Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3 Pt 1
|
| pubmed:dateCreated |
1998-4-24
|
| pubmed:abstractText |
We have investigated control mechanisms involved in the propagation of agonist-induced Ca2+ waves in isolated mouse pancreatic acinar cells. Using a confocal laser-scanning microscope, we were able to show that maximal stimulation of cells with acetylcholine (ACh, 500 nM) or bombesin (1 nM) caused an initial Ca2+ release of comparable amounts with both agonists at the luminal cell pole. Subsequent Ca2+ spreading to the basolateral membrane was faster with ACh (17.3 +/- 5.4 microns/s) than with bombesin (8.0 +/- 2.2 microns/s). The speed of bombesin-induced Ca2+ waves could be increased up to the speed of ACh-induced Ca2+ waves by inhibition of protein kinase C (PKC). Activation of PKC significantly decreased the speed of ACh-induced Ca2+ waves but had only little effect on bombesin-evoked Ca2+ waves. Within 3 s after stimulation, production of inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] was higher in the presence of ACh compared with bombesin, whereas bombesin induced higher levels of diacylglycerol (DAG) than ACh. These data suggest that the slower propagation speed of bombesin-induced Ca2+ waves is due to higher activation of PKC in the presence of bombesin compared with ACh. The higher increase in bombesin-compared with ACh-induced DAG production is probably due to activation of phospholipase D (PLD). Inhibition of the PLD-dependent DAG production by preincubation with 0.3% butanol led to an acceleration of the bombesin-induced Ca2+ wave. In further experiments, we could show that ruthenium red (100 microM), an inhibitor of Ca(2+)-induced Ca2+ release in skeletal muscle, also decreased the speed of ACh-induced Ca2+ waves. The effect of ruthenium red was not additive to the effect of PKC activation. From the data, we conclude that, following Ins(1,4,5)P3-induced Ca2+ release in the luminal cell pole, secondary Ca2+ release from stores, which are located in series between the luminal and the basal plasma membrane, modifies Ca2+ spreading toward the basolateral cell side by Ca(2+)-induced Ca2+ release. Activation of PKC leads to a reduction in Ca2+ release from these stores and therefore could explain the slower propagation of Ca2+ waves in the presence of bombesin compared with ACh.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2-tert-butylhydroquinone,
http://linkedlifedata.com/resource/pubmed/chemical/Acetylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Bombesin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Transporting ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 4,5-Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Ruthenium Red,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
|
| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0002-9513
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
274
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
C663-72
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:9530097-Acetylcholine,
pubmed-meshheading:9530097-Animals,
pubmed-meshheading:9530097-Bombesin,
pubmed-meshheading:9530097-Calcium,
pubmed-meshheading:9530097-Calcium Channels,
pubmed-meshheading:9530097-Calcium-Transporting ATPases,
pubmed-meshheading:9530097-Endoplasmic Reticulum,
pubmed-meshheading:9530097-Enzyme Activation,
pubmed-meshheading:9530097-Enzyme Inhibitors,
pubmed-meshheading:9530097-Hydroquinones,
pubmed-meshheading:9530097-Indicators and Reagents,
pubmed-meshheading:9530097-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:9530097-Male,
pubmed-meshheading:9530097-Mice,
pubmed-meshheading:9530097-Pancreatic Neoplasms,
pubmed-meshheading:9530097-Periodicity,
pubmed-meshheading:9530097-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:9530097-Protein Kinase C,
pubmed-meshheading:9530097-Ruthenium Red,
pubmed-meshheading:9530097-Signal Transduction,
pubmed-meshheading:9530097-Type C Phospholipases
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| pubmed:year |
1998
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| pubmed:articleTitle |
Control of Ca2+ wave propagation in mouse pancreatic acinar cells.
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| pubmed:affiliation |
Institute of Physiology II, University of the Saarland, Homburg, Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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