Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increasee polyspermy during porcine fertilization in vitro

0329730 - BTÚ 2011 US eng A - Abstrakt
Yi, Y. J. - Manandhar, G. - Sutovsky, M. - Jonáková, Věra - Park, CH. S. - Sutovsky, P.
Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increasee polyspermy during porcine fertilization in vitro.
Biology of Reproduction 2009 Supplement. Madison: Society for the Study of Reproduction, 2009 - (Robaire, B.; Murphy, B.). s. 123. ISSN 0006-3363. E-ISSN 1529-7268.
[SSR 42nd Annual Meeting. 18.07.2009-22.07.2009, Pittsburgh]
Výzkumný záměr: CEZ:AV0Z50520701
Klíčová slova: ubiquitin * polyspermy * spermadhesins
Kód oboru RIV: CE - Biochemie

The 26S proteasome is a multi-subunit protease specific to ubiquitinated substrate proteins. It is composed of a 20S proteasomal core and a 19S cap/regulatory complex. PSMD8, subunit of the 19S complex has been suggested to anchor deubiquitinating enzymes to the 19S lid. The study examined the role of sperm PSMD8 during porcine in vitro fertilization (IVF). PSMD8 was detected on the outer acrosomal membrane, in the acrosomal matrix and on the inner acrosomal membrane. Fertilization and polyspermy rates were increased significantly by adding anti-PSMD8 antibody to fertilization medium. Subunit PSMD8 co-immunoprecipitated with acrosomal surface-associated spermadhesin AQN1. Affinity purification of ubiquitinated proteins with p62 matrix revealed the presence of ubiquitinated AQN1 molecules in boar sperm extracts. The activity of the 19S complex may therefore be a rate limiting factor contributing to anti-polyspermy defense during porcine fertilization.
Trvalý link: http://hdl.handle.net/11104/0175681