title: The N-terminal segment of protein AA determines its fibrillogenic property.
abstract: The amyloid fibril protein AA consists of a varying long N-terminal part of the precursor protein serum AA. By using synthetic peptides corresponding to human and murine protein AA segments and cyanogen bromide fragments of human protein AA, we show evidence that the amyloidogenic part of the molecule is the first 10-15 amino acid long segment. Amino acid substitutions in this part of the molecule may explain why only one of the two mouse SAA isoforms is amyloidogenic.
authors.affiliation: Department of Pathology, University of Linköping, Sweden.
authors.forename: G T
authors.initials: GT
authors.lastname: Westermark
authors.forename: U
authors.initials: U
authors.lastname: Engström
authors.forename: P
authors.initials: P
authors.lastname: Westermark
mesh_terms: D000595:Amino Acid Sequence; D000686:Amyloidosis / Q000378:metabolism / Q000473:pathology; D000818:Animals; D006801:Humans; D007668:Kidney / Q000378:metabolism / Q000473:pathology; D051379:Mice; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis; D000685:Serum Amyloid A Protein / Q000235:genetics / Q000502:physiology / Q000648:ultrastructure*
chemical_list: D009842:Oligopeptides; D000685:Serum Amyloid A Protein