Amyloidosis of the joints: evidence that human hip capsules have a unique predisposition for amyloid of the senile systemic type.
Amyloid-containing tissues were sampled from 19 capsules and 10 cartilages from hip, knee and sternoclavicular joints of 16 elderly patients. Heart ventricles from 3 of these patients were also studied. Histochemistry and immunofluorescence were performed and amyloid fibrils extracted from one hip capsule. The results indicate that 9 of 13 hip capsules contained prealbumin-like amyloid fibril protein ASc1, a finding characteristic of senile systemic amyloidosis. The amyloid of 16 out of 17 other joint structures showed no reaction with anti-ASc1 or antisera to 3 other systemic forms of amyloid, indicating that they represent localized forms of amyloid.
D000368:Aged; D000369:Aged, 80 and over; D000682:Amyloid / Q000032:analysis*; D002358:Cartilage, Articular / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D006621:Hip Joint / Q000032:analysis*; D006651:Histocytochemistry; D006801:Humans; D008854:Microscopy, Electron; D011228:Prealbumin / Q000032:analysis*
D000682:Amyloid; D011228:Prealbumin; C050627:senile amyloid fibril protein ASc(1); C041120:amyloid prealbumin