Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (Acipenser ruthenus)
Identifieur interne : 000819 ( Istex/Corpus ); précédent : 000818; suivant : 000820Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (Acipenser ruthenus)
Auteurs : A. Shaliutina ; M. Hulak ; P. Li ; M. Sulc ; B. Dzyuba ; O. LinhartSource :
- Reproduction in Domestic Animals [ 0936-6768 ] ; 2013-02.
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.
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DOI: 10.1111/j.1439-0531.2012.02118.x
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Li</name><affiliation><mods:affiliation>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, Czech Republic</mods:affiliation></affiliation></author><author><name sortKey="Sulc, M" sort="Sulc, M" uniqKey="Sulc M" first="M" last="Sulc">M. Sulc</name><affiliation><mods:affiliation>Institute of Microbiology, AS CR, v.v.i., Videnska, Prague, Czech Republic</mods:affiliation></affiliation></author><author><name sortKey="Dzyuba, B" sort="Dzyuba, B" uniqKey="Dzyuba B" first="B" last="Dzyuba">B. Dzyuba</name><affiliation><mods:affiliation>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, Czech Republic</mods:affiliation></affiliation></author><author><name sortKey="Linhart, O" sort="Linhart, O" uniqKey="Linhart O" first="O" last="Linhart">O. Linhart</name><affiliation><mods:affiliation>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, Czech Republic</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Reproduction in Domestic Animals</title><idno type="ISSN">0936-6768</idno><idno type="eISSN">1439-0531</idno><imprint><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="2013-02">2013-02</date><biblScope unit="volume">48</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="156">156</biblScope><biblScope unit="page" to="159">159</biblScope></imprint><idno type="ISSN">0936-6768</idno></series><idno type="istex">F1FF12EEB8BEDF836D137CA0A8D46C1547728F80</idno><idno type="DOI">10.1111/j.1439-0531.2012.02118.x</idno><idno type="ArticleID">RDA2118</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0936-6768</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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. 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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. 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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. 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E‐mail: <email>a_shalutyna@mail.ru</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:RDA.RDA2118.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Submitted: 16 Jan 2012; Accepted: 26 Apr 2012</unparsedEditorialHistory><countGroup><count type="figureTotal" number="1"></count><count type="tableTotal" number="1"></count></countGroup><titleGroup><title type="main">Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (<i>Acipenser ruthenus</i>)</title><title type="shortAuthors">A Shaliutina, M Hulak, P Li, M Sulc, B Dzyuba and O Linhart</title><title type="short">Protein Profiles in Fish Seminal Plasma</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>A</givenNames><familyName>Shaliutina</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>M</givenNames><familyName>Hulak</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a1"><personName><givenNames>P</givenNames><familyName>Li</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a2"><personName><givenNames>M</givenNames><familyName>Sulc</familyName></personName></creator><creator creatorRole="author" xml:id="cr5" affiliationRef="#a1"><personName><givenNames>B</givenNames><familyName>Dzyuba</familyName></personName></creator><creator creatorRole="author" xml:id="cr6" affiliationRef="#a1"><personName><givenNames>O</givenNames><familyName>Linhart</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="CZ"><unparsedAffiliation>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, Czech Republic</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="CZ"><unparsedAffiliation>Institute of Microbiology, AS CR, v.v.i., Videnska, Prague, Czech Republic</unparsedAffiliation></affiliation></affiliationGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Contents</title><p>Seminal plasma of sterlet <i>Acipenser ruthenus</i> 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.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (Acipenser ruthenus)</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Protein Profiles in Fish Seminal Plasma</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Comparison of Protein Fractions in Seminal Plasma from Multiple Sperm Collections in Sterlet (Acipenser ruthenus)</title></titleInfo><name type="personal"><namePart type="given">A</namePart><namePart type="family">Shaliutina</namePart><affiliation>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, Czech Republic</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M</namePart><namePart type="family">Hulak</namePart><affiliation>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, Czech Republic</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">P</namePart><namePart type="family">Li</namePart><affiliation>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, Czech Republic</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M</namePart><namePart type="family">Sulc</namePart><affiliation>Institute of Microbiology, AS CR, v.v.i., Videnska, Prague, Czech Republic</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B</namePart><namePart type="family">Dzyuba</namePart><affiliation>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, Czech Republic</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">O</namePart><namePart type="family">Linhart</namePart><affiliation>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, Czech Republic</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2013-02</dateIssued><edition>Submitted: 16 Jan 2012; Accepted: 26 Apr 2012</edition><copyrightDate encoding="w3cdtf">2013</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">1</extent><extent unit="tables">1</extent></physicalDescription><abstract lang="en">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.</abstract><relatedItem type="host"><titleInfo><title>Reproduction in Domestic Animals</title></titleInfo><genre type="journal">journal</genre><identifier type="ISSN">0936-6768</identifier><identifier type="eISSN">1439-0531</identifier><identifier type="DOI">10.1111/(ISSN)1439-0531</identifier><identifier type="PublisherID">RDA</identifier><part><date>2013</date><detail type="volume"><caption>vol.</caption><number>48</number></detail><detail type="issue"><caption>no.</caption><number>1</number></detail><extent unit="pages"><start>156</start><end>159</end><total>4</total></extent></part></relatedItem><identifier type="istex">F1FF12EEB8BEDF836D137CA0A8D46C1547728F80</identifier><identifier type="DOI">10.1111/j.1439-0531.2012.02118.x</identifier><identifier type="ArticleID">RDA2118</identifier><accessCondition type="use and reproduction" contentType="copyright">© 2012 Blackwell Verlag GmbH</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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