Source:http://linkedlifedata.com/resource/pubmed/id/20668218
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2010-8-20
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pubmed:abstractText |
Extracellular HSP90 associated with Ag peptides have been demonstrated to efficiently cross-prime T cells, following internalization by dendritic cells (DCs). In addition, the nature of cell-associated Ags required for cross-priming is implicated as peptides and proteins chaperoned by heat shock protein (HSP). However, the role of endogenous HSP in DCs during cross-presentation remains elusive. In this paper, we show that endogenous HSP90 is essential for cross-presentation of both soluble and cell-associated Ags in DCs. Cross-presentation of soluble OVA and OVA-loaded transporter associated with Ag processing-1-deficient cells by bone marrow-derived DCs and DC-like cell line DC2.4 was profoundly blocked by HSP90 inhibitors, whereas presentation of endogenously expressed OVA was only partially suppressed. Assays using small interfering RNA and heat shock factor-1-deficient DCs (with defective expression of HSP90alpha) revealed the pivotal role of HSP90alpha in cross-presentation. The results suggest that in addition to HSP90 in Ag donor cells, endogenous HSP90 in DCs plays an essential role during Ag cross-presentation and, moreover, points to a link between heat shock factor-1-dependent induction of HSP90alpha within DC and cytotoxic T cell immunity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1550-6606
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
185
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2693-700
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pubmed:meshHeading |
pubmed-meshheading:20668218-Animals,
pubmed-meshheading:20668218-Antigen Presentation,
pubmed-meshheading:20668218-Bone Marrow Cells,
pubmed-meshheading:20668218-Cell Line,
pubmed-meshheading:20668218-Cells, Cultured,
pubmed-meshheading:20668218-Coculture Techniques,
pubmed-meshheading:20668218-Cross-Priming,
pubmed-meshheading:20668218-Dendritic Cells,
pubmed-meshheading:20668218-HSP90 Heat-Shock Proteins,
pubmed-meshheading:20668218-Mice,
pubmed-meshheading:20668218-Mice, Inbred C57BL,
pubmed-meshheading:20668218-Mice, Knockout,
pubmed-meshheading:20668218-Mice, Transgenic,
pubmed-meshheading:20668218-Ovalbumin,
pubmed-meshheading:20668218-Peptide Fragments,
pubmed-meshheading:20668218-Signal Transduction,
pubmed-meshheading:20668218-Solubility
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pubmed:year |
2010
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pubmed:articleTitle |
Essential role of endogenous heat shock protein 90 of dendritic cells in antigen cross-presentation.
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pubmed:affiliation |
Laboratory for Immunochaperones, Research Center for Allergy and Immunology, RIKEN, Yokohama Institute, Tsurumi-Ku, Yokohama, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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