Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)

Autores
Da Ros, V.G.; Maldera, J.A.; Willis, W.D.; Cohen, D.J.; Goulding, E.H.; Gelman, D.M.; Rubinstein, M.; Eddy, E.M.; Cuasnicu, P.S.
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. Epididymal protein CRISP1, a member of the Cysteine-RIch Secretory Protein (CRISP) family, was identified by our laboratory and postulated to participate in both sperm-zona pellucida (ZP) interaction and gamete fusion by binding to egg-complementary sites. To elucidate the functional role of CRISP1 in vivo, we disrupted the Crisp1 gene and evaluated the effect on animal fertility and several sperm parameters. Male and female Crisp1-/- animals exhibited no differences in fertility compared to controls. Sperm motility and the ability to undergo a spontaneous or progesterone-induced acrosome reaction were neither affected in Crisp1-/- mice. However, the level of protein tyrosine phosphorylation during capacitation was clearly lower in mutant sperm than in controls. In vitro fertilization assays showed that Crisp1-/- sperm also exhibited a significantly reduced ability to penetrate both ZP-intact and ZP-free eggs. Moreover, when ZP-free eggs were simultaneously inseminated with Crisp1+/+ and Crisp1-/- sperm in a competition assay, the mutant sperm exhibited a greater disadvantage in their fusion ability. Finally, the finding that the fusion ability of Crisp1-/- sperm was further inhibited by the presence of CRISP1 or CRISP2 during gamete co-incubation, supports that another CRISP cooperates with CRISP1 during fertilization and might compensate for its lack in the mutant mice. Together, these results indicate that CRISP proteins are players in the mammalian fertilization process. To our knowledge this is the first knockout mice generated for a CRISP protein. The information obtained might have important functional implications for other members of the widely distributed and evolutionarily conserved CRISP family. © 2008 Elsevier Inc.
Fil:Da Ros, V.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Cohen, D.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Gelman, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Rubinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Cuasnicu, P.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Dev. Biol. 2008;320(1):12-18
Materia
CRISP
Egg
Fertilization
Sperm
cysteine rich secretory protein 1
DNA
RNA
secretory protein
tyrosine
acrosome reaction
animal cell
animal experiment
animal tissue
article
controlled study
female
fertility
fertilization
fertilization in vitro
gene disruption
genotype
immunoblotting
male
mouse
mutant
nonhuman
priority journal
protein phosphorylation
reverse transcription polymerase chain reaction
sperm
spermatozoon capacitation
spermatozoon motility
zona pellucida
Animalia
Mammalia
Mus
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_00121606_v320_n1_p12_DaRos

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oai_identifier_str paperaa:paper_00121606_v320_n1_p12_DaRos
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)Da Ros, V.G.Maldera, J.A.Willis, W.D.Cohen, D.J.Goulding, E.H.Gelman, D.M.Rubinstein, M.Eddy, E.M.Cuasnicu, P.S.CRISPEggFertilizationSpermcysteine rich secretory protein 1DNARNAsecretory proteintyrosineacrosome reactionanimal cellanimal experimentanimal tissuearticlecontrolled studyfemalefertilityfertilizationfertilization in vitrogene disruptiongenotypeimmunoblottingmalemousemutantnonhumanpriority journalprotein phosphorylationreverse transcription polymerase chain reactionspermspermatozoon capacitationspermatozoon motilityzona pellucidaAnimaliaMammaliaMusMammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. Epididymal protein CRISP1, a member of the Cysteine-RIch Secretory Protein (CRISP) family, was identified by our laboratory and postulated to participate in both sperm-zona pellucida (ZP) interaction and gamete fusion by binding to egg-complementary sites. To elucidate the functional role of CRISP1 in vivo, we disrupted the Crisp1 gene and evaluated the effect on animal fertility and several sperm parameters. Male and female Crisp1-/- animals exhibited no differences in fertility compared to controls. Sperm motility and the ability to undergo a spontaneous or progesterone-induced acrosome reaction were neither affected in Crisp1-/- mice. However, the level of protein tyrosine phosphorylation during capacitation was clearly lower in mutant sperm than in controls. In vitro fertilization assays showed that Crisp1-/- sperm also exhibited a significantly reduced ability to penetrate both ZP-intact and ZP-free eggs. Moreover, when ZP-free eggs were simultaneously inseminated with Crisp1+/+ and Crisp1-/- sperm in a competition assay, the mutant sperm exhibited a greater disadvantage in their fusion ability. Finally, the finding that the fusion ability of Crisp1-/- sperm was further inhibited by the presence of CRISP1 or CRISP2 during gamete co-incubation, supports that another CRISP cooperates with CRISP1 during fertilization and might compensate for its lack in the mutant mice. Together, these results indicate that CRISP proteins are players in the mammalian fertilization process. To our knowledge this is the first knockout mice generated for a CRISP protein. The information obtained might have important functional implications for other members of the widely distributed and evolutionarily conserved CRISP family. © 2008 Elsevier Inc.Fil:Da Ros, V.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Cohen, D.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Gelman, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Rubinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Cuasnicu, P.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.2008info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_00121606_v320_n1_p12_DaRosDev. Biol. 2008;320(1):12-18reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-10-16T09:29:59Zpaperaa:paper_00121606_v320_n1_p12_DaRosInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-10-16 09:30:00.107Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
title Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
spellingShingle Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
Da Ros, V.G.
