Inositol trisphosphate independent increase of intracellular free calcium and amylase secretion in pancreatic acini

Ashok K. Saluja, Robert E. Powers, Michael L. Steer

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

It is generally believed that the activation of various cell surface receptors results in the phospholipase C-catalyzed production of inositol trisphosphate which, in turn, increases the intracellular concentration of free Ca2+ by stimulating its release from non-mitochondrial sources. We have investigated both the production of inositol trisphosphate and changes in intracellular Ca2+ concentration in rat pancreatic acini in response to caerulein and CCK-JMV-180, two analogs of cholecystokinin. Both of these analogs cause comparable increases in the rate of amylase secretion and in intracellular Ca2+ concentration but their effects on inositol phosphate generation are dramatically different; caerulein stimulates significant production of inositol phosphates within 1 min of its addition, whereas no detectable levels of inositol phosphates were generated within the same time after addition of CCK-JMV-180. These results suggest that the CCK-JMV-180 stimulated release of intracellular Ca2+ is not mediated by inositol trisphosphate but some other as yet unidentified messenger.

Original languageEnglish (US)
Pages (from-to)8-13
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume164
Issue number1
DOIs
StatePublished - Oct 16 1989
Externally publishedYes

Bibliographical note

Funding Information:
We would like to thank Dr. Roberto Bruzzone for many helpful discussions and Ms. Anne Zavertnik and Mr. Wayne Glover for their superb technical assistance. This work was supported in part by NIH grant #AM31914.

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