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Distinct activation of Na sup + -H sup + exchange by gastrin and CCK peptide in acini from guinea pig

Journal Article · · American Journal of Physiology; (USA)
OSTI ID:6993114
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  1. Institut National de la Sante et de la Recherche Medicale, Toulouse (France)
The effect of cholecystokinin (CCK)-gastrin family peptides (caerulein, unsulfated gastrin-17, and pentagastrin) and secretin in activating amiloride-sensitive {sup 22}Na uptake were investigated in guinea pig pancreatic acini. Secretin had no effect, but CCK-gastrin peptides stimulated the amiloride-sensitive {sup 22}Na uptake. The effect of caerulein was inhibited by dibutyryl guanosine 3{prime},5{prime}-cyclic monophosphate (cGMP) and asperlicin, indicating that activation of the Na{sup +}-H{sup +} antiport caused by caerulein is mediated by CCK receptors. The effect of gastrin was dibutyryl cGMP and asperlicin insensitive, whereas the effect of pentagastrin was inhibited by the CCK antagonists but with a low affinity, indicating that the effect of gastrin and that of pentagastrin was CCK receptor independent. The calcium ionophore A23187 caused an increase in amiloride-sensitive {sup 22}Na uptake. However, the effect of caerulein, which increased internal calcium concentration, was not modified after depletion of intracellular calcium, and that of CCK-gastrin family peptides was not dependent on external calcium concentration. Activation of amiloride-sensitive {sup 22}Na uptake was also induced by 12-O-tetradecanoylphorbol 13-acetate and 1-oleoyl-2-acetyl-glycerol. Activation of protein kinase c may be involved in the mechanism of caerulein or gastrin in activating the Na{sup +}-H{sup +} exchange.
OSTI ID:
6993114
Journal Information:
American Journal of Physiology; (USA), Journal Name: American Journal of Physiology; (USA) Vol. 254:1; ISSN 0002-9513; ISSN AJPHA
Country of Publication:
United States
Language:
English