title: Normal transthyretin and synthetic transthyretin fragments form amyloid-like fibrils in vitro.
abstract: In two general forms of amyloidosis, senile systemic amyloidosis and several familial amyloidoses the amyloid fibrils are built up by transthyretin and fragments of the molecule. It has previously been demonstrated that other amyloid fibril proteins e.g. atrial natriuretic factor and islet amyloid polypeptide form amyloid-like fibrils in vitro. In this study we used normal transthyretin and synthetic polypeptides corresponding to segments of the transthyretin molecule. We show that normal transthyretin and two of our tested polypeptides, which corresponded to the beta-strands A and G, easily form amyloid-like fibrils in vitro.
authors.affiliation: Department of Pathology I, University of Linköping, Sweden.
authors.forename: A
authors.initials: A
authors.lastname: Gustavsson
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 / Q000473:pathology; D006801:Humans; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D011228:Prealbumin / Q000648:ultrastructure*
chemical_list: D009842:Oligopeptides; D010446:Peptide Fragments; D011228:Prealbumin