title: [Alpha-Synuclein in blood and cerebrospinal fluid of patients with alpha-synucleinopathy].
abstract: Alpha-Synuclein protein(alphaS) aggregates from a monomer to assemblies such as oligomers, protofibrils, and mature fibrils. The early intermediate aggregate, that is, the oligomer, has been reported to be the most toxic species. We recently reported that melatonin inhibits alphaS aggregation, including protofibril and oligomer formations. While the alphaS concentration in cerebrospinal fluid was reported to significantly decrease in patients with Parkinson's disease (PD) and dementia with Lewy bodies, there have been reports that the alphaS oligomer concentration was elevated in the cerebrospinal fluid of PD patients. Moreover, it was reported that the alphaS oligomer concentration was also elevated in the blood of PD patients. Further studies may establish alphaS in cerebrospinal fluid and blood as a biomarker of alpha-synucleinopathies, including PD.
authors.forename: Kenjiro
authors.initials: K
authors.lastname: Ono
authors.forename: Masahito
authors.initials: M
authors.lastname: Yamada
mesh_terms: D000818:Animals; D004722:Endoribonucleases / Q000378:metabolism; D006801:Humans; D007473:Ion Channels / Q000378:metabolism; D016631:Lewy Bodies / Q000378:metabolism; D020961:Lewy Body Disease / Q000097:blood* / Q000134:cerebrospinal fluid*; D010300:Parkinson Disease / Q000097:blood* / Q000134:cerebrospinal fluid* / Q000503:physiopathology; D051844:alpha-Synuclein / Q000097:blood* / Q000134:cerebrospinal fluid*
chemical_list: D007473:Ion Channels; D051844:alpha-Synuclein; D004722:Endoribonucleases; C051012:splicing endonuclease