title: MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide and induces its fibrillization.
abstract: Increasing evidence supports the contribution of local inflammation to the development of Alzheimer's disease (AD) pathology, although the precise mechanisms are not clear. In this study, we demonstrate that the pro-inflammatory protein S100A9 interacts with the Aβ1-40 peptide and promotes the formation of fibrillar β-amyloid structures. This interaction also results in reduced S100A9 cytotoxicity by the binding of S100A9 toxic species to Aβ1-40 amyloid structures. These results suggest that secretion of S100A9 during inflammation promotes the formation of amyloid plaques. By acting as a sink for toxic species, plaque formation may be the result of a protective response within the brain of AD patients, in part mediated by S100A9.
authors.affiliation: Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden. phyzce@nus.edu.sg
authors.forename: Ce
authors.initials: C
authors.lastname: Zhang
authors.forename: Yonggang
authors.initials: Y
authors.lastname: Liu
authors.forename: Jonathan
authors.initials: J
authors.lastname: Gilthorpe
authors.forename: Johan R C
authors.initials: JR
authors.lastname: van der Maarel
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D040502:Calgranulin B / Q000737:chemistry / Q000378:metabolism*; D002460:Cell Line; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D024202:Electrophoretic Mobility Shift Assay; D006801:Humans; D007700:Kinetics; D018625:Microscopy, Atomic Force; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary
chemical_list: D016229:Amyloid beta-Peptides; D040502:Calgranulin B; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)