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Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increases polyspermy during porcine fertilization in vitro
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SYSNO ASEP 0346866 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increases polyspermy during porcine fertilization in vitro Author(s) Yi, Y.J. (KR)
Manandhar, G. (US)
Sutovsky, M. (US)
Jonáková, Věra (BTO-N) RID
Park, Ch.S. (KR)
Sutovsky, P. (US)Number of authors 6 Source Title Journal of Reproductive Immunology. - : Elsevier - ISSN 0165-0378
Roč. 84, č. 2 (2010), s. 154-163Number of pages 10 s. Language eng - English Country IE - Ireland Keywords Sperm ; Proteasome ; Fertilization ; Zona pellucida ; Acrosome Subject RIV EC - Immunology R&D Projects 1M06011 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA303/09/1285 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50520701 - BTO-N (2007-2013) UT WOS 000273605500318 DOI 10.1016/j.jri.2009.11.002 Annotation The 26S proteoasome is composed of a 20S core with substrate degradation activity, and a 19S regulatory complex that acts in substrate recognition, deubiquitination, priming and transport to the 20S core. The study examined the role of PSMD8, a subunit of the 19S complex, in sperm-ZP penetration during porcine fertilization in vitro (IVF). Immunofluorescence localized PSMD8 to the outer acrosomal membrane, acrosomal matrix and the inner acrosomal membrane. Subunit PSMD8 co-immunoprecipitated with acrosomal surface-associated spermadhesin AQN1. This association indicates that the sperm acrosome-borne proteasomes become exposed onto the sperm surface following the acrosomal exocytosis. Since immunological blocking of subunit PSMD8 increases the rate of polyspermy during porcine fertilization, the activity of the 19S complex may be a rate-limiting factor contributing to anti-polyspermy defense during porcine fertilization. Workplace Institute of Biotechnology Contact Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Year of Publishing 2011
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