Perfringolysin O as a useful tool to study human sperm physiology

Autores
Pocognoni, Cristián Adrián; de Blas, Gerardo Andrés; Heuck, Alejandro P.; Belmonte, Silvia Alejandra; Mayorga, Luis Segundo
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Objective: To evaluate perfringolysin O, a cholesterol-dependent pore-forming cytolysin, as a tool to study several aspects of human sperm physiology. Design: Prospective study. Setting: Basic research laboratory. Patient(s): Human semen samples with normal parameters obtained from healthy donors. Intervention(s): Interaction of recombinant perfringolysin O with human spermatozoa. Main Outcome Measure(s): Assessment of perfringolysin O binding to spermatozoa, tests for acrosome and plasma membrane integrity, and acrosomal exocytosis assays. Result(s): Perfringolysin O associated with human spermatozoa at 4 C. The binding was sensitive to changes in cholesterol concentrations and distribution occurring in the plasma membrane of these cells during capacitation. When perfringolysin O–treated sperm were incubated at 37 C, the plasma membrane became permeable, whereas the acrosome membrane remained intact. Permeabilized spermatozoa were able to respond to exocytic stimuli. The process was inhibited by proteins that interfere with membrane fusion, indicating that large molecules, including antibodies, were able to permeate into the spermatozoa. Conclusion(s): PFO is a useful probe to assess changes in the amount and distribution of the active sterol fraction present in the sperm plasma membrane. The toxin can be used for the efficient and selective permeabilization of this membrane, rendering a flexible experimental model suitable for studying molecular processes occurring in the sperm cytoplasm. (Fertil Steril 2013;99:99–106. 2013 by American Society for Reproductive Medicine).
Fil: Pocognoni, Cristián Adrián. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: de Blas, Gerardo Andrés. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: Heuck, Alejandro P.. University of Massachusett. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Belmonte, Silvia Alejandra. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Materia
Perfringgolysin O
Acrosome Reaction
Human Sperm
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10332

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network_name_str CONICET Digital (CONICET)
spelling Perfringolysin O as a useful tool to study human sperm physiologyPocognoni, Cristián Adriánde Blas, Gerardo AndrésHeuck, Alejandro P.Belmonte, Silvia AlejandraMayorga, Luis SegundoPerfringgolysin OAcrosome ReactionHuman Spermhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Objective: To evaluate perfringolysin O, a cholesterol-dependent pore-forming cytolysin, as a tool to study several aspects of human sperm physiology. Design: Prospective study. Setting: Basic research laboratory. Patient(s): Human semen samples with normal parameters obtained from healthy donors. Intervention(s): Interaction of recombinant perfringolysin O with human spermatozoa. Main Outcome Measure(s): Assessment of perfringolysin O binding to spermatozoa, tests for acrosome and plasma membrane integrity, and acrosomal exocytosis assays. Result(s): Perfringolysin O associated with human spermatozoa at 4 C. The binding was sensitive to changes in cholesterol concentrations and distribution occurring in the plasma membrane of these cells during capacitation. When perfringolysin O–treated sperm were incubated at 37 C, the plasma membrane became permeable, whereas the acrosome membrane remained intact. Permeabilized spermatozoa were able to respond to exocytic stimuli. The process was inhibited by proteins that interfere with membrane fusion, indicating that large molecules, including antibodies, were able to permeate into the spermatozoa. Conclusion(s): PFO is a useful probe to assess changes in the amount and distribution of the active sterol fraction present in the sperm plasma membrane. The toxin can be used for the efficient and selective permeabilization of this membrane, rendering a flexible experimental model suitable for studying molecular processes occurring in the sperm cytoplasm. (Fertil Steril 2013;99:99–106. 2013 by American Society for Reproductive Medicine).Fil: Pocognoni, Cristián Adrián. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; ArgentinaFil: de Blas, Gerardo Andrés. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; ArgentinaFil: Heuck, Alejandro P.. University of Massachusett. Department of Biochemistry and Molecular Biology; Estados UnidosFil: Belmonte, Silvia Alejandra. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; ArgentinaFil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; ArgentinaElsevier2013-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10332Pocognoni, Cristián Adrián; de Blas, Gerardo Andrés; Heuck, Alejandro P.; Belmonte, Silvia Alejandra; Mayorga, Luis Segundo; Perfringolysin O as a useful tool to study human sperm physiology; Elsevier; Fertility And Sterility; 99; 1; 1-2013; 99-106.e20015-0282enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0015028212021401info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fertnstert.2012.08.052info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-29T12:02:52Zoai:ri.conicet.gov.ar:11336/10332instacron: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:34982025-10-29 12:02:52.854CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Perfringolysin O as a useful tool to study human sperm physiology
title Perfringolysin O as a useful tool to study human sperm physiology
spellingShingle Perfringolysin O as a useful tool to study human sperm physiology
Pocognoni, Cristián Adrián
Perfringgolysin O
Acrosome Reaction
Human Sperm
title_short Perfringolysin O as a useful tool to study human sperm physiology
title_full Perfringolysin O as a useful tool to study human sperm physiology
title_fullStr Perfringolysin O as a useful tool to study human sperm physiology
title_full_unstemmed Perfringolysin O as a useful tool to study human sperm physiology
title_sort Perfringolysin O as a useful tool to study human sperm physiology
dc.creator.none.fl_str_mv Pocognoni, Cristián Adrián
de Blas, Gerardo Andrés
Heuck, Alejandro P.
