Water-soluble Antioxidants Inhibit Macrophage Recognition of Oxidized Erythrocytes

Effect of exogenously added water-soluble antioxidants on the mouse macrophage lectin-like receptor activity for oxidized erythrocytes was investigated. A monolayer of thioglycollate-induced mouse peritoneal macrophages was preincubated with each of the antioxidants at 37°C for 1 h, and the binding for mouse erythrocytes oxidized with ADP-chelated Fe(III) was examined. The binding was decreased by preincubation of macrophages with ascorbic acid-related compounds including ascorbic acid, erythorbic acid and dehydroascorbic acid in a dose-dependent fashion at relatively high concentrations above 10 μM. The binding was similarly decreased by preincubation of macrophages with catechin compounds including epicatechin, epigallocatechin, epicatechin gallate and epigallocatechin gallate in a dose-dependent fashion at 0.01-100 μM. The binding was more effectively decreased by preincubation of macrophages with thiol-related compounds including glutathione, oxidized glutathione, glutathione isopropyl ester and N-acetylcysteine in a dose dependent fashion at relatively low doses below 1 μM. These results showed that water-soluble antioxidants especially glutathione and its derivatives reduced the ability of macrophages to bind oxidized erythrocytes, suggesting that the activity of lectin-like receptors of macrophages for oxidized erythrocytes was regulated by oxidative mechanisms.