Lactotransferrin in Asian elephant (Elephas maximus) seminal plasma correlates with semen quality
Asian elephants (Elephas maximus) have highly variable ejaculate quality within individuals, greatly reducing the efficacy of artificial insemination and making it difficult to devise a sperm cryopreservation protocol for this endangered species. Because seminal plasma influences sperm function and...
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description | Asian elephants (Elephas maximus) have highly variable ejaculate quality within individuals, greatly reducing the efficacy of artificial insemination and making it difficult to devise a sperm cryopreservation protocol for this endangered species. Because seminal plasma influences sperm function and physiology, including sperm motility, the objectives of this study were to characterize the chemistry and protein profiles of Asian elephant seminal plasma and to determine the relationships between seminal plasma components and semen quality. Ejaculates exhibiting good sperm motility (≥65%) expressed higher percentages of spermatozoa with normal morphology (80.3±13.0 vs. 44.9±30.8%) and positive Spermac staining (51.9±14.5 vs. 7.5±14.4%), in addition to higher total volume (135.1±89.6 vs. 88.8±73.1 ml) and lower sperm concentration (473.0±511.2 vs. 1313.8±764.7×10⁶ cells ml⁻¹) compared to ejaculates exhibiting poor sperm motility (≤10%; P |
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Because seminal plasma influences sperm function and physiology, including sperm motility, the objectives of this study were to characterize the chemistry and protein profiles of Asian elephant seminal plasma and to determine the relationships between seminal plasma components and semen quality. Ejaculates exhibiting good sperm motility (≥65%) expressed higher percentages of spermatozoa with normal morphology (80.3±13.0 vs. 44.9±30.8%) and positive Spermac staining (51.9±14.5 vs. 7.5±14.4%), in addition to higher total volume (135.1±89.6 vs. 88.8±73.1 ml) and lower sperm concentration (473.0±511.2 vs. 1313.8±764.7×10⁶ cells ml⁻¹) compared to ejaculates exhibiting poor sperm motility (≤10%; P<0.05). Comparison of seminal plasma from ejaculates with good versus poor sperm motility revealed significant differences in concentrations of creatine phosphokinase, alanine aminotransferase, phosphorus, sodium, chloride, magnesium, and glucose. These observations suggest seminal plasma influences semen quality in elephants. One- and two-dimensional (2D) gel electrophoresis revealed largely similar compositional profiles of seminal plasma proteins between good and poor motility ejaculates. However, a protein of ∼80 kDa was abundant in 85% of ejaculates with good motility, and was absent in 90% of poor motility ejaculates (P<0.05). We used mass spectrometry to identify this protein as lactotransferrin, and immunoblot analysis to confirm this identification. Together, these findings lay a functional foundation for understanding the contributions of seminal plasma in the regulation of Asian elephant sperm motility, and for improving semen collection and storage in this endangered species.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0071033</identifier><identifier>PMID: 23976974</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Alanine ; Alanine transaminase ; Analysis ; Anesthesia ; Animals ; Artificial insemination ; Biology ; Blood proteins ; Conservation biology ; Creatine ; Creatine kinase ; Cryopreservation ; Elephants ; Elephants - physiology ; Endangered Species ; Gel electrophoresis ; Identification ; Insemination, Artificial ; Lactoferrin - isolation & purification ; Lactoferrin - physiology ; Magnesium ; Male ; Mass Spectrometry ; Mass spectroscopy ; Methods ; Morphology ; Motility ; Phosphorus ; Physiology ; Plasma proteins ; Proteins ; Proteomics ; Quality ; Reproduction (biology) ; Scientific imaging ; Semen ; Semen - chemistry ; Semen - metabolism ; Semen Analysis ; Semen Preservation ; Sodium ; Specimen Handling ; Sperm ; Sperm Count ; Sperm Motility ; Spermatozoa ; Spermatozoa - physiology ; Spermatozoa - ultrastructure ; Veterinary colleges ; Veterinary medicine ; Veterinary Science ; Wildlife conservation ; Zoology</subject><ispartof>PloS one, 2013-08, Vol.8 (8), p.e71033-e71033</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013. This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c593t-acaedb9e78295a14a7f2473627d46ef1a91258ca25babfac4b99a0e3a8ee467a3</citedby><cites>FETCH-LOGICAL-c593t-acaedb9e78295a14a7f2473627d46ef1a91258ca25babfac4b99a0e3a8ee467a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3745378/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3745378/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2919,23857,27915,27916,53782,53784,79361,79362</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23976974$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Wicker-Thomas, Claude</contributor><creatorcontrib>Kiso, Wendy