HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity

Autores
Prince, Thomas L.; Lang, Benjamin J.; Guerrero Gimenez, Martin Eduardo; Fernandez Muñoz, Juan Manuel; Ackerman, Andrew; Calderwood, Stuart K.
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Heat shock factor 1 (HSF1) is the primary component for initiation of the powerful heat shock response (HSR) in eukaryotes. The HSR is an evolutionarily conserved mechanism for responding to proteotoxic stress and involves the rapid expression of heat shock protein (HSP) molecular chaperones that promote cell viability by facilitating proteostasis. HSF1 activity is amplified in many tumor contexts in a manner that resembles a chronic state of stress, characterized by high levels of HSP gene expression as well as HSF1-mediated non-HSP gene regulation. HSF1 and its gene targets are essential for tumorigenesis across several experimental tumor models, and facilitate metastatic and resistant properties within cancer cells. Recent studies have suggested the significant potential of HSF1 as a therapeutic target and have motivated research efforts to understand the mechanisms of HSF1 regulation and develop methods for pharmacological intervention. We review what is currently known regarding the contribution of HSF1 activity to cancer pathology, its regulation and expression across human cancers, and strategies to target HSF1 for cancer therapy.
Fil: Prince, Thomas L.. Geisinger Clinic. Department of Molecular Functional Genomics; Estados Unidos
Fil: Lang, Benjamin J.. Harvard Medical School; Estados Unidos
Fil: Guerrero Gimenez, Martin Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina
Fil: Fernandez Muñoz, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina
Fil: Ackerman, Andrew. Geisinger Clinic. Department of Molecular Functional Genomics; Estados Unidos
Fil: Calderwood, Stuart K.. Harvard Medical School; Estados Unidos
Materia
CANCER
CANCER THERAPY
HEAT SHOCK FACTOR 1
HEAT SHOCK PROTEINS
HEAT SHOCK RESPONSE
HSF1
HSF1 EXPRESSION IN CANCER
HSF1 IN CANCER
HSPS
HSR
METASTASIS
MOLECULAR CHAPERONES
TUMORIGENESIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/126784
Acceder
id CONICETDig_1789498b11bd721d6f2c5a0e9ed59c59
oai_identifier_str oai:ri.conicet.gov.ar:11336/126784
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer MorbidityPrince, Thomas L.Lang, Benjamin J.Guerrero Gimenez, Martin EduardoFernandez Muñoz, Juan ManuelAckerman, AndrewCalderwood, Stuart K.CANCERCANCER THERAPYHEAT SHOCK FACTOR 1HEAT SHOCK PROTEINSHEAT SHOCK RESPONSEHSF1HSF1 EXPRESSION IN CANCERHSF1 IN CANCERHSPSHSRMETASTASISMOLECULAR CHAPERONESTUMORIGENESIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Heat shock factor 1 (HSF1) is the primary component for initiation of the powerful heat shock response (HSR) in eukaryotes. The HSR is an evolutionarily conserved mechanism for responding to proteotoxic stress and involves the rapid expression of heat shock protein (HSP) molecular chaperones that promote cell viability by facilitating proteostasis. HSF1 activity is amplified in many tumor contexts in a manner that resembles a chronic state of stress, characterized by high levels of HSP gene expression as well as HSF1-mediated non-HSP gene regulation. HSF1 and its gene targets are essential for tumorigenesis across several experimental tumor models, and facilitate metastatic and resistant properties within cancer cells. Recent studies have suggested the significant potential of HSF1 as a therapeutic target and have motivated research efforts to understand the mechanisms of HSF1 regulation and develop methods for pharmacological intervention. We review what is currently known regarding the contribution of HSF1 activity to cancer pathology, its regulation and expression across human cancers, and strategies to target HSF1 for cancer therapy.Fil: Prince, Thomas L.. Geisinger Clinic. Department of Molecular Functional Genomics; Estados UnidosFil: Lang, Benjamin J.. Harvard Medical School; Estados UnidosFil: Guerrero Gimenez, Martin Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; ArgentinaFil: Fernandez Muñoz, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; ArgentinaFil: Ackerman, Andrew. Geisinger Clinic. Department of Molecular Functional Genomics; Estados UnidosFil: Calderwood, Stuart K.. Harvard Medical School; Estados UnidosMDPI2020-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/126784Prince, Thomas L.; Lang, Benjamin J.; Guerrero Gimenez, Martin Eduardo; Fernandez Muñoz, Juan Manuel; Ackerman, Andrew; et al.; HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity; MDPI; Cells; 9; 4; 4-2020; 1-272073-4409CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4409/9/4/1046info:eu-repo/semantics/altIdentifier/doi/10.3390/cells9041046info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:41:01Zoai:ri.conicet.gov.ar:11336/126784instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:41:01.601CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
title HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
spellingShingle HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
Prince, Thomas L.
