Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F12%3A00367613" target="_blank" >RIV/86652036:_____/12:00367613 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1111/j.1365-2605.2011.01217.x" target="_blank" >http://dx.doi.org/10.1111/j.1365-2605.2011.01217.x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/j.1365-2605.2011.01217.x" target="_blank" >10.1111/j.1365-2605.2011.01217.x</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization
Popis výsledku v původním jazyce
Protein ubiquitination is covalent post-translational modification that targets proteins for proteolysis by the 26S proteasome. The E1-type ubiquitin-activating enzyme (UBA1) is responsible for the initial step of ubiquitin?protein ligation. Proteasomalproteolysis of ubiquitinated spermatozoa and oocyte proteins occurs during mammalian fertilization. UBA1 was detected in boar sperm-acrosomal extracts by Western blotting (WB) and by IMF in the acrosomal caps. A specific UBA1 inhibitor, PYR-41, altered the outer acrosomal membrane during sperm capacitation and reduced fertilization rates during in vitro fertilization. WB with antiphosphotyrosine antibodies and antibodies against acrosomal proteins SPINK2 (acrosin inhibitor) and AQN1 (spermadhesin) revealed that the capacitationinduced modification of those proteins was altered by PYR-41. It appears that de novo protein ubiquitination involving UBA1 contributes to sperm capacitation and acrosomal function during fertilization.
Název v anglickém jazyce
Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization
Popis výsledku anglicky
Protein ubiquitination is covalent post-translational modification that targets proteins for proteolysis by the 26S proteasome. The E1-type ubiquitin-activating enzyme (UBA1) is responsible for the initial step of ubiquitin?protein ligation. Proteasomalproteolysis of ubiquitinated spermatozoa and oocyte proteins occurs during mammalian fertilization. UBA1 was detected in boar sperm-acrosomal extracts by Western blotting (WB) and by IMF in the acrosomal caps. A specific UBA1 inhibitor, PYR-41, altered the outer acrosomal membrane during sperm capacitation and reduced fertilization rates during in vitro fertilization. WB with antiphosphotyrosine antibodies and antibodies against acrosomal proteins SPINK2 (acrosin inhibitor) and AQN1 (spermadhesin) revealed that the capacitationinduced modification of those proteins was altered by PYR-41. It appears that de novo protein ubiquitination involving UBA1 contributes to sperm capacitation and acrosomal function during fertilization.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2012
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
International Journal of Andrology
ISSN
0105-6263
e-ISSN
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Svazek periodika
35
Číslo periodika v rámci svazku
2
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
15
Strana od-do
196-210
Kód UT WoS článku
000301442200012
EID výsledku v databázi Scopus
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