Free radicals inactivate human neutrophil elastase and its inhibitors with comparable efficiency.
Free radicals produced in a Fenton reaction (H202/Cu), modelling some xenobiotic and cell-mediated inflammatory affronts, efficiently inactivated the elastase-inhibitor eglin, but equally, human neutrophil elastase itself. Elastase activity was not regenerated from proteinase/inhibitor complexes during radical attack. Three different elastase inhibitors, eglin, secretory leukocyte proteinase inhibitor and alpha-1-proteinase inhibitor were all similarly sensitive to inactivation. Unlike certain oxidants which can selectively inactivate alpha-1-proteinase inhibitor, free radicals may influence comparably the availability of both proteinase inhibitors and their targets.
Dean
R T
RT
Ciba-Geigy, Basel, Switzerland.
Nick
H P
HP
Schnebli
H P
HP
D001798:Blood Proteins / Q000037:antagonists & inhibitors; D003300:Copper / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005609:Free Radicals; D006801:Humans; D006861:Hydrogen Peroxide; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism / Q000494:pharmacology*; D011506:Proteins / Q000037:antagonists & inhibitors / Q000494:pharmacology; D015843:Serpins; D000515:alpha 1-Antitrypsin
D001798:Blood Proteins; D005609:Free Radicals; D011480:Protease Inhibitors; D011506:Proteins; D015843:Serpins; D000515:alpha 1-Antitrypsin; C028656:eglin proteinase inhibitors; D003300:Copper; D006861:Hydrogen Peroxide; D010196:Pancreatic Elastase