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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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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/58460

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)

Submitter: 田村 保明

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