Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction

Autores
Busso, Dolores; Cohen, Debora Juana; Hayashi, M.; Kasahara, M.; Cuasnicu, Patricia Sara
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Testicular protein Tpx-1, also known as CRISP-2, is a cysteine-rich secretory protein specifically expressed in the male reproductive tract. Since the information available on the human protein is limited to the identification and expression of its gene, in this work we have studied the presence and localization of human Tpx-1 (TPX1) in sperm, its fate after capacitation and acrosome reaction (AR), and its possible involvement in gamete interaction. Indirect immunofluorescence studies revealed the absence of significant staining in live or fixed non-permeabilized sperm, in contrast to a clear labelling in the acrosomal region of permeabilized sperm. These results, together with complementary evidence from protein extraction procedures strongly support that TPX1 would be mainly an intra-acrosomal protein in fresh sperm. After in vitro capacitation and ionophore-induced AR, TPX1 remained associated with the equatorial segment of the acrosome. The lack of differences in the electrophoretic mobility of TPX1 before and after capacitation and AR indicates that the protein would not undergo proteolytical modifications during these processes. The possible involvement of TPX1 in gamete interaction was evaluated by the hamster oocyte penetration test. The presence of anti-TPX1 during gamete co-incubation produced a significant and dose-dependent inhibition in the percentage of penetrated zona-free hamster oocytes without affecting sperm motility, the AR or sperm binding to the oolema. Together, these results indicate that human TPX1 would be a component of the sperm acrosome that remains associated with sperm after capacitation and AR, and is relevant for sperm-oocyte interaction.
Fil: Busso, Dolores. 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: Cohen, Debora Juana. 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: Hayashi, M.. Hokkaido University Graduate School Of Medicine; Japón
Fil: Kasahara, M.. Hokkaido University Graduate School Of Medicine; Japón
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
Materia
Sperm
Egg
Fertilization
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:11336/31466
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/31466
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interactionBusso, DoloresCohen, Debora JuanaHayashi, M.Kasahara, M.Cuasnicu, Patricia SaraSpermEggFertilizationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Testicular protein Tpx-1, also known as CRISP-2, is a cysteine-rich secretory protein specifically expressed in the male reproductive tract. Since the information available on the human protein is limited to the identification and expression of its gene, in this work we have studied the presence and localization of human Tpx-1 (TPX1) in sperm, its fate after capacitation and acrosome reaction (AR), and its possible involvement in gamete interaction. Indirect immunofluorescence studies revealed the absence of significant staining in live or fixed non-permeabilized sperm, in contrast to a clear labelling in the acrosomal region of permeabilized sperm. These results, together with complementary evidence from protein extraction procedures strongly support that TPX1 would be mainly an intra-acrosomal protein in fresh sperm. After in vitro capacitation and ionophore-induced AR, TPX1 remained associated with the equatorial segment of the acrosome. The lack of differences in the electrophoretic mobility of TPX1 before and after capacitation and AR indicates that the protein would not undergo proteolytical modifications during these processes. The possible involvement of TPX1 in gamete interaction was evaluated by the hamster oocyte penetration test. The presence of anti-TPX1 during gamete co-incubation produced a significant and dose-dependent inhibition in the percentage of penetrated zona-free hamster oocytes without affecting sperm motility, the AR or sperm binding to the oolema. Together, these results indicate that human TPX1 would be a component of the sperm acrosome that remains associated with sperm after capacitation and AR, and is relevant for sperm-oocyte interaction.Fil: Busso, Dolores. 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: Cohen, Debora Juana. 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: Hayashi, M.. Hokkaido University Graduate School Of Medicine; JapónFil: Kasahara, M.. Hokkaido University Graduate School Of Medicine; JapónFil: 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; ArgentinaOxford University Press2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31466Busso, Dolores; Cohen, Debora Juana; Hayashi, M.; Kasahara, M.; Cuasnicu, Patricia Sara; Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction; Oxford University Press; Molecular Human Reproduction; 11; 4; 2005; 299-3051360-99471460-2407CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/molehr/article/11/4/299/1080163info:eu-repo/semantics/altIdentifier/doi/10.1093/molehr/gah156info:eu-repo/semantics/altIdentifier/pmid/15734896info:eu-repo/semantics/altIdentifier/url/http://sfx.metabib.ch/sfx_locater?sid=Entrez:PubMed&id=pmid:15734896info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:32Zoai:ri.conicet.gov.ar:11336/31466instacron: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:34982025-09-03 09:59:32.446CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
title Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
spellingShingle Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
Busso, Dolores
Sperm
Egg
Fertilization
title_short Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
title_full Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
title_fullStr Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
title_full_unstemmed Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
title_sort Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction
dc.creator.none.fl_str_mv Busso, Dolores
Cohen, Debora Juana
Hayashi, M.
