The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes
Aquaglyceroporins are known as channel proteins, and are able to transport water and small neutral solutes. In this study, we evaluate the effect of exposure of in vitro matured bovine oocytes to hyperosmotic solutions containing ethylene glycol (EG), dimethyl sulfoxide (Me<sub>2</sub>SO...
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| Format: | Article |
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MDPI AG
2022-02-01
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| Series: | Animals |
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| Online Access: | https://www.mdpi.com/2076-2615/12/4/530 |
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| author | Tania García-Martínez Iris Martínez-Rodero Joan Roncero-Carol Meritxell Vendrell-Flotats Jaume Gardela Alfonso Gutiérrez-Adán Priscila Ramos-Ibeas Adam Z. Higgins Teresa Mogas |
| author_facet | Tania García-Martínez Iris Martínez-Rodero Joan Roncero-Carol Meritxell Vendrell-Flotats Jaume Gardela Alfonso Gutiérrez-Adán Priscila Ramos-Ibeas Adam Z. Higgins Teresa Mogas |
| author_sort | Tania García-Martínez |
| collection | DOAJ |
| description | Aquaglyceroporins are known as channel proteins, and are able to transport water and small neutral solutes. In this study, we evaluate the effect of exposure of in vitro matured bovine oocytes to hyperosmotic solutions containing ethylene glycol (EG), dimethyl sulfoxide (Me<sub>2</sub>SO) or sucrose on the expression levels of AQP3, AQP7 and AQP9. Moreover, we studied whether artificial protein expression of AQP7 in bovine oocytes increases their permeability to water and cryoprotectants. Exposure to hyperosmotic solutions stimulated AQP3 and AQP7 but not AQP9 expression. Oocytes exposed to hyperosmotic Me<sub>2</sub>SO solution exhibited upregulated AQP3 expression, while AQP7 expression was upregulated by EG hyperosmotic exposure. Microinjection of oocytes at the germinal vesicle stage with enhanced green fluorescent protein (EGFP) or EGFP+AQP7 cRNAs resulted in the expression of the corresponding proteins in ≈86% of the metaphase-II stage oocytes. AQP7 facilitated water diffusion when bovine MII oocytes were in presence of Me<sub>2</sub>SO solution but not EG or sucrose solution. However, the overexpression of this aquaporin did not increase membrane permeability to Me<sub>2</sub>SO or EG. In summary, cryoprotectant-induced increase of AQP3 and AQP7 expression could be one of the mechanisms underlying oocyte tolerance to hyperosmotic stress. Water diffusion appears to be improved when AQP7 overexpressed oocytes are exposed to Me<sub>2</sub>SO, shortening the time required for oocytes to achieve osmotic balance with cryoprotectant solutions. |
| first_indexed | 2024-03-09T22:47:20Z |
| format | Article |
| id | doaj.art-5a427976b22742df9bb569d0b39bb88f |
| institution | Directory Open Access Journal |
| issn | 2076-2615 |
| language | English |
| last_indexed | 2024-03-09T22:47:20Z |
| publishDate | 2022-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Animals |
| spelling | doaj.art-5a427976b22742df9bb569d0b39bb88f2023-11-23T18:26:43ZengMDPI AGAnimals2076-26152022-02-0112453010.3390/ani12040530The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured OocytesTania García-Martínez0Iris Martínez-Rodero1Joan Roncero-Carol2Meritxell Vendrell-Flotats3Jaume Gardela4Alfonso Gutiérrez-Adán5Priscila Ramos-Ibeas6Adam Z. Higgins7Teresa Mogas8Department of Animal Medicine and Surgery, Autonomous University of Barcelona, ES-08193 Cerdanyola del Vallès, SpainDepartment of Animal Medicine and Surgery, Autonomous University of Barcelona, ES-08193 Cerdanyola del Vallès, SpainDepartment of Animal Medicine and Surgery, Autonomous University of Barcelona, ES-08193 Cerdanyola del Vallès, SpainDepartment of Animal Medicine and Surgery, Autonomous University of Barcelona, ES-08193 Cerdanyola del Vallès, SpainDepartment of Animal Health and Anatomy, Autonomous University of Barcelona, ES-08193 Cerdanyola del Vallès, SpainDepartment of Animal Reproduction, National Institute for Agriculture and Food Research and Technology (INIA), Avda. Puerta de Hierro 12, Local 10, 28040 Madrid, SpainDepartment of Animal Reproduction, National Institute for Agriculture and Food Research and Technology (INIA), Avda. Puerta de Hierro 12, Local 10, 28040 Madrid, SpainSchool of Chemical, Biological and Environmental Engineering, Oregon State University, Corvallis, OR 97331-2702, USADepartment of Animal Medicine and Surgery, Autonomous University of Barcelona, ES-08193 Cerdanyola del Vallès, SpainAquaglyceroporins are known as channel proteins, and are able to transport water and small neutral solutes. In this study, we evaluate the effect of exposure of in vitro matured bovine oocytes to hyperosmotic solutions containing ethylene glycol (EG), dimethyl sulfoxide (Me<sub>2</sub>SO) or sucrose on the expression levels of AQP3, AQP7 and AQP9. Moreover, we studied whether artificial protein expression of AQP7 in bovine oocytes increases their permeability to water and cryoprotectants. Exposure to hyperosmotic solutions stimulated AQP3 and AQP7 but not AQP9 expression. Oocytes exposed to hyperosmotic Me<sub>2</sub>SO solution exhibited upregulated AQP3 expression, while AQP7 expression was upregulated by EG hyperosmotic exposure. Microinjection of oocytes at the germinal vesicle stage with enhanced green fluorescent protein (EGFP) or EGFP+AQP7 cRNAs resulted in the expression of the corresponding proteins in ≈86% of the metaphase-II stage oocytes. AQP7 facilitated water diffusion when bovine MII oocytes were in presence of Me<sub>2</sub>SO solution but not EG or sucrose solution. However, the overexpression of this aquaporin did not increase membrane permeability to Me<sub>2</sub>SO or EG. In summary, cryoprotectant-induced increase of AQP3 and AQP7 expression could be one of the mechanisms underlying oocyte tolerance to hyperosmotic stress. Water diffusion appears to be improved when AQP7 overexpressed oocytes are exposed to Me<sub>2</sub>SO, shortening the time required for oocytes to achieve osmotic balance with cryoprotectant solutions.https://www.mdpi.com/2076-2615/12/4/530cell membrane permeabilitycryoprotective agentsartificial protein expressionaquaporin 3aquaporin 9cryopreservation |
| spellingShingle | Tania García-Martínez Iris Martínez-Rodero Joan Roncero-Carol Meritxell Vendrell-Flotats Jaume Gardela Alfonso Gutiérrez-Adán Priscila Ramos-Ibeas Adam Z. Higgins Teresa Mogas The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes Animals cell membrane permeability cryoprotective agents artificial protein expression aquaporin 3 aquaporin 9 cryopreservation |
| title | The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes |
| title_full | The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes |
| title_fullStr | The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes |
| title_full_unstemmed | The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes |
| title_short | The Role of Aquaporin 7 in the Movement of Water and Cryoprotectants in Bovine In Vitro Matured Oocytes |
| title_sort | role of aquaporin 7 in the movement of water and cryoprotectants in bovine in vitro matured oocytes |
| topic | cell membrane permeability cryoprotective agents artificial protein expression aquaporin 3 aquaporin 9 cryopreservation |
| url | https://www.mdpi.com/2076-2615/12/4/530 |
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