Source:http://linkedlifedata.com/resource/pubmed/id/15383626
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2004-11-24
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pubmed:abstractText |
Using single cell, real-time imaging, this study compared the impact of members of the B/R4 subfamily of the regulators of G-protein signaling (RGS) (RGS2, -3, and -4) on receptor-mediated inositol 1,4,5-trisphosphate [Ins(1,4,5)P3], diacylglycerol, and Ca2+ signaling. In human embryonic kidney (HEK) 293 cells expressing recombinant Galpha(q/11)-coupled muscarinic M3 receptors, transient coexpression of RGS proteins with fluorescently-tagged biosensors for either Ins(1,4,5)P3 or diacylglycerol demonstrated that RGS2 and 3 inhibited receptor-mediated events. Although gross indices of signaling were unaffected by RGS4, it slowed the rate of increase in Ins(1,4,5)P3 levels. At equivalent levels of expression, myc-tagged RGS proteins showed inhibitory activity on the order RGS3 > or = RGS2 > RGS4. In HEK293 cells, stable expression of myc-tagged RGS2, -3, or -4 at equivalent levels also inhibited phosphoinositide and Ca2+ signaling by endogenously expressed muscarinic M3 receptors in the order RGS3 > or = RGS2 > RGS4. In these cells, RGS2 or -3 reduced receptor-mediated inositol phosphate generation in cell populations and reduced both the magnitude and kinetics (rise-time) of single cell Ca2+ signals. Furthermore, at low levels of receptor activation, oscillatory Ca2+ signals were dampened or abolished, whereas at higher levels, RGS2 and -3 promoted the conversion of more stable Ca2+ elevations into oscillatory signals. Despite little or no effect on responses to maximal receptor activation, RGS4 produced effects on the magnitude, kinetics, and oscillatory behavior of Ca2+ signaling at submaximal levels that were consistent with those of RGS2 and -3.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Methacholine Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/RGS Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RGS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RGS3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RGS4 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Muscarinic M3,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0026-895X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1453-64
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15383626-Calcium,
pubmed-meshheading:15383626-Cell Line,
pubmed-meshheading:15383626-GTP-Binding Protein alpha Subunits, Gq-G11,
pubmed-meshheading:15383626-GTP-Binding Proteins,
pubmed-meshheading:15383626-GTPase-Activating Proteins,
pubmed-meshheading:15383626-Genes, myc,
pubmed-meshheading:15383626-Homeostasis,
pubmed-meshheading:15383626-Humans,
pubmed-meshheading:15383626-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:15383626-Kidney,
pubmed-meshheading:15383626-Methacholine Chloride,
pubmed-meshheading:15383626-Microscopy, Confocal,
pubmed-meshheading:15383626-RGS Proteins,
pubmed-meshheading:15383626-Receptor, Muscarinic M3,
pubmed-meshheading:15383626-Recombinant Proteins,
pubmed-meshheading:15383626-Signal Transduction,
pubmed-meshheading:15383626-Transfection,
pubmed-meshheading:15383626-Type C Phospholipases
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pubmed:year |
2004
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pubmed:articleTitle |
Single-cell imaging of intracellular Ca2+ and phospholipase C activity reveals that RGS 2, 3, and 4 differentially regulate signaling via the Galphaq/11-linked muscarinic M3 receptor.
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pubmed:affiliation |
Department of Cell Physiology and Pharmacology, University of Leicester, Leicester, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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