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Department of Pharmacology and Toxicology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205
ANG II exerts a biphasic effect on
Na+ transport in the kidney through its effects on
Na+-K+-ATPase activity. Beginning at
10
13 M, ANG II increased
Na+-K+-ATPase activity in freshly isolated rat
proximal tubules to a maximum stimulation at 1011 M of
1.43 ± 0.08-fold above control. Stimulation decreased
progressively at concentrations >1010 M to a value of
0.96 ± 0.1-fold at 107 M. In the presence of
additional L-arginine, the substrate for NO synthesis, the
stimulatory effect of ANG II (1011 M) was lost.
Conversely, N-monomethyl-L-arginine
(L-NMMA), the nitric oxide (NO) synthase inhibitor,
unmasked the stimulatory effect of ANG II at 107 M
(1.40 ± 0.1-fold).
1H-[1,2,4]oxadiazole-[4,3-a]quinoxalin-1-one, the
soluble guanylyl cyclase inhibitor, like L-NMMA, unmasked the stimulatory effect of ANG II at 107 M (1.30 ± 0.1-fold). The intracellular cGMP concentration was increased 1.58 ± 0.28-fold at 107 M ANG II. The ANG II AT1
receptor antagonist SK&F 108566 blocked the stimulatory effect of ANG
II at 1011 M. These data suggest that the NO/cGMP
signaling pathway serves as a negative component in the regulation of
Na+-K+-ATPase activity by ANG II.
N-monomethyl-L-arginine; 1H-[1,2,4]oxadiazole-[4,3-a]quinoxalin-1-one; SK&F 108566; angiotensin II
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