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Section of Digestive and Liver Diseases, Department of Medicine, University of Illinois at Chicago and West Side Veterans Affairs Medical Center, Chicago, Illinois 60612
The effect of nitric oxide (NO) on
Na+/H+ exchange (NHE) activity was investigated
utilizing Caco-2 cells as an experimental model. Incubation of Caco-2
cells with 10
3 M
S-nitroso-N-acetylpenicillamine (SNAP), a conventional
donor of NO, for 20 min resulted in a ~45% dose-dependent decrease
in NHE activity, as determined by assay of
ethylisopropylamiloride-sensitive 22Na uptake. A similar
decrease in NHE activity was observed utilizing another NO-specific
donor, sodium nitroprusside. SNAP-mediated inhibition of NHE activity
was not secondary to a loss of cell viability. NHE3 activity was
significantly reduced by SNAP (P < 0.05), whereas NHE2
activity was essentially unaltered. The effects of SNAP were mediated
by the cGMP-dependent signal transduction pathway as follows:
1) LY-83583 and
1H-(1,2,4)oxadiazolo(4,3-a)quinoxalin-1-one (ODQ), specific inhibitors of soluble guanylate cyclase, blocked the
inhibitory effect of SNAP on NHE; 2) 8-bromo-cGMP mimicked the effects of SNAP on NHE activity; 3) the SNAP-induced
decrease in NHE activity was counteracted by a specific protein
kinase G inhibitor, KT-5823 (1 µM); 4) chelerythrine
chloride (2 µM) or calphostin C (200 nM), specific protein kinase C
inhibitors, did not affect inhibition of NHE activity by SNAP;
5) there was no cross activation by the protein kinase
A-dependent pathway, as the inhibitory effects of SNAP were not blocked
by Rp-cAMPS (25 µM), a specific protein kinase A inhibitor. These
data provide novel evidence that NO inhibits NHE3 activity via
activation of soluble guanylate cyclase, resulting in an increase in
intracellular cGMP levels and activation of protein kinase G.
S-nitroso-N-acetylpenicillamine; cGMP; sodium/hydrogen exchanger
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