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A defect of neuronal nitric oxide synthase increases superoxide anion and attenuates the control of myocardial oxygen consumption by nitric oxide derived from endothelial nitric oxide synthase



A defect of neuronal nitric oxide synthase increases superoxide anion and attenuates the control of myocardial oxygen consumption by nitric oxide derived from endothelial nitric oxide synthase



FASEB Journal 18(4-5): Abst 859 5



Endothelial nitric oxide synthase (eNOS)- derived nitric oxide (NO) plays an important role in the control of myocardial oxygen consumption (MVO2) by inhibiting mitochondrial respiration. It has been shown that NOS is present in cardiac mitochondria and it is derived from neuronal NOS (nNOS). However, the role of nNOS in the control of MVO2 remains unknown. VO2 in left ventricular tissues from mice with defects in the expression of nNOS (nNOS (-/-)) was measured with a Clark-type oxygen electrode. The rate of decrease in oxygen concentration was expressed as a percentage of the baseline. Stimulation of NO production by bradykinin (BK, 100 μmol/L) and carbachol (CCh, 100 μmol/L) induced decreases in VO2 in nNOS (+/+) (-26±2%, n = 8 or -32±3%, n = 6). In contrast to nNOS (+/+), BK- or CCh-induced reduction in VO2 were attenuated in nNOS (-/-) (-16±1%, n = 25 or -17±3%, n = 6). Responses to BK in nNOS (-/-) were restored by pre-incubation with Tiron (10 mmol/L, -26±2%, n = 5) or oxypurinol (100 μmol/L, -30±2%, n = 5). There was increase in lucigenin (5 μmol/L)-detectable superoxide anion (O2-) in nNOS (-/-) compared to nNOS (+/+). Tiron or oxypurinol decreased superoxide anion in all groups to levels that were not different from each other. These results indicate that a defect of nNOS increases O2- through the activation of xanthine oxidase and attenuates the control of MVO2 by NO derived from eNOS. NIH PO-1 43023.

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