| pubmed-article:10215601 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0040132 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0443213 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:10215601 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:10215601 | pubmed:dateCreated | 1999-6-24 | lld:pubmed |
| pubmed-article:10215601 | pubmed:abstractText | Redox modulation is involved in the regulation of the intracellular free calcium concentration ([Ca2+]i) in several cell types. In thyroid cells, including thyroid FRTL-5 cells, changes in [Ca2+]i regulate important functions. In the present study we investigated the effects of the oxidizing compounds thimerosal and t-butyl hydroperoxide on [Ca2+]i in thyroid FRTL-5 cells. Thimerosal mobilized sequestered calcium, and evoked modest store-dependent calcium entry. Both compounds potently attenuated the increase in [Ca2+]i when store-operated calcium entry was evoked with thapsigargin. The entry of barium was not attenuated. Experiments performed with high extracellular pH, in sodium-free buffer and in the presence of vanadate suggested that thimerosal decreased [Ca2+]i by activating a calcium extrusion mechanism, probably a plasma membrane Ca2+-ATPase. All the observed effects were abrogated by the reducing agent beta-mercaptoethanol. The mechanism of action was apparently mediated via activation of protein kinase C, as thimerosal potently stimulated binding of [3H]phorbol 12, 13-dibutyrate, and was without effect on store-operated calcium entry in cells treated with staurosporine or in cells with down-regulated protein kinase C. Thimerosal did not depolarize the membrane potential, as evaluated using patch-clamp in the whole-cell mode. In immunoprecipitates obtained with an antibody against plasma membrane Ca2+-ATPase, we observed several phosphorylated bands in cells stimulated with thimerosal. In conclusion, we have shown that thimerosal attenuates an increase in [Ca2+]i, probably by activating a plasma membrane Ca2+-ATPase. | lld:pubmed |
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| pubmed-article:10215601 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10215601 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10215601 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10215601 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10215601 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10215601 | pubmed:month | May | lld:pubmed |
| pubmed-article:10215601 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:10215601 | pubmed:author | pubmed-author:TuominenRR | lld:pubmed |
| pubmed-article:10215601 | pubmed:author | pubmed-author:TörnquistKK | lld:pubmed |
| pubmed-article:10215601 | pubmed:author | pubmed-author:VainioPP | lld:pubmed |
| pubmed-article:10215601 | pubmed:author | pubmed-author:DuguéBB | lld:pubmed |
| pubmed-article:10215601 | pubmed:author | pubmed-author:TitievskyAA | lld:pubmed |
| pubmed-article:10215601 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10215601 | pubmed:day | 1 | lld:pubmed |