Belmonte, Silvia Alejandra
Mayorga, Luis Segundo
author Pocognoni, Cristián Adrián
author_facet Pocognoni, Cristián Adrián
de Blas, Gerardo Andrés
Heuck, Alejandro P.
Belmonte, Silvia Alejandra
Mayorga, Luis Segundo
author_role author
author2 de Blas, Gerardo Andrés
Heuck, Alejandro P.
Belmonte, Silvia Alejandra
Mayorga, Luis Segundo
author2_role author
author
author
author
dc.subject.none.fl_str_mv Perfringgolysin O
Acrosome Reaction
Human Sperm
topic Perfringgolysin O
Acrosome Reaction
Human 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 Objective: To evaluate perfringolysin O, a cholesterol-dependent pore-forming cytolysin, as a tool to study several aspects of human sperm physiology. Design: Prospective study. Setting: Basic research laboratory. Patient(s): Human semen samples with normal parameters obtained from healthy donors. Intervention(s): Interaction of recombinant perfringolysin O with human spermatozoa. Main Outcome Measure(s): Assessment of perfringolysin O binding to spermatozoa, tests for acrosome and plasma membrane integrity, and acrosomal exocytosis assays. Result(s): Perfringolysin O associated with human spermatozoa at 4 C. The binding was sensitive to changes in cholesterol concentrations and distribution occurring in the plasma membrane of these cells during capacitation. When perfringolysin O–treated sperm were incubated at 37 C, the plasma membrane became permeable, whereas the acrosome membrane remained intact. Permeabilized spermatozoa were able to respond to exocytic stimuli. The process was inhibited by proteins that interfere with membrane fusion, indicating that large molecules, including antibodies, were able to permeate into the spermatozoa. Conclusion(s): PFO is a useful probe to assess changes in the amount and distribution of the active sterol fraction present in the sperm plasma membrane. The toxin can be used for the efficient and selective permeabilization of this membrane, rendering a flexible experimental model suitable for studying molecular processes occurring in the sperm cytoplasm. (Fertil Steril 2013;99:99–106. 2013 by American Society for Reproductive Medicine).
Fil: Pocognoni, Cristián Adrián. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: de Blas, Gerardo Andrés. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: Heuck, Alejandro P.. University of Massachusett. Department of Biochemistry and Molecular Biology; Estados Unidos
Fil: Belmonte, Silvia Alejandra. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
Fil: Mayorga, Luis Segundo. Consejo Nacional de Investigaciones Científicas y Tecnicas. Centro Cientifico Tecnologico Mendoza. Instituto Histologia y Embriologia de Mendoza "Dr. M. Burgos"; Argentina
description Objective: To evaluate perfringolysin O, a cholesterol-dependent pore-forming cytolysin, as a tool to study several aspects of human sperm physiology. Design: Prospective study. Setting: Basic research laboratory. Patient(s): Human semen samples with normal parameters obtained from healthy donors. Intervention(s): Interaction of recombinant perfringolysin O with human spermatozoa. Main Outcome Measure(s): Assessment of perfringolysin O binding to spermatozoa, tests for acrosome and plasma membrane integrity, and acrosomal exocytosis assays. Result(s): Perfringolysin O associated with human spermatozoa at 4 C. The binding was sensitive to changes in cholesterol concentrations and distribution occurring in the plasma membrane of these cells during capacitation. When perfringolysin O–treated sperm were incubated at 37 C, the plasma membrane became permeable, whereas the acrosome membrane remained intact. Permeabilized spermatozoa were able to respond to exocytic stimuli. The process was inhibited by proteins that interfere with membrane fusion, indicating that large molecules, including antibodies, were able to permeate into the spermatozoa. Conclusion(s): PFO is a useful probe to assess changes in the amount and distribution of the active sterol fraction present in the sperm plasma membrane. The toxin can be used for the efficient and selective permeabilization of this membrane, rendering a flexible experimental model suitable for studying molecular processes occurring in the sperm cytoplasm. (Fertil Steril 2013;99:99–106. 2013 by American Society for Reproductive Medicine).
publishDate 2013
dc.date.none.fl_str_mv 2013-01
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/11336/10332
Pocognoni, Cristián Adrián; de Blas, Gerardo Andrés; Heuck, Alejandro P.; Belmonte, Silvia Alejandra; Mayorga, Luis Segundo; Perfringolysin O as a useful tool to study human sperm physiology; Elsevier; Fertility And Sterility; 99; 1; 1-2013; 99-106.e2
0015-0282
url http://hdl.handle.net/11336/10332
identifier_str_mv Pocognoni, Cristián Adrián; de Blas, Gerardo Andrés; Heuck, Alejandro P.; Belmonte, Silvia Alejandra; Mayorga, Luis Segundo; Perfringolysin O as a useful tool to study human sperm physiology; Elsevier; Fertility And Sterility; 99; 1; 1-2013; 99-106.e2
0015-0282
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0015028212021401
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.fertnstert.2012.08.052
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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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