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lüll Cefoperazone prevents the inactivation of alpha(1)-antitrypsin by activated neutrophils Dallegri F; Dapino P; Arduino N; Bertolotto M; Ottonello LAntimicrob Agents Chemother 1999[Sep]; 43 (9): 2307-10At sites of neutrophilic inflammation, tissue injury by neutrophil elastase is favored by phagocyte-induced hypochlorous acid-dependent inactivation of the natural elastase inhibitor alpha(1)-antitrypsin. In the present study, cefoperazone prevented alpha(1)-antitrypsin inactivation by neutrophils and reduced the recovery of hypochlorous acid from these cells. Moreover, the antibiotic reduced the free elastase activity in a neutrophil suspension supplemented with alpha(1)-antitrypsin without affecting the cells' ability to release elastase. These data suggest that the drug inactivates hypochlorous acid before its reaction with alpha(1)-antitrypsin, thereby permitting the antiprotease-mediated blockade of released elastase. In conclusion, cefoperazone appears to have the potential for limiting elastase-antielastase imbalances, attenuating the related tissue injury at sites of inflammation.|Cefoperazone/*pharmacology[MESH]|Cephalosporins/*pharmacology[MESH]|Drug Interactions[MESH]|Humans[MESH]|Hypochlorous Acid/antagonists & inhibitors/pharmacology[MESH]|Neutrophils/*drug effects/enzymology[MESH]|Pancreatic Elastase/*metabolism[MESH]|alpha 1-Antitrypsin/drug effects/*metabolism[MESH] |