title: Structural analyses of fibrinogen amyloid fibrils.
abstract: Hereditary fibrinogen amyloidosis is characterized by deposition of amyloid fibrils in renal glomeruli. The subunit protein of the amyloid fibrils is a proteolytic fragment of the fibrinogen Aalpha-chain. To investigate the structure of fibrinogen amyloid, fibrils were extracted from the tissues of a patient and studied by X-ray fiber diffraction and electron microscopy. We have carried out a full structural characterization of amyloid fibrils taken from disease tissue. These studies revealed that ex vivo fibrinogen amyloid fibrils have a cross-beta structure similar to other chemical types of amyloid fibrils.
authors: Biochemistry, University of Sussex, John Maynard-Smith Building, Falmer, Brighton, UK. L.C.Serpell@sussex.ac.uk
authors: Louise C
authors: LC
authors: Serpell
authors: Merrill
authors: M
authors: Benson
authors: Juris J
authors: JJ
authors: Liepnieks
authors: Paul E
authors: PE
authors: Fraser
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000648:ultrastructure*; D000686:Amyloidosis / Q000473:pathology; D005340:Fibrinogen / Q000737:chemistry / Q000648:ultrastructure*; D006801:Humans; D017433:Protein Structure, Secondary; D013154:Spleen / Q000737:chemistry / Q000473:pathology; D014961:X-Ray Diffraction
chemical_list: D000682:Amyloid; C464794:fibrinogen Aalpha; D005340:Fibrinogen