Oct 16, 1989

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

Biochemical and Biophysical Research Communications
A K SalujaM L Steer

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 nonmitochondrial 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.

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  • Citations13

References

Mentioned in this Paper

Cholecystokinin
Inositol Phosphates
Calcium
Protoplasm
August Rats
Cholecystokinin Measurement
Analog
Calcium ion
Receptors, Cell Surface
Process of Secretion

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