Activation of Progelatinase B by Membranes of Human Polymorphonuclear Granulocytes
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Hansjörg Kolkenbrock
Abstract
Isolated human granulocyte plasma membranes contain progelatinase B. The binding of progelatinase B to the membrane, however, is relatively weak, and a considerable part of progelatinase B can be removed by simply washing the membrane with buffer. This detachment does not depend on the ionic strength of the buffer, indicating that electrostatic forces do not play an important role in the binding of progelatinase B to the membrane. A complete removal of progelatinase B is achieved by chromatography of neutrophil membranes on gelatin-agarose.
The plasma membrane of human granulocytes activates added progelatinase B. This activation is inhibited by soybean trypsin inhibitor and is thus performed by membrane bound serine proteinases. In contrast to other reports that claimed an important role of elastase in activating progelatinase B, we found that this activation is mostly inhibited by chymostatin and not by elastatinal and is thus primarily due to cathepsin G. Proteinase 3 was shown to activate progelatinase B as efficient as neutrophil elastase, i. e. much weaker than cathepsin G. Binding of cathepsin G and elastase to the neutrophil membrane does not change their ability to activate progelatinase B. However, cathepsin G , the most potent activator of the three neutrophil serine proteinases, is only a weak activator, when compared to stromelysin-1. This, as well as only a weak binding of progelatinase B, make it doubtful that activation of membrane-bound progelatinase B by membrane-bound serine proteinases is of significant physiological importance.
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
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- Structural Analysis of Modified Forms of Recombinant IFN-β Produced under Stress-Simulating Conditions
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- Neoglycolipids Derived from Phosphatidylethanolamine Serve as Probes in Cell Culture Studies on Glycolipid Metabolism
- Anomalous Binding of MgADP to Myosin of Skeletal Muscle
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- Bait Region Cleavage and Complex Formation of Human α2M with a Porphyromonas gingivalisW50 Protease Is Not Accompanied by Enzyme Inhibition
- Adjuvant and Haemolytic Activities of 47 Saponins Derived from Medicinal and Food Plants
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