Kasahara, M.
Cuasnicu, Patricia Sara
author Busso, Dolores
author_facet Busso, Dolores
Cohen, Debora Juana
Hayashi, M.
Kasahara, M.
Cuasnicu, Patricia Sara
author_role author
author2 Cohen, Debora Juana
Hayashi, M.
Kasahara, M.
Cuasnicu, Patricia Sara
author2_role author
author
author
author
dc.subject.none.fl_str_mv Sperm
Egg
Fertilization
topic Sperm
Egg
Fertilization
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Testicular protein Tpx-1, also known as CRISP-2, is a cysteine-rich secretory protein specifically expressed in the male reproductive tract. Since the information available on the human protein is limited to the identification and expression of its gene, in this work we have studied the presence and localization of human Tpx-1 (TPX1) in sperm, its fate after capacitation and acrosome reaction (AR), and its possible involvement in gamete interaction. Indirect immunofluorescence studies revealed the absence of significant staining in live or fixed non-permeabilized sperm, in contrast to a clear labelling in the acrosomal region of permeabilized sperm. These results, together with complementary evidence from protein extraction procedures strongly support that TPX1 would be mainly an intra-acrosomal protein in fresh sperm. After in vitro capacitation and ionophore-induced AR, TPX1 remained associated with the equatorial segment of the acrosome. The lack of differences in the electrophoretic mobility of TPX1 before and after capacitation and AR indicates that the protein would not undergo proteolytical modifications during these processes. The possible involvement of TPX1 in gamete interaction was evaluated by the hamster oocyte penetration test. The presence of anti-TPX1 during gamete co-incubation produced a significant and dose-dependent inhibition in the percentage of penetrated zona-free hamster oocytes without affecting sperm motility, the AR or sperm binding to the oolema. Together, these results indicate that human TPX1 would be a component of the sperm acrosome that remains associated with sperm after capacitation and AR, and is relevant for sperm-oocyte interaction.
Fil: Busso, Dolores. 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: Cohen, Debora Juana. 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: Hayashi, M.. Hokkaido University Graduate School Of Medicine; Japón
Fil: Kasahara, M.. Hokkaido University Graduate School Of Medicine; Japón
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
description Testicular protein Tpx-1, also known as CRISP-2, is a cysteine-rich secretory protein specifically expressed in the male reproductive tract. Since the information available on the human protein is limited to the identification and expression of its gene, in this work we have studied the presence and localization of human Tpx-1 (TPX1) in sperm, its fate after capacitation and acrosome reaction (AR), and its possible involvement in gamete interaction. Indirect immunofluorescence studies revealed the absence of significant staining in live or fixed non-permeabilized sperm, in contrast to a clear labelling in the acrosomal region of permeabilized sperm. These results, together with complementary evidence from protein extraction procedures strongly support that TPX1 would be mainly an intra-acrosomal protein in fresh sperm. After in vitro capacitation and ionophore-induced AR, TPX1 remained associated with the equatorial segment of the acrosome. The lack of differences in the electrophoretic mobility of TPX1 before and after capacitation and AR indicates that the protein would not undergo proteolytical modifications during these processes. The possible involvement of TPX1 in gamete interaction was evaluated by the hamster oocyte penetration test. The presence of anti-TPX1 during gamete co-incubation produced a significant and dose-dependent inhibition in the percentage of penetrated zona-free hamster oocytes without affecting sperm motility, the AR or sperm binding to the oolema. Together, these results indicate that human TPX1 would be a component of the sperm acrosome that remains associated with sperm after capacitation and AR, and is relevant for sperm-oocyte interaction.
publishDate 2005
dc.date.none.fl_str_mv 2005
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/11336/31466
Busso, Dolores; Cohen, Debora Juana; Hayashi, M.; Kasahara, M.; Cuasnicu, Patricia Sara; Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction; Oxford University Press; Molecular Human Reproduction; 11; 4; 2005; 299-305
1360-9947
1460-2407
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31466
identifier_str_mv Busso, Dolores; Cohen, Debora Juana; Hayashi, M.; Kasahara, M.; Cuasnicu, Patricia Sara; Human testicular protein TPX-1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction; Oxford University Press; Molecular Human Reproduction; 11; 4; 2005; 299-305
1360-9947
1460-2407
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/molehr/article/11/4/299/1080163
info:eu-repo/semantics/altIdentifier/doi/10.1093/molehr/gah156
info:eu-repo/semantics/altIdentifier/pmid/15734896
info:eu-repo/semantics/altIdentifier/url/http://sfx.metabib.ch/sfx_locater?sid=Entrez:PubMed&id=pmid:15734896
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
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
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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