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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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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. |
format | Online Article Text |
id | pubmed-6721579 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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