Milk proteins interact with goat Binder of SPerm (BSP) proteins and decrease their binding to sperm
Seminal plasma Binder of SPerm (BSP) proteins bind to sperm at ejaculation and promote capacitation. When in excess, however, BSP proteins damage the sperm membrane. It has been suggested that milk components of semen extenders associate with BSP proteins, potentially protecting sperm. Thus, this st...
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| Veröffentlicht in: | Cell and tissue research 2016-11, Vol.366 (2), p.427-442 |
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| description | Seminal plasma Binder of SPerm (BSP) proteins bind to sperm at ejaculation and promote capacitation. When in excess, however, BSP proteins damage the sperm membrane. It has been suggested that milk components of semen extenders associate with BSP proteins, potentially protecting sperm. Thus, this study was conducted to investigate if milk proteins interact with BSP proteins and reduce BSP binding to goat sperm. Using gel filtration chromatography, milk was incubated with goat seminal plasma proteins and loaded onto columns with and without calcium. Milk was also fractionated into parts containing mostly whey proteins or mostly caseins, incubated with seminal plasma proteins and subjected to gel filtration. Eluted fractions were evaluated by immunoblot using anti-goat BSP antibodies, confirming milk protein–BSP protein interactions. As determined by ELISA, milk proteins coated on polystyrene wells bound to increasing of goat BSP proteins. Far-western dot blots confirmed that BSP proteins bound to caseins and β-lactoglobulin in a concentration-dependent manner. Then, cauda epididymal sperm from five goats was incubated with seminal plasma; seminal plasma followed by milk; and milk followed by seminal plasma. Sperm membrane proteins were extracted and evaluated by immunoblotting. The pattern of BSP binding to sperm membrane proteins was reduced by 59.3 % when epididymal sperm were incubated with seminal plasma and then with skimmed milk (
p
0.05). In conclusion, goat BSP proteins have an affinity for caseins and whey proteins. Milk reduces BSP binding to goat sperm, depending whether or not sperm had been previously exposed to seminal plasma. Such events may explain the protective effect of milk during goat sperm preservation. |
| doi_str_mv | 10.1007/s00441-016-2438-2 |
| format | Article |
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p
< 0.05). When epididymal sperm were treated with milk followed by seminal plasma, coating of sperm with BSP proteins was not significantly reduced (57.6 %;
p
> 0.05). In conclusion, goat BSP proteins have an affinity for caseins and whey proteins. Milk reduces BSP binding to goat sperm, depending whether or not sperm had been previously exposed to seminal plasma. Such events may explain the protective effect of milk during goat sperm preservation.</description><identifier>ISSN: 0302-766X</identifier><identifier>EISSN: 1432-0878</identifier><identifier>DOI: 10.1007/s00441-016-2438-2</identifier><identifier>PMID: 27432314</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Animal reproduction ; Animals ; Antibodies ; Biomedical and Life Sciences ; Biomedicine ; Blotting, Western ; Calcium - pharmacology ; Chromatography, Gel ; Enzyme-Linked Immunosorbent Assay ; Epididymis - metabolism ; Goats ; Goats - metabolism ; Human Genetics ; Male ; Mediation ; Membrane Proteins - metabolism ; Milk ; Milk Proteins - metabolism ; Models, Biological ; Molecular Medicine ; Protein Aggregates - drug effects ; Protein binding ; Protein Binding - drug effects ; Proteins ; Proteomics ; Regular Article ; Seminal Vesicle Secretory Proteins - metabolism ; Sperm ; Spermatozoa - drug effects ; Spermatozoa - metabolism</subject><ispartof>Cell and tissue research, 2016-11, Vol.366 (2), p.427-442</ispartof><rights>Springer-Verlag Berlin Heidelberg 2016</rights><rights>COPYRIGHT 2016 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-3eaf86ccab1c1ac1873a141f25c8de7f3097a5776aa7e382e3f72c965d8bd083</citedby><cites>FETCH-LOGICAL-c472t-3eaf86ccab1c1ac1873a141f25c8de7f3097a5776aa7e382e3f72c965d8bd083</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00441-016-2438-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00441-016-2438-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27432314$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de Menezes, Erika Bezerra</creatorcontrib><creatorcontrib>van Tilburg, Mauricio</creatorcontrib><creatorcontrib>Plante, Geneviève</creatorcontrib><creatorcontrib>de Oliveira, Rodrigo V.</creatorcontrib><creatorcontrib>Moura, Arlindo A.