title: A primed state exists in vivo following histological regression of amyloidosis.
abstract: Using a sensitive, quantitative, and non-invasive in vivo method, based on the specific binding of serum amyloid P component to amyloid fibrils, we have directly documented the spontaneous resolution of AA amyloid deposits in mice, and the prolonged existence thereafter of a primed state of enhanced susceptibility to further amyloid deposition. These results may have important implications for understanding and management of amyloidosis in humans.
authors.affiliation: Department of Medicine, Royal Postgraduate Medical School, London, England, UK.
authors.forename: P N
authors.initials: PN
authors.lastname: Hawkins
authors.forename: M B
authors.initials: MB
authors.lastname: Pepys
mesh_terms: D000682:Amyloid / Q000378:metabolism; D000686:Amyloidosis / Q000276:immunology / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D000936:Antigen-Antibody Complex / Q000276:immunology; D005260:Female; D006023:Glycoproteins; D006801:Humans; D007457:Iodine Radioisotopes; D008099:Liver / Q000378:metabolism; D051379:Mice; D008808:Mice, Inbred CBA; D012075:Remission, Spontaneous; D000683:Serum Amyloid P-Component / Q000378:metabolism / Q000493:pharmacokinetics; D013154:Spleen / Q000378:metabolism
chemical_list: D000682:Amyloid; D000936:Antigen-Antibody Complex; D006023:Glycoproteins; D007457:Iodine Radioisotopes; D000683:Serum Amyloid P-Component; C046748:amyloid enhancing factor