Abstract
Efficacy of HOCl scavenging by sulfur-containing compounds: antioxidant activity of glutathione disulfide?
den Hartog GJ, Haenen GR, Vegt E, van der Vijgh WJ, Bast A.
Department of Pharmacology and Toxicology, Maastricht University, The Netherlands.
Hypochlorous acid (HOCl) is a bactericidal compound formed by activated neutrophils during inflammation. Overproduction of HOCl causes damage to tissues at the site of neutrophil accumulation. The deleterious effects of excessive HOCl formation can be attenuated using antioxidants. Thiols and thioethers are known to be very effective HOCl scavengers. In the present study, the potency of several sulfur-containing compounds to protect acetylcholinesterase, glutathione S-transferase P1-1 (GST P1-1) and alpha1-antiproteinease against inactivation by HOCl was determined. Surprisingly, glutathione disulfide was an effective protector of acetylcholinesterase against hypochlorous acid. Glutathione disulfide did not provide protection for GST P1-1 and alpha1-antiproteinease against oxidative inactivation by HOCl. The implications of this finding are discussed.
den Hartog GJ, Haenen GR, Vegt E, van der Vijgh WJ, Bast A.
Department of Pharmacology and Toxicology, Maastricht University, The Netherlands.
Hypochlorous acid (HOCl) is a bactericidal compound formed by activated neutrophils during inflammation. Overproduction of HOCl causes damage to tissues at the site of neutrophil accumulation. The deleterious effects of excessive HOCl formation can be attenuated using antioxidants. Thiols and thioethers are known to be very effective HOCl scavengers. In the present study, the potency of several sulfur-containing compounds to protect acetylcholinesterase, glutathione S-transferase P1-1 (GST P1-1) and alpha1-antiproteinease against inactivation by HOCl was determined. Surprisingly, glutathione disulfide was an effective protector of acetylcholinesterase against hypochlorous acid. Glutathione disulfide did not provide protection for GST P1-1 and alpha1-antiproteinease against oxidative inactivation by HOCl. The implications of this finding are discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 709-713 |
| Number of pages | 5 |
| Journal | Biological Chemistry |
| Volume | 383 |
| Issue number | 3-4 |
| Publication status | Published - 1 Jan 2002 |