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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.contributor.authorde Freitas, André Teves Aquino Gonçalves [UNESP]
dc.contributor.authorRibeiro, Mariana Antunes [UNESP]
dc.contributor.authorPinho, Cristiane Figueiredo [UNESP]
dc.contributor.authorPeixoto, André Rebelo [UNESP]
dc.contributor.authorDomeniconi, Raquel Fantin [UNESP]
dc.contributor.authorScarano, Wellerson R. [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2018-12-11T17:27:38Z
dc.date.available2018-12-11T17:27:38Z
dc.date.issued2016-08-01
dc.description.abstractThe 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.en
dc.description.affiliationInstitute of Biosciences UNESP
dc.description.affiliationDepartment of Anatomy Institute of Biosciences UNESP
dc.description.affiliationDepartment of Morphology Institute of Biosciences UNESP
dc.description.affiliationUnespInstitute of Biosciences UNESP
dc.description.affiliationUnespDepartment of Anatomy Institute of Biosciences UNESP
dc.description.affiliationUnespDepartment of Morphology Institute of Biosciences UNESP
dc.format.extent1-7
dc.identifierhttp://dx.doi.org/10.1016/j.tiv.2016.02.017
dc.identifier.citationToxicology in Vitro, v. 34, p. 1-7.
dc.identifier.doi10.1016/j.tiv.2016.02.017
dc.identifier.file2-s2.0-84961880678.pdf
dc.identifier.issn1879-3177
dc.identifier.issn0887-2333
dc.identifier.lattes5481756528299469
dc.identifier.orcid0000-0003-2938-010X
dc.identifier.scopus2-s2.0-84961880678
dc.identifier.urihttp://hdl.handle.net/11449/177908
dc.language.isoeng
dc.relation.ispartofToxicology in Vitro
dc.relation.ispartofsjr0,931
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subject(HSeC) Human Sertoli cells
dc.subjectBisphenol A
dc.subjectBlood-testis barrier
dc.subjectEndocrine disruptors
dc.subjectMale reproductive function
dc.subjectMonobutyl phthalate
dc.titleRegulatory and junctional proteins of the blood-testis barrier in human Sertoli cells are modified by monobutyl phthalate (MBP) and bisphenol A (BPA) exposureen
dc.typeArtigo
dspace.entity.typePublication
unesp.author.lattes5481756528299469[5]
unesp.author.orcid0000-0003-2938-010X[5]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Botucatupt
unesp.departmentAnatomia - IBBpt

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