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Annals of the Rheumatic Diseases logoLink to Annals of the Rheumatic Diseases
. 1984 Feb;43(1):50–55. doi: 10.1136/ard.43.1.50

Synovial protease/inhibitor ratios in erosive and nonerosive arthropathies.

M H Pritchard
PMCID: PMC1001219  PMID: 6364998

Abstract

Although rheumatoid joint fluids contain numerous polymorphs capable of secreting neutral proteases known to be able to digest cartilage, the high level of inhibitors (mainly alpha 1-antitrypsin and alpha 2-macroglobulin) has always been considered to be more than sufficient to inhibit their activity completely. Consequently little interest has been paid to the potential role of these enzymes in cartilage damage. Four arthropathies of different erosive potential are here compared: spondyloarthropathies, rheumatoid arthritis with and without gold or D-penicillamine therapy, and septic arthritis. The synovial concentration of the inhibitors alpha 1-antitrypsin and alpha 2-macroglobulin has been compared with the polymorph enzyme output, as measured by beta-glucuronidase. Total haemolytic complement, white cell count, and C-reactive protein have also been measured in the joint fluid. The range of white cell count and inhibitors was the same in all 4 groups, while the enzyme output varied substantially from low levels in the spondyloarthropathies to very high levels in the septic joints. The higher the erosive potential of the disease, therefore, the more disadvantageous is the inhibitor/enzyme ratio. It is also pointed out that cartilage has physiochemical properties which facilitate and enhance polymorph enzyme output while severely curtailing the activity of the inhibitors. The observation that synovial fluid is inhibitory in vitro may therefore bear little relationship to the situation at the cartilage surface in vivo.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cooke T. D., Hurd E. R., Jasin H. E., Bienenstock J., Ziff M. Identification of immunoglobulins and complement in rheumatoid articular collagenous tissues. Arthritis Rheum. 1975 Nov-Dec;18(6):541–551. doi: 10.1002/art.1780180603. [DOI] [PubMed] [Google Scholar]
  2. Dingle J. T. Articular damage in arthritis and its control. Ann Intern Med. 1978 Jun;88(6):821–826. doi: 10.7326/0003-4819-88-6-821. [DOI] [PubMed] [Google Scholar]
  3. Dingle J. T. Heberden oration 1978. Recent studies on the control of joint damage: the contribution of the Strangeways Research Laboratory. Ann Rheum Dis. 1979 Jun;38(3):201–214. doi: 10.1136/ard.38.3.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fishman W. H., Kato K., Anstiss C. L., Green S. Human serum beta-glucuronidase; its measurement and some of its properties. Clin Chim Acta. 1967 Mar;15(3):435–447. doi: 10.1016/0009-8981(67)90008-3. [DOI] [PubMed] [Google Scholar]
  5. Hadler N. M., Johnson A. M., Spitznagel J. K., Quinet R. J. Protease inhibitors in inflammatory synovial effusions. Ann Rheum Dis. 1981 Feb;40(1):55–59. doi: 10.1136/ard.40.1.55. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Henson P. M. Interaction of cells with immune complexes: adherence, release of constituents, and tissue injury. J Exp Med. 1971 Sep 1;134(3 Pt 2):114s–135s. [PubMed] [Google Scholar]
  7. James H. L., Cohen A. B. Mechanism of inhibition of porcine elastase by human alpha-1-antitrypsin. J Clin Invest. 1978 Dec;62(6):1344–1353. doi: 10.1172/JCI109255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Laurell C. B. Electroimmuno assay. Scand J Clin Lab Invest Suppl. 1972;124:21–37. doi: 10.3109/00365517209102748. [DOI] [PubMed] [Google Scholar]
  9. Ohlsson K., Laurell C. B. The disappearance of enzyme-inhibitor complexes from the circulation of man. Clin Sci Mol Med. 1976 Jul;51(1):87–92. doi: 10.1042/cs0510087. [DOI] [PubMed] [Google Scholar]
  10. Oronsky A., Ignarro L., Perper R. Release of cartilage mucopolysaccharide-degrading neutral protease from human leukocytes. J Exp Med. 1973 Aug 1;138(2):461–472. doi: 10.1084/jem.138.2.461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pritchard M. H., Nuki G. Gold and penicillamine: a proposed mode of action in rheumatoid arthritis, based on synovial fluid analysis. Ann Rheum Dis. 1978 Dec;37(6):493–503. doi: 10.1136/ard.37.6.493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Ugai K., Ziff M., Jasin H. E. Interaction of polymorphonuclear leukocytes with immune complexes trapped in joint collagenous tissues. Arthritis Rheum. 1979 Apr;22(4):353–364. doi: 10.1002/art.1780220407. [DOI] [PubMed] [Google Scholar]
  13. Zvaifler N. J. The immunopathology of joint inflammation in rheumatoid arthritis. Adv Immunol. 1973;16(0):265–336. doi: 10.1016/s0065-2776(08)60299-0. [DOI] [PubMed] [Google Scholar]

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