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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3 Pt 1
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pubmed:dateCreated |
1997-4-24
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pubmed:abstractText |
Sphingosine derivatives are potent mitogens in several cell types. Many mitogens activate the Na+/H+ exchange, although the interrelationships between Na+/H+ exchange and mitogenesis are unclear. The present investigation in thyroid FRTL-5 cells shows that sphingosine 1-phosphate (SPP) activates Na+/H+ exchange in a dose-dependent manner in acid-loaded cells. The effect of SPP was abolished in a Na+-free buffer and by pretreatment of the cells with ethylisopropylamiloride. SPP did not affect basal intracellular pH (pHi). SPP stimulated the release of sequestered Ca2+ and a substantial entry of Ca2+. The effect of SPP on pH(i) was abolished in cells incubated in a Ca2+-free buffer, and in cells loaded with the intracellular Ca2+ chelator 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid. Furthermore, the effect of SPP was abolished in pertussis toxin (PTX)-treated cells. PTX decreased Ca2+ entry only, without affecting the release from intracellular stores. Phosphatidic acid (PA) did not activate Na+/H+ exchange, suggesting that the effect of SPP was not mediated via activation of phospholipase D and the production of PA. Thus one mechanism of action of SPP in FRTL-5 cells appears to be to activate Na+/H+ exchange. This action is mediated via a G protein-dependent mechanism and requires an increase in intracellular free Ca2+.
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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 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella,
http://linkedlifedata.com/resource/pubmed/chemical/sphingosine 1-phosphate
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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
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C1052-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9124507-Animals,
pubmed-meshheading:9124507-Biological Transport,
pubmed-meshheading:9124507-Calcium,
pubmed-meshheading:9124507-Cell Line,
pubmed-meshheading:9124507-Cytoplasm,
pubmed-meshheading:9124507-GTP-Binding Proteins,
pubmed-meshheading:9124507-Hydrogen-Ion Concentration,
pubmed-meshheading:9124507-Lysophospholipids,
pubmed-meshheading:9124507-Pertussis Toxin,
pubmed-meshheading:9124507-Phosphatidic Acids,
pubmed-meshheading:9124507-Phospholipase D,
pubmed-meshheading:9124507-Rats,
pubmed-meshheading:9124507-Sodium,
pubmed-meshheading:9124507-Sphingosine,
pubmed-meshheading:9124507-Thyroid Gland,
pubmed-meshheading:9124507-Virulence Factors, Bordetella
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pubmed:year |
1997
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pubmed:articleTitle |
Sphingosine 1-phosphate stimulates Na+/H+ exchange in thyroid FRTL-5 cells.
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pubmed:affiliation |
Department of Biosciences, University of Helsinki, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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