Abstract
In circular smooth muscle strips of porcine gastric fundus, polyethylene-glycol-superoxide dismutase, a membrane-permeable analogue of endogenous copper/zinc (Cu/Zn) superoxide dismutase, reversed the inhibitory effect of the superoxide anion generator 6-anilino-5,8-quinolinedione (LY83583) on electrically induced nitrergic relaxations of fundic tissues which are depleted of the endogenous antioxidant Cu/Zn superoxide dismutase by diethyldithiocarbamate, to the same extent as exogenously added Cu/Zn superoxide dismutase. Addition of a second antioxidant together with Cu/Zn superoxide dismutase does not result in a higher degree of reversal of the inhibitory effect of LY83583. Depletion of either tissue glutathione or tissue catalase in combination with diethyldithiocarbamate does not increase the inhibitory action of LY83583 or the nitric oxide (NO)-scavenger hydroxocobalamin upon nitrergic relaxations (electrically induced or by exogenous NO) when compared to their action in the presence of diethyldithiocarbamate alone. In conclusion, these results demonstrate that endogenous Cu/Zn superoxide dismutase is the essential antioxidant responsible for safeguarding peripheral nitrergic neurotransmission, whereby extracellular protection of endogenous NO is most important.
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