CANCER
CANCER THERAPY
HEAT SHOCK FACTOR 1
HEAT SHOCK PROTEINS
HEAT SHOCK RESPONSE
HSF1
HSF1 EXPRESSION IN CANCER
HSF1 IN CANCER
HSPS
HSR
METASTASIS
MOLECULAR CHAPERONES
TUMORIGENESIS
title_short HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
title_full HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
title_fullStr HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
title_full_unstemmed HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
title_sort HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity
dc.creator.none.fl_str_mv Prince, Thomas L.
Lang, Benjamin J.
Guerrero Gimenez, Martin Eduardo
Fernandez Muñoz, Juan Manuel
Ackerman, Andrew
Calderwood, Stuart K.
author Prince, Thomas L.
author_facet Prince, Thomas L.
Lang, Benjamin J.
Guerrero Gimenez, Martin Eduardo
Fernandez Muñoz, Juan Manuel
Ackerman, Andrew
Calderwood, Stuart K.
author_role author
author2 Lang, Benjamin J.
Guerrero Gimenez, Martin Eduardo
Fernandez Muñoz, Juan Manuel
Ackerman, Andrew
Calderwood, Stuart K.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv CANCER
CANCER THERAPY
HEAT SHOCK FACTOR 1
HEAT SHOCK PROTEINS
HEAT SHOCK RESPONSE
HSF1
HSF1 EXPRESSION IN CANCER
HSF1 IN CANCER
HSPS
HSR
METASTASIS
MOLECULAR CHAPERONES
TUMORIGENESIS
topic CANCER
CANCER THERAPY
HEAT SHOCK FACTOR 1
HEAT SHOCK PROTEINS
HEAT SHOCK RESPONSE
HSF1
HSF1 EXPRESSION IN CANCER
HSF1 IN CANCER
HSPS
HSR
METASTASIS
MOLECULAR CHAPERONES
TUMORIGENESIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Heat shock factor 1 (HSF1) is the primary component for initiation of the powerful heat shock response (HSR) in eukaryotes. The HSR is an evolutionarily conserved mechanism for responding to proteotoxic stress and involves the rapid expression of heat shock protein (HSP) molecular chaperones that promote cell viability by facilitating proteostasis. HSF1 activity is amplified in many tumor contexts in a manner that resembles a chronic state of stress, characterized by high levels of HSP gene expression as well as HSF1-mediated non-HSP gene regulation. HSF1 and its gene targets are essential for tumorigenesis across several experimental tumor models, and facilitate metastatic and resistant properties within cancer cells. Recent studies have suggested the significant potential of HSF1 as a therapeutic target and have motivated research efforts to understand the mechanisms of HSF1 regulation and develop methods for pharmacological intervention. We review what is currently known regarding the contribution of HSF1 activity to cancer pathology, its regulation and expression across human cancers, and strategies to target HSF1 for cancer therapy.
Fil: Prince, Thomas L.. Geisinger Clinic. Department of Molecular Functional Genomics; Estados Unidos
Fil: Lang, Benjamin J.. Harvard Medical School; Estados Unidos
Fil: Guerrero Gimenez, Martin Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina
Fil: Fernandez Muñoz, Juan Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Medicina y Biología Experimental de Cuyo; Argentina
Fil: Ackerman, Andrew. Geisinger Clinic. Department of Molecular Functional Genomics; Estados Unidos
Fil: Calderwood, Stuart K.. Harvard Medical School; Estados Unidos
description Heat shock factor 1 (HSF1) is the primary component for initiation of the powerful heat shock response (HSR) in eukaryotes. The HSR is an evolutionarily conserved mechanism for responding to proteotoxic stress and involves the rapid expression of heat shock protein (HSP) molecular chaperones that promote cell viability by facilitating proteostasis. HSF1 activity is amplified in many tumor contexts in a manner that resembles a chronic state of stress, characterized by high levels of HSP gene expression as well as HSF1-mediated non-HSP gene regulation. HSF1 and its gene targets are essential for tumorigenesis across several experimental tumor models, and facilitate metastatic and resistant properties within cancer cells. Recent studies have suggested the significant potential of HSF1 as a therapeutic target and have motivated research efforts to understand the mechanisms of HSF1 regulation and develop methods for pharmacological intervention. We review what is currently known regarding the contribution of HSF1 activity to cancer pathology, its regulation and expression across human cancers, and strategies to target HSF1 for cancer therapy.
publishDate 2020
dc.date.none.fl_str_mv 2020-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/126784
Prince, Thomas L.; Lang, Benjamin J.; Guerrero Gimenez, Martin Eduardo; Fernandez Muñoz, Juan Manuel; Ackerman, Andrew; et al.; HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity; MDPI; Cells; 9; 4; 4-2020; 1-27
2073-4409
CONICET Digital
CONICET
url http://hdl.handle.net/11336/126784
identifier_str_mv Prince, Thomas L.; Lang, Benjamin J.; Guerrero Gimenez, Martin Eduardo; Fernandez Muñoz, Juan Manuel; Ackerman, Andrew; et al.; HSF1: Primary Factor in Molecular Chaperone Expression and a Major Contributor to Cancer Morbidity; MDPI; Cells; 9; 4; 4-2020; 1-27
2073-4409
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4409/9/4/1046
info:eu-repo/semantics/altIdentifier/doi/10.3390/cells9041046
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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