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Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells
Heat shock protein 70 (Hsp70; also known as HSP70A1A) is one of the most induced proteins in cancer cells; however, its role in cancer has not yet been fully elucidated. In the present study, we proposed a hypothetical model in which the silencing of Hsp70 enhanced the metastatic properties of the H...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
D.A. Spandidos
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6365026/ https://www.ncbi.nlm.nih.gov/pubmed/30569142 http://dx.doi.org/10.3892/ijo.2018.4666 |
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author | Kasioumi, Panagiota Vrazeli, Paraskevi Vezyraki, Patra Zerikiotis, Stelios Katsouras, Christos Damalas, Alexander Angelidis, Charalampos |
author_facet | Kasioumi, Panagiota Vrazeli, Paraskevi Vezyraki, Patra Zerikiotis, Stelios Katsouras, Christos Damalas, Alexander Angelidis, Charalampos |
author_sort | Kasioumi, Panagiota |
collection | PubMed |
description | Heat shock protein 70 (Hsp70; also known as HSP70A1A) is one of the most induced proteins in cancer cells; however, its role in cancer has not yet been fully elucidated. In the present study, we proposed a hypothetical model in which the silencing of Hsp70 enhanced the metastatic properties of the HeLa, A549 and MCF7 cancer cell lines. We consider that the inability of cells to form cadherin-catenin complexes in the absence of Hsp70 stimulates their detachment from neighboring cells, which is the first step of anoikis and metastasis. Under these conditions, an epithelial-to-mesenchymal transition (EMT) pathway is activated that causes cancer cells to acquire a mesenchymal phenotype, which is known to possess a higher ability for migration. Therefore, we herein provide evidence of the dual role of Hsp70 which, according to international literature, first establishes a cancerous environment and then, as suggested by our team, regulates the steps of the metastatic process, including EMT and migration. Finally, the trigger for the anti-metastatic properties that are acquired by cancer cells in the absence of Hsp70 appears to be the destruction of the Hsp70-dependent heterocomplexes of E-cadherin/catenins, which function like an anchor between neighboring cells. |
format | Online Article Text |
id | pubmed-6365026 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | D.A. Spandidos |
record_format | MEDLINE/PubMed |
spelling | pubmed-63650262019-02-19 Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells Kasioumi, Panagiota Vrazeli, Paraskevi Vezyraki, Patra Zerikiotis, Stelios Katsouras, Christos Damalas, Alexander Angelidis, Charalampos Int J Oncol Articles Heat shock protein 70 (Hsp70; also known as HSP70A1A) is one of the most induced proteins in cancer cells; however, its role in cancer has not yet been fully elucidated. In the present study, we proposed a hypothetical model in which the silencing of Hsp70 enhanced the metastatic properties of the HeLa, A549 and MCF7 cancer cell lines. We consider that the inability of cells to form cadherin-catenin complexes in the absence of Hsp70 stimulates their detachment from neighboring cells, which is the first step of anoikis and metastasis. Under these conditions, an epithelial-to-mesenchymal transition (EMT) pathway is activated that causes cancer cells to acquire a mesenchymal phenotype, which is known to possess a higher ability for migration. Therefore, we herein provide evidence of the dual role of Hsp70 which, according to international literature, first establishes a cancerous environment and then, as suggested by our team, regulates the steps of the metastatic process, including EMT and migration. Finally, the trigger for the anti-metastatic properties that are acquired by cancer cells in the absence of Hsp70 appears to be the destruction of the Hsp70-dependent heterocomplexes of E-cadherin/catenins, which function like an anchor between neighboring cells. D.A. Spandidos 2018-12-12 /pmc/articles/PMC6365026/ /pubmed/30569142 http://dx.doi.org/10.3892/ijo.2018.4666 Text en Copyright: © Kasioumi et al. This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made. |
spellingShingle | Articles Kasioumi, Panagiota Vrazeli, Paraskevi Vezyraki, Patra Zerikiotis, Stelios Katsouras, Christos Damalas, Alexander Angelidis, Charalampos Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells |
title | Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells |
title_full | Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells |
title_fullStr | Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells |
title_full_unstemmed | Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells |
title_short | Hsp70 (HSP70A1A) downregulation enhances the metastatic ability of cancer cells |
title_sort | hsp70 (hsp70a1a) downregulation enhances the metastatic ability of cancer cells |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6365026/ https://www.ncbi.nlm.nih.gov/pubmed/30569142 http://dx.doi.org/10.3892/ijo.2018.4666 |
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