The identification of proteomic markers of sperm freezing resilience in ram seminal plasma.
Identifieur interne : 002A40 ( PubMed/Curation ); précédent : 002A39; suivant : 002A41The identification of proteomic markers of sperm freezing resilience in ram seminal plasma.
Auteurs : J P Rickard [Australie] ; T. Leahy [Australie] ; C. Soleilhavoup [France] ; G. Tsikis [France] ; V. Labas [France] ; G. Harichaux [France] ; G W Lynch [Australie] ; X. Druart [France] ; S P De Graaf [Australie]Source :
- Journal of proteomics [ 1876-7737 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Marqueurs biologiques, Protéines du plasma séminal, Spermatozoïdes, Sperme.
- Animaux, Cryoconservation, Mâle, Ovis, Protéomique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Biomarkers, Seminal Plasma Proteins.
- metabolism : Semen, Spermatozoa.
- Animals, Cryopreservation, Male, Proteomics, Sheep.
Abstract
The source and composition of seminal plasma has previously been shown to alter the ability of spermatozoa to survive cryopreservation. In the present study, the ionic and proteomic composition of seminal plasma from rams with high (HSP; n = 3) or low (LSP; n = 3) freezing resilient spermatozoa was assessed. 75 proteins were identified to be more abundant in HSP and 48 proteins were identified to be more abundant in LSP. Individual seminal plasma proteomes were established for each of the six rams examined. For each ram, correlations were conducted between previously recorded freezing resilience [1] and individual spectral counts in order to identify markers of freezing resilience. 26S proteasome complex, acylamino acid releasing enzyme, alpha mannosidase class 2C, heat shock protein 90, tripeptidyl-peptidase 2, TCP-1 complex, sorbitol dehydrogenase and transitional endoplasmic reticulum ATPase were found to be positively correlated (r(2) > 0.7) with freezing resilience. Cystatin, zinc-2-alpha glycoprotein, angiogenin-2-like protein, cartilage acidic protein-1, cathepsin B and ribonuclease 4 isoform 1 were found to be negatively correlated (r(2) > 0.7) with freezing resilience. Several negative markers were found to originate from the accessory sex glands, whereas many positive markers originated from spermatozoa and were part of or associated with the 26S proteasome or CCT complex.
DOI: 10.1016/j.jprot.2015.05.017
PubMed: 26025878
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Electronic address: jessica.rickard@sydney.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Veterinary Science, The University of Sydney, NSW 2006</wicri:regionArea></affiliation></author><author><name sortKey="Leahy, T" sort="Leahy, T" uniqKey="Leahy T" first="T" last="Leahy">T. Leahy</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Veterinary Science, The University of Sydney, NSW 2006</wicri:regionArea></affiliation></author><author><name sortKey="Soleilhavoup, C" sort="Soleilhavoup, C" uniqKey="Soleilhavoup C" first="C" last="Soleilhavoup">C. Soleilhavoup</name><affiliation wicri:level="1"><nlm:affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly</wicri:regionArea></affiliation></author><author><name sortKey="Tsikis, G" sort="Tsikis, G" uniqKey="Tsikis G" first="G" last="Tsikis">G. Tsikis</name><affiliation wicri:level="1"><nlm:affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly</wicri:regionArea></affiliation></author><author><name sortKey="Labas, V" sort="Labas, V" uniqKey="Labas V" first="V" last="Labas">V. Labas</name><affiliation wicri:level="1"><nlm:affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; INRA, Plate-forme d'Analyse Intégrative des Biomolécules, Phénomique des Animaux d'Intérêt Bio-agronomique, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; INRA, Plate-forme d'Analyse Intégrative des Biomolécules, Phénomique des Animaux d'Intérêt Bio-agronomique, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly</wicri:regionArea></affiliation></author><author><name sortKey="Harichaux, G" sort="Harichaux, G" uniqKey="Harichaux G" first="G" last="Harichaux">G. Harichaux</name><affiliation wicri:level="1"><nlm:affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; INRA, Plate-forme d'Analyse Intégrative des Biomolécules, Phénomique des Animaux d'Intérêt Bio-agronomique, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; INRA, Plate-forme d'Analyse Intégrative des Biomolécules, Phénomique des Animaux d'Intérêt Bio-agronomique, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly</wicri:regionArea></affiliation></author><author><name sortKey="Lynch, G W" sort="Lynch, G