Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (Acipenser ruthenus)
Identifieur interne : 000382 ( Main/Exploration ); précédent : 000381; suivant : 000383Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (Acipenser ruthenus)
Auteurs : A. Shaliutina [République tchèque] ; M. Hulak [République tchèque] ; P. Li [République tchèque] ; M. Sulc [République tchèque] ; B. Dzyuba [République tchèque] ; O. Linhart [République tchèque]Source :
- Reproduction in Domestic Animals [ 0936-6768 ] ; 2013-02.
English descriptors
- KwdEn :
- MESH :
- chemical , physiology : Fish Proteins.
- physiology : Fishes, Gene Expression Regulation, Semen, Spermatozoa.
- Animals, Electrophoresis, Polyacrylamide Gel, Male, Time Factors.
Abstract
Seminal plasma of sterlet Acipenser ruthenus was evaluated using comparative proteomics to characterize its protein fractions and to determine any influence of multiple sperm collections on these proteins. An experimental group of fish was used, in which sperm was collected three times at 5 h intervals. Protein fractions of seminal plasma were determined by SDS‐gel electrophoresis (SDS‐PAGE) and two‐dimensional electrophoresis high‐resolution gels (2D). At all stripping times, five protein bands with molecular weights of 93, 53, 48, 33 and 28 kDa were identified using SDS‐PAGE. No significant differences (p > 0.05) in relative mass of protein bands among collections were observed. At the third collection, 20 protein spots were detected from the two‐dimensional gels, compared to 17 found at the first and second collections. Ten protein spots, from the third stripping, were analysed. Screening of these spots by mass spectrometric analysis showed positive results for spot 10. Direct comparison across public databases revealed sequence similarity with two hypothetical proteins, MCAG_00854 and IscW_ISCW011489. Differences in the seminal plasma protein fractions were found at the third stripping compared to the first two. It is hypothesized that these extra proteins after the third collection could be involved in some step of intracellular mechanism which is responsible for regulating of spermatozoa motility. However, protein identification revealed no significant distinction for any protein spot and protein sequences available in public databases. These results highlighted the need for a complete genome sequences for sturgeons.
Url:
DOI: 10.1111/j.1439-0531.2012.02118.x
Affiliations:
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Li</name><affiliation wicri:level="1"><country xml:lang="fr">République tchèque</country><wicri:regionArea>Faculty of Fisheries and Protection of Waters, South Bohemian Research Center of Aquaculture and Biodiversity of Hydrocenoses, University of South Bohemia in Ceske Budejovice, Vodnany</wicri:regionArea><wicri:noRegion>Vodnany</wicri:noRegion></affiliation></author><author><name sortKey="Sulc, M" sort="Sulc, M" uniqKey="Sulc M" first="M" last="Sulc">M. Sulc</name><affiliation wicri:level="3"><country xml:lang="fr">République tchèque</country><wicri:regionArea>Institute of Microbiology, AS CR, v.v.i., Videnska, Prague</wicri:regionArea><placeName><settlement type="city">Prague</settlement><region type="région" nuts="2">Bohême centrale</region></placeName></affiliation></author><author><name sortKey="Dzyuba, B" sort="Dzyuba, B" uniqKey="Dzyuba B" first="B" last="Dzyuba">B. 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An experimental group of fish was used, in which sperm was collected three times at 5 h intervals. Protein fractions of seminal plasma were determined by SDS‐gel electrophoresis (SDS‐PAGE) and two‐dimensional electrophoresis high‐resolution gels (2D). At all stripping times, five protein bands with molecular weights of 93, 53, 48, 33 and 28 kDa were identified using SDS‐PAGE. No significant differences (p > 0.05) in relative mass of protein bands among collections were observed. At the third collection, 20 protein spots were detected from the two‐dimensional gels, compared to 17 found at the first and second collections. Ten protein spots, from the third stripping, were analysed. Screening of these spots by mass spectrometric analysis showed positive results for spot 10. Direct comparison across public databases revealed sequence similarity with two hypothetical proteins, MCAG_00854 and IscW_ISCW011489. Differences in the seminal plasma protein fractions were found at the third stripping compared to the first two. It is hypothesized that these extra proteins after the third collection could be involved in some step of intracellular mechanism which is responsible for regulating of spermatozoa motility. However, protein identification revealed no significant distinction for any protein spot and protein sequences available in public databases. These results highlighted the need for a complete genome sequences for sturgeons.</div></front></TEI><affiliations><list><country><li>République tchèque</li></country><region><li>Bohême centrale</li></region><settlement><li>Prague</li></settlement></list><tree><country name="République tchèque"><noRegion><name sortKey="Shaliutina, A" sort="Shaliutina, A" uniqKey="Shaliutina A" first="A" last="Shaliutina">A. Shaliutina</name></noRegion><name sortKey="Dzyuba, B" sort="Dzyuba, B" uniqKey="Dzyuba B" first="B" last="Dzyuba">B. Dzyuba</name><name sortKey="Hulak, M" sort="Hulak, M" uniqKey="Hulak M" first="M" last="Hulak">M. Hulak</name><name sortKey="Li, P" sort="Li, P" uniqKey="Li P" first="P" last="Li">P. Li</name><name sortKey="Linhart, O" sort="Linhart, O" uniqKey="Linhart O" first="O" last="Linhart">O. Linhart</name><name sortKey="Sulc, M" sort="Sulc, M" uniqKey="Sulc M" first="M" last="Sulc">M. Sulc</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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