Effect of Plant Kunitz Inhibitors from Bauhinia bauhinioides and Bauhinia rufa on Pulmonary Edema Caused by Activated Neutrophils
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C. Neuhof
Abstract
Mediators released from polymorphonuclear neutrophils, in particular elastase, are known to induce acute edematous lung injury. In this study we show that the pulmonary edema in isolated perfused rabbit lungs caused by activated neutrophils via release of elastase is significantly decreased by the Kunitztype Inhibitor BbCI (10 -5 M) from Bauhinia bauhinoides to the same degree as by eglin C (10 -5 M) from Hirudo medicinalis, which was used as a reference. The highly homologous proteinase inhibitor BrPI (10 -5 M) from Bauhinia rufa, however, did not reduce edema formation. The major difference between these inhibitors is the much higher Ki value of BrPI (Ki = 38 nM) for elastase compared to BbCI (Ki = 5.3 nM) and eglin C (Ki = 0.2 nM), respectively. Elastase liberation from activated PMNs was not influenced by the inhibitors. Our results indicate that BbCI can be a useful tool to study the role of neutrophil elastase in pathophysiological processes.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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- Vito Turk – 30 Years of Research on Cysteine Proteases and Their Inhibitors
- Family C1 Cysteine Proteases: Biological Diversity or Redundancy?
- Molecular Regulation of Human Cathepsin B: Implication in Pathologies
- Caspases and Neuronal Development
- Structural Basis of the Matrix Metalloproteinases and Their Physiological Inhibitors, the Tissue Inhibitors of Metalloproteinases
- Managing Peptidases in the Genomic Era
- Insights into the Roles of Cathepsins in Antigen Processing and Presentation Revealed by Specific Inhibitors
- Cleavage Site Specificity of Cathepsin K toward Cartilage Proteoglycans and Protease Complex Formation
- Toward Computer-Based Cleavage Site Prediction of Cysteine Endopeptidases
- Isolation and Characterization of a Novel and Potent Inhibitor of Arg-Gingipain from Streptomyces sp. Strain FA-70
- Procongopain from Trypanosoma congolense Is Processed at Basic pH: An Unusual Feature among Cathepsin L-Like Cysteine Proteases
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