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Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease

Heat shock proteins 70 and heat shock proteins 90 (Hsp70/90) have been implicated in many crucial steps of carcinogenesis: stabilizing oncogenic proteins, inhibiting programmed cell death and replicative senescence, induction of tumor angiogenesis, and activation of the invasion and metastasis. Plen...

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Autores principales: Wang, Hao, Tan, Meng-Shan, Lu, Rui-Chun, Yu, Jin-Tai, Tan, Lan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4131517/
https://www.ncbi.nlm.nih.gov/pubmed/25147790
http://dx.doi.org/10.1155/2014/239164
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author Wang, Hao
Tan, Meng-Shan
Lu, Rui-Chun
Yu, Jin-Tai
Tan, Lan
author_facet Wang, Hao
Tan, Meng-Shan
Lu, Rui-Chun
Yu, Jin-Tai
Tan, Lan
author_sort Wang, Hao
collection PubMed
description Heat shock proteins 70 and heat shock proteins 90 (Hsp70/90) have been implicated in many crucial steps of carcinogenesis: stabilizing oncogenic proteins, inhibiting programmed cell death and replicative senescence, induction of tumor angiogenesis, and activation of the invasion and metastasis. Plenty of cancer related proteins have the ability of regulating the expression of Hsp70/90 through heat shock factor 1. Cancer and Alzheimer's disease (AD) have plenty of overlapping regions in molecular genetics and cell biology associated with Hsp70/90. The Hsp70, as a protein stabilizer, has a cellular protection against neurodegeneration of the central nervous system, while Hsp90 promote neurodegenerative disorders indirectly through regulating the expression of Hsp70 and other chaperones. All these make existing anticancer drugs target Hsp70/90 which might be used in AD therapy.
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spelling pubmed-41315172014-08-21 Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease Wang, Hao Tan, Meng-Shan Lu, Rui-Chun Yu, Jin-Tai Tan, Lan Biomed Res Int Review Article Heat shock proteins 70 and heat shock proteins 90 (Hsp70/90) have been implicated in many crucial steps of carcinogenesis: stabilizing oncogenic proteins, inhibiting programmed cell death and replicative senescence, induction of tumor angiogenesis, and activation of the invasion and metastasis. Plenty of cancer related proteins have the ability of regulating the expression of Hsp70/90 through heat shock factor 1. Cancer and Alzheimer's disease (AD) have plenty of overlapping regions in molecular genetics and cell biology associated with Hsp70/90. The Hsp70, as a protein stabilizer, has a cellular protection against neurodegeneration of the central nervous system, while Hsp90 promote neurodegenerative disorders indirectly through regulating the expression of Hsp70 and other chaperones. All these make existing anticancer drugs target Hsp70/90 which might be used in AD therapy. Hindawi Publishing Corporation 2014 2014-07-24 /pmc/articles/PMC4131517/ /pubmed/25147790 http://dx.doi.org/10.1155/2014/239164 Text en Copyright © 2014 Hao Wang et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Wang, Hao
Tan, Meng-Shan
Lu, Rui-Chun
Yu, Jin-Tai
Tan, Lan
Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
title Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
title_full Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
title_fullStr Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
title_full_unstemmed Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
title_short Heat Shock Proteins at the Crossroads between Cancer and Alzheimer's Disease
title_sort heat shock proteins at the crossroads between cancer and alzheimer's disease
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4131517/
https://www.ncbi.nlm.nih.gov/pubmed/25147790
http://dx.doi.org/10.1155/2014/239164
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