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.

• Authors: P N Hawkins
• Journal: Clinical science (London, England : 1979) (Clin Sci (Lond)) Vol. 87 Issue 3 Pg. 289-95 (Sep 1994) ISSN: 0143-5221 [Print] England
• PMID: 7955904 (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 (diagnostic imaging, metabolism)
• Animals
• Humans
• Iodine Radioisotopes
• Radionuclide Imaging
• Serum Amyloid P-Component (pharmacokinetics)