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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
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| Title: | Heat shock protein 90 targets a chaperoned peptide to the static early endosome for efficient cross-presentation by human dendritic cells |
| Authors: | Tanaka, Tsutomu Browse this author | | Okuya, Koichi Browse this author | | Kutomi, Goro Browse this author | | Takaya, Akari Browse this author | | Kajiwara, Toshimitsu Browse this author | | Kanaseki, Takayuki Browse this author | | Tsukahara, Tomohide Browse this author | | Hirohashi, Yoshihiko Browse this author | | Torigoe, Toshihiko Browse this author | | Hirata, Koichi Browse this author | | Okamoto, Yoshiharu Browse this author | | Sato, Noriyuki Browse this author | | Tamura, Yasuaki Browse this author →KAKEN DB |
| Keywords: | Antigen presentation | | processing | | dendritic cells | | heat shock protein | | T cells | | tumor immunity |
| Issue Date: | Jan-2015 |
| Publisher: | Wiley-Blackwell |
| Journal Title: | Cancer Science |
| Volume: | 106 |
| Issue: | 1 |
| Start Page: | 18 |
| End Page: | 24 |
| Publisher DOI: | 10.1111/cas.12570 |
| Abstract: | 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. |
| Rights: | http://creativecommons.org/licenses/by-nc/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/58460 |
| Appears in Collections: | 産学・地域協働推進機構 (Institute for the Promotion of Business-Regional Collaboration) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 田村 保明
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