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dc.creatorDematteis, Andrea-
dc.creatorMiranda, Sabrina Desiree-
dc.creatorNovella, María de Lourdes-
dc.creatorMaldonado, Cristina Alicia-
dc.creatorPonce, Rubén Hugo-
dc.creatorMaldera, Julieta Antonella-
dc.creatorCuasnicu, Patricia Sara-
dc.creatorCoronel, Carlos Enrique-
dc.date2017-10-10T15:09:34Z-
dc.date2017-10-10T15:09:34Z-
dc.date2008-
dc.date2017-10-04T16:55:28Z-
dc.date.accessioned2019-04-29T15:40:16Z-
dc.date.available2019-04-29T15:40:16Z-
dc.date.issued2017-10-10T15:09:34Z-
dc.date.issued2017-10-10T15:09:34Z-
dc.date.issued2008-
dc.date.issued2017-10-04T16:55:28Z-
dc.identifierDematteis, Andrea; Miranda, Sabrina Desiree; Novella, María de Lourdes; Maldonado, Cristina Alicia; Ponce, Rubén Hugo; et al.; Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation; Society for the Study of Reproduction; Biology of Reproduction; 79; 3; -1-2008; 493-500-
dc.identifier0006-3363-
dc.identifierhttp://hdl.handle.net/11336/26330-
dc.identifier1529-7268-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/299080-
dc.descriptionCaltrin is a small and basic protein of the seminal vesicle secretion that inhibits sperm calcium uptake. The influence of rat caltrin on sperm physiological processes related to fertilizing competence was studied by examining its effect on 1) spontaneous acrosomal exocytosis, 2) protein tyrosine phosphorylation, and 3) sperm-egg interaction. Results show that the presence of caltrin during in vitro capacitation both reduced the rate of spontaneous acrosomal exocytosis without altering the pattern of protein tyrosine phosphorylation, and enhanced the sperm ability to bind to the zona pellucida (ZP). The significantly higher proportion of sperm with intact acrosome observed in the presence of caltrin was accompanied by a strong inhibition in the acrosomal hyaluronidase release. Enhancement of sperm-ZP binding was evident by the increase in the percentage of eggs with bound spermatozoa as well as in the number of bound sperm per egg. Similar results were obtained when the assays were performed using spermatozoa preincubated with caltrin and then washed to remove the unbound protein, indicating that the sperm-bound caltrin was the one involved in both acrosomal exocytosis inhibition and sperm-ZP binding enhancement. Caltrin bound to the sperm head was partially released during the acrosomal exocytosis induced by Ca-ionophore A23187. Indirect immunofluorescence and immunoelectron microscopy studies revealed that caltrin molecules distributed on the dorsal sperm surface disappeared after ionophore exposure, whereas those on the ventral region remained in this localization after the treatment. The present data suggest that rat caltrin molecules bound to the sperm head during ejaculation prevent the occurrence of the spontaneous acrosomal exocytosis along the female reproductive tract. Consequently, more competent spermatozoa with intact and functional acrosome would be available in the oviduct to participate in fertilization.-
dc.descriptionFil: Dematteis, Andrea. Universidad Nacional de Córdoba; Argentina-
dc.descriptionFil: Miranda, Sabrina Desiree. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Novella, María de Lourdes. Universidad Nacional de Córdoba; Argentina-
dc.descriptionFil: Maldonado, Cristina Alicia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopia Electronica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Ponce, Rubén Hugo. Universidad Nacional de Córdoba; Argentina-
dc.descriptionFil: Maldera, Julieta Antonella. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina-
dc.descriptionFil: Cuasnicu, Patricia Sara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina-
dc.descriptionFil: Coronel, Carlos Enrique. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
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dc.languageeng-
dc.publisherSociety for the Study of Reproduction-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/biolreprod/article-lookup/doi/10.1095/biolreprod.107.067538-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1095/biolreprod.107.067538-
dc.relationinfo:eu-repo/semantics/altIdentifier/pmid/18550793-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectACROSOME REACTION-
dc.subjectCALCIUM-
dc.subjectMALE REPRODUCTIVE TRACT-
dc.subjectSPERM CAPACITATION-
dc.subjectMALE REPRODUCTIVE TRACT-
dc.subjectBioquímica y Biología Molecular-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleRat caltrin protein modulates the acrosomal exocytosis during sperm capacitation-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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