| pubmed-article:19148288 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19148288 | lifeskim:mentions | umls-concept:C0079731 | lld:lifeskim |
| pubmed-article:19148288 | lifeskim:mentions | umls-concept:C0003272 | lld:lifeskim |
| pubmed-article:19148288 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:19148288 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:19148288 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:19148288 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19148288 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19148288 | pubmed:dateCreated | 2009-1-16 | lld:pubmed |
| pubmed-article:19148288 | pubmed:abstractText | Macrophages are important effectors in the clearance of antibody-coated tumor cells. However, the signaling pathways that regulate macrophage-induced ADCC are poorly defined. To understand the regulation of macrophage-mediated ADCC, we used human B cell lymphoma coated with Rituximab as the tumor target and murine macrophages primed with IFNgamma as the effectors. Our data demonstrate that the PtdIns 3-kinase/Akt pathway is activated during macrophage-induced ADCC and that the inhibition of PtdIns 3-kinase results in the inhibition of macrophage-mediated cytotoxicity. Interestingly, downstream of PtdIns 3-kinase, expression of constitutively active Akt (Myr-Akt) in macrophages significantly enhanced their ability to mediate ADCC. Further analysis revealed that in this model, macrophage-mediated ADCC is dependent upon the release of nitric oxide (NO). However, the PtdIns 3-kinase/Akt pathway does not appear to regulate NO production. An examination of the role of the PtdIns 3-kinase/Akt pathway in regulating conjugate formation indicated that macrophages treated with an inhibitor of PtdIns 3-kinase fail to polarize the cytoskeleton at the synapse and show a significant reduction in the number of conjugates formed with tumor targets. Further, inhibition of PtdIns 3-kinase also reduced macrophage spreading on Rituximab-coated surfaces. On the other hand, Myr-Akt expressing macrophages displayed a significantly greater ability to form conjugates with tumor cells. Taken together, these findings illustrate that the PtdIns 3-kinase/Akt pathway plays a critical role in macrophage ADCC through its influence on conjugate formation between macrophages and antibody-coated tumor cells. | lld:pubmed |
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| pubmed-article:19148288 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19148288 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19148288 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19148288 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:TridandapaniS... | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:OstrowskiMich... | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:ByrdJohn CJC | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:CheneyCarolyn... | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:MuthusamyNata... | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:GanesanLatha... | lld:pubmed |
| pubmed-article:19148288 | pubmed:author | pubmed-author:JoshiTruptiT | lld:pubmed |
| pubmed-article:19148288 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19148288 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:19148288 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19148288 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19148288 | pubmed:pagination | e4208 | lld:pubmed |
| pubmed-article:19148288 | pubmed:dateRevised | 2011-5-27 | lld:pubmed |
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