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Sperm surface protein AQ1 spermadhesin and ubiquitin-proteasome pathway in porcine anti-polyspermy defense
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SYSNO ASEP 0380390 Druh ASEP A - Abstrakt Zařazení RIV Není vybrán druh dokumentu Název Sperm surface protein AQ1 spermadhesin and ubiquitin-proteasome pathway in porcine anti-polyspermy defense Tvůrce(i) Jonáková, Věra (BTO-N) RID
Postlerová, Pavla (BTO-N) ORCID, RID
Young-Joo, Y. (KR)
Sutovsky, P. (US)
Pěknicová, Jana (BTO-N) RIDCelkový počet autorů 5 Zdroj.dok. American Journal of Reproductive Immunology - ISSN 1046-7408
Roč. 67, Issue Supplement s1 (2012), s. 8-9Poč.str. 2 s. Akce 13th International Symposium for Immunology of reproduction "From the roots to the tops of Reproductive Immunology" Datum konání 22.06.2012-24.06.2012 Místo konání Varna Země BG - Bulharsko Typ akce WRD Jazyk dok. eng - angličtina Země vyd. DK - Dánsko Klíč. slova spermadhesin ; ubiquitin ; proteasome Vědní obor RIV CE - Biochemie CEP GA523/09/1793 GA ČR - Grantová agentura ČR GAP503/12/1834 GA ČR - Grantová agentura ČR CEZ AV0Z50520701 - BTO-N (2007-2013) Anotace Problem. One of the boar seminal plasma proteins called AQN1 spermadhesin binds to the sperm plasma membrane at ejaculation. This protein has been implicated in sperm binding to zona pellucid of the ovum as well as in sperm interactions with the epithelium of the oviductal sperm reservoir. The 26S proteasome is a multi-subunit protease specific to ubiquitinated substrate proteins. It is composed of a 20S proteasomal core with substrate degradation activity, and a 19S regulatory complex that acts in substrate recognition, deubiquitination, priming and transport to the 20S core. A high proteasome degradation activity and a high deubiquitinating activity were detected in the acrosome of boar spermatozoa. This study examined the role of two components of the 19S proteasome regulatory complex with deubiquitinating activity, ubiquitin C-terminal hydrolase UCHL3 and PSMD8, in the AQN1 spermadhesin-mediated boar sperm binding to zona pellucida. Results. We found that the activity and turnover of the porcine AQN1 sperm plasma membrane protein (and thus the efficiency of the sperm-ovum recognition process) may be controlled by elements of the sperm surface-bound ubiquitin-proteasome pathway, in particular by UCHL3, and by subunit PSMD8 of the 19S proteasomal regulatory complex. Ubiquitinated isoforms of AQN1 were detected in boar sperm extracts. The UCH inhibitor ubiquitin aldehyde and the antibodies against UCHL3 or PSMD8 increased the rate of sperm-ZP penetration and polyspermy during porcine in vitro fertilization. In contrast, the addition of recombinant UCHL3 into fertilization medium reduced polyspermy rates while maintaining a satisfactory monospermic fertilization rate of approx. 50%. Conclusion. These results are of practical significance. They suggest that reduction of the unfavorably high level of polyspermy (~50%), currently observed during porcine IVF for commercial embryo transfer, might be achieved e.g. by the modulation of the UCHL and/or PSMD8 activity. Pracoviště Biotechnologický ústav Kontakt Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Rok sběru 2013
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