K</creatorcontrib><creatorcontrib>Selvaraj, Vimal</creatorcontrib><creatorcontrib>Nagashima, Jennifer</creatorcontrib><creatorcontrib>Asano, Atsushi</creatorcontrib><creatorcontrib>Brown, Janine L</creatorcontrib><creatorcontrib>Schmitt, Dennis L</creatorcontrib><creatorcontrib>Leszyk, John</creatorcontrib><creatorcontrib>Travis, Alexander J</creatorcontrib><creatorcontrib>Pukazhenthi, Budhan S</creatorcontrib><title>Lactotransferrin in Asian elephant (Elephas maximus) seminal plasma correlates with semen quality</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Asian elephants (Elephas maximus) have highly variable ejaculate quality within individuals, greatly reducing the efficacy of artificial insemination and making it difficult to devise a sperm cryopreservation protocol for this endangered species. Because seminal plasma influences sperm function and physiology, including sperm motility, the objectives of this study were to characterize the chemistry and protein profiles of Asian elephant seminal plasma and to determine the relationships between seminal plasma components and semen quality. Ejaculates exhibiting good sperm motility (≥65%) expressed higher percentages of spermatozoa with normal morphology (80.3±13.0 vs. 44.9±30.8%) and positive Spermac staining (51.9±14.5 vs. 7.5±14.4%), in addition to higher total volume (135.1±89.6 vs. 88.8±73.1 ml) and lower sperm concentration (473.0±511.2 vs. 1313.8±764.7×10⁶ cells ml⁻¹) compared to ejaculates exhibiting poor sperm motility (≤10%; P<0.05). Comparison of seminal plasma from ejaculates with good versus poor sperm motility revealed significant differences in concentrations of creatine phosphokinase, alanine aminotransferase, phosphorus, sodium, chloride, magnesium, and glucose. These observations suggest seminal plasma influences semen quality in elephants. One- and two-dimensional (2D) gel electrophoresis revealed largely similar compositional profiles of seminal plasma proteins between good and poor motility ejaculates. However, a protein of ∼80 kDa was abundant in 85% of ejaculates with good motility, and was absent in 90% of poor motility ejaculates (P<0.05). We used mass spectrometry to identify this protein as lactotransferrin, and immunoblot analysis to confirm this identification. Together, these findings lay a functional foundation for understanding the contributions of seminal plasma in the regulation of Asian elephant sperm motility, and for improving semen collection and storage in this endangered species.</description><subject>Alanine</subject><subject>Alanine transaminase</subject><subject>Analysis</subject><subject>Anesthesia</subject><subject>Animals</subject><subject>Artificial insemination</subject><subject>Biology</subject><subject>Blood proteins</subject><subject>Conservation biology</subject><subject>Creatine</subject><subject>Creatine kinase</subject><subject>Cryopreservation</subject><subject>Elephants</subject><subject>Elephants - physiology</subject><subject>Endangered Species</subject><subject>Gel electrophoresis</subject><subject>Identification</subject><subject>Insemination, Artificial</subject><subject>Lactoferrin - isolation & purification</subject><subject>Lactoferrin - physiology</subject><subject>Magnesium</subject><subject>Male</subject><subject>Mass Spectrometry</subject><subject>Mass spectroscopy</subject><subject>Methods</subject><subject>Morphology</subject><subject>Motility</subject><subject>Phosphorus</subject><subject>Physiology</subject><subject>Plasma proteins</subject><subject>Proteins</subject><subject>Proteomics</subject><subject>Quality</subject><subject>Reproduction (biology)</subject><subject>Scientific imaging</subject><subject>Semen</subject><subject>Semen - chemistry</subject><subject>Semen - metabolism</subject><subject>Semen Analysis</subject><subject>Semen Preservation</subject><subject>Sodium</subject><subject>Specimen Handling</subject><subject>Sperm</subject><subject>Sperm Count</subject><subject>Sperm Motility</subject><subject>Spermatozoa</subject><subject>Spermatozoa - physiology</subject><subject>Spermatozoa - ultrastructure</subject><subject>Veterinary colleges</subject><subject>Veterinary medicine</subject><subject>Veterinary Science</subject><subject>Wildlife conservation</subject><subject>Zoology</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</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><sourceid>DOA</sourceid><recordid>eNptUttq3DAQNaWlubR_UFpDX9KH3epmy3opLCFtAwt9aZ_FWB7varGljWSnzd9HzjohW4IEGmbOnLnoZNkHSpaUS_p158fgoFvuvcMlIZISzl9lp1RxtigZ4a-f2SfZWYw7QgpeleXb7IRxJUslxWkGazCDHwK42GII1uXprqIFl2OH-y24Ib-4erBi3sM_24_xSx6xt6l2vu8g9pAbHwJ2MGDM_9phO4XR5TcjdHa4e5e9aaGL-H5-z7M_369-X_5crH_9uL5crRemUHxYgAFsaoWyYqoAKkC2TEheMtmIElsKirKiMsCKGuoWjKiVAoIcKkRRSuDn2acD777zUc_biZoKTmRVVIonxPUB0XjY6X2wPYQ77cHqB4cPGw1hsKZDXQEobAsqVUNEVRaKsabFuqENFoKbMnF9m6uNdY-NQZd22B2RHkec3eqNv9VcioLLKhFczATB34wYB93baLDrwKEfp75ZxSRJ1RP083_Ql6ebURtIA1jXTr9qJlK9EmmrRcW4TKjlC6h0mvSlJkmptcl_lCAOCSb4GAO2TzNSoichPjajJyHqWYgp7ePz_TwlPSqP3wOb49yv</recordid><startdate>20130816</startdate><enddate>20130816</enddate><creator>Kiso, Wendy