15 – Caveolin-1-Dependent Regulation of Cellular Metabolism Involves Nrf-2 and SOD2

The lactoperoxidase-catalyzed oxidation of glutathione (GSH) and thiocyanate (SCN−) was studied. Oxidation of SCN− was recorded by ultraviolet spectroscopy and by electron spin resonance (ESR). Consumption of GSH was measured by amperometric titration. One or two moles of GSH was oxidized per mole of H2O2 added, depending on the reaction conditions. Omission of SCN− prevented the oxidation of GSH. The oxidation of GSH required only catalytic amounts of SCN−, which was therefore recycled. Iodide (I−) could replace SCN−, while chloride or bromide were ineffective. The apparent Michaelis constant for SCN− was 17 μM. Oxidation of SCN− gave rise to two reactive intemediates, one stable and one unstable. The stable intermediate (−OSC·  N−(?)) decayed by a second-order reaction with a rate constant of 1.1 M−1 s−1. The decay of the unstable radical was very fast. The data (a) explain the short- and long-term antibacterial effects of lactoperoxidase-halide-H2O2 system. (b) point to possible deleterious effects due to glutathione depletion, (c) are of relevance for free radical disease involving sulphur-centered free radicals, and (d) support previous ovservations on lipid peroxidation/halogenation in biological membranes, liposomes, and unsaturated fatty acis.