A new CCK analogue differentiates two functionally distinct CCK receptors in rat and mouse pancreatic acini.

The American Journal of Physiology
T MatozakiJ A Williams

Abstract

Analysis of the competitive inhibition of 125I-labeled cholecystokinin octapeptide (CCK-8) binding to isolated rat or mouse pancreatic acini showed that in both species CCK-8 interacts with two different affinity sites. A newly synthesized CCK analogue modified at the COOH-terminal phenylalanine residue totally inhibited 125I-CCK binding. This interaction occurred with sites of a single affinity in rat acini but with two different affinity sites in mouse acini. When acini were incubated with increasing concentrations of CCK-8, a biphasic stimulation of amylase release was observed. By use of rat acini, the analogs stimulated amylase release but caused no inhibition at supramaximal concentrations. By contrast, in mouse pancreatic acini, analogues showed a biphasic stimulation of amylase release similar to CCK-8. Both CCK-8 and the analogue stimulated [3H]leucine incorporation into protein at low concentrations in rat pancreatic acini. Higher concentrations of CCK-8 profoundly inhibited [3H]leucine incorporation, whereas the analogue had no inhibitory effect. Moreover, the analogue at higher concentrations blocked the inhibition of [3H]leucine incorporation caused by CCK-8 but did not affect carbamylcholine-induced inhibition. In...Continue Reading

Citations

Jan 24, 2002·American Journal of Physiology. Gastrointestinal and Liver Physiology·Maria Dolors SansJohn A Williams
Apr 14, 2007·American Journal of Physiology. Gastrointestinal and Liver Physiology·Constanze H Kubisch, Craig D Logsdon
May 23, 2002·American Journal of Physiology. Gastrointestinal and Liver Physiology·Tim O LankischChung Owyang
Feb 9, 2000·American Journal of Physiology. Cell Physiology·B Han, C D Logsdon
May 30, 2003·American Journal of Physiology. Gastrointestinal and Liver Physiology·Maria Dolors SansJohn A Williams

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