pubmed-article:17346313 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0023861 | lld:lifeskim |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0042219 | lld:lifeskim |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0070410 | lld:lifeskim |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0257694 | lld:lifeskim |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0549099 | lld:lifeskim |
pubmed-article:17346313 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:17346313 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:17346313 | pubmed:dateCreated | 2007-6-20 | lld:pubmed |
pubmed-article:17346313 | pubmed:abstractText | Three proteins secreted by Listeria monocytogenes facilitate escape from macrophage vacuoles: the cholesterol-dependent cytolysin listeriolysin O (LLO), a phosphoinositide-specific phospholipase C (PI-PLC) and a broad-range phospholipase C (PC-PLC). LLO and PI-PLC can activate several members of the protein kinase C (PKC) family during infection. PKCepsilon is a novel PKC that contributes to macrophage activation, defence against bacterial infection, and phagocytosis; however, a role for PKCepsilon in Lm infections has not been described. To study PKCepsilon dynamics, PKCepsilon-YFP chimeras were visualized in macrophages during Lm infection. PKCepsilon-YFP was recruited to forming vacuoles during macrophage phagocytosis of Lm and again later to fully formed Lm vacuoles. The PKCepsilon-YFP localization to the fully formed Lm vacuole was LLO-dependent but independent of PI-PLC or PC-PLC. PKCepsilon-YFP recruitment often followed LLO perforation of the membrane, as indicated by localization of PKCepsilon-YFP to Lm vacuoles after they released small fluorescent dyes into the cytoplasm. PKCepsilon-YFP recruitment to vesicles also followed phagocytosis of LLO-containing liposomes or osmotic lysis of endocytic vesicles, indicating that vacuole perforation by LLO was the chief cause of the PKCepsilon response. These studies implicate PKCepsilon in a cellular mechanism for recognizing damaged membranous organelles, including the disrupted vacuoles created when Lm escapes into cytoplasm. | lld:pubmed |
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pubmed-article:17346313 | pubmed:language | eng | lld:pubmed |
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pubmed-article:17346313 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17346313 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17346313 | pubmed:month | Jul | lld:pubmed |
pubmed-article:17346313 | pubmed:issn | 1462-5814 | lld:pubmed |
pubmed-article:17346313 | pubmed:author | pubmed-author:SwansonJoel... | lld:pubmed |
pubmed-article:17346313 | pubmed:author | pubmed-author:LippPeterP | lld:pubmed |
pubmed-article:17346313 | pubmed:author | pubmed-author:LeeKyung-Dall... | lld:pubmed |
pubmed-article:17346313 | pubmed:author | pubmed-author:ShaughnessyLe... | lld:pubmed |
pubmed-article:17346313 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17346313 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:17346313 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17346313 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17346313 | pubmed:pagination | 1695-704 | lld:pubmed |
pubmed-article:17346313 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
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pubmed-article:17346313 | pubmed:meshHeading | pubmed-meshheading:17346313... | lld:pubmed |
pubmed-article:17346313 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17346313 | pubmed:articleTitle | Localization of protein kinase C epsilon to macrophage vacuoles perforated by Listeria monocytogenes cytolysin. | lld:pubmed |
pubmed-article:17346313 | pubmed:affiliation | Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | lld:pubmed |
pubmed-article:17346313 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17346313 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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