Preparation and characterization of neurotoxic tau oligomers.
Tau aggregation is a pathological hallmark of Alzheimer's disease, Parkinson's disease, and many other neurodegenerative disorders known as tauopathies. Tau aggregates take on many forms, and their formation is a multistage process with intermediate stages. Recently, tau oligomers have emerged as the pathogenic species in tauopathies and a possible mediator of amyloid-β toxicity in Alzheimer's disease. Here, we use a novel, physiologically relevant method (oligomer cross-seeding) to prepare homogeneous populations of tau oligomers and characterize these oligomers in vitro. We show that both Aβ and α-synuclein oligomers induce tau aggregation and the formation of β-sheet-rich neurotoxic tau oligomers.
The George P. and Cynthia Woods Mitchell Center for Neurodegenerative Diseases, Department of Neurology, University of Texas Medical Branch, Galveston, Texas 77555-1045, United States.
Cristian A
CA
Lasagna-Reeves
Diana L
DL
Castillo-Carranza
Marcos J
MJ
Guerrero-Muoz
George R
GR
Jackson
Rakez
R
Kayed
D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000494:pharmacology; D045744:Cell Line, Tumor; D006801:Humans; D019636:Neurodegenerative Diseases / Q000188:drug therapy; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D051844:alpha-Synuclein / Q000494:pharmacology; D016875:tau Proteins / Q000737:chemistry / Q000633:toxicity
D016229:Amyloid beta-Peptides; D051844:alpha-Synuclein; D016875:tau Proteins