| pubmed-article:15996195 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0022567 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0021753 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0442027 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0109272 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C1366765 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C1553423 | lld:lifeskim |
| pubmed-article:15996195 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:15996195 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:15996195 | pubmed:dateCreated | 2005-7-5 | lld:pubmed |
| pubmed-article:15996195 | pubmed:abstractText | Heat shock proteins (HSP) are released by cells in response to stress signals. It is hypothesized that pathogenic bacteria stimulate the cells in the periodontium to up-regulate the expression of HSP60, which would stimulate macrophages, and possibly other cells, to produce proinflammatory cytokines. We sought to determine whether oral keratinocytes responded to recombinant human HSP60 and to identify the signalling pathways involved. In addition, whether oral keratinocytes are a source of endogenous HSP60 was also investigated. RT-PCR revealed that rhHSP60 induced expression of the IL-1beta gene in the Human Oral Keratinocyte (HOK-16B) cell line and it was highest at the lowest concentration used (0.1 microg/ml). These responses were mediated via activation of p44/42 MAP-kinases and to a lesser extend the MAP-kinase SAP/JNK. Similar data was obtained from analysis of intracellular signalling pathways in HOK-16B cells by rhHSP70 and LPS (from both E. coli and the oral pathogen Porphyromonas gingivalis). However, there was little activation of p38 by rhHSP60. Blocking of the p44/42 pathway decreased HSP60-induced IL-1beta gene expression and protein secretion. In addition, we discovered that self-HSP60 proteins were constitutively secreted by HOK-16B cells. Secretion of self-HSP60 was up-regulated in cells treated with LPS from P. gingivalis, but down-regulated with LPS from E. coli. To summarize, oral keratinocytes respond to exogenous HSP60 by triggering expression of the inflammatory cytokine IL-1beta through activation of p44/42 MAP kinase. Oral keratinocytes are also a source for self-HSP60 and the secretion of this protein may be differentially modified by LPS from different bacterial species. These results highlight the importance of oral keratinocytes and HSPs in the development of an immune response against bacterial infection. | lld:pubmed |
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| pubmed-article:15996195 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15996195 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15996195 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15996195 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15996195 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15996195 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15996195 | pubmed:issn | 0009-9104 | lld:pubmed |
| pubmed-article:15996195 | pubmed:author | pubmed-author:TaylorJ JJJ | lld:pubmed |
| pubmed-article:15996195 | pubmed:author | pubmed-author:KapasSS | lld:pubmed |
| pubmed-article:15996195 | pubmed:author | pubmed-author:PleguezuelosO... | lld:pubmed |
| pubmed-article:15996195 | pubmed:author | pubmed-author:DaintyS JSJ | lld:pubmed |
| pubmed-article:15996195 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15996195 | pubmed:volume | 141 | lld:pubmed |
| pubmed-article:15996195 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15996195 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15996195 | pubmed:pagination | 307-14 | lld:pubmed |
| pubmed-article:15996195 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:15996195 | pubmed:meshHeading | pubmed-meshheading:15996195... | lld:pubmed |
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| pubmed-article:15996195 | pubmed:meshHeading | pubmed-meshheading:15996195... | lld:pubmed |
| pubmed-article:15996195 | pubmed:meshHeading | pubmed-meshheading:15996195... | lld:pubmed |
| pubmed-article:15996195 | pubmed:meshHeading | pubmed-meshheading:15996195... | lld:pubmed |
| pubmed-article:15996195 | pubmed:meshHeading | pubmed-meshheading:15996195... | lld:pubmed |
| pubmed-article:15996195 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15996195 | pubmed:articleTitle | A human oral keratinocyte cell line responds to human heat shock protein 60 through activation of ERK1/2 MAP kinases and up- regulation of IL-1beta. | lld:pubmed |
| pubmed-article:15996195 | pubmed:affiliation | Oral Microbiology and Host Responses Group, School of Dental Sciences, Faculty of Medical Sciences, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4BW, UK. | lld:pubmed |
| pubmed-article:15996195 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15996195 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15996195 | lld:pubmed |
