Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F14%3A43886838" target="_blank" >RIV/60076658:12520/14:43886838 - isvavai.cz</a>
Výsledek na webu
<a href="http://link.springer.com/article/10.1007%2Fs10695-014-9933-8" target="_blank" >http://link.springer.com/article/10.1007%2Fs10695-014-9933-8</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s10695-014-9933-8" target="_blank" >10.1007/s10695-014-9933-8</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity
Popis výsledku v původním jazyce
In mammals, proteases are present in sperm acrosome and play key role in fertilization. Sturgeon sperm has an acrosome, but its physiology, biochemistry, and potential role in fertilization are unknown. In the present study, we have observed high protease activity in acidic extract of intact sperm compared to that of seminal plasma in sterlet (Acipenser ruthenus). The protease activity was decreased and increased in acidic extract of motility-activated sperm and in the activation medium, respectively. Molecular analysis revealed total protease and serine (acrosin) protease activities in sperm acidic extract which was accumulated in a protein band with relative molecular mass of 35 kDa. Immunoelectron microscopy using an affinity-purified polyclonal antibody for boar acrosin localized the protease at the acrosome region. Moreover, initiation of sperm motility was inhibited after activation in the presence of inhibitors for both trypsin-like and chymotrypsin-like proteases, while the eff
Název v anglickém jazyce
Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity
Popis výsledku anglicky
In mammals, proteases are present in sperm acrosome and play key role in fertilization. Sturgeon sperm has an acrosome, but its physiology, biochemistry, and potential role in fertilization are unknown. In the present study, we have observed high protease activity in acidic extract of intact sperm compared to that of seminal plasma in sterlet (Acipenser ruthenus). The protease activity was decreased and increased in acidic extract of motility-activated sperm and in the activation medium, respectively. Molecular analysis revealed total protease and serine (acrosin) protease activities in sperm acidic extract which was accumulated in a protein band with relative molecular mass of 35 kDa. Immunoelectron microscopy using an affinity-purified polyclonal antibody for boar acrosin localized the protease at the acrosome region. Moreover, initiation of sperm motility was inhibited after activation in the presence of inhibitors for both trypsin-like and chymotrypsin-like proteases, while the eff
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EB - Genetika a molekulární biologie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2014
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Fish Physiology and Biochemistry
ISSN
0920-1742
e-ISSN
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Svazek periodika
40
Číslo periodika v rámci svazku
5
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
6
Strana od-do
1393-1398
Kód UT WoS článku
000341498900008
EID výsledku v databázi Scopus
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