CRISP
Egg
Fertilization
Sperm
cysteine rich secretory protein 1
DNA
RNA
secretory protein
tyrosine
acrosome reaction
animal cell
animal experiment
animal tissue
article
controlled study
female
fertility
fertilization
fertilization in vitro
gene disruption
genotype
immunoblotting
male
mouse
mutant
nonhuman
priority journal
protein phosphorylation
reverse transcription polymerase chain reaction
sperm
spermatozoon capacitation
spermatozoon motility
zona pellucida
Animalia
Mammalia
Mus
title_short Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
title_full Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
title_fullStr Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
title_full_unstemmed Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
title_sort Impaired sperm fertilizing ability in mice lacking Cysteine-RIch Secretory Protein 1 (CRISP1)
dc.creator.none.fl_str_mv Da Ros, V.G.
Maldera, J.A.
Willis, W.D.
Cohen, D.J.
Goulding, E.H.
Gelman, D.M.
Rubinstein, M.
Eddy, E.M.
Cuasnicu, P.S.
author Da Ros, V.G.
author_facet Da Ros, V.G.
Maldera, J.A.
Willis, W.D.
Cohen, D.J.
Goulding, E.H.
Gelman, D.M.
Rubinstein, M.
Eddy, E.M.
Cuasnicu, P.S.
author_role author
author2 Maldera, J.A.
Willis, W.D.
Cohen, D.J.
Goulding, E.H.
Gelman, D.M.
Rubinstein, M.
Eddy, E.M.
Cuasnicu, P.S.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CRISP
Egg
Fertilization
Sperm
cysteine rich secretory protein 1
DNA
RNA
secretory protein
tyrosine
acrosome reaction
animal cell
animal experiment
animal tissue
article
controlled study
female
fertility
fertilization
fertilization in vitro
gene disruption
genotype
immunoblotting
male
mouse
mutant
nonhuman
priority journal
protein phosphorylation
reverse transcription polymerase chain reaction
sperm
spermatozoon capacitation
spermatozoon motility
zona pellucida
Animalia
Mammalia
Mus
topic CRISP
Egg
Fertilization
Sperm
cysteine rich secretory protein 1
DNA
RNA
secretory protein
tyrosine
acrosome reaction
animal cell
animal experiment
animal tissue
article
controlled study
female
fertility
fertilization
fertilization in vitro
gene disruption
genotype
immunoblotting
male
mouse
mutant
nonhuman
priority journal
protein phosphorylation
reverse transcription polymerase chain reaction
sperm
spermatozoon capacitation
spermatozoon motility
zona pellucida
Animalia
Mammalia
Mus
dc.description.none.fl_txt_mv Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. Epididymal protein CRISP1, a member of the Cysteine-RIch Secretory Protein (CRISP) family, was identified by our laboratory and postulated to participate in both sperm-zona pellucida (ZP) interaction and gamete fusion by binding to egg-complementary sites. To elucidate the functional role of CRISP1 in vivo, we disrupted the Crisp1 gene and evaluated the effect on animal fertility and several sperm parameters. Male and female Crisp1-/- animals exhibited no differences in fertility compared to controls. Sperm motility and the ability to undergo a spontaneous or progesterone-induced acrosome reaction were neither affected in Crisp1-/- mice. However, the level of protein tyrosine phosphorylation during capacitation was clearly lower in mutant sperm than in controls. In vitro fertilization assays showed that Crisp1-/- sperm also exhibited a significantly reduced ability to penetrate both ZP-intact and ZP-free eggs. Moreover, when ZP-free eggs were simultaneously inseminated with Crisp1+/+ and Crisp1-/- sperm in a competition assay, the mutant sperm exhibited a greater disadvantage in their fusion ability. Finally, the finding that the fusion ability of Crisp1-/- sperm was further inhibited by the presence of CRISP1 or CRISP2 during gamete co-incubation, supports that another CRISP cooperates with CRISP1 during fertilization and might compensate for its lack in the mutant mice. Together, these results indicate that CRISP proteins are players in the mammalian fertilization process. To our knowledge this is the first knockout mice generated for a CRISP protein. The information obtained might have important functional implications for other members of the widely distributed and evolutionarily conserved CRISP family. © 2008 Elsevier Inc.
Fil:Da Ros, V.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Cohen, D.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Gelman, D.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Rubinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Cuasnicu, P.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. Epididymal protein CRISP1, a member of the Cysteine-RIch Secretory Protein (CRISP) family, was identified by our laboratory and postulated to participate in both sperm-zona pellucida (ZP) interaction and gamete fusion by binding to egg-complementary sites. To elucidate the functional role of CRISP1 in vivo, we disrupted the Crisp1 gene and evaluated the effect on animal fertility and several sperm parameters. Male and female Crisp1-/- animals exhibited no differences in fertility compared to controls. Sperm motility and the ability to undergo a spontaneous or progesterone-induced acrosome reaction were neither affected in Crisp1-/- mice. However, the level of protein tyrosine phosphorylation during capacitation was clearly lower in mutant sperm than in controls. In vitro fertilization assays showed that Crisp1-/- sperm also exhibited a significantly reduced ability to penetrate both ZP-intact and ZP-free eggs. Moreover, when ZP-free eggs were simultaneously inseminated with Crisp1+/+ and Crisp1-/- sperm in a competition assay, the mutant sperm exhibited a greater disadvantage in their fusion ability. Finally, the finding that the fusion ability of Crisp1-/- sperm was further inhibited by the presence of CRISP1 or CRISP2 during gamete co-incubation, supports that another CRISP cooperates with CRISP1 during fertilization and might compensate for its lack in the mutant mice. Together, these results indicate that CRISP proteins are players in the mammalian fertilization process. To our knowledge this is the first knockout mice generated for a CRISP protein. The information obtained might have important functional implications for other members of the widely distributed and evolutionarily conserved CRISP family. © 2008 Elsevier Inc.
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/20.500.12110/paper_00121606_v320_n1_p12_DaRos
url http://hdl.handle.net/20.500.12110/paper_00121606_v320_n1_p12_DaRos
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Dev. Biol. 2008;320(1):12-18
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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