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Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?

Heat shock protein 27 (HSP27), induced by heat shock, environmental, and pathophysiological stressors, is a multi-functional protein that acts as a protein chaperone and an antioxidant. HSP27 plays a significant role in the inhibition of apoptosis and actin cytoskeletal remodeling. HSP27 is upregula...

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Autores principales: Choi, Seul-Ki, Kam, Heejin, Kim, Kye-Young, Park, Suk In, Lee, Yun-Sil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721579/
https://www.ncbi.nlm.nih.gov/pubmed/31426426
http://dx.doi.org/10.3390/cancers11081195
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author Choi, Seul-Ki
Kam, Heejin
Kim, Kye-Young
Park, Suk In
Lee, Yun-Sil
author_facet Choi, Seul-Ki
Kam, Heejin
Kim, Kye-Young
Park, Suk In
Lee, Yun-Sil
author_sort Choi, Seul-Ki
collection PubMed
description Heat shock protein 27 (HSP27), induced by heat shock, environmental, and pathophysiological stressors, is a multi-functional protein that acts as a protein chaperone and an antioxidant. HSP27 plays a significant role in the inhibition of apoptosis and actin cytoskeletal remodeling. HSP27 is upregulated in many cancers and is associated with a poor prognosis, as well as treatment resistance, whereby cells are protected from therapeutic agents that normally induce apoptosis. This review highlights the most recent findings and role of HSP27 in cancer, as well as the strategies for using HSP27 inhibitors for therapeutic purposes.
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spelling pubmed-67215792019-09-10 Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment? Choi, Seul-Ki Kam, Heejin Kim, Kye-Young Park, Suk In Lee, Yun-Sil Cancers (Basel) Review Heat shock protein 27 (HSP27), induced by heat shock, environmental, and pathophysiological stressors, is a multi-functional protein that acts as a protein chaperone and an antioxidant. HSP27 plays a significant role in the inhibition of apoptosis and actin cytoskeletal remodeling. HSP27 is upregulated in many cancers and is associated with a poor prognosis, as well as treatment resistance, whereby cells are protected from therapeutic agents that normally induce apoptosis. This review highlights the most recent findings and role of HSP27 in cancer, as well as the strategies for using HSP27 inhibitors for therapeutic purposes. MDPI 2019-08-16 /pmc/articles/PMC6721579/ /pubmed/31426426 http://dx.doi.org/10.3390/cancers11081195 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Choi, Seul-Ki
Kam, Heejin
Kim, Kye-Young
Park, Suk In
Lee, Yun-Sil
Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
title Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
title_full Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
title_fullStr Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
title_full_unstemmed Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
title_short Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
title_sort targeting heat shock protein 27 in cancer: a druggable target for cancer treatment?
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721579/
https://www.ncbi.nlm.nih.gov/pubmed/31426426
http://dx.doi.org/10.3390/cancers11081195
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