Article
Mutants of plasminogen activator inhibitor-1 designed to inhibit neutrophil elastase and cathepsin G are more effective in vivo than their endogenous inhibitors.
The Journal of biological chemistry - 16 Jul 2004
Stefansson Steingrimur, Yepes Manuel, Gorlatova Natalia, Day Duane E, Moore Elisabeth G, Zabaleta Adriana, McMahon Grainne A, Lawrence Daniel A
Abstract excerpt
Neutrophil elastase and cathepsin G are abundant intracellular neutrophil proteinases that have an important role in destroying ingested particles. However, when neutrophils degranulate, these proteinases are released and can cause irreparable damage by degrading host connective tissue proteins. Despite abundant endogenous inhibitors, these proteinases are protected from inhibition because of their ability to...
Topics
- Animals
- Anions
- Cathepsin G
- Cathepsins
- Dose-Response Relationship, Drug
- Endocytosis
- Endothelial Cells
- Enzyme Inhibitors
- Humans
- Inflammation