Studies with radiolabelled serum amyloid P component provide evidence for turnover and regression of amyloid deposits in vivo.
1. Quantitative scintigraphic and turnover studies, utilizing the specific binding affinity of serum amyloid P component for amyloid fibrils, have been developed as a tool for evaluating amyloid deposits in vivo. 2. Serial studies in over 300 patients have shown characteristic, diagnostic tissue distributions of amyloid in different types of amyloidosis. There is generally a poor correlation between quantity of amyloid and associated organ dysfunction. 3. Contrary to previous expectations, regression of amyloid has been demonstrated systematically for the first time: AA, AL and variant transthyretin-associated amyloid deposits often regress rapidly, and sometimes completely, if the supply of fibril protein precursors is substantially reduced.
Hawkins
P N
PN
Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London, U.K.
D000682:Amyloid / Q000378:metabolism*; D000686:Amyloidosis / Q000000981:diagnostic imaging / Q000378:metabolism*; D000818:Animals; D006801:Humans; D007457:Iodine Radioisotopes; D011877:Radionuclide Imaging; D000683:Serum Amyloid P-Component / Q000493:pharmacokinetics*
D000682:Amyloid; D007457:Iodine Radioisotopes; D000683:Serum Amyloid P-Component