Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets

<b>Background</b>: Upregulation of Heath Shock Protein 70 (HSP70) chaperones supports cancer cell survival. Their high homology causes a challenge to differentiate them in experimental or prevention and treatment strategies. The objective of this investigation was to determine similariti...

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Autores principales:	Rajani Rai, Amy L. Kennedy, Zitha Redempta Isingizwe, Pouya Javadian, Doris Mangiaracina Benbrook
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	Hsp70 hsc70 Grp78 mortalin chaperone cancer Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/c5d1c5e489af4d60bc96fcf6d3d211bc
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spelling	oai:doaj.org-article:c5d1c5e489af4d60bc96fcf6d3d211bc2021-11-25T17:10:13ZSimilarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets10.3390/cells101129962073-4409https://doaj.org/article/c5d1c5e489af4d60bc96fcf6d3d211bc2021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4409/10/11/2996https://doaj.org/toc/2073-4409<b>Background</b>: Upregulation of Heath Shock Protein 70 (HSP70) chaperones supports cancer cell survival. Their high homology causes a challenge to differentiate them in experimental or prevention and treatment strategies. The objective of this investigation was to determine similarities and differences of Hsp70, hsc70, Grp78 and Mortalin members of the HSP70 family encoded by <i>HSPA1</i>, <i>HSPA8</i>, <i>HSPA5</i> and <i>HSPA9</i> genes, respectively. <b>Methods:</b> Literature reviews were conducted using <i>HSPA1</i>, <i>HSPA5</i>, <i>HSPA8</i> and <i>HSPA9</i> gene or protein names or synonyms combined with biological or cancer-relevant terms. Ingenuity Pathway Analysis was used to identify and compare profiles of proteins that directly bind individual chaperones and their associated pathways. TCGA data was probed to identify associations of hsc70 with cancer patient survival. ClinicalTrials.gov was used to identify HSP70 family studies. <b>Results:</b> The chaperones have similar protein folding functions. Their different cellular effects are determined by co-chaperones and client proteins combined with their intra- and extra-cellular localizations. Their upregulation is associated with worse patient prognosis in multiple cancers and can stimulate tumor immune responses or drug resistance. Their inhibition selectively kills cancer over healthy cells. <b>Conclusions:</b> Differences in Hsp70, hsc70, Grp78 and mortalin provide opportunities to calibrate HSP70 inhibitors for individual cancers and combination therapies.Rajani RaiAmy L. KennedyZitha Redempta IsingizwePouya JavadianDoris Mangiaracina BenbrookMDPI AGarticleHsp70hsc70Grp78mortalinchaperonecancerBiology (General)QH301-705.5ENCells, Vol 10, Iss 2996, p 2996 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Hsp70 hsc70 Grp78 mortalin chaperone cancer Biology (General) QH301-705.5
spellingShingle	Hsp70 hsc70 Grp78 mortalin chaperone cancer Biology (General) QH301-705.5 Rajani Rai Amy L. Kennedy Zitha Redempta Isingizwe Pouya Javadian Doris Mangiaracina Benbrook Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets
description	<b>Background</b>: Upregulation of Heath Shock Protein 70 (HSP70) chaperones supports cancer cell survival. Their high homology causes a challenge to differentiate them in experimental or prevention and treatment strategies. The objective of this investigation was to determine similarities and differences of Hsp70, hsc70, Grp78 and Mortalin members of the HSP70 family encoded by <i>HSPA1</i>, <i>HSPA8</i>, <i>HSPA5</i> and <i>HSPA9</i> genes, respectively. <b>Methods:</b> Literature reviews were conducted using <i>HSPA1</i>, <i>HSPA5</i>, <i>HSPA8</i> and <i>HSPA9</i> gene or protein names or synonyms combined with biological or cancer-relevant terms. Ingenuity Pathway Analysis was used to identify and compare profiles of proteins that directly bind individual chaperones and their associated pathways. TCGA data was probed to identify associations of hsc70 with cancer patient survival. ClinicalTrials.gov was used to identify HSP70 family studies. <b>Results:</b> The chaperones have similar protein folding functions. Their different cellular effects are determined by co-chaperones and client proteins combined with their intra- and extra-cellular localizations. Their upregulation is associated with worse patient prognosis in multiple cancers and can stimulate tumor immune responses or drug resistance. Their inhibition selectively kills cancer over healthy cells. <b>Conclusions:</b> Differences in Hsp70, hsc70, Grp78 and mortalin provide opportunities to calibrate HSP70 inhibitors for individual cancers and combination therapies.
format	article
author	Rajani Rai Amy L. Kennedy Zitha Redempta Isingizwe Pouya Javadian Doris Mangiaracina Benbrook
author_facet	Rajani Rai Amy L. Kennedy Zitha Redempta Isingizwe Pouya Javadian Doris Mangiaracina Benbrook
author_sort	Rajani Rai
title	Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets
title_short	Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets
title_full	Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets
title_fullStr	Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets
title_full_unstemmed	Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets
title_sort	similarities and differences of hsp70, hsc70, grp78 and mortalin as cancer biomarkers and drug targets
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/c5d1c5e489af4d60bc96fcf6d3d211bc
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_version_	1718412676411949056

Similarities and Differences of Hsp70, hsc70, Grp78 and Mortalin as Cancer Biomarkers and Drug Targets

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