K</creator><creator>Selvaraj, Vimal</creator><creator>Nagashima, Jennifer</creator><creator>Asano, Atsushi</creator><creator>Brown, Janine L</creator><creator>Schmitt, Dennis L</creator><creator>Leszyk, John</creator><creator>Travis, Alexander J</creator><creator>Pukazhenthi, Budhan S</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20130816</creationdate><title>Lactotransferrin in Asian elephant (Elephas maximus) seminal plasma correlates with semen quality</title><author>Kiso, Wendy K ; Selvaraj, Vimal ; Nagashima, Jennifer ; Asano, Atsushi ; Brown, Janine L ; Schmitt, Dennis L ; Leszyk, John ; Travis, Alexander J ; Pukazhenthi, Budhan S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c593t-acaedb9e78295a14a7f2473627d46ef1a91258ca25babfac4b99a0e3a8ee467a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Alanine</topic><topic>Alanine transaminase</topic><topic>Analysis</topic><topic>Anesthesia</topic><topic>Animals</topic><topic>Artificial insemination</topic><topic>Biology</topic><topic>Blood proteins</topic><topic>Conservation biology</topic><topic>Creatine</topic><topic>Creatine kinase</topic><topic>Cryopreservation</topic><topic>Elephants</topic><topic>Elephants - physiology</topic><topic>Endangered Species</topic><topic>Gel electrophoresis</topic><topic>Identification</topic><topic>Insemination, Artificial</topic><topic>Lactoferrin - isolation & purification</topic><topic>Lactoferrin - physiology</topic><topic>Magnesium</topic><topic>Male</topic><topic>Mass Spectrometry</topic><topic>Mass spectroscopy</topic><topic>Methods</topic><topic>Morphology</topic><topic>Motility</topic><topic>Phosphorus</topic><topic>Physiology</topic><topic>Plasma proteins</topic><topic>Proteins</topic><topic>Proteomics</topic><topic>Quality</topic><topic>Reproduction (biology)</topic><topic>Scientific imaging</topic><topic>Semen</topic><topic>Semen - chemistry</topic><topic>Semen - metabolism</topic><topic>Semen Analysis</topic><topic>Semen Preservation</topic><topic>Sodium</topic><topic>Specimen Handling</topic><topic>Sperm</topic><topic>Sperm Count</topic><topic>Sperm Motility</topic><topic>Spermatozoa</topic><topic>Spermatozoa - physiology</topic><topic>Spermatozoa - 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Because seminal plasma influences sperm function and physiology, including sperm motility, the objectives of this study were to characterize the chemistry and protein profiles of Asian elephant seminal plasma and to determine the relationships between seminal plasma components and semen quality. Ejaculates exhibiting good sperm motility (≥65%) expressed higher percentages of spermatozoa with normal morphology (80.3±13.0 vs. 44.9±30.8%) and positive Spermac staining (51.9±14.5 vs. 7.5±14.4%), in addition to higher total volume (135.1±89.6 vs. 88.8±73.1 ml) and lower sperm concentration (473.0±511.2 vs. 1313.8±764.7×10⁶ cells ml⁻¹) compared to ejaculates exhibiting poor sperm motility (≤10%; P<0.05). Comparison of seminal plasma from ejaculates with good versus poor sperm motility revealed significant differences in concentrations of creatine phosphokinase, alanine aminotransferase, phosphorus, sodium, chloride, magnesium, and glucose. These observations suggest seminal plasma influences semen quality in elephants. One- and two-dimensional (2D) gel electrophoresis revealed largely similar compositional profiles of seminal plasma proteins between good and poor motility ejaculates. However, a protein of ∼80 kDa was abundant in 85% of ejaculates with good motility, and was absent in 90% of poor motility ejaculates (P<0.05). We used mass spectrometry to identify this protein as lactotransferrin, and immunoblot analysis to confirm this identification. Together, these findings lay a functional foundation for understanding the contributions of seminal plasma in the regulation of Asian elephant sperm motility, and for improving semen collection and storage in this endangered species.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23976974</pmid><doi>10.1371/journal.pone.0071033</doi><oa>free_for_read</oa></addata></record> |
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subjects | Alanine Alanine transaminase Analysis Anesthesia Animals Artificial insemination Biology Blood proteins Conservation biology Creatine Creatine kinase Cryopreservation Elephants Elephants - physiology Endangered Species Gel electrophoresis Identification Insemination, Artificial Lactoferrin - isolation & purification Lactoferrin - physiology Magnesium Male Mass Spectrometry Mass spectroscopy Methods Morphology Motility Phosphorus Physiology Plasma proteins Proteins Proteomics Quality Reproduction (biology) Scientific imaging Semen Semen - chemistry Semen - metabolism Semen Analysis Semen Preservation Sodium Specimen Handling Sperm Sperm Count Sperm Motility Spermatozoa Spermatozoa - physiology Spermatozoa - ultrastructure Veterinary colleges Veterinary medicine Veterinary Science Wildlife conservation Zoology |
title | Lactotransferrin in Asian elephant (Elephas maximus) seminal plasma correlates with semen quality |
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