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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-8-3
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pubmed:abstractText |
We have previously reported that extracellular ATP stimulates Ca2+ influx from extracellular space, resulting in the production of prostaglandin E2 which mediates, at least in part, its proliferative effect on osteoblast-like MC3T3-E1 cells, and that the activation of protein kinase C (PKC) stimulates phospholipase D in these cells. In the present study, we examined the effect of extracellular ATP on phosphatidylcholine-hydrolysing phospholipase D activity in MC3T3-E1 cells. ATP stimulated the formation of both choline and inositol phosphates dose-dependently in the range between 0.1 and 1 mM. The formation of choline by a combination of ATP and NaF, an activator of GTP-binding protein, was synergistic, whereas that of inositol phosphates was not. A combination of ATP and 12-O-tetradecanoylphorbol-13-acetate, a PKC activating phorbol ester, additively stimulated the formation of choline. Staurosporine, an inhibitor of PKC, had little effect on ATP-stimulated formation of choline. Choline formation was significantly reduced by chelating extracellular Ca2+ with EGTA, while being inhibited by W-7, an antagonist of calmodulin. These results suggest that extracellular ATP stimulates phospholipase D in a Ca2+/calmodulin-dependent manner in osteoblast-like cells, and that neither PKC activation nor GTP-binding protein is involved in this mechanism.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Choline,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfonamides,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/W 7
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-0795
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
145
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
81-6
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:7798033-Adenosine Triphosphate,
pubmed-meshheading:7798033-Animals,
pubmed-meshheading:7798033-Calmodulin,
pubmed-meshheading:7798033-Cell Line,
pubmed-meshheading:7798033-Choline,
pubmed-meshheading:7798033-Dose-Response Relationship, Drug,
pubmed-meshheading:7798033-Egtazic Acid,
pubmed-meshheading:7798033-Extracellular Space,
pubmed-meshheading:7798033-Mice,
pubmed-meshheading:7798033-Osteoblasts,
pubmed-meshheading:7798033-Phospholipase D,
pubmed-meshheading:7798033-Stimulation, Chemical,
pubmed-meshheading:7798033-Sulfonamides,
pubmed-meshheading:7798033-Tetradecanoylphorbol Acetate
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pubmed:year |
1995
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pubmed:articleTitle |
Mechanism of phospholipase D activation induced by extracellular ATP in osteoblast-like cells.
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pubmed:affiliation |
First Department of Internal Medicine, Nagoya University School of Medicine, Japan.
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pubmed:publicationType |
Journal Article
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