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
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/10332
Ver los metadatos del registro completo
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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 |
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2013-01 |
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publishedVersion |
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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 |
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eng |
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