Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study

Abstract

Aim: Depending on the findings resulting from the knock-downing of ezrin and of fascin 1 in vivo, we aim to show the defects or disruption of the blood-testis barrier (BTB) structure and F-actin bundling after Perfluorooctanesulfonate (PFOS) treatment in primary Sertoli cell culture. Methods: Study Design: Primary Sertoli cell isolation was occurred with control and PFOS-treated (20M) groups. Sertoli cells were prepared for both experiments as 0.5 x 106 cell/ml. Method: Dual-labeled immunofluorescence analysis to assess co-localization of fascin 1 with ezrin both in Sertoli cells was performed, and Co-IP, by using lysates of seminiferous tubules, was performed using actin and ezrin proteins to identify specific protein-protein interaction with fascin 1. Results: Firstly, we showed that ezrin and fascin 1, which were components of the ectoplasmic specialization were co-localized in the Sertoli cells and also they were interacted each other. Secondly, we indicated that they were dislocated in the PFOS-treated Sertoli cells in vitro. Because of PFOS (20M), the actin-based cytoskeleton was no longer capable of supporting the distribution and/or localization of actin-regulatory proteins at the cell-cell interface necessary to maintain localization of actin-regulatory at the BTB.Conclusion: In summary, these findings suggest that ezrin and fascin 1 can work together to preserve BTB integrity by regulating F-actin organization in the PFOS-mediated Sertoli cell disruption.

Keywords

• kan-testis bariyeri
• ektoplazma özelleşmesi
• f-aktin
• ezrin
• fascin-1
• pfos
• blood-testis barrier
• ectoplasmic specialization
• f-actin
• fascin-1
• pfos