| pubmed-article:18769043 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18769043 | lifeskim:mentions | umls-concept:C0024880 | lld:lifeskim |
| pubmed-article:18769043 | lifeskim:mentions | umls-concept:C1153415 | lld:lifeskim |
| pubmed-article:18769043 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:18769043 | pubmed:issue | 1-4 | lld:pubmed |
| pubmed-article:18769043 | pubmed:dateCreated | 2008-9-4 | lld:pubmed |
| pubmed-article:18769043 | pubmed:abstractText | Stimulation of the mast cell IgE-receptor (FcepsilonRI) by antigen leads to stimulation of Ca(2+) entry with subsequent mast cell degranulation and release of inflammatory mediators. Ca(2+) further activates Ca(2+)-activated K(+) channels, which in turn provide the electrical driving force for Ca(2+) entry. Since phosphatidylinositol (PI)-3-kinase has previously been shown to be required for mast cell activation and degranulation, we explored, whether mast cell Ca(2+) and Ca(2+)-activated K(+) channels may be sensitive to PI3-kinase activity. Whole-cell patch clamp experiments and Fura-2 fluorescence measurements for determination of cytosolic Ca(2+) concentration were performed in mouse bone marrow-derived mast cells either treated or untreated with the PI3-kinase inhibitors LY-294002 (10 muM) and wortmannin (100 nM). Antigen-stimulated Ca(2+) entry but not Ca(2+) release from the intracellular stores was dramatically reduced upon PI3-kinase inhibition. Ca(2+) entry was further inhibited by TRPV blocker ruthenium red (10 muM). Ca(2+) entry following readdition after Ca(+)-store depletion with thapsigargin was again decreased by LY-294002, pointing to inhibition of store-operated channels (SOCs). Moreover, inhibition of PI3-kinase abrogated IgE-stimulated, but not ionomycin-induced stimulation of Ca(2+)-activated K(+) channels. These observations disclose PI3-kinase-dependent regulation of Ca(2+) entry and Ca(2+)-activated K(+)-channels, which in turn participate in triggering mast cell degranulation. | lld:pubmed |
| pubmed-article:18769043 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18769043 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18769043 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18769043 | pubmed:issn | 1421-9778 | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:LangFlorianF | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:HuberStephan... | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:FelderEdwardE | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:DietlPaulP | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:LamRebecca... | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:ShumilinaEkat... | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:SobiesiakMalg... | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:LangCameliaC | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:MatznerNicole... | lld:pubmed |
| pubmed-article:18769043 | pubmed:author | pubmed-author:ZemtsovaIrina... | lld:pubmed |
| pubmed-article:18769043 | pubmed:copyrightInfo | Copyright 2008 S. Karger AG, Basel. | lld:pubmed |
| pubmed-article:18769043 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18769043 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:18769043 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18769043 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18769043 | pubmed:pagination | 169-76 | lld:pubmed |
| pubmed-article:18769043 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:18769043 | pubmed:meshHeading | pubmed-meshheading:18769043... | lld:pubmed |
| pubmed-article:18769043 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18769043 | pubmed:articleTitle | Phosphatidylinositol-3-kinase regulates mast cell ion channel activity. | lld:pubmed |
| pubmed-article:18769043 | pubmed:affiliation | Department of Physiology, University of Tübingen, Germany. | lld:pubmed |
| pubmed-article:18769043 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18769043 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:18708 | entrezgene:pubmed | pubmed-article:18769043 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18769043 | lld:entrezgene |
