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The proteome of pig spermatozoa Is remodeled during ejaculation

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dc.contributor.authorPérez-Patiño, Cristina
dc.contributor.authorParrilla, Inmaculada
dc.contributor.authorLi, Junwei
dc.contributor.authorBarranco, Isabel
dc.contributor.authorMartínez, Emilio A.
dc.contributor.authorRodríguez-Martínez, Heriberto
dc.contributor.authorRoca, Jordi
dc.contributor.departmentMedicina y Cirugía Animal
dc.date.accessioned2024-09-13T07:13:21Z
dc.date.available2024-09-13T07:13:21Z
dc.date.issued2019-01
dc.description© 2019 Pérez-Patiño et al. This manuscript version is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by/4.0/ This document is the Published version of a Published Work that appeared in final form in Molecular & Cellular Proteomics (MCP). To access the final edited and published work see https://doi.org/10.1074/mcp.RA118.000840
dc.description.abstractProteins are essential for sperm function, including their fertilizing capacity. Pig spermatozoa, emitted in well-defined ejaculate fractions, vary in their functionality, which could be related to different sperm protein composition. This study aimed (i) to update the porcine sperm proteome and (ii) to identify proteins differentially expressed in mature spermatozoa from cauda epididymis and those delivered in separate ejaculate fractions. Ejaculates from nine mature and fertile boars were manually collected in three separate portions: the first 10 ml of the sperm-rich ejaculate fraction (SRF), the rest of the SRF and the post-SRF. The contents of cauda epididymides of the boars were collected post-mortem by retrograde duct perfusion, generating four different semen sources for each boar. Following centrifugation, the resulting pellets of each semen source were initially pooled and later split to generate two technical replicates per source. The resulting eight sperm samples (two per semen source) were subjected to iTRAQ-based 2D-LC-MS/MS for protein identification and quantification. A total of 1,723 proteins were identified (974 of Sus scrofa taxonomy) and 1,602 of them were also quantified (960 of Sus scrofa taxonomy). After an ANOVA test, 32 Sus scrofa proteins showed quantitative differences (p < 0.01) among semen sources, which was particularly relevant for sperm functionality in the post-SRF. The present study showed that the proteome of boar spermatozoa is remodeled during ejaculation involving proteins clearly implicated in sperm function. The findings provide valuable groundwork for further studies focused on identifying protein biomarkers of sperm fertility.es
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dc.format.extent11es
dc.identifier.citationMolecular & Cellular Proteomics (MCP), 2019, Vol. 18 (1), pp. 41-50
dc.identifier.doihttps://doi.org/10.1074/mcp.RA118.000840
dc.identifier.issnElectronic: 1535-9484
dc.identifier.urihttp://hdl.handle.net/10201/143931
dc.languageenges
dc.publisherElsevier
dc.relationThis study was supported by MINECO (Spain) and FEDER funds (EU) (AGL2015-69738-R), and Seneca Foundation Murcia, Spain (19892/GERM-15); FORSS (745971) and The Swedish Research Council FORMAS (2017-00946), Stockholm, Sweden. C. Perez Patin˜o, I. Barranco and J. Li were financially supported by Seneca Foundation (Murcia, Spain), MECD (Madrid, Spain) and the China Scholarship Council, respectively.es
dc.relation.publisherversionhttps://www.mcponline.org/article/S1535-9476(20)34100-1/fulltextes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectBoares
dc.subjectClinical Proteomics
dc.subjectEjaculate
dc.subjectEpididymis
dc.subjectProtein Identification
dc.subjectQuantification
dc.subjectTandem Mass Spectrometry
dc.subjectiTRAQ
dc.titleThe proteome of pig spermatozoa Is remodeled during ejaculationes
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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