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α2M-Proteinase Complexes are Taken up by Macrophages During Joint Inflammation

  • T. L. Vischer
  • E. Flory
  • K. Muirden
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 155)

Abstract

During inflammation, proteinases are released by inflammatory and tissue cells. The activation of the complement, the coagulation and the fibrinolytic systems produces additional proteinases. Active proteinases become inactivated by various inhibitors in the circulation and tissues. Among the plasma proteinase inhibitors, alpha1 -antiproteinase and α2-macroglobulin (α2M) are most abundant (1). The α2M-proteinase complexes are removed from the circulation by fixed tissue macrophages in the liver and spleen and broken down (2,3). In the experiments summarized in this paper, we have looked for the presence of α2M-proteinase complexes in phagocytic cells of synovial tissues and exudates from patients with joint diseases. In parallel, we established that only α2M-proteinase complexes and not free α2M or proteinases are taken up by phagocytic cells.

Keywords

Synovial Tissue Phagocytic Cell Joint Inflammation Cytoplasmic Inclusion Fibrinolytic System 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Heimburger, N., in “Proteases and Biological Control” (E. Reich, D. B. Rifkin, E. Shaw, eds.), PP. 367-386, Cold Spring Harbor Laboratory, Cold Spring Harbor, 1975.Google Scholar
  2. 2.
    Ohlsson, K., Acta Physiol. Scand. 81:269, 1971.PubMedCrossRefGoogle Scholar
  3. 3.
    Ohlsson, K., and Laurell, C. B., Clin. Sci. Mol. Med. 51:87, 1976.PubMedGoogle Scholar
  4. 4.
    Dolovich, J., Debanne, M. T., and Bell, R., Am. Rev. Resp. Dis. 112:521, 1975.PubMedGoogle Scholar
  5. 5.
    Debanne, M. T., Bell, R., and Dolovich, J., Biochim. Biophys. Acta 411:295, 1975.PubMedCrossRefGoogle Scholar
  6. 6.
    Debanne, M. T., Bell, R., and Dolovich, J., Biochim. Biophys. Acta 428:466, 1976.PubMedCrossRefGoogle Scholar
  7. 7.
    Flory, E., and Vischer, T. L., Rheumatol. Int. 1:61, 1981.PubMedCrossRefGoogle Scholar
  8. 8.
    Fraser, J. R. E., and Catt, K. S., Lancet 30:1437, 1961.CrossRefGoogle Scholar
  9. 9.
    Clarris, B. J., Fraser, J. R. E., Moran, C. J., and Muirden, K. D., Ann. Rheum. Dis. 36:293, 1977.PubMedCrossRefGoogle Scholar
  10. 10.
    Flory, E. D., Clarris, B. J., and Muirden, K. D., Ann. Rheum. Dis., 1982, in press.Google Scholar
  11. 11.
    Vischer, T. L., and Berger, D., J. Reticuloendothelial Soc. 28:427, 1980.Google Scholar
  12. 12.
    Hubbard, W. J., Hess, A. D., Hsia, S., and Arnos, D. B., J. Immunol. 126:292, 1981.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • T. L. Vischer
    • 1
    • 2
  • E. Flory
    • 1
    • 2
  • K. Muirden
    • 1
    • 2
  1. 1.Division of RheumatologyHôpital Cantonal UniversitaireGenevaSwitzerland
  2. 2.Department of MedicineUniversity of MelbourneAustralia

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