Sperm surface protein AQ1 spermadhesin and ubiquitin-proteasome pathway in porcine anti-polyspermy defense

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F12%3A00380390" target="_blank" >RIV/86652036:_____/12:00380390 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Sperm surface protein AQ1 spermadhesin and ubiquitin-proteasome pathway in porcine anti-polyspermy defense

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

Sperm surface protein AQ1 spermadhesin and ubiquitin-proteasome pathway in porcine anti-polyspermy defense

Popis výsledku anglicky

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

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů