Source:http://linkedlifedata.com/resource/pubmed/id/12526888
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2003-1-15
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| pubmed:abstractText |
It was previously shown that in rat thyroid PC-Cl3 cell line, a purinergic P2Y receptor increases the concentration of free cytosolic Ca(2+) ([Ca(2+)](i)) via phospholipase C activation. We here studied whether in a transformed cell line (PC-E1Araf) derived from parental PC-Cl3 cells, ATP is still able to transduce the [Ca(2+)](i)-based intracellular signal.We demonstrate the expression of mRNA for P2Y2 in both PC-Cl3 and PC-E1Araf cells; mRNAs for P2Y1, P2Y4, P2Y6 and P2Y11 were absent. In both cell lines activation of P2Y2 receptor provokes a transient increase in [Ca(2+)](i) followed by a lower sustained phase persisting for over 5min in PC-Cl3 and only 1.5 min in PC-E1Araf cells. In both cell lines the [Ca(2+)](i) reached a plateau level significantly higher than the basal [Ca(2+)](i) level persisting for over 10 min. Removal of extracellular Ca(2+) reduced the initial transient response to ATP in PC-Cl3, but not in PC-E1Araf cells, and completely abolished the plateau phase in both cell lines. In the presence of extracellular Ca(2+) thapsigargin (TG) caused a rise in [Ca(2+)](i) significantly higher in PC-Cl3 than transformed PC-E1Araf cells, while in Ca(2+)-free medium the effect of TG was similar in both cell lines. The capacitative Ca(2+)-entry in PC-Cl3 resulted significantly higher than in PC-E1Araf cells. Further studies were performed in order to investigate whether the different effects of ATP on [Ca(2+)](i) was due to variation in divalent cation plasma membrane permeability. PC-E1Araf cells showed a much lower permeability to Ca(2+), Ba(2+), Sr(2+), Mn(2+), and Co(2+) that may be responsible for the differences in purinergic Ca(2+) signaling pathway with respect to parental PC-Cl3 cells.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/P2ry2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2Y2
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0143-4160
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
33
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
59-68
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:12526888-Adenosine Triphosphate,
pubmed-meshheading:12526888-Animals,
pubmed-meshheading:12526888-Calcium,
pubmed-meshheading:12526888-Calcium Signaling,
pubmed-meshheading:12526888-Cations,
pubmed-meshheading:12526888-Cell Line, Transformed,
pubmed-meshheading:12526888-Cell Membrane,
pubmed-meshheading:12526888-Cell Membrane Permeability,
pubmed-meshheading:12526888-Enzyme Inhibitors,
pubmed-meshheading:12526888-Epithelial Cells,
pubmed-meshheading:12526888-Extracellular Space,
pubmed-meshheading:12526888-Gene Expression,
pubmed-meshheading:12526888-RNA, Messenger,
pubmed-meshheading:12526888-Rats,
pubmed-meshheading:12526888-Receptors, Purinergic P2,
pubmed-meshheading:12526888-Receptors, Purinergic P2Y2,
pubmed-meshheading:12526888-Thyroid Gland,
pubmed-meshheading:12526888-Up-Regulation
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| pubmed:year |
2003
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| pubmed:articleTitle |
Disturbances in purinergic [Ca2+]i signaling pathways in a transformed rat thyroid cell line.
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| pubmed:affiliation |
Laboratorio di Fisiologia, Dipartimento di Scienze e Tecnologie Biologiche e Ambientali, Università di Lecce, 73100 Lecce, Italy.
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| pubmed:publicationType |
Journal Article
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