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Articles in PresS, published online ahead of print January 28, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00218.2001
Submitted on July 9, 2001
Accepted on January 7, 2002
1 Department of Physiology, Medical College of Wisconsin, Milwaukee, WI, USA
We recently reported that NADH oxidase is one of the major enzymes responsible for superoxide (O2.-) production in the rat kidney. However, the functional significance of NADH oxidase-mediated O2.- production and the mechanisms regulating this enzyme activity are poorly understood. Using fluorescence microscopic imaging analysis, the present study demonstrated that thick ascending limbs of Henle's loop (TALHs) exhibited red fluorescence when incubated with dihydroethidium (DHE), suggesting that O2.- is produced in this tubular segment. Compared with other nephron segments, TALHs from both renal cortex and medulla showed the highest fluorescence intensity. By incubating TALHs with the substrates of NADH oxidase, xanthine oxidase, nitric oxide synthase, arachidonic acid-metabolizing enzymes and intra-mitochondrial oxidases, NADH oxidase was found to be one of the most important enzyme for O2.- production in this tubular segment. The NADH oxidase inhibitor, diphenyleneiodonium (DPI, 100 µM), completely blocked NADH-induced O2.- production in TALHs. Inhibition of ion transport activity by incubation of TALHs with furosemide (5 mM) substantially inhibited NADH oxidase activity, but exposure of TALHs to low PO2 (5-10 mmHg) significantly increased O2.-production regardless of the absence or presence of NADH. Furthermore, angiotensin II (100 nM) increased the NADH oxidase activity by 32%, which was completely blocked by DPI. These results suggest that NADH oxidase is a major enzyme responsible for O2.- production in TALH and that the production of O2.- via NADH oxidase may be regulated by tubular metabolic activity and circulating hormones.
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