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Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets

Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from t...

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Detalles Bibliográficos
Autores principales: Shevtsov, Maxim, Balogi, Zsolt, Khachatryan, William, Gao, Huile, Vígh, László, Multhoff, Gabriele
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7290778/
https://www.ncbi.nlm.nih.gov/pubmed/32443761
http://dx.doi.org/10.3390/cells9051263
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author Shevtsov, Maxim
Balogi, Zsolt
Khachatryan, William
Gao, Huile
Vígh, László
Multhoff, Gabriele
author_facet Shevtsov, Maxim
Balogi, Zsolt
Khachatryan, William
Gao, Huile
Vígh, László
Multhoff, Gabriele
author_sort Shevtsov, Maxim
collection PubMed
description Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics.
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spelling pubmed-72907782020-06-17 Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets Shevtsov, Maxim Balogi, Zsolt Khachatryan, William Gao, Huile Vígh, László Multhoff, Gabriele Cells Review Heat shock proteins (HSPs) constitute a large family of conserved proteins acting as molecular chaperones that play a key role in intracellular protein homeostasis, regulation of apoptosis, and protection from various stress factors (including hypoxia, thermal stress, oxidative stress). Apart from their intracellular localization, members of different HSP families such as small HSPs, HSP40, HSP60, HSP70 and HSP90 have been found to be localized on the plasma membrane of malignantly transformed cells. In the current article, the role of membrane-associated molecular chaperones in normal and tumor cells is comprehensively reviewed with implications of these proteins as plausible targets for cancer therapy and diagnostics. MDPI 2020-05-20 /pmc/articles/PMC7290778/ /pubmed/32443761 http://dx.doi.org/10.3390/cells9051263 Text en © 2020 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
Shevtsov, Maxim
Balogi, Zsolt
Khachatryan, William
Gao, Huile
Vígh, László
Multhoff, Gabriele
Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
title Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
title_full Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
title_fullStr Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
title_full_unstemmed Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
title_short Membrane-Associated Heat Shock Proteins in Oncology: From Basic Research to New Theranostic Targets
title_sort membrane-associated heat shock proteins in oncology: from basic research to new theranostic targets
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7290778/
https://www.ncbi.nlm.nih.gov/pubmed/32443761
http://dx.doi.org/10.3390/cells9051263
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