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The Complex Function of Hsp70 in Metastatic Cancer

Elevated expression of the inducible heat shock protein 70 (Hsp70) is known to correlate with poor prognosis in many cancers. Hsp70 confers survival advantage as well as resistance to chemotherapeutic agents, and promotes tumor cell invasion. At the same time, tumor-derived extracellular Hsp70 has b...

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Autores principales: Juhasz, Kata, Lipp, Anna-Maria, Nimmervoll, Benedikt, Sonnleitner, Alois, Hesse, Jan, Haselgruebler, Thomas, Balogi, Zsolt
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3980608/
https://www.ncbi.nlm.nih.gov/pubmed/24362507
http://dx.doi.org/10.3390/cancers6010042
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author Juhasz, Kata
Lipp, Anna-Maria
Nimmervoll, Benedikt
Sonnleitner, Alois
Hesse, Jan
Haselgruebler, Thomas
Balogi, Zsolt
author_facet Juhasz, Kata
Lipp, Anna-Maria
Nimmervoll, Benedikt
Sonnleitner, Alois
Hesse, Jan
Haselgruebler, Thomas
Balogi, Zsolt
author_sort Juhasz, Kata
collection PubMed
description Elevated expression of the inducible heat shock protein 70 (Hsp70) is known to correlate with poor prognosis in many cancers. Hsp70 confers survival advantage as well as resistance to chemotherapeutic agents, and promotes tumor cell invasion. At the same time, tumor-derived extracellular Hsp70 has been recognized as a “chaperokine”, activating antitumor immunity. In this review we discuss localization dependent functions of Hsp70 in the context of invasive cancer. Understanding the molecular principles of metastasis formation steps, as well as interactions of the tumor cells with the microenvironment and the immune system is essential for fighting metastatic cancer. Although Hsp70 has been implicated in different steps of the metastatic process, the exact mechanisms of its action remain to be explored. Known and potential functions of Hsp70 in controlling or modulating of invasion and metastasis are discussed.
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spelling pubmed-39806082014-04-09 The Complex Function of Hsp70 in Metastatic Cancer Juhasz, Kata Lipp, Anna-Maria Nimmervoll, Benedikt Sonnleitner, Alois Hesse, Jan Haselgruebler, Thomas Balogi, Zsolt Cancers (Basel) Review Elevated expression of the inducible heat shock protein 70 (Hsp70) is known to correlate with poor prognosis in many cancers. Hsp70 confers survival advantage as well as resistance to chemotherapeutic agents, and promotes tumor cell invasion. At the same time, tumor-derived extracellular Hsp70 has been recognized as a “chaperokine”, activating antitumor immunity. In this review we discuss localization dependent functions of Hsp70 in the context of invasive cancer. Understanding the molecular principles of metastasis formation steps, as well as interactions of the tumor cells with the microenvironment and the immune system is essential for fighting metastatic cancer. Although Hsp70 has been implicated in different steps of the metastatic process, the exact mechanisms of its action remain to be explored. Known and potential functions of Hsp70 in controlling or modulating of invasion and metastasis are discussed. MDPI 2013-12-20 /pmc/articles/PMC3980608/ /pubmed/24362507 http://dx.doi.org/10.3390/cancers6010042 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Juhasz, Kata
Lipp, Anna-Maria
Nimmervoll, Benedikt
Sonnleitner, Alois
Hesse, Jan
Haselgruebler, Thomas
Balogi, Zsolt
The Complex Function of Hsp70 in Metastatic Cancer
title The Complex Function of Hsp70 in Metastatic Cancer
title_full The Complex Function of Hsp70 in Metastatic Cancer
title_fullStr The Complex Function of Hsp70 in Metastatic Cancer
title_full_unstemmed The Complex Function of Hsp70 in Metastatic Cancer
title_short The Complex Function of Hsp70 in Metastatic Cancer
title_sort complex function of hsp70 in metastatic cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3980608/
https://www.ncbi.nlm.nih.gov/pubmed/24362507
http://dx.doi.org/10.3390/cancers6010042
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