In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis

Detalhes bibliográficos
Autor(a) principal: Noguti, Juliana [UNIFESP]
Data de Publicação: 2012
Outros Autores: Barbisan, Luis Fernando, Cesar, Augusto [UNIFESP], Pereira, Camilo Dias Seabra [UNIFESP], Choueri, Rodrigo Brasil [UNIFESP], Ribeiro, Daniel Araki [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://iv.iiarjournals.org/content/26/4/647.full
http://repositorio.unifesp.br/handle/11600/43917
Resumo: The Glutatione-S-transferases (GSTs) comprise a family of enzymes closely associated with the cell detoxification of xenobiotics. GSTs exist as homo- or heterodimers 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 ready-excretion. Placental GST, known as GST-P 7-7, is the main isoform found in normal placental tissue and comprises 67% of the total GST concentration in this tissue. During development, GST-P 7-7 decreases in concentration and is absent in adult tissues. Interestingly, GST-P 7-7 expression has 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. In this article, we review a series of studies involving GST-P 7-7 expression as a suitable tool for understanding cancer pathogenesis, especially cancer risk.
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spelling In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer PathogenesisCancerin vivo modelsGST-P 7-7reviewThe Glutatione-S-transferases (GSTs) comprise a family of enzymes closely associated with the cell detoxification of xenobiotics. GSTs exist as homo- or heterodimers 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 ready-excretion. Placental GST, known as GST-P 7-7, is the main isoform found in normal placental tissue and comprises 67% of the total GST concentration in this tissue. During development, GST-P 7-7 decreases in concentration and is absent in adult tissues. Interestingly, GST-P 7-7 expression has 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. In this article, we review a series of studies involving GST-P 7-7 expression as a suitable tool for understanding cancer pathogenesis, especially cancer risk.Univ Fed Sao Paulo, Univ Fed Sao Paulo, Dept Biosci, Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Univ Fed Sao Paulo, Dept Pathol, Sao Paulo, SP, BrazilUNESP, Sao Paulo State Univ, Dept Morphol, Inst Biosci, Botucatu, SP, BrazilUniv Fed Sao Paulo, Univ Fed Sao Paulo, Dept Biosci, Sao Paulo, SP, BrazilUniv Fed Sao Paulo, Univ Fed Sao Paulo, Dept Pathol, Sao Paulo, SP, BrazilWeb of ScienceInt Inst Anticancer ResearchUniversidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Noguti, Juliana [UNIFESP]Barbisan, Luis FernandoCesar, Augusto [UNIFESP]Pereira, Camilo Dias Seabra [UNIFESP]Choueri, Rodrigo Brasil [UNIFESP]Ribeiro, Daniel Araki [UNIFESP]2018-06-15T17:38:31Z2018-06-15T17:38:31Z2012-07-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion647-650http://iv.iiarjournals.org/content/26/4/647.fullIn Vivo. Athens: Int Inst Anticancer Research, v. 26, n. 4, p. 647-650, 2012.0258-851Xhttp://repositorio.unifesp.br/handle/11600/43917WOS:000306397000018engIn Vivoinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-04-26T11:27:23Zoai:repositorio.unifesp.br/:11600/43917Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-04-26T11:27:23Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
title In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
spellingShingle In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
Noguti, Juliana [UNIFESP]
Cancer
in vivo models
GST-P 7-7
review
title_short In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
title_full In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
title_fullStr In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
title_full_unstemmed In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
title_sort In Vivo Models for Measuring Placental Glutatione-S-transferase (GST-P 7-7) Levels: A Suitable Biomarker for Understanding Cancer Pathogenesis
author Noguti, Juliana [UNIFESP]
author_facet Noguti, Juliana [UNIFESP]
Barbisan, Luis Fernando
Cesar, Augusto [UNIFESP]
Pereira, Camilo Dias Seabra [UNIFESP]
Choueri, Rodrigo Brasil [UNIFESP]
Ribeiro, Daniel Araki [UNIFESP]
author_role author
author2 Barbisan, Luis Fernando
Cesar, Augusto [UNIFESP]
Pereira, Camilo Dias Seabra [UNIFESP]
Choueri, Rodrigo Brasil [UNIFESP]
Ribeiro, Daniel Araki [UNIFESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Noguti, Juliana [UNIFESP]
Barbisan, Luis Fernando
Cesar, Augusto [UNIFESP]
Pereira, Camilo Dias Seabra [UNIFESP]
Choueri, Rodrigo Brasil [UNIFESP]
Ribeiro, Daniel Araki [UNIFESP]
dc.subject.por.fl_str_mv Cancer
in vivo models
GST-P 7-7
review
topic Cancer
in vivo models
GST-P 7-7
review
description The Glutatione-S-transferases (GSTs) comprise a family of enzymes closely associated with the cell detoxification of xenobiotics. GSTs exist as homo- or heterodimers 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 ready-excretion. Placental GST, known as GST-P 7-7, is the main isoform found in normal placental tissue and comprises 67% of the total GST concentration in this tissue. During development, GST-P 7-7 decreases in concentration and is absent in adult tissues. Interestingly, GST-P 7-7 expression has 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. In this article, we review a series of studies involving GST-P 7-7 expression as a suitable tool for understanding cancer pathogenesis, especially cancer risk.
publishDate 2012
dc.date.none.fl_str_mv 2012-07-01
2018-06-15T17:38:31Z
2018-06-15T17:38:31Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://iv.iiarjournals.org/content/26/4/647.full
In Vivo. Athens: Int Inst Anticancer Research, v. 26, n. 4, p. 647-650, 2012.
0258-851X
http://repositorio.unifesp.br/handle/11600/43917
WOS:000306397000018
url http://iv.iiarjournals.org/content/26/4/647.full
http://repositorio.unifesp.br/handle/11600/43917
identifier_str_mv In Vivo. Athens: Int Inst Anticancer Research, v. 26, n. 4, p. 647-650, 2012.
0258-851X
WOS:000306397000018
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv In Vivo
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 647-650
dc.publisher.none.fl_str_mv Int Inst Anticancer Research
publisher.none.fl_str_mv Int Inst Anticancer Research
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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