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dc.contributor.authorManandhar, Gaurishankar-
dc.contributor.authorMiranda-Vizuete, Antonio-
dc.contributor.authorPedrajas, José R.-
dc.contributor.authorKrause, William J.-
dc.contributor.authorZimmerman, Shawn-
dc.contributor.authorSutovsky, Miriam-
dc.contributor.authorSutovsky, Peter-
dc.date.accessioned2012-03-07T13:22:27Z-
dc.date.available2012-03-07T13:22:27Z-
dc.date.issued2009-06-01-
dc.identifier.citationBiology of Reproduction 80(6): 1168-1177 (2009)es_ES
dc.identifier.issn0006-3363-
dc.identifier.otherPMID: 19208552-
dc.identifier.urihttp://hdl.handle.net/10261/46716-
dc.description10 páginas, 6 figuras, 2 tablas.es_ES
dc.description.abstractPeroxiredoxin 2 (PRDX2) is a highly efficient redox protein that neutralizes hydrogen peroxide, resulting in protection of cells from oxidative damage and in regulation of peroxide-mediated signal transduction events. The oxidized form of PRDX2 is reverted back to the reduced form by the thioredoxin system. In the present study, we investigated the presence of PRDX2 in mouse and boar spermatozoa and in mouse spermatids using proteomic techniques and immunocytochemistry. Sperm and spermatid extracts displayed a 20-kDa PRDX2 band on Western blotting. PRDX2 occurred as a Triton-soluble form in spermatids and as a Triton-insoluble form in mature spermatozoa. Boar seminiferous tubule extracts were immunoprecipitated with PRDX2 antibody and separated by SDS-PAGE. Peptide mass fingerprinting by matrix-assisted laser desorption ionization-time of flight (TOF) and microsequencing by nanospray quadrupole-quadrupole TOF tandem mass spectrometry revealed the presence of PRDX2 ions in the immunoprecipitated band, along with sperm mitochondria-associated cysteine-rich protein, cellular nucleic acid-binding protein, and glutathione peroxidase 4. In mouse spermatocytes and spermatids, diffuse labeling of PRDX2 was observed in the cytoplasm and residual bodies. After spermiation, PRDX2 localization became confined to the mitochondrial sheath of the sperm tail midpiece. Boar spermatozoa displayed similar PRDX2 localization as in mouse spermatozoa. Boar spermatozoa with disrupted acrosomes expressed PRDX2 in the postacrosomal sheath region. Peroxidase enzyme activity of boar sperm extracts was evaluated by estimating the rate of NADPH oxidation in the presence or absence of a glutathione depletor (diethyl maleate) or a glutathione reductase inhibitor (carmustine). Diethyl maleate partially inhibited peroxidase activity, whereas carmustine showed an insignificant effect. These observations suggest that glutathione and glutathione reductase activity contribute only partially to the total peroxidase activity of the sperm extract. While the specific role of PRDX2 in the total peroxidase activity of sperm extract is still an open question, the present study for the first time (to our knowledge) shows the presence of PRDX2 in mammalian spermatozoa. Peroxidase activity in sperm extracts is not due to the glutathione system and therefore possibly involves PRDX2 and other peroxiredoxins.es_ES
dc.description.sponsorshipSupported in part by the Food for the 21st Century Program of the University of Missouri and by National Research Initiative Competitive Grant No. 2007-01319 from the USDA CSREES to P.S.es_ES
dc.language.isoenges_ES
dc.publisherSociety for the Study of Reproductiones_ES
dc.rightsclosedAccesses_ES
dc.subjectCarmustinees_ES
dc.subjectDiethyl maleatees_ES
dc.subjectPeroxidase activityes_ES
dc.subjectPeroxiredoxin 2es_ES
dc.subjectReactive oxygenes_ES
dc.subjectSpermes_ES
dc.subjectSpermatozoaes_ES
dc.subjectSperm proteomees_ES
dc.subjectSperm proteomicses_ES
dc.titlePeroxiredoxin 2 and Peroxidase Enzymatic Activity of Mammalian Spermatozoaes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1095/​biolreprod.108.071738-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1095/​biolreprod.108.071738es_ES
dc.identifier.e-issn1529-7268-
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