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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Detalles Bibliográficos
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
Descripción
Sumario: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.