PN-positive and alpha-synuclein-positive filamentous components, suggesting that these filamentous components originate from neurofilaments with partially reduced immunoreactivity and alpha-synuclein accumulation. However, tubulin-positive LB were composed of tubulin-positive and alpha-synuclein-positive tubular components, suggesting that these tubular components originate from microtubules with diffusely reduced immunoreactivity and alpha-synuclein accumulation. The results of the present study suggest that alpha-synuclein accumulates in different cytoskeletons in the LB in DLB brains presumably due to a blockage of axonal transport.
Iseki
E
E
Department of Psychiatry, Yokohama City University School of Medicine, 3-9 Fukuura, Kanazawa-ku, 236-0004, Yokohama, Japan.
Marui
W
W
Sawada
H
H
Uéda
K
K
Kosaka
K
K
D000368:Aged; D001923:Brain Chemistry; D002540:Cerebral Cortex / Q000378:metabolism* / Q000473:pathology; D003599:Cytoskeleton / Q000378:metabolism* / Q000473:pathology; D003704:Dementia / Q000378:metabolism* / Q000473:pathology*; D006801:Humans; D007150:Immunohistochemistry; D016631:Lewy Bodies / Q000378:metabolism / Q000473:pathology*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D051843:Synucleins; D051844:alpha-Synuclein
D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; C497604:SNCA protein, human; D051843:Synucleins; D051844:alpha-Synuclein