Evidence of native α-synuclein conformers in the human brain.
α-Synuclein aggregation is central to the pathogenesis of several brain disorders. However, the native conformations and functions of this protein in the human brain are not precisely known. The native state of α-synuclein was probed by gel filtration coupled with native gradient gel separation, an array of antibodies with non-overlapping epitopes, and mass spectrometry. The existence of metastable conformers and stable monomer was revealed in the human brain.
From the Departments of Pediatrics and Pharmacology, The Children's Hospital of Philadelphia Research Institute and.
Neal
N
Gould
Danielle E
DE
Mor
Richard
R
Lightfoot
Kristen
K
Malkus
Benoit
B
Giasson
Harry
H
Ischiropoulos
D001921:Brain / Q000378:metabolism*; D002850:Chromatography, Gel; D018604:Epitope Mapping; D000939:Epitopes / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D013058:Mass Spectrometry; D019636:Neurodegenerative Diseases / Q000378:metabolism; D010300:Parkinson Disease / Q000378:metabolism; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013395:Sucrose / Q000737:chemistry; D014461:Ultracentrifugation; D051844:alpha-Synuclein / Q000737:chemistry*
D000939:Epitopes; D051844:alpha-Synuclein; D013395:Sucrose
Alpha-Synuclein; Human Brain; Native State; Neurodegenerative Diseases; Parkinson Disease; Protein Conformation; Protein Folding