Inositol trisphosphate production and amylase secretion in mouse pancreatic acini

R. E. Powers; A. K. Saluja; M. J. Houlihan; M. L. Steer

doi:10.1016/0006-291X(85)91800-5

Inositol trisphosphate production and amylase secretion in mouse pancreatic acini

R. E. Powers, A. K. Saluja, M. J. Houlihan, M. L. Steer

Research output: Contribution to journal › Article › peer-review

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Abstract

Dispersed mouse pancreatic acini prelabelled with (³H)-myoinositol generated (³H)-inositol trisphosphate (³H-IP₃), (³H)-IP₂ and (³H)-IP₁ in response to both cholinergic and cholecystokinin analogues. The generation of (³H)-IP₃ was very rapid, reaching a maximal value within 5 seconds following hormone stimulation. Stimulation with 10^-3M carbachol increased (³H)-IP₃ to a value which was 13 times that found in unstimulated acini. These results indicate that the mechanism of stimulus-secretion coupling in mouse pancreatic acini may proceed by a mechanism similar to many other systems, including rat pancreatic acini. This sequence includes hormone-stimulated phosphatidylinositol turnover and Ca²⁺ mobilization, i.e. secretagogue-stimulated generation of IP₃ which induces the subsequent release of intracellular Ca²⁺. These observations differ from those recently reported by Hokin-Neaverson and Sadeghian (J. Biol. Chem. 259: 1346 1984), in which no hormone stimulated IP₃ generation was detected in mouse pancreatic acini.

Original language	English (US)
Pages (from-to)	284-288
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	131
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(85)91800-5
State	Published - Aug 30 1985
Externally published	Yes

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title = "Inositol trisphosphate production and amylase secretion in mouse pancreatic acini",

abstract = "Dispersed mouse pancreatic acini prelabelled with (3H)-myoinositol generated (3H)-inositol trisphosphate (3H-IP3), (3H)-IP2 and (3H)-IP1 in response to both cholinergic and cholecystokinin analogues. The generation of (3H)-IP3 was very rapid, reaching a maximal value within 5 seconds following hormone stimulation. Stimulation with 10-3M carbachol increased (3H)-IP3 to a value which was 13 times that found in unstimulated acini. These results indicate that the mechanism of stimulus-secretion coupling in mouse pancreatic acini may proceed by a mechanism similar to many other systems, including rat pancreatic acini. This sequence includes hormone-stimulated phosphatidylinositol turnover and Ca2+ mobilization, i.e. secretagogue-stimulated generation of IP3 which induces the subsequent release of intracellular Ca2+. These observations differ from those recently reported by Hokin-Neaverson and Sadeghian (J. Biol. Chem. 259: 1346 1984), in which no hormone stimulated IP3 generation was detected in mouse pancreatic acini.",

author = "Powers, {R. E.} and Saluja, {A. K.} and Houlihan, {M. J.} and Steer, {M. L.}",

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T1 - Inositol trisphosphate production and amylase secretion in mouse pancreatic acini

AU - Powers, R. E.

AU - Saluja, A. K.

AU - Houlihan, M. J.

AU - Steer, M. L.

N1 - Funding Information: this conclusion has been supported by the

PY - 1985/8/30

Y1 - 1985/8/30

N2 - Dispersed mouse pancreatic acini prelabelled with (3H)-myoinositol generated (3H)-inositol trisphosphate (3H-IP3), (3H)-IP2 and (3H)-IP1 in response to both cholinergic and cholecystokinin analogues. The generation of (3H)-IP3 was very rapid, reaching a maximal value within 5 seconds following hormone stimulation. Stimulation with 10-3M carbachol increased (3H)-IP3 to a value which was 13 times that found in unstimulated acini. These results indicate that the mechanism of stimulus-secretion coupling in mouse pancreatic acini may proceed by a mechanism similar to many other systems, including rat pancreatic acini. This sequence includes hormone-stimulated phosphatidylinositol turnover and Ca2+ mobilization, i.e. secretagogue-stimulated generation of IP3 which induces the subsequent release of intracellular Ca2+. These observations differ from those recently reported by Hokin-Neaverson and Sadeghian (J. Biol. Chem. 259: 1346 1984), in which no hormone stimulated IP3 generation was detected in mouse pancreatic acini.

AB - Dispersed mouse pancreatic acini prelabelled with (3H)-myoinositol generated (3H)-inositol trisphosphate (3H-IP3), (3H)-IP2 and (3H)-IP1 in response to both cholinergic and cholecystokinin analogues. The generation of (3H)-IP3 was very rapid, reaching a maximal value within 5 seconds following hormone stimulation. Stimulation with 10-3M carbachol increased (3H)-IP3 to a value which was 13 times that found in unstimulated acini. These results indicate that the mechanism of stimulus-secretion coupling in mouse pancreatic acini may proceed by a mechanism similar to many other systems, including rat pancreatic acini. This sequence includes hormone-stimulated phosphatidylinositol turnover and Ca2+ mobilization, i.e. secretagogue-stimulated generation of IP3 which induces the subsequent release of intracellular Ca2+. These observations differ from those recently reported by Hokin-Neaverson and Sadeghian (J. Biol. Chem. 259: 1346 1984), in which no hormone stimulated IP3 generation was detected in mouse pancreatic acini.

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Inositol trisphosphate production and amylase secretion in mouse pancreatic acini

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