Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation

Autores
Dematteis, Andrea; Miranda, Sabrina Desiree; Novella, María de Lourdes; Maldonado, Cristina Alicia; Ponce, Rubén Hugo; Maldera, Julieta Antonella; Cuasnicu, Patricia Sara; Coronel, Carlos Enrique
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Caltrin 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.
Fil: Dematteis, Andrea. Universidad Nacional de Córdoba; Argentina
Fil: Miranda, Sabrina Desiree. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Novella, María de Lourdes. Universidad Nacional de Córdoba; Argentina
Fil: Maldonado, Cristina Alicia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopia Electronica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ponce, Rubén Hugo. Universidad Nacional de Córdoba; Argentina
Fil: 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
Fil: 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
Fil: Coronel, Carlos Enrique. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Acrosome Reaction
Calcium
Male Reproductive Tract
Sperm Capacitation
Male Reproductive Tract
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/26330
Acceder
id CONICETDig_75a5fe91e1f809d487b1d311575e1b65
oai_identifier_str oai:ri.conicet.gov.ar:11336/26330
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitationDematteis, AndreaMiranda, Sabrina DesireeNovella, María de LourdesMaldonado, Cristina AliciaPonce, Rubén HugoMaldera, Julieta AntonellaCuasnicu, Patricia SaraCoronel, Carlos EnriqueAcrosome ReactionCalciumMale Reproductive TractSperm CapacitationMale Reproductive Tracthttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Caltrin 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.Fil: Dematteis, Andrea. Universidad Nacional de Córdoba; ArgentinaFil: Miranda, Sabrina Desiree. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Novella, María de Lourdes. Universidad Nacional de Córdoba; ArgentinaFil: Maldonado, Cristina Alicia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopia Electronica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Ponce, Rubén Hugo. Universidad Nacional de Córdoba; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaFil: Coronel, Carlos Enrique. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaSociety for the Study of Reproduction2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26330Dematteis, 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; 493-5000006-33631529-7268CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/biolreprod/article-lookup/doi/10.1095/biolreprod.107.067538info:eu-repo/semantics/altIdentifier/doi/10.1095/biolreprod.107.067538info:eu-repo/semantics/altIdentifier/pmid/18550793info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:24:26Zoai:ri.conicet.gov.ar:11336/26330instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:24:26.413CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
title Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
spellingShingle Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
Dematteis, Andrea
Acrosome Reaction
Calcium
Male Reproductive Tract
Sperm Capacitation
Male Reproductive Tract
title_short Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
title_full Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
title_fullStr Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
title_full_unstemmed Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
title_sort Rat caltrin protein modulates the acrosomal exocytosis during sperm capacitation
dc.creator.none.fl_str_mv Dematteis, Andrea
Miranda, Sabrina Desiree
Novella, María de Lourdes
Maldonado, Cristina Alicia
Ponce, Rubén Hugo
Maldera, Julieta Antonella
Cuasnicu, Patricia Sara
Coronel, Carlos Enrique
author Dematteis, Andrea
author_facet Dematteis, Andrea
Miranda, Sabrina Desiree
Novella, María de Lourdes
Maldonado, Cristina Alicia
Ponce, Rubén Hugo
Maldera, Julieta Antonella
Cuasnicu, Patricia Sara
Coronel, Carlos Enrique
author_role author
author2 Miranda, Sabrina Desiree
Novella, María de Lourdes
Maldonado, Cristina Alicia
Ponce, Rubén Hugo
Maldera, Julieta Antonella
Cuasnicu, Patricia Sara
Coronel, Carlos Enrique
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Acrosome Reaction
Calcium
Male Reproductive Tract
Sperm Capacitation
Male Reproductive Tract
topic Acrosome Reaction
Calcium
Male Reproductive Tract
Sperm Capacitation
Male Reproductive Tract
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Caltrin 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.
Fil: Dematteis, Andrea. Universidad Nacional de Córdoba; Argentina
Fil: Miranda, Sabrina Desiree. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Novella, María de Lourdes. Universidad Nacional de Córdoba; Argentina
Fil: Maldonado, Cristina Alicia. Universidad Nacional de Córdoba. Facultad de Medicina. Centro de Microscopia Electronica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Ponce, Rubén Hugo. Universidad Nacional de Córdoba; Argentina
Fil: 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
Fil: 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
Fil: Coronel, Carlos Enrique. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Caltrin 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.
publishDate 2008
dc.date.none.fl_str_mv 2008
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/26330
Dematteis, 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
0006-3363
1529-7268
CONICET Digital
CONICET
url http://hdl.handle.net/11336/26330
identifier_str_mv Dematteis, 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
0006-3363
1529-7268
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/biolreprod/article-lookup/doi/10.1095/biolreprod.107.067538
info:eu-repo/semantics/altIdentifier/doi/10.1095/biolreprod.107.067538
info:eu-repo/semantics/altIdentifier/pmid/18550793
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Society for the Study of Reproduction
publisher.none.fl_str_mv Society for the Study of Reproduction
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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