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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Campbell, E. J. Sannes, P. L. Owen, C. A. Campbell, M. A. Boukedes, S. S. |
| Description | Author Affiliation: Owen CA ( Department of Medicine, University of Utah Health Sciences Center, Salt Lake City 84132, USA.) |
| Abstract | Serine proteinases of human polymorphonuclear neutrophils play an important role in neutrophil-mediated proteolytic events; however, the non-oxidative mechanisms by which the cells can degrade extracellular matrix in the presence of proteinase inhibitors have not been elucidated. Herein, we provide the first report that human neutrophils express persistently active cell surface-bound human leukocyte elastase and cathepsin G on their cell surface. Unstimulated neutrophils have minimal cell surface expression of these enzymes; however, phorbol ester induces a 30-fold increase. While exposure of neutrophils to chemoattractants (fMLP and C5a) stimulates modest (two- to threefold) increases in cell surface expression of serine proteinases, priming with concentrations of lipopolysaccharide as low as 100 fg/ml leads to striking (up to 10-fold) increase in chemoattractant-induced cell surface expression, even in the presence of serum proteins. LPS-primed and fMLP-stimulated neutrophils have approximately 100 ng of cell surface human leukocyte elastase activity per 10(6) cells. Cell surface- bound human leukocyte elastase is catalytically active, yet is remarkably resistant to inhibition by naturally occurring proteinase inhibitors. These data indicate that binding of serine proteinases to the cell surface focuses and preserves their catalytic activity, even in the presence of proteinase inhibitors. Upregulated expression of persistently active cell surface-bound serine proteinases on activated neutrophils provides a novel mechanism to facilitate their egress from the vasculature, penetration of tissue barriers, and recruitment into sites of inflammation. Dysregulation of the cell surface expression of these enzymes has the potential to cause tissue destruction during inflammation. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 3 |
| Volume Number | 131 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1995-11-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cathepsins Metabolism Leukocyte Elastase Neutrophils Enzymology Pancreatic Elastase Serine Endopeptidases Cathepsin G Chemotactic Factors Pharmacology Enzyme Inhibitors Extracellular Matrix Immunohistochemistry Lipopolysaccharides Membrane Proteins Physiology Molecular Weight Oxidation-Reduction Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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