title: Amyloidosis.
abstract: Recent studies have provided new insight into the pathogenesis of amyloidosis and have broadened our knowledge of the mechanisms of deposition and resolution of amyloid. In particular, the structure, synthesis and plasma clearance of the inflammation-associated amyloid precursor, SAA, have been extensively studied and the precursor-product relationship between circulating SAA, protein AA and fibrillar amyloid A clarified. Information has been accumulating about the enzymatic processes involved in the cleavage of SAA and the degradation of protein AA and a new view has been presented on the possible role of amyloid P component in AA amyloidogenesis. The current model of AA pathogenesis emphasizes the dynamic character of amyloid.
authors.affiliation: Fourth Department of Medicine, University of Helsinki, Finland.
authors.forename: C P
authors.initials: CP
authors.lastname: Maury
mesh_terms: D000686:Amyloidosis / Q000503:physiopathology*; D005819:Genetic Markers; D006684:HLA-DR Antigens / Q000276:immunology; D006801:Humans; D008954:Models, Biological; D011110:Polymorphism, Genetic; D012217:Rheumatoid Factor / Q000276:immunology; D000685:Serum Amyloid A Protein / Q000502:physiology*; D000683:Serum Amyloid P-Component / Q000502:physiology
chemical_list: D005819:Genetic Markers; D006684:HLA-DR Antigens; D000685:Serum Amyloid A Protein; D000683:Serum Amyloid P-Component; D012217:Rheumatoid Factor