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Departments of Physiology and Pharmacology and Toxicology, Medical College of Wisconsin, Milwaukee, Wisconsin 53226
The purpose of this study was to determine whether
superoxide anions (O
1 · mg protein1.
The O1 · mg
protein1. Superoxide dismutase (SOD) with catalase
produced a concentration-dependent reduction of 5'-ND activity in renal
tissue homogenate, while the SOD inhibitor diethyldithiocarbamic
acid significantly increased 5'-ND activity. Inhibition of disulfide
bond formation by thioredoxin or thioredoxin reductase
significantly decreased xanthine/xanthine oxidase-induced activation of
renal 5'-ND. In in vivo experiments, inhibition of SOD by
diethyldithiocarbamic acid (0.5 mg · kg1 · min1 iv)
enhanced renal vasoconstriction induced by endogenously produced adenosine and increased renal tissue adenosine concentrations under
control condition and in ischemia and reperfusion. We conclude that oxidative stress activates 5'-ND and increases adenosine production in the kidney and that this redox regulatory mechanism of
adenosine production is important in the control of renal vascular tone
and glomerular perfusion.
redox signaling; renal hemodynamics; reactive oxygen species; nucleotide
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