Modifications of the 26S proteasome during boar sperm capacitation.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F18%3A00492931" target="_blank" >RIV/86652036:_____/18:00492931 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1007/s00441-017-2786-6" target="_blank" >http://dx.doi.org/10.1007/s00441-017-2786-6</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00441-017-2786-6" target="_blank" >10.1007/s00441-017-2786-6</a>
Alternative languages
Result language
angličtina
Original language name
Modifications of the 26S proteasome during boar sperm capacitation.
Original language description
Protein ubiquitination is a stable, reversible post-translational modification, targeting proteins for degradation/recycling by the 26S proteasome in a well-characterized enzymatic cascade. Studies have revealed the role of UPS in the regulation of fertilization, including sperm-zona pellucida interactions and the early event of sperm capacitation. The present study investigates the changes in proteasome compartmentalization, subunit composition and post-translational modifications during in vitro capacitation of fresh boar spermatozoa. We observed capacitation-dependent shedding of both 20S core and 19S regulatory particles from the acrosome that was associated with decreased plasma membrane integrity, independent of proteasomal inhibition. Subunits PSMA1-7 of the 20S core did not appear to undergo post-translational modifications during capacitation, based on invariant molecular masses before and after capacitation, however, we observed multiple PSMD4 forms of 19S regulatory particles (50, 53, 70, 115-140, 160 and > 176 kDa) sequentially released from spermatozoa. PSMD4 subunit was found to be post-translationally modified during the course of capacitation, resulting in changes of apparent molecular mass, some of which were dependent on proteasomal inhibition. These results show that the sperm proteasomes are being modified during sperm capacitation. Additional studies of individual 26S proteasome subunits will be required to elucidate these modifications and to understand how UPS modulates sperm capacitation.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/ED1.1.00%2F02.0109" target="_blank" >ED1.1.00/02.0109: Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Cell and Tissue Research
ISSN
0302-766X
e-ISSN
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Volume of the periodical
372
Issue of the periodical within the volume
3
Country of publishing house
DE - GERMANY
Number of pages
11
Pages from-to
591-601
UT code for WoS article
000432109000010
EID of the result in the Scopus database
2-s2.0-85041136516