Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure

The blood-testis barrier (BTB) is responsible for providing a protected environment and coordinating the spermatogenesis. Endocrine disruptors (EDs) might lead to infertility, interfering in the BTB structure and modulation. This study aimed to correlate the actions of two EDs, monobutyl phthalate (...

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Autores: de Freitas, André Teves Aquino Gonçalves [UNESP], Ribeiro, Mariana Antunes [UNESP], Pinho, Cristiane Figueiredo [UNESP], Peixoto, André Rebelo [UNESP], Domeniconi, Raquel Fantin [UNESP], Scarano, Wellerson R. [UNESP]
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2016
País:Brasil
Institución:Universidade Estadual Paulista (UNESP)
Repositorio:Repositório Institucional da UNESP
Idioma:inglés
OAI Identifier:oai:repositorio.unesp.br:11449/177908
Acceso en línea:http://dx.doi.org/10.1016/j.tiv.2016.02.017
http://hdl.handle.net/11449/177908
Access Level:acceso abierto
Palabra clave:(HSeC) Human Sertoli cells
Bisphenol A
Blood-testis barrier
Endocrine disruptors
Male reproductive function
Monobutyl phthalate
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spelling Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure(HSeC) Human Sertoli cellsBisphenol ABlood-testis barrierEndocrine disruptorsMale reproductive functionMonobutyl phthalateThe blood-testis barrier (BTB) is responsible for providing a protected environment and coordinating the spermatogenesis. Endocrine disruptors (EDs) might lead to infertility, interfering in the BTB structure and modulation. This study aimed to correlate the actions of two EDs, monobutyl phthalate (MBP) and bisphenol A (BPA) in different periods of exposure, in a low toxicity dose to the human Sertoli cells (HSeC) and its effects on the proteins of the BTB and regulatory proteins involved in its modulation. HSeC cells were exposed to MBP (10 μM) and BPA (20 μM) for 6 and 48 h. Western Blot assay indicated that MBP was able to reduce the expression of occludin, ZO-1, N-cadherin and Androgen Receptor (AR), while BPA leads to a reduction of occludin, ZO-1, β-catenin and AR. TGF-β2 and F-actin were not modified. Phalloidin and Hematoxylin and Eosin assay revealed phenotically disruption in Sertoli cells adhesion, without changes in F-actin expression or localization. Our data suggested both EDs present potential for disrupting the structure and maintenance of the human BTB by AR dependent pathway.Institute of Biosciences UNESPDepartment of Anatomy Institute of Biosciences UNESPDepartment of Morphology Institute of Biosciences UNESPInstitute of Biosciences UNESPDepartment of Anatomy Institute of Biosciences UNESPDepartment of Morphology Institute of Biosciences UNESPUniversidade Estadual Paulista (Unesp)2018-12-11T17:27:38Z2018-12-11T17:27:38Z2016-08-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1-7application/pdfhttp://dx.doi.org/10.1016/j.tiv.2016.02.017Toxicology in Vitro, v. 34, p. 1-7.1879-31770887-2333http://hdl.handle.net/11449/17790810.1016/j.tiv.2016.02.0172-s2.0-849618806782-s2.0-84961880678.pdf54817565282994690000-0003-2938-010XScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengToxicology in Vitro0,931info:eu-repo/semantics/openAccessde Freitas, André Teves Aquino Gonçalves [UNESP]Ribeiro, Mariana Antunes [UNESP]Pinho, Cristiane Figueiredo [UNESP]Peixoto, André Rebelo [UNESP]Domeniconi, Raquel Fantin [UNESP]Scarano, Wellerson R. [UNESP]2025-10-24T04:00:33Zoai:repositorio.unesp.br:11449/177908Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462025-10-24T04:00:33Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
title Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
spellingShingle Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
de Freitas, André Teves Aquino Gonçalves [UNESP]
(HSeC) Human Sertoli cells
Bisphenol A
Blood-testis barrier
Endocrine disruptors
Male reproductive function
Monobutyl phthalate
title_short Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
title_full Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
title_fullStr Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
title_full_unstemmed Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
title_sort Regulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposure
dc.creator.none.fl_str_mv de Freitas, André Teves Aquino Gonçalves [UNESP]
Ribeiro, Mariana Antunes [UNESP]
Pinho, Cristiane Figueiredo [UNESP]
Peixoto, André Rebelo [UNESP]
Domeniconi, Raquel Fantin [UNESP]
Scarano, Wellerson R. [UNESP]
author de Freitas, André Teves Aquino Gonçalves [UNESP]
author_facet de Freitas, André Teves Aquino Gonçalves [UNESP]
Ribeiro, Mariana Antunes [UNESP]
Pinho, Cristiane Figueiredo [UNESP]
Peixoto, André Rebelo [UNESP]
Domeniconi, Raquel Fantin [UNESP]
Scarano, Wellerson R. [UNESP]
author_role author
author2 Ribeiro, Mariana Antunes [UNESP]
Pinho, Cristiane Figueiredo [UNESP]
Peixoto, André Rebelo [UNESP]
Domeniconi, Raquel Fantin [UNESP]
Scarano, Wellerson R. [UNESP]
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.subject.por.fl_str_mv (HSeC) Human Sertoli cells
Bisphenol A
Blood-testis barrier
Endocrine disruptors
Male reproductive function
Monobutyl phthalate
topic (HSeC) Human Sertoli cells
Bisphenol A
Blood-testis barrier
Endocrine disruptors
Male reproductive function
Monobutyl phthalate
description The blood-testis barrier (BTB) is responsible for providing a protected environment and coordinating the spermatogenesis. Endocrine disruptors (EDs) might lead to infertility, interfering in the BTB structure and modulation. This study aimed to correlate the actions of two EDs, monobutyl phthalate (MBP) and bisphenol A (BPA) in different periods of exposure, in a low toxicity dose to the human Sertoli cells (HSeC) and its effects on the proteins of the BTB and regulatory proteins involved in its modulation. HSeC cells were exposed to MBP (10 μM) and BPA (20 μM) for 6 and 48 h. Western Blot assay indicated that MBP was able to reduce the expression of occludin, ZO-1, N-cadherin and Androgen Receptor (AR), while BPA leads to a reduction of occludin, ZO-1, β-catenin and AR. TGF-β2 and F-actin were not modified. Phalloidin and Hematoxylin and Eosin assay revealed phenotically disruption in Sertoli cells adhesion, without changes in F-actin expression or localization. Our data suggested both EDs present potential for disrupting the structure and maintenance of the human BTB by AR dependent pathway.
publishDate 2016
dc.date.none.fl_str_mv 2016-08-01
2018-12-11T17:27:38Z
2018-12-11T17:27:38Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.tiv.2016.02.017
Toxicology in Vitro, v. 34, p. 1-7.
1879-3177
0887-2333
http://hdl.handle.net/11449/177908
10.1016/j.tiv.2016.02.017
2-s2.0-84961880678
2-s2.0-84961880678.pdf
5481756528299469
0000-0003-2938-010X
url http://dx.doi.org/10.1016/j.tiv.2016.02.017
http://hdl.handle.net/11449/177908
identifier_str_mv Toxicology in Vitro, v. 34, p. 1-7.
1879-3177
0887-2333
10.1016/j.tiv.2016.02.017
2-s2.0-84961880678
2-s2.0-84961880678.pdf
5481756528299469
0000-0003-2938-010X
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Toxicology in Vitro
0,931
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1-7
application/pdf
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 repositoriounesp@unesp.br
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score 15.300724

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