Endothelial serpins—protectors of the vasculature?
| Autor: | I. Beckman, Kevin D. Forsyth, V. Talbot |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Adult
Lipopolysaccharides animal structures Cathepsin G Endothelium Neutrophils alpha 1-Antichymotrypsin Immunology Inflammation Serpin Alpha 1-antichymotrypsin chemistry.chemical_compound medicine Humans Immunology and Allergy Cells Cultured Serpins Cathepsin biology Serine Endopeptidases Elastase Cathepsins medicine.anatomical_structure chemistry alpha 1-Antitrypsin biology.protein Serine Proteinase Inhibitors Endothelium Vascular medicine.symptom Research Article |
| Zdroj: | Clinical and Experimental Immunology. 95:277-282 |
| ISSN: | 1365-2249 0009-9104 |
| DOI: | 10.1111/j.1365-2249.1994.tb06523.x |
| Popis: | SUMMARY Vascular damage, initiated by host inflammatory cells, is a component of the pathophysiology of many acute and chronic inflammatory disorders. Neutrophil-mediated tissue damage is mediated primarily by proteinases, particularly elastase and cathepsin G. In this study we have identified endothelial binding of two key serine proteinase inhibitors (serpins), α-antitrypsin, the inhibitor of elastase, and α1-antichymotrypsin, the inhibitor of cathepsin G. These serpins are shed from the endothelium into the supernatant when neutrophils adherent to the endothelium are activated. Endothelium activated by lipopolysaccharide (LPS) augments this process. Serpin-proteinase complexes activate neutrophils and induce further cytokine release, thereby amplifying inflammatory processes. Strategies aimed at preventing endothelial serpin depletion may help minimize vascular damage during inflammation. |
| Databáze: | OpenAIRE |
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