| pubmed-article:16951338 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C1367307 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0026473 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C1383501 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0003692 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0217250 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:16951338 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:16951338 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16951338 | pubmed:dateCreated | 2006-9-4 | lld:pubmed |
| pubmed-article:16951338 | pubmed:abstractText | Our previous studies demonstrated that the IL-13-induced 15-lipoxygenase expression in primary human monocytes is regulated by the activation of both Stat1 and Stat3 and by protein kinase C (PKC)delta. IL-13 stimulated the phosphorylation of Stat3 on both Tyr705 and Ser727. In this study we show that IL-13 induces the association of PKCdelta with Stat3, not with Stat1, and is required for Stat3 Ser727 phosphorylation. We found a novel IL-13-dependent cytosolic signaling complex of PKCdelta and tyrosine-phosphorylated Stat3. A tyrosine kinase inhibitor blocked PKCdelta association with Stat3 as well as Stat3 Ser727 phosphorylation. We therefore hypothesized that tyrosine phosphorylation was required for Stat3 interaction with PKCdelta and subsequent PKCdelta-dependent phosphorylation of Stat3 Ser727. We developed an efficient transfection protocol for human monocytes. Expression of Stat3 containing a mutation in Tyr705 inhibited the association of PKCdelta with Stat3 and blocked Stat3 Ser727 phosphorylation, whereas transfection with wild-type Stat3 did not. Furthermore, by transfecting monocytes with Stat3 containing mutations in Tyr705 or Ser727 or with wild-type Stat3, we demonstrated that both Stat3 tyrosine and serine phosphorylations are required for optimal binding of Stat3 with DNA and maximal expression of 15-lipoxygenase, an important regulator of inflammation and apoptosis. | lld:pubmed |
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| pubmed-article:16951338 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16951338 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:16951338 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16951338 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16951338 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:16951338 | pubmed:author | pubmed-author:LinN SNS | lld:pubmed |
| pubmed-article:16951338 | pubmed:author | pubmed-author:FeldmanGerald... | lld:pubmed |
| pubmed-article:16951338 | pubmed:author | pubmed-author:CathcartMarth... | lld:pubmed |
| pubmed-article:16951338 | pubmed:author | pubmed-author:FranzDavid... | lld:pubmed |
| pubmed-article:16951338 | pubmed:author | pubmed-author:Bhattacharjee... | lld:pubmed |
| pubmed-article:16951338 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16951338 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16951338 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:16951338 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16951338 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16951338 | pubmed:pagination | 3771-81 | lld:pubmed |
| pubmed-article:16951338 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16951338 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16951338 | pubmed:articleTitle | Monocyte 15-lipoxygenase expression is regulated by a novel cytosolic signaling complex with protein kinase C delta and tyrosine-phosphorylated Stat3. | lld:pubmed |
| pubmed-article:16951338 | pubmed:affiliation | Department of Cell Biology, Cleveland Clinic Foundation, Cleveland Clinic Lerner College of Medicine, Case Western Reserve University, Cleveland, OH 44195, USA. | lld:pubmed |
| pubmed-article:16951338 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16951338 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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