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Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development
Mammalian oocyte asymmetric division relies on the eccentric positioning of the spindle, resulting in the polar body formation. Small signaling G protein Rac1 is a member of GTPases, which regulates a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5046063/ https://www.ncbi.nlm.nih.gov/pubmed/27694954 http://dx.doi.org/10.1038/srep34415 |
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author | Song, Si-Jing Wang, Qiao-Chu Jia, Ru-Xia Cui, Xiang-Shun Kim, Nam-Hyung Sun, Shao-Chen |
author_facet | Song, Si-Jing Wang, Qiao-Chu Jia, Ru-Xia Cui, Xiang-Shun Kim, Nam-Hyung Sun, Shao-Chen |
author_sort | Song, Si-Jing |
collection | PubMed |
description | Mammalian oocyte asymmetric division relies on the eccentric positioning of the spindle, resulting in the polar body formation. Small signaling G protein Rac1 is a member of GTPases, which regulates a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. However, effects of Rac1 on the porcine oocyte maturation and early embryo development are not fully understood. In present study we investigated the role of Rac1 in oocyte maturation and embryo cleavage. We first found that Rac1 localized at the cortex of the porcine oocytes, and disrupting the Rac1 activities by treating with NSC 23766 led to the failure of polar body emission. In addition, a majority of treated oocytes exhibited abnormal spindle morphology, indicating that Rac1 may involve into porcine oocyte spindle formation. This might be due to the regulation of Rac1 on MAPK, since p-MAPK expression decreased after NSC 23766 treatments. Moreover, we found that the position of most meiotic spindles in treated oocytes were away from the cortex, indicating the roles of Rac1 on meiotic spindle positioning. Our results also showed that inhibition of Rac1 activity caused the failure of early embryo development. Therefore, our study showed the critical roles of Rac1 GTPase on porcine oocyte maturation and early embryo cleavage. |
format | Online Article Text |
id | pubmed-5046063 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-50460632016-10-11 Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development Song, Si-Jing Wang, Qiao-Chu Jia, Ru-Xia Cui, Xiang-Shun Kim, Nam-Hyung Sun, Shao-Chen Sci Rep Article Mammalian oocyte asymmetric division relies on the eccentric positioning of the spindle, resulting in the polar body formation. Small signaling G protein Rac1 is a member of GTPases, which regulates a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. However, effects of Rac1 on the porcine oocyte maturation and early embryo development are not fully understood. In present study we investigated the role of Rac1 in oocyte maturation and embryo cleavage. We first found that Rac1 localized at the cortex of the porcine oocytes, and disrupting the Rac1 activities by treating with NSC 23766 led to the failure of polar body emission. In addition, a majority of treated oocytes exhibited abnormal spindle morphology, indicating that Rac1 may involve into porcine oocyte spindle formation. This might be due to the regulation of Rac1 on MAPK, since p-MAPK expression decreased after NSC 23766 treatments. Moreover, we found that the position of most meiotic spindles in treated oocytes were away from the cortex, indicating the roles of Rac1 on meiotic spindle positioning. Our results also showed that inhibition of Rac1 activity caused the failure of early embryo development. Therefore, our study showed the critical roles of Rac1 GTPase on porcine oocyte maturation and early embryo cleavage. Nature Publishing Group 2016-10-03 /pmc/articles/PMC5046063/ /pubmed/27694954 http://dx.doi.org/10.1038/srep34415 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Song, Si-Jing Wang, Qiao-Chu Jia, Ru-Xia Cui, Xiang-Shun Kim, Nam-Hyung Sun, Shao-Chen Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development |
title | Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development |
title_full | Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development |
title_fullStr | Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development |
title_full_unstemmed | Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development |
title_short | Inhibition of Rac1 GTPase activity affects porcine oocyte maturation and early embryo development |
title_sort | inhibition of rac1 gtpase activity affects porcine oocyte maturation and early embryo development |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5046063/ https://www.ncbi.nlm.nih.gov/pubmed/27694954 http://dx.doi.org/10.1038/srep34415 |
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