Risk of cancer associated with measures of placental glutathione S-transferase (GST-P 7-7): A comprehensive review
Autor(a) principal: | |
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Data de Publicação: | 2013 |
Outros Autores: | , , , , , , , , |
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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Repositório Institucional da UNESP |
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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 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/bookPart |
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 |
eu_rights_str_mv |
openAccess |
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) |
repository.mail.fl_str_mv |
|
_version_ |
1808129560903942144 |