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The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer

Pancreatic cancer is one of most aggressive forms of cancer. After clinical detection it exhibits fast metastatic growth. Heat shock protein 27 (HSP27; HSPB1) has been characterized as a molecular chaperone which modifies the structures and functions of other proteins in cells when they are exposed...

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Autores principales: Okuno, Mitsuru, Adachi, Seiji, Kozawa, Osamu, Shimizu, Masahito, Yasuda, Ichiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730376/
https://www.ncbi.nlm.nih.gov/pubmed/26805817
http://dx.doi.org/10.3390/ijms17010137
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author Okuno, Mitsuru
Adachi, Seiji
Kozawa, Osamu
Shimizu, Masahito
Yasuda, Ichiro
author_facet Okuno, Mitsuru
Adachi, Seiji
Kozawa, Osamu
Shimizu, Masahito
Yasuda, Ichiro
author_sort Okuno, Mitsuru
collection PubMed
description Pancreatic cancer is one of most aggressive forms of cancer. After clinical detection it exhibits fast metastatic growth. Heat shock protein 27 (HSP27; HSPB1) has been characterized as a molecular chaperone which modifies the structures and functions of other proteins in cells when they are exposed to various stresses, such as chemotherapy. While the administration of gemcitabine, an anti-tumor drug, has been the standard treatment for patients with advanced pancreatic cancer, accumulating evidence shows that HSP27 plays a key role in the chemosensitivity to gemcitabine. In addition, phosphorylated HSP27 induced by gemcitabine has been associated with the inhibition of pancreatic cancer cell growth. In this review, we summarize the role of phosphorylated HSP27, as well as HSP27, in the regulation of chemosensitivity in pancreatic cancer.
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spelling pubmed-47303762016-02-11 The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer Okuno, Mitsuru Adachi, Seiji Kozawa, Osamu Shimizu, Masahito Yasuda, Ichiro Int J Mol Sci Review Pancreatic cancer is one of most aggressive forms of cancer. After clinical detection it exhibits fast metastatic growth. Heat shock protein 27 (HSP27; HSPB1) has been characterized as a molecular chaperone which modifies the structures and functions of other proteins in cells when they are exposed to various stresses, such as chemotherapy. While the administration of gemcitabine, an anti-tumor drug, has been the standard treatment for patients with advanced pancreatic cancer, accumulating evidence shows that HSP27 plays a key role in the chemosensitivity to gemcitabine. In addition, phosphorylated HSP27 induced by gemcitabine has been associated with the inhibition of pancreatic cancer cell growth. In this review, we summarize the role of phosphorylated HSP27, as well as HSP27, in the regulation of chemosensitivity in pancreatic cancer. MDPI 2016-01-21 /pmc/articles/PMC4730376/ /pubmed/26805817 http://dx.doi.org/10.3390/ijms17010137 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Okuno, Mitsuru
Adachi, Seiji
Kozawa, Osamu
Shimizu, Masahito
Yasuda, Ichiro
The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer
title The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer
title_full The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer
title_fullStr The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer
title_full_unstemmed The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer
title_short The Clinical Significance of Phosphorylated Heat Shock Protein 27 (HSPB1) in Pancreatic Cancer
title_sort clinical significance of phosphorylated heat shock protein 27 (hspb1) in pancreatic cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4730376/
https://www.ncbi.nlm.nih.gov/pubmed/26805817
http://dx.doi.org/10.3390/ijms17010137
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