W" uniqKey="Lynch G" first="G W" last="Lynch">G W Lynch</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia; Faculty of Medicine and Dentistry, The University of Sydney, NSW 2006, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia; Faculty of Medicine and Dentistry, The University of Sydney, NSW 2006</wicri:regionArea></affiliation></author><author><name sortKey="Druart, X" sort="Druart, X" uniqKey="Druart X" first="X" last="Druart">X. Druart</name><affiliation wicri:level="1"><nlm:affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly</wicri:regionArea></affiliation></author><author><name sortKey="De Graaf, S P" sort="De Graaf, S P" uniqKey="De Graaf S" first="S P" last="De Graaf">S P De Graaf</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Faculty of Veterinary Science, The University of Sydney, NSW 2006</wicri:regionArea></affiliation></author></analytic><series><title level="j">Journal of proteomics</title><idno type="eISSN">1876-7737</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Biomarkers (metabolism)</term><term>Cryopreservation</term><term>Male</term><term>Proteomics</term><term>Semen (metabolism)</term><term>Seminal Plasma Proteins (metabolism)</term><term>Sheep</term><term>Spermatozoa (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cryoconservation</term><term>Marqueurs biologiques (métabolisme)</term><term>Mâle</term><term>Ovis</term><term>Protéines du plasma séminal (métabolisme)</term><term>Protéomique</term><term>Spermatozoïdes (métabolisme)</term><term>Sperme (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Biomarkers</term><term>Seminal Plasma Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Semen</term><term>Spermatozoa</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Marqueurs biologiques</term><term>Protéines du plasma séminal</term><term>Spermatozoïdes</term><term>Sperme</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cryopreservation</term><term>Male</term><term>Proteomics</term><term>Sheep</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cryoconservation</term><term>Mâle</term><term>Ovis</term><term>Protéomique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The source and composition of seminal plasma has previously been shown to alter the ability of spermatozoa to survive cryopreservation. In the present study, the ionic and proteomic composition of seminal plasma from rams with high (HSP; n = 3) or low (LSP; n = 3) freezing resilient spermatozoa was assessed. 75 proteins were identified to be more abundant in HSP and 48 proteins were identified to be more abundant in LSP. Individual seminal plasma proteomes were established for each of the six rams examined. For each ram, correlations were conducted between previously recorded freezing resilience [1] and individual spectral counts in order to identify markers of freezing resilience. 26S proteasome complex, acylamino acid releasing enzyme, alpha mannosidase class 2C, heat shock protein 90, tripeptidyl-peptidase 2, TCP-1 complex, sorbitol dehydrogenase and transitional endoplasmic reticulum ATPase were found to be positively correlated (r(2) > 0.7) with freezing resilience. Cystatin, zinc-2-alpha glycoprotein, angiogenin-2-like protein, cartilage acidic protein-1, cathepsin B and ribonuclease 4 isoform 1 were found to be negatively correlated (r(2) > 0.7) with freezing resilience. Several negative markers were found to originate from the accessory sex glands, whereas many positive markers originated from spermatozoa and were part of or associated with the 26S proteasome or CCT complex.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26025878</PMID><DateCreated><Year>2015</Year><Month>08</Month><Day>03</Day></DateCreated><DateCompleted><Year>2016</Year><Month>05</Month><Day>30</Day></DateCompleted><DateRevised><Year>2015</Year><Month>08</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1876-7737</ISSN><JournalIssue CitedMedium="Internet"><Volume>126</Volume><PubDate><Year>2015</Year><Month>Aug</Month><Day>03</Day></PubDate></JournalIssue><Title>Journal of proteomics</Title><ISOAbbreviation>J Proteomics</ISOAbbreviation></Journal><ArticleTitle>The identification of proteomic markers of sperm freezing resilience in ram seminal plasma.</ArticleTitle><Pagination><MedlinePgn>303-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jprot.2015.05.017</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1874-3919(15)30014-2</ELocationID><Abstract><AbstractText>The source and composition of seminal plasma has previously been shown to alter the ability of spermatozoa to survive cryopreservation. In the present study, the ionic and proteomic composition of seminal plasma from rams with high (HSP; n = 3) or low (LSP; n = 3) freezing resilient spermatozoa was assessed. 