author_facet Jin, Yong-Xun
Zheng, Zhong
Yu, Xian-Feng
Zhang, Jia-Bao
Namgoong, Suk
Cui, Xiang-Shun
Hyun, Sang-Hwan
Kim, Nam-Hyung
Jin, Yong-Xun
Zheng, Zhong
Yu, Xian-Feng
Zhang, Jia-Bao
Namgoong, Suk
Cui, Xiang-Shun
Hyun, Sang-Hwan
Kim, Nam-Hyung
author Jin, Yong-Xun
Zheng, Zhong
Yu, Xian-Feng
Zhang, Jia-Bao
Namgoong, Suk
Cui, Xiang-Shun
Hyun, Sang-Hwan
Kim, Nam-Hyung
spellingShingle Jin, Yong-Xun
Zheng, Zhong
Yu, Xian-Feng
Zhang, Jia-Bao
Namgoong, Suk
Cui, Xiang-Shun
Hyun, Sang-Hwan
Kim, Nam-Hyung
Zygote
Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
Cell Biology
Developmental Biology
author_sort jin, yong-xun
spelling Jin, Yong-Xun Zheng, Zhong Yu, Xian-Feng Zhang, Jia-Bao Namgoong, Suk Cui, Xiang-Shun Hyun, Sang-Hwan Kim, Nam-Hyung 0967-1994 1469-8730 Cambridge University Press (CUP) Cell Biology Developmental Biology http://dx.doi.org/10.1017/s0967199414000689 <jats:title>Summary</jats:title><jats:p>The mitochondrial genome is maternally inherited in animals, despite the fact that paternal mitochondria enter oocytes during fertilization. Autophagy and ubiquitin-mediated degradation are responsible for the elimination of paternal mitochondria in <jats:italic>Caenorhabditis elegans</jats:italic>; however, the involvement of these two processes in the degradation of paternal mitochondria in mammals is not well understood. We investigated the localization patterns of light chain 3 (LC3) and ubiquitin in mouse and porcine embryos during preimplantation development. We found that LC3 and ubiquitin localized to the spermatozoon midpiece at 3 h post-fertilization, and that both proteins were colocalized with paternal mitochondria and removed upon fertilization during the 4-cell stage in mouse and the zygote stage in porcine embryos. Sporadic paternal mitochondria were present beyond the morula stage in the mouse, and paternal mitochondria were restricted to one blastomere of 4-cell embryos. An autophagy inhibitor, 3-methyladenine (3-MA), did not affect the distribution of paternal mitochondria compared with the positive control, while an autophagy inducer, rapamycin, accelerated the removal of paternal mitochondria compared with the control. After the intracytoplasmic injection of intact spermatozoon into mouse oocytes, LC3 and ubiquitin localized to the spermatozoon midpiece, but remnants of undegraded paternal mitochondria were retained until the blastocyst stage. Our results show that paternal mitochondria colocalize with autophagy receptors and ubiquitin and are removed after <jats:italic>in vitro</jats:italic> fertilization, but some remnants of sperm mitochondrial sheath may persist up to morula stage after intracytoplasmic spermatozoon injection (ICSI).</jats:p> Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos Zygote
doi_str_mv 10.1017/s0967199414000689
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title Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_unstemmed Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_full Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_fullStr Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_full_unstemmed Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_short Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_sort autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
topic Cell Biology
Developmental Biology
url http://dx.doi.org/10.1017/s0967199414000689
publishDate 2016
physical 31-41
description <jats:title>Summary</jats:title><jats:p>The mitochondrial genome is maternally inherited in animals, despite the fact that paternal mitochondria enter oocytes during fertilization. Autophagy and ubiquitin-mediated degradation are responsible for the elimination of paternal mitochondria in <jats:italic>Caenorhabditis elegans</jats:italic>; however, the involvement of these two processes in the degradation of paternal mitochondria in mammals is not well understood. We investigated the localization patterns of light chain 3 (LC3) and ubiquitin in mouse and porcine embryos during preimplantation development. We found that LC3 and ubiquitin localized to the spermatozoon midpiece at 3 h post-fertilization, and that both proteins were colocalized with paternal mitochondria and removed upon fertilization during the 4-cell stage in mouse and the zygote stage in porcine embryos. Sporadic paternal mitochondria were present beyond the morula stage in the mouse, and paternal mitochondria were restricted to one blastomere of 4-cell embryos. An autophagy inhibitor, 3-methyladenine (3-MA), did not affect the distribution of paternal mitochondria compared with the positive control, while an autophagy inducer, rapamycin, accelerated the removal of paternal mitochondria compared with the control. After the intracytoplasmic injection of intact spermatozoon into mouse oocytes, LC3 and ubiquitin localized to the spermatozoon midpiece, but remnants of undegraded paternal mitochondria were retained until the blastocyst stage. Our results show that paternal mitochondria colocalize with autophagy receptors and ubiquitin and are removed after <jats:italic>in vitro</jats:italic> fertilization, but some remnants of sperm mitochondrial sheath may persist up to morula stage after intracytoplasmic spermatozoon injection (ICSI).</jats:p>
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author Jin, Yong-Xun, Zheng, Zhong, Yu, Xian-Feng, Zhang, Jia-Bao, Namgoong, Suk, Cui, Xiang-Shun, Hyun, Sang-Hwan, Kim, Nam-Hyung
