Autoprocessing of neutrophil elastase near its active site reduces the efficiency of natural and synthetic elastase inhibitors

An imbalance between neutrophil-derived proteases and extracellular inhibitors is widely regarded as an important pathogenic mechanism for lung injury. Despite intense efforts over the last three decades, attempts to develop small-molecule inhibitors for neutrophil elastase have failed in the clinic...

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Veröffentlicht in:	Nature communications 2015-04, Vol.6 (1), p.6722-6722, Article 6722
Hauptverfasser:	Dau, T., Sarker, R. S. J., Yildirim, A. O., Eickelberg, O., Jenne, D. E.
Format:	Artikel
Sprache:	eng
Schlagworte:	13 631/45/607/468 64/60 692/308 82 82/1 82/29 82/80 82/81 82/83 alpha 1-Antitrypsin - pharmacology Amino Acid Sequence Animals Catalytic Domain Cytokines - biosynthesis Female Gene Expression HEK293 Cells Humanities and Social Sciences Humans Leukocyte Elastase - administration & dosage Leukocyte Elastase - antagonists & inhibitors Leukocyte Elastase - chemistry Leukocyte Elastase - metabolism Lung - drug effects Lung - enzymology Lung - pathology Macrophages - drug effects Macrophages - pathology Mice Mice, Inbred C57BL Molecular Sequence Data multidisciplinary Neurosciences Neutrophils Neutrophils - drug effects Neutrophils - enzymology Neutrophils - pathology Peptides - administration & dosage Peptides - antagonists & inhibitors Peptides - chemistry Peptides - metabolism Proteinase Inhibitory Proteins, Secretory - pharmacology Proteolysis Pulmonary Emphysema - chemically induced Pulmonary Emphysema - drug therapy Pulmonary Emphysema - enzymology Pulmonary Emphysema - pathology Recombinant Proteins - administration & dosage Recombinant Proteins - chemistry Recombinant Proteins - metabolism Science Science (multidisciplinary) Sequence Homology, Amino Acid Small Molecule Libraries - pharmacology
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