ATP-promoted amyloidosis of an amyloid beta peptide.
Amyloidosis is implicated in the aetiology of a number of disorders of human health. The factors that influence its instigation and subsequent rate of progress are the subject of a considerable research effort. The peptide fragment A beta(25-35) is amyloidogenic and has proven to be a useful model of the processes involved in amyloidosis. It is demonstrated herein that the assembly of A beta(25-35) into thioflavin T-reactive fibrils and their subsequent rearrangement into advanced glycation endproducts is accelerated by ATP. Aluminium potentiated these effects of ATP, suggesting a possible link with the aetiology of amyloidoses in vivo.
Exley
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Birchall Centre for Inorganic Chemistry and Materials Science, Department of Chemistry, Keele University, Staffordshire, UK.
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000535:Aluminum / Q000633:toxicity; D016229:Amyloid beta-Peptides / Q000633:toxicity*; D000686:Amyloidosis / Q000139:chemically induced / Q000378:metabolism*; D052160:Benzothiazoles; D002478:Cells, Cultured; D005456:Fluorescent Dyes; D005947:Glucose / Q000378:metabolism; D006801:Humans; D009412:Nerve Fibers / Q000378:metabolism; D010446:Peptide Fragments / Q000633:toxicity*; D013844:Thiazoles
D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D010446:Peptide Fragments; D013844:Thiazoles; C074636:amyloid beta-protein (25-35); C009462:thioflavin T; D000255:Adenosine Triphosphate; D000535:Aluminum; D005947:Glucose