Reactive (secondary) amyloidosis and its pathogenesis.
Recent advances in amyloid research have broadened our understanding of amyloidogenesis in connection with chronic inflammatory and infectious conditions. Experimental and clinical studies have clarified many of the mechanisms of induction, synthesis and regulation of the amyloid-related serum component SAA and have shed light on the enzymatic processes involved in the cleavage of SAA and degradation of fibrillar AA protein. The current pathogenetic model emphasizes the dynamic character of amyloid disease.
D000682:Amyloid / Q000378:metabolism*; D000686:Amyloidosis / Q000209:etiology* / Q000276:immunology / Q000378:metabolism; D000818:Animals; D001171:Arthritis, Juvenile / Q000150:complications; D001172:Arthritis, Rheumatoid / Q000150:complications; D001402:B-Lymphocytes / Q000276:immunology; D006801:Humans; D010447:Peptide Hydrolases / Q000378:metabolism; D010586:Phagocytes / Q000276:immunology; D000685:Serum Amyloid A Protein / Q000096:biosynthesis / Q000378:metabolism*; D013601:T-Lymphocytes / Q000276:immunology; D000515:alpha 1-Antitrypsin / Q000378:metabolism; D000511:alpha-Macroglobulins / Q000378:metabolism
D000682:Amyloid; D000685:Serum Amyloid A Protein; D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins; D010447:Peptide Hydrolases