Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease.
The precursor of non-amyloid beta protein component of Alzheimer's disease amyloid (NACP/alpha-synuclein) is aggregated and fibrillated under certain conditions, i.e., increasing time lag, high temperature and low pH. These in vitro aggregates form Thioflavine-S-positive filamentous structures, reminiscent of amyloid-like fibrils. Since some Lewy bodies in Parkinson's disease display Thioflavine-S reactivity, our results may suggest that amyloidogenic properties of NACP/alpha-synuclein may play a crucial role in pathogenesis of disorders with Lewy bodies such as Parkinson's disease.
Hashimoto
M
M
Department of Neurosciences, School of Medicine, University of California-San Diego, La Jolla, CA 92093-0624, USA.
Hsu
L J
LJ
Sisk
A
A
Xia
Y
Y
Takeda
A
A
Sundsmo
M
M
Masliah
E
E
D052160:Benzothiazoles; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009419:Nerve Tissue Proteins / Q000502:physiology* / Q000648:ultrastructure; D009994:Osmolar Concentration; D010300:Parkinson Disease / Q000209:etiology; D011994:Recombinant Proteins; D051843:Synucleins; D013696:Temperature; D013844:Thiazoles / Q000378:metabolism; D013997:Time Factors
D052160:Benzothiazoles; D009419:Nerve Tissue Proteins; D011994:Recombinant Proteins; D051843:Synucleins; D013844:Thiazoles; C009462:thioflavin T