Degradation in vivo of articular cartilage in rheumatoid arthritis and juvenile chronic arthritis by cathepsin G and elastase from polymorphonuclear leukocytes
- 1 January 1987
- journal article
- research article
- Published by Springer Nature in Rheumatology International
- Vol. 7 (5) , 195-202
- https://doi.org/10.1007/bf00541377
Abstract
Summary Peroxidase-anti-peroxidase (PAP) staining and specific antibodies against cathepsin G and elastase from polymorphonuclear leukocytes (PMN) were applied to pannus-free and microscopically intact superficial articular cartilage. Restricted local deposits containing cathepsin G and elastase were found in three of ten patients with seropositive rheumatoid arthritis (RA), in one of three patients with seronegative RA and in one patient with juvenile chronic arthritis (JCA). Similarly, localized deposits of IgG and C3 were found in the patients with seropositive RA and JCA, but not in the patient with seronegative RA. Adjacent sections exhibited esterase activity in and around the PMN. In proteinase-positive areas from patients with seropositive RA the inhibitors α1-proteinase inhibitor (α1-PI) and α2-macroglobulin (α2-MG) were present in two of three and one of three patients, respectively. In JCA only α1-proteinase inhibitor was present, and in seronegative RA no inhibitors were found. No staining of articular cartilage was observed in a patient with psoriatic arthritis. One of three cases with osteoarthritis exhibited patchy superficial staining for IgG only. In articular cartilage covered by pannus, in three patients with seropositive RA, in one with seronegative RA and in the patient with JCA a few regions with variably dense PMN infiltrates were observed. Cathepsin G, elastase and esterase activity were found in and around the PMN. In one of the three patients with seropositive RA the adjacent cartilage-pannus junction exhibited distinct staining for cathepsin G and elastase, but not for IgG/C3 and proteinase inhibitors. The findings suggest that cathepsin G and elastase from PMN are involved in the breakdown of rheumatoid articular cartilage in the presence, as well as in the absence, of entrapped immune-complex-like material, and that proteinase inhibitors are often lacking in such regions.Keywords
This publication has 46 references indexed in Scilit:
- Induction of neutrophil enzyme release by rheumatoid factors: Evidence for differences based on molecular characteristicsClinical Immunology and Immunopathology, 1986
- Synovial protease/inhibitor ratios in erosive and nonerosive arthropathies.Annals of the Rheumatic Diseases, 1984
- Cytokine modulation of chondrocyte proteinase releaseArthritis & Rheumatism, 1984
- Cathepsin G from human polymorphonuclear leukocytes cleaves human IgMMolecular Immunology, 1982
- Isolation and properties of oxidized alpha-1-proteinase inhibitor from human rheumatoid synovial fluidBiochemical and Biophysical Research Communications, 1980
- Absence of immunoglobulins in rheumatoid cartilage‐pannus junctionsArthritis & Rheumatism, 1980
- Mechanism of Inhibition of Porcine Elastase by Human Alpha-1-AntitrypsinJournal of Clinical Investigation, 1978
- Electron Microscopy and Synovial PathologyAustralian and New Zealand Journal of Medicine, 1978
- Electron microscopic morphology of immunoglobulin aggregates and their interactions in rheumatoid articular collagenous tissuesArthritis & Rheumatism, 1978
- The possible role of neutrophil proteinases in damage to articular cartilageInflammation Research, 1978