Regulatory mediators in Arthus reactions: lysosomal enzymes in biopsy and serum

  • K. M. Debatin
  • D. Gemsa
  • G. Till
Part of the Inflammation: Mechanisms and Treatment book series (FTIN, volume 4)


The accumulation of polymorphonuclear leukocytes (PMN) has been demonstrated as a central pathogenic event in inflammatory lesions like the Arthus reaction1. During the last decade, the possible role of these cells in acute inflammatory processes has been studied extensively in vitro. As a main focus of these investigations it has become clear that PMN, whenever they encounter immunological stimuli like immune complexes or C5a, release their granule constituents2, 3. The various hydrolytic enzymes stored within different granules take part in the cellular bactericidal systems as well as in the digestion of ingested material (bacteria, immune complexes). However, they have also been demonstrated to degrade a wide variety of tissue substrates in vitro (for review see reference 3). Therefore, the release of proteolytic activities could be an important contribution to the injury which occurs in the inflamed tissue in vivo.


Normal Skin Neutral Protease Regulatory Mediator Elastase Activity Human Polymorphonuclear Leukocyte 
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  1. 1.
    Cochrane, C. G. (1968). Immunologic tissue injury mediated by neutrophilic leukocytes. Adv. Immunol., 9, 97PubMedCrossRefGoogle Scholar
  2. 2.
    Weissmann, G., Smolen, J. E. and Hoffstein, S. (1978). Polymorphonuclear leukocytes as secretory organs of inflammation. J. Invest. Dermatol., 71, 95PubMedCrossRefGoogle Scholar
  3. 3.
    Goldstein, I. M. (1976). Polymorphonuclear leukocyte lysosomes and immune tissue injury. Prog. Allergy, 20, 301PubMedCrossRefGoogle Scholar
  4. 4.
    Janoff, A. and Zeligs, J. D. (1968). Vascular injury and lysis of basement membrane in vitro by neutral protease of human leukocytes. Science, 161, 702PubMedCrossRefGoogle Scholar
  5. 5.
    Taylor, J. C., Crawford, I. P. and Hugh, T. E. (1977). Limited degradation of the third component (C3) of human complement by human leukocyte elastase (HLE): Partial characterization of C3 fragments. Biochemistry, 16, 3390PubMedCrossRefGoogle Scholar
  6. 6.
    Brozna, J. P., Senior R.M., Kreutzer, D.L. and Ward, P. A. (1977). Chemotactic factor inactivators in human granulocytes. J. Clin. Invest, 60, 1280PubMedCrossRefGoogle Scholar
  7. 7.
    Schmidt, M.E., Douglas, S.D., Quie, P. et al. (1978). Effect of neutral granulocyte proteases on human immunocompetent cells: Action of elastase-like protease and chymotrypsin-like protease on mononuclear phagocytes. In Havemann, K. and Janoff, A. (eds.) Neutral proteases of human polymorphonuclear leukocytes, p. 298. (Baltimore-Munich: Urban and Schwarzenberg)Google Scholar
  8. 8.
    Vischer, T. L., Bretz, U. and Baggiolini, M. (1976). In vitro stimulation of lymphocytes by neutral proteinases from human polymorphonuclear leukocyte granules. J. Exp. Med., 144, 863PubMedCrossRefGoogle Scholar
  9. 9.
    Goetzl, E.J. and Austen, K.F. (1972). A neutrophil immobilizing factor derived from human leukocytes. I. Generation and partial characterization, J. Exp. Med., 136, 1564PubMedCrossRefGoogle Scholar
  10. 10.
    Till, G., Debatin, K. M. and Gemsa, D. (1980): Regulatory mediators in Arthus reactions: demonstration of chemotactic factor inactivator and cell directed inhibitor activity. This volume, Chap. 90Google Scholar
  11. 11.
    Wroblewski, F. and La Due, J. S. (1955). Lactic dehydrogenase activity in blood. Proc. Soc. Exp. Biol. Med., 90, 210PubMedGoogle Scholar
  12. 12.
    Gordon, S., Todd, J. and Cohn, Z. A. (1974). In vitro synthesis and secretion of lysozyme by mononuclear phagocytes. J. Exp. Med., 139, 1228PubMedCrossRefGoogle Scholar
  13. 13.
    Pütter, J. (1974). Peroxidasen. In Bergmeyer, H. U. (ed.) Methoden der enzymatischen Analyse, p. 725. (Weinheim: Verlag Chemie).Google Scholar
  14. 14.
    Fishman, W. H. (1974). β-glucuronidase. In Bergmeyer, H. U. (ed.) Methoden der enzymatischen Analyse, p. 964. (Weinheim: Verlag Chemie)Google Scholar
  15. 15.
    Bieth, J., Spiess, B. and Wermuth, C. G. (1974). The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biochem. Med., 11, 350PubMedCrossRefGoogle Scholar
  16. 16.
    Barrett, A. J. (1970). CathepsinD. Purification of isoenzymes from human and chicken liver. Biochem. J., 117, 601PubMedGoogle Scholar
  17. 17.
    Ohlsson, K. and Olsson, J. (1977). The extracellular release of granulocyte collagenase and elastase during phagocytosis and inflammatory process. Scand. J. Haematol, 19, 145PubMedCrossRefGoogle Scholar
  18. 18.
    Ohlsson, K. (1978). Interaction of granulocyte neutral proteases with alpha,-antitrypsin, alpha2-macroglobulin and alpha,-antichymotrypsin. In Havemann, K. and Janoff, A. eds. Neutral proteases of human polymorphonuclear leukocytes, p. 167. (Baltimore-Munich: Urban & Schwarzenberg)Google Scholar

Copyright information

© MTP Press Limited 1980

Authors and Affiliations

  • K. M. Debatin
    • 1
  • D. Gemsa
    • 1
  • G. Till
    • 1
  1. 1.West Germany

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