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Statements

Subject Item
n2:RIV%2F60076658%3A12520%2F14%3A43886838%21RIV15-GA0-12520___
rdf:type
skos:Concept n12:Vysledek
rdfs:seeAlso
http://link.springer.com/article/10.1007%2Fs10695-014-9933-8
dcterms:description
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 effects of protease inhibitors on sperm velocity were uncertain. Our results indicate similarities in physiology and biochemistry of acrosome between sturgeon and mammals and suggest potential role of protease in the initiation of sperm motility in sturgeon. 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 effects of protease inhibitors on sperm velocity were uncertain. Our results indicate similarities in physiology and biochemistry of acrosome between sturgeon and mammals and suggest potential role of protease in the initiation of sperm motility in sturgeon.
dcterms:title
Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity
skos:prefLabel
Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity Protease in sturgeon sperm and the effects of protease inhibitors on sperm motility and velocity
skos:notation
RIV/60076658:12520/14:43886838!RIV15-GA0-12520___
n4:aktivita
n11:P
n4:aktivity
P(ED2.1.00/01.0024), P(GAP503/12/1834), P(GP13-34049P)
n4:cisloPeriodika
5
n4:dodaniDat
n10:2015
n4:domaciTvurceVysledku
n7:1593579 n7:6919707 n7:9895744 Hatef, Azadeh
n4:druhVysledku
n13:J
n4:duvernostUdaju
n8:S
n4:entitaPredkladatele
n19:predkladatel
n4:idSjednocenehoVysledku
40448
n4:idVysledku
RIV/60076658:12520/14:43886838
n4:jazykVysledku
n18:eng
n4:klicovaSlova
TPCK; Sperm motility; Electron microscopy; AGB; Acrosome
n4:klicoveSlovo
n6:TPCK n6:AGB n6:Acrosome n6:Sperm%20motility n6:Electron%20microscopy
n4:kodStatuVydavatele
NL - Nizozemsko
n4:kontrolniKodProRIV
[A1091D84C29C]
n4:nazevZdroje
Fish Physiology and Biochemistry
n4:obor
n20:EB
n4:pocetDomacichTvurcuVysledku
4
n4:pocetTvurcuVysledku
8
n4:projekt
n16:GP13-34049P n16:ED2.1.00%2F01.0024 n16:GAP503%2F12%2F1834
n4:rokUplatneniVysledku
n10:2014
n4:svazekPeriodika
40
n4:tvurceVysledku
Pšenička, Martin Postlerova-Manaskova, Pavla Ciereszko, Andrzej Linhart, Otomar Hatef, Azadeh Peknicova, Jana Inaba, Kazuo Alavi, Sayyed Mohammad Hadi
n4:wos
000341498900008
s:issn
0920-1742
s:numberOfPages
6
n17:doi
10.1007/s10695-014-9933-8
n9:organizacniJednotka
12520