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Heat Shock Proteins in Cancer Immunotherapy

Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining th...

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Autores principales: Das, Jugal Kishore, Xiong, Xiaofang, Ren, Xingcong, Yang, Jin-Ming, Song, Jianxun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927063/
https://www.ncbi.nlm.nih.gov/pubmed/31885572
http://dx.doi.org/10.1155/2019/3267207
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author Das, Jugal Kishore
Xiong, Xiaofang
Ren, Xingcong
Yang, Jin-Ming
Song, Jianxun
author_facet Das, Jugal Kishore
Xiong, Xiaofang
Ren, Xingcong
Yang, Jin-Ming
Song, Jianxun
author_sort Das, Jugal Kishore
collection PubMed
description Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contributing to their metastatic phenotype. Upregulation of these HSPs is associated with the poor outcome of anticancer therapy in clinical settings. On the other hand, these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. This review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy.
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spelling pubmed-69270632019-12-29 Heat Shock Proteins in Cancer Immunotherapy Das, Jugal Kishore Xiong, Xiaofang Ren, Xingcong Yang, Jin-Ming Song, Jianxun J Oncol Review Article Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contributing to their metastatic phenotype. Upregulation of these HSPs is associated with the poor outcome of anticancer therapy in clinical settings. On the other hand, these highly expressed HSPs may be exploited as viable immunotherapeutic targets for different types of cancers. This review discusses recent advances and perspectives on the research of HSP-based cancer immunotherapy. Hindawi 2019-12-11 /pmc/articles/PMC6927063/ /pubmed/31885572 http://dx.doi.org/10.1155/2019/3267207 Text en Copyright © 2019 Jugal Kishore Das et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Das, Jugal Kishore
Xiong, Xiaofang
Ren, Xingcong
Yang, Jin-Ming
Song, Jianxun
Heat Shock Proteins in Cancer Immunotherapy
title Heat Shock Proteins in Cancer Immunotherapy
title_full Heat Shock Proteins in Cancer Immunotherapy
title_fullStr Heat Shock Proteins in Cancer Immunotherapy
title_full_unstemmed Heat Shock Proteins in Cancer Immunotherapy
title_short Heat Shock Proteins in Cancer Immunotherapy
title_sort heat shock proteins in cancer immunotherapy
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927063/
https://www.ncbi.nlm.nih.gov/pubmed/31885572
http://dx.doi.org/10.1155/2019/3267207
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