Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg

Autores
Cohen, Debora Juana; Ellerman, Diego Andrés; Busso, Dolores; Morgenfeld, Mauro Miguel; Piazza, Alejandra D.; Hayashi, Masaru; Young, Edgardo; Kasahara, Masanori; Cuasnicu, Patricia Sara
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Human epididymal sperm protein ARP, a member of the cysteine-rich secretory proteins (CRISP) family, exhibits significant homology with rat epididymal protein DE, a candidate molecule for mediating sperm-egg fusion in rodents. The aim of this study was to investigate the involvement of ARP in human gamete fusion. Sequential extraction of proteins from ejaculated human sperm revealed the existence of a population of ARP that is tightly associated with the sperm surface and thus, potentially capable of participating in gamete interaction. Exposure of capacitated human sperm to a polyclonal antibody against recombinant ARP (anti-ARP) produced a significant and concentration-dependent inhibition in the ability of human sperm to penetrate zona-free hamster eggs. This inhibition was not due to a deleterious effect on the gametes because anti-ARP affected neither sperm viability or motility, nor egg penetrability. The antibody did not inhibit the occurrence of spontaneous or Ca(2+) ionophore-induced acrosome reaction, nor did it inhibit the ability of sperm to bind to the oolema, supporting a specific inhibition of the antibody at the sperm-egg fusion level. As a relevant evidence for a role of ARP in gamete fusion, the existence of complementary sites for this protein on the surface of human eggs was investigated. Experiments in which zona-free human oocytes discarded from in vitro fertilization programs were exposed to ARP, fixed, and subjected to indirect immunofluorescence revealed the presence of specific ARP-binding sites on the entire surface of the human egg, in agreement with the fusogenic properties of the human oolema. Together, these results strongly support the participation of ARP in the sperm-egg fusion process, suggesting that this protein would be the functional homologue of DE in humans.
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: Ellerman, Diego Andrés. 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: 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: Morgenfeld, Mauro Miguel. 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: Piazza, Alejandra D.. Instituto de Ginecología y Fertilidad; Argentina
Fil: Hayashi, Masaru. Hokkaido University School of Medicine; Japón
Fil: Young, Edgardo. Instituto de Ginecología y Fertilidad; Argentina
Fil: Kasahara, Masanori. Hokkaido University 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
Epidymis
Fertilization
Gamete Biology
Ovum
Sperm
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:11336/31337
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/31337
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human eggCohen, Debora JuanaEllerman, Diego AndrésBusso, DoloresMorgenfeld, Mauro MiguelPiazza, Alejandra D.Hayashi, MasaruYoung, EdgardoKasahara, MasanoriCuasnicu, Patricia SaraEpidymisFertilizationGamete BiologyOvumSpermhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Human epididymal sperm protein ARP, a member of the cysteine-rich secretory proteins (CRISP) family, exhibits significant homology with rat epididymal protein DE, a candidate molecule for mediating sperm-egg fusion in rodents. The aim of this study was to investigate the involvement of ARP in human gamete fusion. Sequential extraction of proteins from ejaculated human sperm revealed the existence of a population of ARP that is tightly associated with the sperm surface and thus, potentially capable of participating in gamete interaction. Exposure of capacitated human sperm to a polyclonal antibody against recombinant ARP (anti-ARP) produced a significant and concentration-dependent inhibition in the ability of human sperm to penetrate zona-free hamster eggs. This inhibition was not due to a deleterious effect on the gametes because anti-ARP affected neither sperm viability or motility, nor egg penetrability. The antibody did not inhibit the occurrence of spontaneous or Ca(2+) ionophore-induced acrosome reaction, nor did it inhibit the ability of sperm to bind to the oolema, supporting a specific inhibition of the antibody at the sperm-egg fusion level. As a relevant evidence for a role of ARP in gamete fusion, the existence of complementary sites for this protein on the surface of human eggs was investigated. Experiments in which zona-free human oocytes discarded from in vitro fertilization programs were exposed to ARP, fixed, and subjected to indirect immunofluorescence revealed the presence of specific ARP-binding sites on the entire surface of the human egg, in agreement with the fusogenic properties of the human oolema. Together, these results strongly support the participation of ARP in the sperm-egg fusion process, suggesting that this protein would be the functional homologue of DE in humans.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; ArgentinaFil: Ellerman, Diego Andrés. 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: 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: Morgenfeld, Mauro Miguel. 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: Piazza, Alejandra D.. Instituto de Ginecología y Fertilidad; ArgentinaFil: Hayashi, Masaru. Hokkaido University School of Medicine; JapónFil: Young, Edgardo. Instituto de Ginecología y Fertilidad; ArgentinaFil: Kasahara, Masanori. Hokkaido University 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; ArgentinaSociety for the Study of Reproduction2001-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31337Cuasnicu, Patricia Sara; Kasahara, Masanori; Young, Edgardo; Hayashi, Masaru; Piazza, Alejandra D.; Morgenfeld, Mauro Miguel; et al.; Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg; Society for the Study of Reproduction; Biology of Reproduction; 65; 4; 5-2001; 1000-10050006-33631529-7268CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.bioone.org/doi/abs/10.1095/biolreprod65.4.1000info:eu-repo/semantics/altIdentifier/doi/10.1095/biolreprod65.4.1000info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/11566719info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:44:52Zoai:ri.conicet.gov.ar:11336/31337instacron: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 09:44:52.774CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
title Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
spellingShingle Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
Cohen, Debora Juana
Epidymis
Fertilization
Gamete Biology
Ovum
Sperm
title_short Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
title_full Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
title_fullStr Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
title_full_unstemmed Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
title_sort Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg
dc.creator.none.fl_str_mv Cohen, Debora Juana
Ellerman, Diego Andrés
Busso, Dolores
Morgenfeld, Mauro Miguel
Piazza, Alejandra D.
