Amyloidosis of the joints: evidence that human hip capsules have a unique predisposition for amyloid of the senile systemic type.

Abstract

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.

• Authors: Y A Goffin, E L McCrickard, J P Ameryckx, C L Malmendier, M Hiden, G G Cornwell 3rd
• Journal: Applied pathology (Appl Pathol) Vol. 3 Issue 1-2 Pg. 88-95 ( 1985) ISSN: 0252-1172 [Print] Switzerland
• PMID: 3915948 (Publication Type: Journal Article)

Chemical References

• Amyloid
• Prealbumin
• senile amyloid fibril protein ASc(1)
• amyloid prealbumin

Topics

• Aged
• Aged, 80 and over
• Amyloid (analysis)
• Cartilage, Articular (analysis)
• Electrophoresis, Polyacrylamide Gel
• Fluorescent Antibody Technique
• Hip Joint (analysis)
• Histocytochemistry
• Humans
• Microscopy, Electron
• Prealbumin (analysis)