TY - JOUR
T1 - The nitric oxide donor, S-nitroso-N-acetyl-penicillamine, inhibits secretory activity in rat isolated parietal cells
AU - Brown, J. F.
AU - Hanson, P. J.
AU - Whittle, B. J. R.
PY - 1993/9/30
Y1 - 1993/9/30
N2 - Accumulation of the weak base aminopyrine was used as an index of acid secretory activity in rat isolated parietal cells. The nitric oxide (NO) donor, S-nitroso-N-acetyl-penicillamine (SNAP) caused a dose-dependent inhibition of aminopyrine accumulation (half-maximally effective concentration 247 μM) which was accompanied by an increase in guanosine 3',5'-cyclic monophosphate (cGMP) but no decrease in cell viability (trypan blue), glucose oxidation or adenosine 3',5'-cyclic monophosphate (cAMP) content. Oxyhaemoglobin (37 μM), which scavenges NO, significantly reduced the inhibitory effect of SNAP (1 mM). Prior exposure of intact cells to SNAP also reduced aminopyrine accumulation in response to ATP in permeabilised cells, an effect prevented by Rp-8-bromoguanosine 3',5'-monophosphorothioate, which inhibits activation of cGMP-dependent protein kinase, but not by the Sp-isomer. NO thus inhibits secretory activity in rat parietal cells by a specific interaction that may involve cGMP.
AB - Accumulation of the weak base aminopyrine was used as an index of acid secretory activity in rat isolated parietal cells. The nitric oxide (NO) donor, S-nitroso-N-acetyl-penicillamine (SNAP) caused a dose-dependent inhibition of aminopyrine accumulation (half-maximally effective concentration 247 μM) which was accompanied by an increase in guanosine 3',5'-cyclic monophosphate (cGMP) but no decrease in cell viability (trypan blue), glucose oxidation or adenosine 3',5'-cyclic monophosphate (cAMP) content. Oxyhaemoglobin (37 μM), which scavenges NO, significantly reduced the inhibitory effect of SNAP (1 mM). Prior exposure of intact cells to SNAP also reduced aminopyrine accumulation in response to ATP in permeabilised cells, an effect prevented by Rp-8-bromoguanosine 3',5'-monophosphorothioate, which inhibits activation of cGMP-dependent protein kinase, but not by the Sp-isomer. NO thus inhibits secretory activity in rat parietal cells by a specific interaction that may involve cGMP.
UR - http://www.scopus.com/inward/record.url?scp=0027527249&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1993.2192
DO - 10.1006/bbrc.1993.2192
M3 - Article
AN - SCOPUS:0027527249
SN - 0006-291X
VL - 195
SP - 1354
EP - 1359
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -