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Neutral protease secretion by human monocytes. Effect of surface-bound immune complexes
The Journal of Experimental Medicine
|April 1, 1979
Summary
Surface-bound immune complexes stimulate human monocytes to secrete plasminogen-independent fibrinolytic proteases, like elastase, while inhibiting plasminogen activator release. This protease secretion may contribute to tissue injury in immune complex diseases.
Area of Science:
- Immunology
- Biochemistry
- Cell Biology
Background:
- Human peripheral monocytes play a role in immune responses.
- Neutral proteases secreted by monocytes can degrade extracellular matrix.
- Immune complexes are implicated in various inflammatory diseases.
Purpose of the Study:
- To investigate the effect of surface-bound immune complexes on neutral protease secretion by human monocytes.
- To characterize the types of proteases secreted and their activity.
- To understand the role of these proteases in potential tissue injury.
Main Methods:
- Monocytes were cultured on 125I-fibrin with and without surface-bound immune complexes.
- Fibrinolytic activity was measured, distinguishing between plasminogen-dependent and independent pathways.
- Protease inhibitors were used to characterize the secreted enzymes.
- Deiodination activity was assessed.
Main Results:
- Monocytes cultured on immune complexes showed a burst of plasminogen-independent fibrinolytic activity.
- This activity was primarily due to leukocyte elastase secreted by monocytes.
- Plasminogen activator secretion was inhibited under these conditions.
- Deiodinating enzymes were also secreted.
Conclusions:
- Surface-bound immune complexes induce monocytes to secrete plasminogen-independent proteases, predominantly elastase, and deiodinating enzymes.
- This secretion occurs with concurrent inhibition of plasminogen activator release.
- These monocyte-derived proteases may contribute to tissue damage in diseases with immune complexes.