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10.1111/cas.12570 http://scihub22266oqcxt.onion/10.1111/cas.12570 C4317773!4317773 !25414129     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25414129 &cmd=llinks): Failed to open stream: HTTP request failed! 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Heat shock protein 90 targets a chaperoned peptide to the static early endosome for efficient cross-presentation by human dendritic cells |pdf=|usr=}}{{25414129 }} gab.com Text Heat shock protein 90 targets a chaperoned peptide to the static early endosome for efficient cross-presentation by human dendritic cells JO: Cancer Sci http://www.kidney.de/pget.php?&tw=1&pmid=25414129 #FOAvip The presentation of an exogenous antigen in a major histocompatibility complex class-I- restricted fashion to CD8(+) T cells is called cross-presentation. Heat shock proteins (HSPs) such as Hsp70, gp96, and Hsp90 have been shown to elicit efficient CTL responses by cross-presentation through an as-yet entirely unknown mechanism. Hsp90 is the most abundant cytosolic HSP and is known to act as a molecular chaperone. We have shown that a tumor antigen peptide complexed with Hsp90 could be cross-presented by dendritic cells (DCs) through an endosomal pathway in a murine system. However, it has not been determined whether human DCs also cross-present an Hsp90-peptide complex and induce peptide-specific CTLs. In this study, we found that an Hsp90-cancer antigen peptide complex was efficiently cross-presented by human monocyte-derived DCs and induced peptide-specific CTLs. Furthermore, we observed that the internalized Hsp90-peptide complex was strictly sorted to the Rab5(+), EEA1(+) static early endosome and the Hsp90-chaperoned peptide was processed and bound to MHC class I molecules through an endosome-recycling pathway. Our data indicate that targeting of the antigen to a "static" early endosome by Hsp90 is essential for efficient cross-presentation. Twit Text FOAVip Heat shock protein 90 targets a chaperoned peptide to the static early endosome for efficient cross-presentation by human dendritic cells ????Cancer Sci http://www.kidney.de/pget.php?&tw=1&pmid=25414129 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25414129 #FOAvip English Wikipedia <ref>{{Cite pmid|25414129 }}</ref> Heat shock protein 90 targets a chaperoned peptide to the static early endosome for efficient cross-presentation by human dendritic cells #MMPMID25414129 Tanaka T ; Okuya K ; Kutomi G ; Takaya A ; Kajiwara T ; Kanaseki T ; Tsukahara T ; Hirohashi Y ; Torigoe T ; Hirata K ; Okamoto Y ; Sato N ; Tamura Y Cancer Sci 2015[Jan]; 106 (1 ): 18-24 PMID25414129 show ga The presentation of an exogenous antigen in a major histocompatibility complex class-I- restricted fashion to CD8(+) T cells is called cross-presentation. Heat shock proteins (HSPs) such as Hsp70, gp96, and Hsp90 have been shown to elicit efficient CTL responses by cross-presentation through an as-yet entirely unknown mechanism. Hsp90 is the most abundant cytosolic HSP and is known to act as a molecular chaperone. We have shown that a tumor antigen peptide complexed with Hsp90 could be cross-presented by dendritic cells (DCs) through an endosomal pathway in a murine system. However, it has not been determined whether human DCs also cross-present an Hsp90-peptide complex and induce peptide-specific CTLs. In this study, we found that an Hsp90-cancer antigen peptide complex was efficiently cross-presented by human monocyte-derived DCs and induced peptide-specific CTLs. Furthermore, we observed that the internalized Hsp90-peptide complex was strictly sorted to the Rab5(+), EEA1(+) static early endosome and the Hsp90-chaperoned peptide was processed and bound to MHC class I molecules through an endosome-recycling pathway. Our data indicate that targeting of the antigen to a "static" early endosome by Hsp90 is essential for efficient cross-presentation. |*Cross-Priming [MESH] |CD8-Positive T-Lymphocytes/immunology [MESH] |Cells, Cultured [MESH] |Dendritic Cells/*immunology [MESH] |Endosomes/*metabolism [MESH] |HSP90 Heat-Shock Proteins/*physiology [MESH] |Humans [MESH] |Inhibitor of Apoptosis Proteins/immunology [MESH] |Peptide Fragments/immunology [MESH] |Protein Transport [MESH] |Survivin [MESH]Heat shock protein 90 targets a chaperoned peptide to the static early(epmc).pdf DeepDyve Pubget Overpricing