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IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis
Heat shock protein 27 (Hsp27) is a key chaperone that interacts with over 200 client proteins. The expression of Hsp27 might be correlated with poor outcome in many types of cancer. Previous study indicated that Hsp27 might be an important biomarker in hepatocellular carcinoma (HCC). However, the de...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals LLC
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5589635/ https://www.ncbi.nlm.nih.gov/pubmed/28903396 http://dx.doi.org/10.18632/oncotarget.18989 |
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author | Hung, Chin-Sheng Huang, Chien-Yu Lee, Chia-Hwa Chen, Wei-Yu Huang, Ming-Te Wei, Po-Li Chang, Yu-Jia |
author_facet | Hung, Chin-Sheng Huang, Chien-Yu Lee, Chia-Hwa Chen, Wei-Yu Huang, Ming-Te Wei, Po-Li Chang, Yu-Jia |
author_sort | Hung, Chin-Sheng |
collection | PubMed |
description | Heat shock protein 27 (Hsp27) is a key chaperone that interacts with over 200 client proteins. The expression of Hsp27 might be correlated with poor outcome in many types of cancer. Previous study indicated that Hsp27 might be an important biomarker in hepatocellular carcinoma (HCC). However, the detailed mechanism is less well understood. The shRNA-mediated silencing of Hsp27 decreased the proliferation, migration and invasion of HCC cells. In a xenograft model, the silencing of Hsp27 reduced tumor progression. We revealed that the silencing of Hsp27 led to a reduction in insulin-like growth factor binding protein 2 (IGFBP2), which might mediate proliferation and metastasis through vimentin, snail and beta-catenin. The overexpression of IGFBP2 reversed the reductions in cell growth, migration and invasion. The tissue array results showed that HCC patients with high Hsp27 expression exhibited poor prognosis and increased metastasis. The Hsp27 expression was highly correlated with IGFPB2 in CRC specimen. ChIP and luciferase assays showed that Hsp27 does not directly bind the IGFBP2 promoter region to regulate the transcription of IGFBP2. In conclusion, our study demonstrated that Hsp27 is a key mediator of HCC progression and metastasis and that Hsp27 might regulate proliferation and metastasis through IGFBP2. This pathway might provide a new direction for the development of a novel therapeutic strategy for HCC. |
format | Online Article Text |
id | pubmed-5589635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-55896352017-09-12 IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis Hung, Chin-Sheng Huang, Chien-Yu Lee, Chia-Hwa Chen, Wei-Yu Huang, Ming-Te Wei, Po-Li Chang, Yu-Jia Oncotarget Research Paper Heat shock protein 27 (Hsp27) is a key chaperone that interacts with over 200 client proteins. The expression of Hsp27 might be correlated with poor outcome in many types of cancer. Previous study indicated that Hsp27 might be an important biomarker in hepatocellular carcinoma (HCC). However, the detailed mechanism is less well understood. The shRNA-mediated silencing of Hsp27 decreased the proliferation, migration and invasion of HCC cells. In a xenograft model, the silencing of Hsp27 reduced tumor progression. We revealed that the silencing of Hsp27 led to a reduction in insulin-like growth factor binding protein 2 (IGFBP2), which might mediate proliferation and metastasis through vimentin, snail and beta-catenin. The overexpression of IGFBP2 reversed the reductions in cell growth, migration and invasion. The tissue array results showed that HCC patients with high Hsp27 expression exhibited poor prognosis and increased metastasis. The Hsp27 expression was highly correlated with IGFPB2 in CRC specimen. ChIP and luciferase assays showed that Hsp27 does not directly bind the IGFBP2 promoter region to regulate the transcription of IGFBP2. In conclusion, our study demonstrated that Hsp27 is a key mediator of HCC progression and metastasis and that Hsp27 might regulate proliferation and metastasis through IGFBP2. This pathway might provide a new direction for the development of a novel therapeutic strategy for HCC. Impact Journals LLC 2017-07-05 /pmc/articles/PMC5589635/ /pubmed/28903396 http://dx.doi.org/10.18632/oncotarget.18989 Text en Copyright: © 2017 Hung et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License 3.0 (http://creativecommons.org/licenses/by/3.0/) (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Paper Hung, Chin-Sheng Huang, Chien-Yu Lee, Chia-Hwa Chen, Wei-Yu Huang, Ming-Te Wei, Po-Li Chang, Yu-Jia IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
title | IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
title_full | IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
title_fullStr | IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
title_full_unstemmed | IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
title_short | IGFBP2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
title_sort | igfbp2 plays an important role in heat shock protein 27-mediated cancer progression and metastasis |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5589635/ https://www.ncbi.nlm.nih.gov/pubmed/28903396 http://dx.doi.org/10.18632/oncotarget.18989 |
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