Biologically-significant scavenging of the myeloperoxidase-derived oxidant hypochlorous acid by some anti-inflammatory drugs.
Neutrophils contain the enzyme myeloperoxidase, which oxidizes Cl- ions into the powerful oxidant hypochlorous acid (HOCl). HOCl inactivates alpha 1-antiprotease, permitting uncontrolled protease activities. Most anti-inflammatory drugs tested are capable of reacting with HOCl, but the reactions seem insufficiently rapid under physiological conditions to protect alpha 1-antiprotease against inactivation by HOCl. However, rapid scavenging of HOCl might contribute to the anti-inflammatory effects of penicillamine, gold sodium thiomalate, phenylbutazone and primaquine.
Wasil
M
M
Department of Biochemistry, King's College (KQC), London, U.K.
Halliwell
B
B
Moorhouse
C P
CP
Hutchison
D C
DC
Baum
H
H
D000818:Animals; D000893:Anti-Inflammatory Agents / Q000494:pharmacology*; D002712:Chlorides / Q000097:blood; D006997:Hypochlorous Acid / Q000097:blood*; D009504:Neutrophils / Q000201:enzymology; D009195:Peroxidase / Q000097:blood*; D000515:alpha 1-Antitrypsin / Q000378:metabolism
D000893:Anti-Inflammatory Agents; D002712:Chlorides; D000515:alpha 1-Antitrypsin; D006997:Hypochlorous Acid; D009195:Peroxidase