Roles of mouse sperm-associated alpha-L-fucosidases in fertilization
Sperm-associated α-L-fucosidases have been implicated in fertilization in many species. Previously, we documented the existence of α-L-fucosidase in mouse cauda epididymal contents, and showed that sperm-associated α-L-fucosidase is cryptically stored within the acrosome and reappears within the spe...
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th-mahidol.313342018-10-19T11:40:18Z Roles of mouse sperm-associated alpha-L-fucosidases in fertilization Kamonrat Phopin Wutigri Nimlamool Linda J. Lowe-Krentz Elijah W. Douglass Jaclyn N. Taroni Barry S. Bean Lehigh University Mahidol University Biochemistry, Genetics and Molecular Biology Sperm-associated α-L-fucosidases have been implicated in fertilization in many species. Previously, we documented the existence of α-L-fucosidase in mouse cauda epididymal contents, and showed that sperm-associated α-L-fucosidase is cryptically stored within the acrosome and reappears within the sperm equatorial segment after the acrosome reaction. The enrichment of sperm membrane-associated α-L-fucosidase within the equatorial segment of acrosome-reacted cells implicates its roles during fertilization. Here, we document the absence of α-L-fucosidase in mouse oocytes and early embryos, and define roles of sperm associated α-L-fucosidase in fertilization using specific inhibitors and competitors. Mouse sperm were pretreated with deoxyfuconojirimycin (DFJ, an inhibitor of α-L-fucosidase) or with anti-fucosidase antibody; alternatively, mouse oocytes were pretreated with purified human liver α-L-fucosidase. Five-millimolar DFJ did not inhibit sperm-zona pellucida (ZP) binding, membrane binding, or fusion and penetration, but anti-fucosidase antibody and purified human liver α-L-fucosidase significantly decreased the frequency of these events. To evaluate sperm-associated α-L-fucosidase enzyme activity in post-fusion events, DFJ-pretreated sperm were microinjected into oocytes, and 2-pronuclear (2-PN) embryos were treated with 5mM DFJ with no significant effects, suggesting that α-L-fucosidase enzyme activity does not play a role in post-fusion events and/or early embryo development in mice. The recognition and binding of mouse sperm to the ZP and oolemma involves the glycoprotein structure of α-L-fucosidase, but not its catalytic action. These observations suggest that deficits in fucosidase protein and/or the presence of anti-fucosidase antibody may be responsible for some types of infertility. © 2013 Wiley Periodicals, Inc. 2018-10-19T04:40:18Z 2018-10-19T04:40:18Z 2013-04-01 Article Molecular Reproduction and Development. Vol.80, No.4 (2013), 273-285 10.1002/mrd.22164 10982795 1040452X 2-s2.0-84876408450 https://repository.li.mahidol.ac.th/handle/123456789/31334 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84876408450&origin=inward |
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Biochemistry, Genetics and Molecular Biology Kamonrat Phopin Wutigri Nimlamool Linda J. Lowe-Krentz Elijah W. Douglass Jaclyn N. Taroni Barry S. Bean Roles of mouse sperm-associated alpha-L-fucosidases in fertilization |
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Sperm-associated α-L-fucosidases have been implicated in fertilization in many species. Previously, we documented the existence of α-L-fucosidase in mouse cauda epididymal contents, and showed that sperm-associated α-L-fucosidase is cryptically stored within the acrosome and reappears within the sperm equatorial segment after the acrosome reaction. The enrichment of sperm membrane-associated α-L-fucosidase within the equatorial segment of acrosome-reacted cells implicates its roles during fertilization. Here, we document the absence of α-L-fucosidase in mouse oocytes and early embryos, and define roles of sperm associated α-L-fucosidase in fertilization using specific inhibitors and competitors. Mouse sperm were pretreated with deoxyfuconojirimycin (DFJ, an inhibitor of α-L-fucosidase) or with anti-fucosidase antibody; alternatively, mouse oocytes were pretreated with purified human liver α-L-fucosidase. Five-millimolar DFJ did not inhibit sperm-zona pellucida (ZP) binding, membrane binding, or fusion and penetration, but anti-fucosidase antibody and purified human liver α-L-fucosidase significantly decreased the frequency of these events. To evaluate sperm-associated α-L-fucosidase enzyme activity in post-fusion events, DFJ-pretreated sperm were microinjected into oocytes, and 2-pronuclear (2-PN) embryos were treated with 5mM DFJ with no significant effects, suggesting that α-L-fucosidase enzyme activity does not play a role in post-fusion events and/or early embryo development in mice. The recognition and binding of mouse sperm to the ZP and oolemma involves the glycoprotein structure of α-L-fucosidase, but not its catalytic action. These observations suggest that deficits in fucosidase protein and/or the presence of anti-fucosidase antibody may be responsible for some types of infertility. © 2013 Wiley Periodicals, Inc. |
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Lehigh University |
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Lehigh University Kamonrat Phopin Wutigri Nimlamool Linda J. Lowe-Krentz Elijah W. Douglass Jaclyn N. Taroni Barry S. Bean |
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Article |
author |
Kamonrat Phopin Wutigri Nimlamool Linda J. Lowe-Krentz Elijah W. Douglass Jaclyn N. Taroni Barry S. Bean |
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Kamonrat Phopin |
title |
Roles of mouse sperm-associated alpha-L-fucosidases in fertilization |
title_short |
Roles of mouse sperm-associated alpha-L-fucosidases in fertilization |
title_full |
Roles of mouse sperm-associated alpha-L-fucosidases in fertilization |
title_fullStr |
Roles of mouse sperm-associated alpha-L-fucosidases in fertilization |
title_full_unstemmed |
Roles of mouse sperm-associated alpha-L-fucosidases in fertilization |
title_sort |
roles of mouse sperm-associated alpha-l-fucosidases in fertilization |
publishDate |
2018 |
url |
https://repository.li.mahidol.ac.th/handle/123456789/31334 |
_version_ |
1763489609246834688 |