Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study
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...
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| Format: | Article |
| Language: | English |
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Alanya Alaaddin Keykubat University
2020-03-01
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| Series: | Acta Medica Alanya |
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| Online Access: | https://dergipark.org.tr/en/pub/medalanya/issue/52507/573983?publisher=alku |
| _version_ | 1797917201758420992 |
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| author | Nazlı Ece Gungor-ordueri̇ |
| author_facet | Nazlı Ece Gungor-ordueri̇ |
| author_sort | Nazlı Ece Gungor-ordueri̇ |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-10T13:09:38Z |
| format | Article |
| id | doaj.art-cac38ce4a4694040a53bbc9c32a4bf5d |
| institution | Directory Open Access Journal |
| issn | 2587-0319 |
| language | English |
| last_indexed | 2024-04-10T13:09:38Z |
| publishDate | 2020-03-01 |
| publisher | Alanya Alaaddin Keykubat University |
| record_format | Article |
| series | Acta Medica Alanya |
| spelling | doaj.art-cac38ce4a4694040a53bbc9c32a4bf5d2023-02-15T16:12:42ZengAlanya Alaaddin Keykubat UniversityActa Medica Alanya2587-03192020-03-0141162010.30565/medalanya.573983727Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro studyNazlı Ece Gungor-ordueri̇0BIRUNI UNIVERSITYAim: 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.https://dergipark.org.tr/en/pub/medalanya/issue/52507/573983?publisher=alkukan-testis bariyeriektoplazma özelleşmesif-aktinezrinfascin-1pfosblood-testis barrierectoplasmic specializationf-actinfascin-1pfos |
| spellingShingle | Nazlı Ece Gungor-ordueri̇ Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study Acta Medica Alanya kan-testis bariyeri ektoplazma özelleşmesi f-aktin ezrin fascin-1 pfos blood-testis barrier ectoplasmic specialization f-actin fascin-1 pfos |
| title | Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study |
| title_full | Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study |
| title_fullStr | Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study |
| title_full_unstemmed | Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study |
| title_short | Evaluation of ezrin and fascin 1 in the PFOS treated Sertoli cell culture: An in vitro study |
| title_sort | evaluation of ezrin and fascin 1 in the pfos treated sertoli cell culture an in vitro study |
| topic | kan-testis bariyeri ektoplazma özelleşmesi f-aktin ezrin fascin-1 pfos blood-testis barrier ectoplasmic specialization f-actin fascin-1 pfos |
| url | https://dergipark.org.tr/en/pub/medalanya/issue/52507/573983?publisher=alku |
| work_keys_str_mv | AT nazlıecegungorordueri evaluationofezrinandfascin1inthepfostreatedsertolicellcultureaninvitrostudy |