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Studies with radiolabelled serum amyloid P component provide evidence for turnover and regression of amyloid deposits in vivo.

Abstract
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.
AuthorsP N Hawkins
JournalClinical science (London, England : 1979) (Clin Sci (Lond)) Vol. 87 Issue 3 Pg. 289-95 (Sep 1994) ISSN: 0143-5221 [Print] ENGLAND
PMID7955904 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
Chemical References
  • Amyloid
  • Iodine Radioisotopes
  • Serum Amyloid P-Component
Topics
  • Amyloid (metabolism)
  • Amyloidosis (metabolism, radionuclide imaging)
  • Animals
  • Humans
  • Iodine Radioisotopes
  • Serum Amyloid P-Component (pharmacokinetics)

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