A primed state exists in vivo following histological regression of amyloidosis

Clin Exp Immunol. 1990 Aug;81(2):325-8. doi: 10.1111/j.1365-2249.1990.tb03339.x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / metabolism
  • Amyloidosis / immunology
  • Amyloidosis / metabolism*
  • Amyloidosis / pathology
  • Animals
  • Antigen-Antibody Complex / immunology
  • Female
  • Glycoproteins
  • Humans
  • Iodine Radioisotopes
  • Liver / metabolism
  • Mice
  • Mice, Inbred CBA
  • Remission, Spontaneous
  • Serum Amyloid P-Component / metabolism
  • Serum Amyloid P-Component / pharmacokinetics
  • Spleen / metabolism

Substances

  • Amyloid
  • Antigen-Antibody Complex
  • Glycoproteins
  • Iodine Radioisotopes
  • Serum Amyloid P-Component
  • amyloid enhancing factor