author_facet Jin, Yong-Xun, Zheng, Zhong, Yu, Xian-Feng, Zhang, Jia-Bao, Namgoong, Suk, Cui, Xiang-Shun, Hyun, Sang-Hwan, Kim, Nam-Hyung, Jin, Yong-Xun, Zheng, Zhong, Yu, Xian-Feng, Zhang, Jia-Bao, Namgoong, Suk, Cui, Xiang-Shun, Hyun, Sang-Hwan, Kim, Nam-Hyung
author_sort jin, yong-xun
container_issue 1
container_start_page 31
container_title Zygote
container_volume 24
description <jats:title>Summary</jats:title><jats:p>The mitochondrial genome is maternally inherited in animals, despite the fact that paternal mitochondria enter oocytes during fertilization. Autophagy and ubiquitin-mediated degradation are responsible for the elimination of paternal mitochondria in <jats:italic>Caenorhabditis elegans</jats:italic>; however, the involvement of these two processes in the degradation of paternal mitochondria in mammals is not well understood. We investigated the localization patterns of light chain 3 (LC3) and ubiquitin in mouse and porcine embryos during preimplantation development. We found that LC3 and ubiquitin localized to the spermatozoon midpiece at 3 h post-fertilization, and that both proteins were colocalized with paternal mitochondria and removed upon fertilization during the 4-cell stage in mouse and the zygote stage in porcine embryos. Sporadic paternal mitochondria were present beyond the morula stage in the mouse, and paternal mitochondria were restricted to one blastomere of 4-cell embryos. An autophagy inhibitor, 3-methyladenine (3-MA), did not affect the distribution of paternal mitochondria compared with the positive control, while an autophagy inducer, rapamycin, accelerated the removal of paternal mitochondria compared with the control. After the intracytoplasmic injection of intact spermatozoon into mouse oocytes, LC3 and ubiquitin localized to the spermatozoon midpiece, but remnants of undegraded paternal mitochondria were retained until the blastocyst stage. Our results show that paternal mitochondria colocalize with autophagy receptors and ubiquitin and are removed after <jats:italic>in vitro</jats:italic> fertilization, but some remnants of sperm mitochondrial sheath may persist up to morula stage after intracytoplasmic spermatozoon injection (ICSI).</jats:p>
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spelling Jin, Yong-Xun Zheng, Zhong Yu, Xian-Feng Zhang, Jia-Bao Namgoong, Suk Cui, Xiang-Shun Hyun, Sang-Hwan Kim, Nam-Hyung 0967-1994 1469-8730 Cambridge University Press (CUP) Cell Biology Developmental Biology http://dx.doi.org/10.1017/s0967199414000689 <jats:title>Summary</jats:title><jats:p>The mitochondrial genome is maternally inherited in animals, despite the fact that paternal mitochondria enter oocytes during fertilization. Autophagy and ubiquitin-mediated degradation are responsible for the elimination of paternal mitochondria in <jats:italic>Caenorhabditis elegans</jats:italic>; however, the involvement of these two processes in the degradation of paternal mitochondria in mammals is not well understood. We investigated the localization patterns of light chain 3 (LC3) and ubiquitin in mouse and porcine embryos during preimplantation development. We found that LC3 and ubiquitin localized to the spermatozoon midpiece at 3 h post-fertilization, and that both proteins were colocalized with paternal mitochondria and removed upon fertilization during the 4-cell stage in mouse and the zygote stage in porcine embryos. Sporadic paternal mitochondria were present beyond the morula stage in the mouse, and paternal mitochondria were restricted to one blastomere of 4-cell embryos. An autophagy inhibitor, 3-methyladenine (3-MA), did not affect the distribution of paternal mitochondria compared with the positive control, while an autophagy inducer, rapamycin, accelerated the removal of paternal mitochondria compared with the control. After the intracytoplasmic injection of intact spermatozoon into mouse oocytes, LC3 and ubiquitin localized to the spermatozoon midpiece, but remnants of undegraded paternal mitochondria were retained until the blastocyst stage. Our results show that paternal mitochondria colocalize with autophagy receptors and ubiquitin and are removed after <jats:italic>in vitro</jats:italic> fertilization, but some remnants of sperm mitochondrial sheath may persist up to morula stage after intracytoplasmic spermatozoon injection (ICSI).</jats:p> Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos Zygote
spellingShingle Jin, Yong-Xun, Zheng, Zhong, Yu, Xian-Feng, Zhang, Jia-Bao, Namgoong, Suk, Cui, Xiang-Shun, Hyun, Sang-Hwan, Kim, Nam-Hyung, Zygote, Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos, Cell Biology, Developmental Biology
title Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_full Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_fullStr Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_full_unstemmed Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_short Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_sort autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
title_unstemmed Autophagy and ubiquitin-mediated proteolysis may not be involved in the degradation of spermatozoon mitochondria in mouse and porcine early embryos
topic Cell Biology, Developmental Biology
url http://dx.doi.org/10.1017/s0967199414000689