Morphologic and chemical variation of the kidney lesions in amyloidosis secondary to rheumatoid arthritis.
The kidneys of 20 patients who died of secondary systemic amyloidosis due to rheumatoid arthritis were studied histologically, and four of these were shown to have an uncommon pattern of deposition with almost no glomerular involvement but heavy deposits in the outer zone of the medulla. In three of the four patients frozen tissue was available. Immunochemical characterization of amyloid fibrils from these three cases showed that the major subunit amyloid fibril protein was protein AA, typical of secondary amyloidosis. Gel chromatography of fibrils revealed an uncommon elution pattern with two retarded major protein peaks. Both these proteins showed immunologic identity with protein AA and had N-terminal amino acid sequences identical with that protein but differed in size obviously due to a shortening of the C-terminal in one of the proteins. The reason for the correlation between the pattern of deposition of amyloid and alterations in protein AA is unclear but might be due to variations in enzymes responsible for the cleavage of the amyloid fibril subunit precursor protein SAA.
D000595:Amino Acid Sequence; D000682:Amyloid / Q000032:analysis; D000686:Amyloidosis / Q000209:etiology / Q000473:pathology*; D001172:Arthritis, Rheumatoid / Q000150:complications*; D006801:Humans; D007668:Kidney / Q000473:pathology; D007674:Kidney Diseases / Q000209:etiology / Q000473:pathology*; D007679:Kidney Medulla / Q000473:pathology; D000685:Serum Amyloid A Protein / Q000032:analysis; D013154:Spleen / Q000473:pathology
D000682:Amyloid; D000685:Serum Amyloid A Protein