Biologically-significant scavenging of the myeloperoxidase-derived oxidant hypochlorous acid by some anti-inflammatory drugs |
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Authors: | M Wasil B Halliwell C P Moorhouse D C Hutchison H Baum |
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Affiliation: | Department of Biochemistry, King's College (KQC), London, U.K. |
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Abstract: | 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. |
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