title: Plasmin cleaves Abeta42 in vitro and prevents its aggregation into beta-pleated sheet structures.
abstract: The formation, aggregation and deposition of amyloid beta peptide (Abeta) is implicated in the aetiology of Alzheimer's disease. Impairment of proteolytic degradation of Abeta may be a key factor in the progression of the disease. We have used RP-HPLC and thioflavin T fluorescence to demonstrate that Abeta42 is rapidly cleaved by the protease plasmin and that cleavage prevented the aggregation of Abeta42, and its cleavage products, into beta-pleated sheet structures. Plasmin may fulfil a similar role in vivo.
authors.affiliation: Birchall Centre for Inorganic Chemistry and Materials Science, School of Chemistry and Physics, Keele University, Staffordshire, ST5 5BG, UK.
authors.forename: C
authors.initials: C
authors.lastname: Exley
authors.forename: O V
authors.initials: OV
authors.lastname: Korchazhkina
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000503:physiopathology; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D052160:Benzothiazoles; D001921:Brain / Q000378:metabolism* / Q000503:physiopathology; D002851:Chromatography, High Pressure Liquid; D004347:Drug Interactions / Q000502:physiology; D005341:Fibrinolysin / Q000378:metabolism*; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*; D017433:Protein Structure, Secondary / Q000187:drug effects / Q000502:physiology; D013844:Thiazoles
chemical_list: D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D010446:Peptide Fragments; D013844:Thiazoles; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42); C009462:thioflavin T; D005341:Fibrinolysin