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Transformation of Amyloid Precursor SAA to Protein AA and Incorporation in Amyloid Fibrils in Vivo
Author(s) -
HUSEBEKK A.,
SKOGEN B.,
HUSBY G.,
MARHAUG G.
Publication year - 1985
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1985.tb01431.x
Subject(s) - serum amyloid a , amyloidosis , radial immunodiffusion , amyloid (mycology) , in vivo , chemistry , serum amyloid a protein , serum amyloid p component , acute phase protein , fibril , immunodiffusion , amyloid fibril , endocrinology , medicine , biochemistry , biology , immunology , amyloid β , antibody , inflammation , c reactive protein , inorganic chemistry , microbiology and biotechnology , disease
Experimental amyloidosis was induced in mice by in t raped toneal injections of endotoxin (lipopolysaccharidc (LPS)). In addition to LPS. a group of mice received high‐density lipoprotein (HDL)‐SAA complexes isolated from human acute‐phase serum, whereas a group of control mice received saline in addition to LPS. Isolated amyloid fibrils from the mice given HDL‐SAA contained human AA protein, as shown by immunodiffusion, immunoblot. and enzyme‐linked Immunosorbent assay techniques, in addition to mouse AA. In contrast, amyloid from the control mice contained exclusively AA of mouse origin. Thus, the experiments provided solid evidence that SAA is the precursor for amyloid fibril proiein AA.