Acrosin inhibitors and their regulation by the ubiquitin-proteasome system in boar reproductive tract

0445149 - BTÚ 2016 US eng A - Abstract
Jonáková, Věra - Yi, Y.J. - Sutovsky, P. - Cozlová, Nina - Postlerová, Pavla
Acrosin inhibitors and their regulation by the ubiquitin-proteasome system in boar reproductive tract.
Abstracts of the 14th International Symposium for Immunology of Reproduction “Progress in Reproductive Immunology”. Hoboken: American Journal of Reproductive Immunology, 2015 - (Mor, G.). s. 18-18. ISSN 1046-7408. E-ISSN 1600-0897.
[14th International Symposium for Immunology of Reproduction "progress in Reproductive Immunology". 22.05.2015-24.05.2015, Varna]
R&D Projects: GA ČR(CZ) GA14-05547S; GA MŠMT(CZ) ED1.1.00/02.0109
Institutional research plan: CEZ:AV0Z50520701
Institutional support: RVO:86652036
Keywords : acrosin inhibitors * boar reproductive tract * epididymis * ubiquitin-proteasome system
Subject RIV: CE - Biochemistry

Seminal plasma acrosin inhibitor (SPAI) and sperm- associated acrosin inhibitor (AI/SPINK2) are structurally related and are members of the Kazal-type subfamily of proteinase inhibitors.Acrosin inhibitor detected in epididymis (AI) is immunologically related to SPAI and AI/SPINK2. We monitored AI in different segments of the epi- didymis by specific polyclonal antibody. Similarly, the AI mRNA expression increased in the epididymal duct to its tail as detected by RT-PCR. AI may regu- late proteolytic processing of epididymalsperm plasma membrane proteins and play a key role at the post-testicular maturation of sperm. AI/SPINK2 could be a factor needed for stabilization of binding sites on the sperm surface important for sperm egg interaction. This study also detected inter- action between PSMD4 subunit of the 19S protea- some regulatory complex, and AI/SPINK2 inhibitor. This provided evidence for the presence of 26S pro- teasomes on the sperm surface. Detection of the ubiquitinated forms of AI/SPINK2 supports the hypothesis that AI/SPINK2 activity is controlled by the ubiquitin-proteasome system.
Permanent Link: http://hdl.handle.net/11104/0255924