Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review

Detalhes bibliográficos
Autor(a) principal: Ribeiro, Daniel Araki
Data de Publicação: 2013
Outros Autores: Noguti, Juliana, César, Augusto, Pereira, Camilo Dias Seabra, Choueri, Rodrigo Brasil, Medalha, Carla Cristina, De Sá, Cristina dos Santos Cardoso, Dedivits, Rogério Aparecido, Barbisan, Luis Fernando [UNESP], Spadari-Bratfisch, Regina Celia
Tipo de documento: Capítulo de livro
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://hdl.handle.net/11449/227591
Resumo: Glutathione S-transferases (GSTs) are a family of crucial enzymes involved in the cell detoxification of xenobiotics. GSTs exist as homo- or hetero-dimers and have been grouped into at least seven distinct classes. The main function of GSTs is to catalyze the conjugation of reduced glutathione (GSH) to an electrophilic site of a broad range of potentially toxic and carcinogenic compounds, thereby making such compounds less dangerous and enabling their readily excretion. Placental GST, known as GST-P 7-7, is the main isoform in normal placental tissue and comprises 67% of the total GST concentration in this phase. During development, GST-P 7-7 decreases in concentration and is absent in adult tissues. Interestingly, GST-P-7-7-positive expression have been detected in adult tissues after exposure to carcinogenic agents in several experimental test-systems being, considered a reliable biomarker of exposure and susceptibility in early phases of carcinogenesis process. In this chapter, we review a series of studies involving GST-P 7-7 positive expression and cancer risk. © 2013 Nova Science Publishers, Inc. All rights reserved.
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spelling Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive reviewGlutathione S-transferases (GSTs) are a family of crucial enzymes involved in the cell detoxification of xenobiotics. GSTs exist as homo- or hetero-dimers and have been grouped into at least seven distinct classes. The main function of GSTs is to catalyze the conjugation of reduced glutathione (GSH) to an electrophilic site of a broad range of potentially toxic and carcinogenic compounds, thereby making such compounds less dangerous and enabling their readily excretion. Placental GST, known as GST-P 7-7, is the main isoform in normal placental tissue and comprises 67% of the total GST concentration in this phase. During development, GST-P 7-7 decreases in concentration and is absent in adult tissues. Interestingly, GST-P-7-7-positive expression have been detected in adult tissues after exposure to carcinogenic agents in several experimental test-systems being, considered a reliable biomarker of exposure and susceptibility in early phases of carcinogenesis process. In this chapter, we review a series of studies involving GST-P 7-7 positive expression and cancer risk. © 2013 Nova Science Publishers, Inc. All rights reserved.Department of Biosciences Federal University of Sao Paulo UNIFESP, Sao PauloDepartment of Human Moviment Science Federal University of Sao Paulo UNIFESP, Sao PauloDepartment of Head and Neck Surgery Ana Costa Hospital and Santa Casa Santos, Santos, Sao PauloInstitute of Biosciences Department of Morphology Sao Paulo State University, UNESP, Botucatu, Sao PauloInstitute of Biosciences Department of Morphology Sao Paulo State University, UNESP, Botucatu, Sao PauloUniversidade de São Paulo (USP)Ana Costa Hospital and Santa Casa SantosUniversidade Estadual Paulista (UNESP)Ribeiro, Daniel ArakiNoguti, JulianaCésar, AugustoPereira, Camilo Dias SeabraChoueri, Rodrigo BrasilMedalha, Carla CristinaDe Sá, Cristina dos Santos CardosoDedivits, Rogério AparecidoBarbisan, Luis Fernando [UNESP]Spadari-Bratfisch, Regina Celia2022-04-29T07:14:00Z2022-04-29T07:14:00Z2013-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookPart199-205Glutathione: Biochemistry, Mechanisms of Action and Biotechnological Implications, p. 199-205.http://hdl.handle.net/11449/2275912-s2.0-84895216478Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengGlutathione: Biochemistry, Mechanisms of Action and Biotechnological Implicationsinfo:eu-repo/semantics/openAccess2022-04-29T07:14:00Zoai:repositorio.unesp.br:11449/227591Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:52:36.203664Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
title Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
spellingShingle Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
Ribeiro, Daniel Araki
title_short Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
title_full Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
title_fullStr Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
title_full_unstemmed Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
title_sort Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
author Ribeiro, Daniel Araki
author_facet Ribeiro, Daniel Araki
Noguti, Juliana
César, Augusto
Pereira, Camilo Dias Seabra
Choueri, Rodrigo Brasil
Medalha, Carla Cristina
De Sá, Cristina dos Santos Cardoso
Dedivits, Rogério Aparecido
Barbisan, Luis Fernando [UNESP]
Spadari-Bratfisch, Regina Celia
author_role author
author2 Noguti, Juliana
César, Augusto
Pereira, Camilo Dias Seabra
Choueri, Rodrigo Brasil
Medalha, Carla Cristina
De Sá, Cristina dos Santos Cardoso
Dedivits, Rogério Aparecido
Barbisan, Luis Fernando [UNESP]
Spadari-Bratfisch, Regina Celia
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade de São Paulo (USP)
Ana Costa Hospital and Santa Casa Santos
Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Ribeiro, Daniel Araki
Noguti, Juliana
César, Augusto
Pereira, Camilo Dias Seabra
Choueri, Rodrigo Brasil
Medalha, Carla Cristina
De Sá, Cristina dos Santos Cardoso
Dedivits, Rogério Aparecido
Barbisan, Luis Fernando [UNESP]
Spadari-Bratfisch, Regina Celia
description Glutathione S-transferases (GSTs) are a family of crucial enzymes involved in the cell detoxification of xenobiotics. GSTs exist as homo- or hetero-dimers and have been grouped into at least seven distinct classes. The main function of GSTs is to catalyze the conjugation of reduced glutathione (GSH) to an electrophilic site of a broad range of potentially toxic and carcinogenic compounds, thereby making such compounds less dangerous and enabling their readily excretion. Placental GST, known as GST-P 7-7, is the main isoform in normal placental tissue and comprises 67% of the total GST concentration in this phase. During development, GST-P 7-7 decreases in concentration and is absent in adult tissues. Interestingly, GST-P-7-7-positive expression have been detected in adult tissues after exposure to carcinogenic agents in several experimental test-systems being, considered a reliable biomarker of exposure and susceptibility in early phases of carcinogenesis process. In this chapter, we review a series of studies involving GST-P 7-7 positive expression and cancer risk. © 2013 Nova Science Publishers, Inc. All rights reserved.
publishDate 2013
dc.date.none.fl_str_mv 2013-02-01
2022-04-29T07:14:00Z
2022-04-29T07:14:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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format bookPart
status_str publishedVersion
dc.identifier.uri.fl_str_mv Glutathione: Biochemistry, Mechanisms of Action and Biotechnological Implications, p. 199-205.
http://hdl.handle.net/11449/227591
2-s2.0-84895216478
identifier_str_mv Glutathione: Biochemistry, Mechanisms of Action and Biotechnological Implications, p. 199-205.
2-s2.0-84895216478
url http://hdl.handle.net/11449/227591
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Glutathione: Biochemistry, Mechanisms of Action and Biotechnological Implications
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv 199-205
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
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