Abstract
At sites of inflammation, proteases are released by inflammatory and tissue cells. The activation of the complement, the coagulation and the fibrinolytic systems produce additional proteases. Active proteases become inactivated by various inhibitors in the circulation and in tissues. Among the plasma protease inhibitors, alpha1-antitrypsin and alpha2-macroglobulin (α2M) are quantitatively the most important ones. In the circulation, proteases bound to alpharantitrypsin are transferred to α2M1. The α2M-protease complexes are then taken up by the fixed tissue macrophages in liver and spleen1,2. In the experiments summarized in this paper, we have studied the effect of α2M-trypsin complexes on macrophages in vitro.
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References
Ohlsson, K. and Laurell, C. B. (1976). The disappearance of enzyme-inhibitor complexes from the circulation of man. Clin. Sci. Mol. Med., 51, 87
Ohlsson, K. (1971). Elimination of 25I-Trypsin-α2-Macroglobulin complexes from blood by reticuloendothelial cells in dog. Acta Physiol. Scand., 81, 269
Dolovich, J., Debanne, M. T. and Bell, R. (1975). The role of α1-antitrypsin and α2-macro-globulin in the uptake of proteinase by rabbit alveolar macrophages. Am. Rev. Resp. Dis., 112, 521
Debanne, M. T., Bell, R. and Dolovich, J. (1975). Uptake of proteinase-α2-macroglobulin complexes by macrophages. Biochim. Biophys. Acta, 411, 295
Debanne, M. T., Bell, R. and Dolovich, J. (1976). Characteristics of the macrophage uptake of proteinase-a2-macroglobulin complexes. Biochim. Biophys. Acta, 428, 466
Gordon, S., Unkeless, J. C. and Cohn, Z. A. (1974). Induction of macrophage plasminogen activator by endotoxin stimulation and phagocytosis. J. Exp. Med., 140, 995
Gordon, S., Newman, W. and Bloom, B. (1978). Macrophage proteases and rheumatic diseases: Regulation of plasminogen activator by thymus-derived lymphocytes. Agents A ctions, 8, 19
Vischer, T. L. and Bertrand, L. (1976). Stimulating effect of neutral proteases on cells in vitro. Agents Actions, 6, 180
Shtacher, G., Maayan, R. and Feinstein, G. (1973). Proteinase inhibitors in human synovial fluid. Biochim. Biophys. Acta, 303, 138
Abe, S. and Nagai, Y. (1973). Evidence for the presence of a complex of collagenase with α2-macroglobulin in human rheumatoid synovial fluid: A possible regulatory mechanism of collagenase activity in vivo. J. Biochem., 73, 897
Ohlsson, K. and Skude, C. (1976). Demonstration and semiquantitative determination of complexes between various proteases and human α2-macroglobulin. Clin. Chim. Acta, 66, 1
Vischer, T. L. and Berger, D. (1980). Activation of macrophages to produce neutral proteinases by endocytosis of α2M-trysin complexes. J. Reticuloendothel. Soc., 28, 427
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© 1980 MTP Press Limited
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Vischer, T.L., Berger, D., Flory, E.D. (1980). Macrophages are activated by endocytosis of α2-macroglobulin-protease complexes to produce neutral proteases. In: Willoughby, D.A., Giroud, J.P. (eds) Inflammation: Mechanisms and Treatment. Inflammation: Mechanisms and Treatment, vol 4. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-9423-8_123
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DOI: https://doi.org/10.1007/978-94-010-9423-8_123
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-9425-2
Online ISBN: 978-94-010-9423-8
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