75 proteins were identified to be more abundant in HSP and 48 proteins were identified to be more abundant in LSP. Individual seminal plasma proteomes were established for each of the six rams examined. For each ram, correlations were conducted between previously recorded freezing resilience [1] and individual spectral counts in order to identify markers of freezing resilience. 26S proteasome complex, acylamino acid releasing enzyme, alpha mannosidase class 2C, heat shock protein 90, tripeptidyl-peptidase 2, TCP-1 complex, sorbitol dehydrogenase and transitional endoplasmic reticulum ATPase were found to be positively correlated (r(2) > 0.7) with freezing resilience. Cystatin, zinc-2-alpha glycoprotein, angiogenin-2-like protein, cartilage acidic protein-1, cathepsin B and ribonuclease 4 isoform 1 were found to be negatively correlated (r(2) > 0.7) with freezing resilience. Several negative markers were found to originate from the accessory sex glands, whereas many positive markers originated from spermatozoa and were part of or associated with the 26S proteasome or CCT complex.</AbstractText><CopyrightInformation>Copyright © 2015 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rickard</LastName><ForeName>J P</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia. Electronic address: jessica.rickard@sydney.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leahy</LastName><ForeName>T</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Soleilhavoup</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tsikis</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Labas</LastName><ForeName>V</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; INRA, Plate-forme d'Analyse Intégrative des Biomolécules, Phénomique des Animaux d'Intérêt Bio-agronomique, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harichaux</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; INRA, Plate-forme d'Analyse Intégrative des Biomolécules, Phénomique des Animaux d'Intérêt Bio-agronomique, Laboratoire de Spectrométrie de Masse, F-37380 Nouzilly, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lynch</LastName><ForeName>G W</ForeName><Initials>GW</Initials><AffiliationInfo><Affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia; Faculty of Medicine and Dentistry, The University of Sydney, NSW 2006, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Druart</LastName><ForeName>X</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>UMR 6175 INRA, CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, Institut National de la Recherche Agronomique, 37380 Nouzilly, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Graaf</LastName><ForeName>S P</ForeName><Initials>SP</Initials><AffiliationInfo><Affiliation>Faculty of Veterinary Science, The University of Sydney, NSW 2006, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Proteomics</MedlineTA><NlmUniqueID>101475056</NlmUniqueID><ISSNLinking>1874-3919</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015415">Biomarkers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029589">Seminal Plasma Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015415" MajorTopicYN="N">Biomarkers</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015925" MajorTopicYN="Y">Cryopreservation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="Y">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012661" MajorTopicYN="N">Semen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029589" MajorTopicYN="N">Seminal Plasma Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012756" MajorTopicYN="N">Sheep</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013094" MajorTopicYN="N">Spermatozoa</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">26S proteosome</Keyword><Keyword MajorTopicYN="N">CCT complex</Keyword><Keyword MajorTopicYN="N">Cryopreservation</Keyword><Keyword MajorTopicYN="N">Proteome</Keyword><Keyword MajorTopicYN="N">Seminal plasma</Keyword><Keyword MajorTopicYN="N">Spermatozoa</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>03</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>05</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>05</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>5</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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