Počet záznamů: 1
Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization
0367613 - BTO-N 2013 RIV US eng J - Článek v odborném periodiku
Yi, Y.-J. - Zimmermann, S.W. - Manandhar, G. - Odhiambo, J.F. - Kennedy, C. - Jonáková, Věra - Maňásková-Postlerová, Pavla - Sutovsky, M. - Park, C.-S. - Sutovsky, P.
Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization.
International Journal of Andrology. Roč. 35, č. 2 (2012), s. 196-210 ISSN 0105-6263
Grant CEP: GA ČR(CZ) GA303/09/1285; GA MŠk(CZ) 1M06011; GA MZd(CZ) NS10009
Výzkumný záměr: CEZ:AV0Z50520701
Klíčová slova: acrosome * capacitation * fertilization * ubiqutin
Kód oboru RIV: CE - Biochemie
Impakt faktor: 3.565, rok: 2012
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. Proteasomal proteolysis 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.
Trvalý link: http://hdl.handle.net/11104/0202217
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