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Cross‐seeding effects of amyloid β‐protein and α‐synuclein
Author(s) -
Ono Kenjiro,
Takahashi Ryoichi,
Ikeda Tokuhei,
Yamada Masahito
Publication year - 2012
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2012.07847.x
Subject(s) - fibril , thioflavin , protein aggregation , amyloid (mycology) , chemistry , in vitro , biophysics , in vivo , pathogenesis , microbiology and biotechnology , biochemistry , biology , alzheimer's disease , pathology , disease , medicine , immunology , genetics , inorganic chemistry
J. Neurochem . (2012) 122 , 883–890. Abstract Amyloid β‐protein (Aβ) and α‐synuclein (αS) are the primary components of amyloid plaques and Lewy bodies (LBs), respectively. Previous in vitro and in vivo studies have suggested that interactions between Aβ and αS are involved in the pathogenesis of Alzheimer’s disease and LB diseases. However, the seeding effects of their aggregates on their aggregation pathways are not completely clear. To investigate the cross‐seeding effects of Aβ and αS, we examined how sonicated fibrils or cross‐linked oligomers of Aβ40, Aβ42, and αS affected their aggregation pathways using thioflavin T(S) assay and electron microscopy. Fibrils and oligomers of Aβ40, Aβ42, and αS acted as seeds, and affected the aggregation pathways within and among species. The seeding effects of αS fibrils were higher than those of Aβ40 and Aβ42 fibrils in the Aβ40 and Aβ42 aggregation pathways, respectively. We showed that Aβ and αS acted as seeds and affected each other’s aggregation pathways in vitro , which may contribute to our understanding of the molecular mechanisms of interactions between Alzheimer’s disease and LB diseases pathologies.