Hayashi, Masaru
Young, Edgardo
Kasahara, Masanori
Cuasnicu, Patricia Sara
author Cohen, Debora Juana
author_facet Cohen, Debora Juana
Ellerman, Diego Andrés
Busso, Dolores
Morgenfeld, Mauro Miguel
Piazza, Alejandra D.
Hayashi, Masaru
Young, Edgardo
Kasahara, Masanori
Cuasnicu, Patricia Sara
author_role author
author2 Ellerman, Diego Andrés
Busso, Dolores
Morgenfeld, Mauro Miguel
Piazza, Alejandra D.
Hayashi, Masaru
Young, Edgardo
Kasahara, Masanori
Cuasnicu, Patricia Sara
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Epidymis
Fertilization
Gamete Biology
Ovum
Sperm
topic Epidymis
Fertilization
Gamete Biology
Ovum
Sperm
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Human epididymal sperm protein ARP, a member of the cysteine-rich secretory proteins (CRISP) family, exhibits significant homology with rat epididymal protein DE, a candidate molecule for mediating sperm-egg fusion in rodents. The aim of this study was to investigate the involvement of ARP in human gamete fusion. Sequential extraction of proteins from ejaculated human sperm revealed the existence of a population of ARP that is tightly associated with the sperm surface and thus, potentially capable of participating in gamete interaction. Exposure of capacitated human sperm to a polyclonal antibody against recombinant ARP (anti-ARP) produced a significant and concentration-dependent inhibition in the ability of human sperm to penetrate zona-free hamster eggs. This inhibition was not due to a deleterious effect on the gametes because anti-ARP affected neither sperm viability or motility, nor egg penetrability. The antibody did not inhibit the occurrence of spontaneous or Ca(2+) ionophore-induced acrosome reaction, nor did it inhibit the ability of sperm to bind to the oolema, supporting a specific inhibition of the antibody at the sperm-egg fusion level. As a relevant evidence for a role of ARP in gamete fusion, the existence of complementary sites for this protein on the surface of human eggs was investigated. Experiments in which zona-free human oocytes discarded from in vitro fertilization programs were exposed to ARP, fixed, and subjected to indirect immunofluorescence revealed the presence of specific ARP-binding sites on the entire surface of the human egg, in agreement with the fusogenic properties of the human oolema. Together, these results strongly support the participation of ARP in the sperm-egg fusion process, suggesting that this protein would be the functional homologue of DE in humans.
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: Ellerman, Diego Andrés. 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: 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: Morgenfeld, Mauro Miguel. 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: Piazza, Alejandra D.. Instituto de Ginecología y Fertilidad; Argentina
Fil: Hayashi, Masaru. Hokkaido University School of Medicine; Japón
Fil: Young, Edgardo. Instituto de Ginecología y Fertilidad; Argentina
Fil: Kasahara, Masanori. Hokkaido University 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 Human epididymal sperm protein ARP, a member of the cysteine-rich secretory proteins (CRISP) family, exhibits significant homology with rat epididymal protein DE, a candidate molecule for mediating sperm-egg fusion in rodents. The aim of this study was to investigate the involvement of ARP in human gamete fusion. Sequential extraction of proteins from ejaculated human sperm revealed the existence of a population of ARP that is tightly associated with the sperm surface and thus, potentially capable of participating in gamete interaction. Exposure of capacitated human sperm to a polyclonal antibody against recombinant ARP (anti-ARP) produced a significant and concentration-dependent inhibition in the ability of human sperm to penetrate zona-free hamster eggs. This inhibition was not due to a deleterious effect on the gametes because anti-ARP affected neither sperm viability or motility, nor egg penetrability. The antibody did not inhibit the occurrence of spontaneous or Ca(2+) ionophore-induced acrosome reaction, nor did it inhibit the ability of sperm to bind to the oolema, supporting a specific inhibition of the antibody at the sperm-egg fusion level. As a relevant evidence for a role of ARP in gamete fusion, the existence of complementary sites for this protein on the surface of human eggs was investigated. Experiments in which zona-free human oocytes discarded from in vitro fertilization programs were exposed to ARP, fixed, and subjected to indirect immunofluorescence revealed the presence of specific ARP-binding sites on the entire surface of the human egg, in agreement with the fusogenic properties of the human oolema. Together, these results strongly support the participation of ARP in the sperm-egg fusion process, suggesting that this protein would be the functional homologue of DE in humans.
publishDate 2001
dc.date.none.fl_str_mv 2001-05
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/11336/31337
Cuasnicu, Patricia Sara; Kasahara, Masanori; Young, Edgardo; Hayashi, Masaru; Piazza, Alejandra D.; Morgenfeld, Mauro Miguel; et al.; Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg; Society for the Study of Reproduction; Biology of Reproduction; 65; 4; 5-2001; 1000-1005
0006-3363
1529-7268
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31337
identifier_str_mv Cuasnicu, Patricia Sara; Kasahara, Masanori; Young, Edgardo; Hayashi, Masaru; Piazza, Alejandra D.; Morgenfeld, Mauro Miguel; et al.; Evidence that human epididymal protein ARP plays a role in gamete fusion through complementary sites on the surface of the human egg; Society for the Study of Reproduction; Biology of Reproduction; 65; 4; 5-2001; 1000-1005
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/http://www.bioone.org/doi/abs/10.1095/biolreprod65.4.1000
info:eu-repo/semantics/altIdentifier/doi/10.1095/biolreprod65.4.1000
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/11566719
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
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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score 13.13397

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