</creatorcontrib><creatorcontrib>Manjunath, Puttaswamy</creatorcontrib><title>Milk proteins interact with goat Binder of SPerm (BSP) proteins and decrease their binding to sperm</title><title>Cell and tissue research</title><addtitle>Cell Tissue Res</addtitle><addtitle>Cell Tissue Res</addtitle><description>Seminal plasma Binder of SPerm (BSP) proteins bind to sperm at ejaculation and promote capacitation. When in excess, however, BSP proteins damage the sperm membrane. It has been suggested that milk components of semen extenders associate with BSP proteins, potentially protecting sperm. Thus, this study was conducted to investigate if milk proteins interact with BSP proteins and reduce BSP binding to goat sperm. Using gel filtration chromatography, milk was incubated with goat seminal plasma proteins and loaded onto columns with and without calcium. Milk was also fractionated into parts containing mostly whey proteins or mostly caseins, incubated with seminal plasma proteins and subjected to gel filtration. Eluted fractions were evaluated by immunoblot using anti-goat BSP antibodies, confirming milk protein–BSP protein interactions. As determined by ELISA, milk proteins coated on polystyrene wells bound to increasing of goat BSP proteins. Far-western dot blots confirmed that BSP proteins bound to caseins and β-lactoglobulin in a concentration-dependent manner. Then, cauda epididymal sperm from five goats was incubated with seminal plasma; seminal plasma followed by milk; and milk followed by seminal plasma. Sperm membrane proteins were extracted and evaluated by immunoblotting. The pattern of BSP binding to sperm membrane proteins was reduced by 59.3 % when epididymal sperm were incubated with seminal plasma and then with skimmed milk (
p
< 0.05). When epididymal sperm were treated with milk followed by seminal plasma, coating of sperm with BSP proteins was not significantly reduced (57.6 %;
p
> 0.05). In conclusion, goat BSP proteins have an affinity for caseins and whey proteins. Milk reduces BSP binding to goat sperm, depending whether or not sperm had been previously exposed to seminal plasma. Such events may explain the protective effect of milk during goat sperm preservation.</description><subject>Animal reproduction</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Blotting, Western</subject><subject>Calcium - pharmacology</subject><subject>Chromatography, Gel</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Epididymis - metabolism</subject><subject>Goats</subject><subject>Goats - metabolism</subject><subject>Human Genetics</subject><subject>Male</subject><subject>Mediation</subject><subject>Membrane Proteins - metabolism</subject><subject>Milk</subject><subject>Milk Proteins - metabolism</subject><subject>Models, Biological</subject><subject>Molecular Medicine</subject><subject>Protein Aggregates - drug effects</subject><subject>Protein binding</subject><subject>Protein Binding - drug effects</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Regular Article</subject><subject>Seminal Vesicle Secretory Proteins - metabolism</subject><subject>Sperm</subject><subject>Spermatozoa - drug effects</subject><subject>Spermatozoa - metabolism</subject><issn>0302-766X</issn><issn>1432-0878</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkk1vVCEUhompsWP1B7hpSLqpi1v5GuAu28avpMYm7cIdYbiHKfVeGIGJ8d_LdWrVRhPDggSe583hcBB6QckJJUS9KoQIQTtCZccE1x17hBZUcNYRrfQeWhBOWKek_LSPnpZySwgVUvZP0D5TjeJULJD7EMbPeJNThRALDrFCtq7ir6He4HWyFZ-FOEDGyeOrS8gTPj67unz5y7BxwAO4DLYArjcQMl41I8Q1rgmXTVOeocfejgWe3-0H6PrN6-vzd93Fx7fvz08vOicUqx0H67V0zq6oo9ZRrbilgnq2dHoA5TnplV0qJa1VwDUD7hVzvVwOejUQzQ_Q8S621fZlC6WaKRQH42gjpG0xVHPFesWp_A-UScW0_pF69AC9Tdsc2zvmwNZSqVsz76m1HcGE6FNtbZxDzalQRC5Zz-ask79QbQ0wBZci-NDO_xDoTnA5lZLBm00Ok83fDCVmHgGzGwHTyjDzCBjWnMO7grerCYZ74-efN4DtgNKu4hryby_6Z-p3diu4rw</recordid><startdate>20161101</startdate><enddate>20161101</enddate><creator>de Menezes, Erika Bezerra</creator><creator>van Tilburg, Mauricio</creator><creator>Plante, Geneviève</creator><creator>de Oliveira, Rodrigo V.</creator><creator>Moura, Arlindo A.</creator><creator>Manjunath, Puttaswamy</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SS</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20161101</creationdate><title>Milk proteins interact with goat Binder of SPerm (BSP) proteins and decrease their binding to sperm</title><author>de Menezes, Erika Bezerra ; van Tilburg, Mauricio ; Plante, Geneviève ; de Oliveira, Rodrigo V. ; Moura, Arlindo A. ; Manjunath, Puttaswamy</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c472t-3eaf86ccab1c1ac1873a141f25c8de7f3097a5776aa7e382e3f72c965d8bd083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animal reproduction</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Blotting, Western</topic><topic>Calcium - pharmacology</topic><topic>Chromatography, Gel</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Epididymis - metabolism</topic><topic>Goats</topic><topic>Goats - metabolism</topic><topic>Human Genetics</topic><topic>Male</topic><topic>Mediation</topic><topic>Membrane Proteins - metabolism</topic><topic>Milk</topic><topic>Milk Proteins - metabolism</topic><topic>Models, Biological</topic><topic>Molecular Medicine</topic><topic>Protein Aggregates - drug effects</topic><topic>Protein binding</topic><topic>Protein Binding - drug effects</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Regular Article</topic><topic>Seminal Vesicle Secretory Proteins - metabolism</topic><topic>Sperm</topic><topic>Spermatozoa - drug effects</topic><topic>Spermatozoa - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de Menezes, Erika Bezerra</creatorcontrib><creatorcontrib>van Tilburg, Mauricio</creatorcontrib><creatorcontrib>Plante, Geneviève</creatorcontrib><creatorcontrib>de Oliveira, Rodrigo V.</creatorcontrib><creatorcontrib>Moura, Arlindo A.</creatorcontrib><creatorcontrib>Manjunath, Puttaswamy</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Cell and tissue research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de Menezes, Erika Bezerra</au><au>van Tilburg, Mauricio</au><au>Plante, Geneviève</au><au>de Oliveira, Rodrigo V.</au><au>Moura, Arlindo A.</au><au>Manjunath, Puttaswamy</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Milk proteins interact with goat Binder of SPerm (BSP) proteins and decrease their binding to sperm</atitle><jtitle>Cell and tissue research</jtitle><stitle>Cell Tissue Res</stitle><addtitle>Cell Tissue Res</addtitle><date>2016-11-01</date><risdate>2016</risdate><volume>366</volume><issue>2</issue><spage>427</spage><epage>442</epage><pages>427-442</pages><issn>0302-766X</issn><eissn>1432-0878</eissn><abstract>Seminal plasma Binder of SPerm (BSP) proteins bind to sperm at ejaculation and promote capacitation. When in excess, however, BSP proteins damage the sperm membrane. It has been suggested that milk components of semen extenders associate with BSP proteins, potentially protecting sperm. Thus, this study was conducted to investigate if milk proteins interact with BSP proteins and reduce BSP binding to goat sperm. Using gel filtration chromatography, milk was incubated with goat seminal plasma proteins and loaded onto columns with and without calcium. Milk was also fractionated into parts containing mostly whey proteins or mostly caseins, incubated with seminal plasma proteins and subjected to gel filtration. Eluted fractions were evaluated by immunoblot using anti-goat BSP antibodies, confirming milk protein–BSP protein interactions. As determined by ELISA, milk proteins coated on polystyrene wells bound to increasing of goat BSP proteins. Far-western dot blots confirmed that BSP proteins bound to caseins and β-lactoglobulin in a concentration-dependent manner. Then, cauda epididymal sperm from five goats was incubated with seminal plasma; seminal plasma followed by milk; and milk followed by seminal plasma. Sperm membrane proteins were extracted and evaluated by immunoblotting. The pattern of BSP binding to sperm membrane proteins was reduced by 59.3 % when epididymal sperm were incubated with seminal plasma and then with skimmed milk (
p
< 0.05). When epididymal sperm were treated with milk followed by seminal plasma, coating of sperm with BSP proteins was not significantly reduced (57.6 %;
p
> 0.05). In conclusion, goat BSP proteins have an affinity for caseins and whey proteins. Milk reduces BSP binding to goat sperm, depending whether or not sperm had been previously exposed to seminal plasma. Such events may explain the protective effect of milk during goat sperm preservation.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>27432314</pmid><doi>10.1007/s00441-016-2438-2</doi><tpages>16</tpages></addata></record> |
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| ispartof | Cell and tissue research, 2016-11, Vol.366 (2), p.427-442 |
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| subjects | Animal reproduction Animals Antibodies Biomedical and Life Sciences Biomedicine Blotting, Western Calcium - pharmacology Chromatography, Gel Enzyme-Linked Immunosorbent Assay Epididymis - metabolism Goats Goats - metabolism Human Genetics Male Mediation Membrane Proteins - metabolism Milk Milk Proteins - metabolism Models, Biological Molecular Medicine Protein Aggregates - drug effects Protein binding Protein Binding - drug effects Proteins Proteomics Regular Article Seminal Vesicle Secretory Proteins - metabolism Sperm Spermatozoa - drug effects Spermatozoa - metabolism |
| title | Milk proteins interact with goat Binder of SPerm (BSP) proteins and decrease their binding to sperm |
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