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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 protein
1.
The O
1 · mg
protein
1. 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 · kg
1 · min
1 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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