000165264 001__ 165264
000165264 005__ 20251219174252.0
000165264 0247_ $$2doi$$a10.1021/acs.jproteome.3c00461
000165264 0248_ $$2sideral$$a136287
000165264 037__ $$aART-2023-136287
000165264 041__ $$aeng
000165264 100__ $$aGacem, Sabrina
000165264 245__ $$aBull Sperm SWATH-MS-Based Proteomics Reveals Link between High Fertility and Energy Production, Motility Structures, and Sperm–Oocyte Interaction
000165264 260__ $$c2023
000165264 5203_ $$aThe prediction of male or semen fertility potential remains a persistent challenge that has yet to be fully resolved. This work analyzed several in vitro parameters and proteome of spermatozoa in bulls cataloged as high- (HF; n = 5) and low-field (LF; n = 5) fertility after more than a thousand artificial inseminations. Sperm motility was evaluated by computer-assisted sperm analysis. Sperm viability, mitochondrial membrane potential (MMP) and reactive oxygen species (mROS) of spermatozoa were assessed by flow cytometry. Proteome was evaluated by the SWATH-MS procedure. Spermatozoa of HF bulls showed significantly higher total motility than the LF group (41.4% vs 29.7%). Rates of healthy sperm (live, high MMP, and low mROS) for HF and LF bull groups were 49% and 43%, respectively (p > 0.05). Spermatozoa of HF bulls showed a higher presence of differentially abundant proteins (DAPs) related to both energy production (COX7C), mainly the OXPHOS pathway, and the development of structures linked with the motility process (TPPP2, SSMEM1, and SPAG16). Furthermore, we observed that equatorin (EQTN), together with other DAPs related to the interaction with the oocyte, was overrepresented in HF bull spermatozoa. The biological processes related to protein processing, catabolism, and protein folding were found to be overrepresented in LF bull sperm in which the HSP90AA1 chaperone was identified as the most DAP. Data are available via ProteomeXchange with identifier PXD042286.
000165264 536__ $$9info:eu-repo/grantAgreement/ES/MICINN-AEI/PRTR-C17.I1
000165264 540__ $$9info:eu-repo/semantics/closedAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000165264 590__ $$a3.8$$b2023
000165264 591__ $$aBIOCHEMICAL RESEARCH METHODS$$b15 / 85 = 0.176$$c2023$$dQ1$$eT1
000165264 592__ $$a1.299$$b2023
000165264 593__ $$aChemistry (miscellaneous)$$c2023$$dQ1
000165264 593__ $$aBiochemistry$$c2023$$dQ1
000165264 594__ $$a9.0$$b2023
000165264 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000165264 700__ $$aCastello-Ruiz, María
000165264 700__ $$aHidalgo, Carlos O.
000165264 700__ $$aTamargo, Carolina
000165264 700__ $$0(orcid)0000-0001-8991-325X$$aSantolaria, Pilar$$uUniversidad de Zaragoza
000165264 700__ $$aSoler, Carles
000165264 700__ $$0(orcid)0000-0001-5316-1703$$aYániz, Jesús L.$$uUniversidad de Zaragoza
000165264 700__ $$aSilvestre, Miguel A.
000165264 7102_ $$12008$$2700$$aUniversidad de Zaragoza$$bDpto. Produc.Animal Cienc.Ali.$$cÁrea Producción Animal
000165264 773__ $$g22, 11 (2023), 3607-3624$$pJ. proteome res.$$tJOURNAL OF PROTEOME RESEARCH$$x1535-3893
000165264 8564_ $$s5465595$$uhttps://zaguan.unizar.es/record/165264/files/texto_completo.pdf$$yVersión publicada
000165264 8564_ $$s2927818$$uhttps://zaguan.unizar.es/record/165264/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000165264 909CO $$ooai:zaguan.unizar.es:165264$$particulos$$pdriver
000165264 951__ $$a2025-12-19-14:44:02
000165264 980__ $$aARTICLE