Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling

Autores
Peñalva, Daniel Alejandro; Hozbor, Federico Andrés; Aveldaño, Marta Isabel; Antollini, Silvia Susana
Año de publicación
2019
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Although the molecular changes that affect the spermatozoa of economically important animals, such as bull and ram, are of great research interest, changes regarding plasma membrane lipid organization as temperature decreases are still poorly understood. Gametes from these mammals contain sphingomyelin (SM) species very long chain n-3 polyunsaturated fatty acids (VLCPUFA). (e.g., 30:6 SM, 32:6 SM and 34:6 SM in ram), while in most mammalian cells SM typically contains saturated and monounsaturated acyl chains (C14 to C24). Also, these spermatozoa have three subclasses of choline glycerophospholipids (CGP) with docosahexaenoic acid (22:6n-3) ester-bound at the sn-2 position of glycerol, the sn-1 position being occupied by a C16 hydrophobic chain bound by an ester, ether o vinyl ether linkage. The aim of this study was to gain information about the supramolecular structural organization of these atypical lipids and their changes in the segregation, topological and thermodynamic coexistence during cooling. After isolation of these SM species and CGP subclasses from ram sperm by a combination of chromatographic techniques, large and giant unilamellar vesicles (LUVs and GUVs) were prepared and examined by fluorescence spectroscopy and microscopy. Whereas the 3 subclasses of CGP remained in the liquid crystalline state, the SM species 30:6 SM, 32:6 SM and 34:6 SM showed gel-liquid crystalline transition temperatures within the 40 °C - 5 °C range (5, 15 y 29 °C, respectively). In ternary PC:Cholesterol:SM systems, 32:6 SM and 34:6 SM showed propensity to promote cholesterol-SM domain formation during cooling, although at different temperatures and rates from those of 16:0 SM, here used as a positive control. In GUVs containing 32:6 SM, the lateral lipid segregation and the process of dye efflux started at comparable temperatures. This coincidence did not occur in GUVs containing 16:0 SM. Thus, whereas at physiological temperatures VLCPUFA containing SM molecular species are in a fluid state and are not involved in cholesterol rich domains, this state is deeply altered at the low temperatures at which these gametes are usually preserved, thereby affecting their membrane stability.
Fil: Peñalva, Daniel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Hozbor, Federico Andrés. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Aveldaño, Marta Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
XLVIII Reunión Anual de la Sociedad Argentina de Biofísica
San Luis
Argentina
Sociedad Argentina de Biofísica
Universidad Nacional de San Luis
Materia
sperm
cholesterol
sphingomyelin
GUVs
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:11336/157367
Acceder
id CONICETDig_4c6fc55bd427ef1f5006dc31ed0e058d
oai_identifier_str oai:ri.conicet.gov.ar:11336/157367
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during coolingPeñalva, Daniel AlejandroHozbor, Federico AndrésAveldaño, Marta IsabelAntollini, Silvia SusanaspermcholesterolsphingomyelinGUVshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Although the molecular changes that affect the spermatozoa of economically important animals, such as bull and ram, are of great research interest, changes regarding plasma membrane lipid organization as temperature decreases are still poorly understood. Gametes from these mammals contain sphingomyelin (SM) species very long chain n-3 polyunsaturated fatty acids (VLCPUFA). (e.g., 30:6 SM, 32:6 SM and 34:6 SM in ram), while in most mammalian cells SM typically contains saturated and monounsaturated acyl chains (C14 to C24). Also, these spermatozoa have three subclasses of choline glycerophospholipids (CGP) with docosahexaenoic acid (22:6n-3) ester-bound at the sn-2 position of glycerol, the sn-1 position being occupied by a C16 hydrophobic chain bound by an ester, ether o vinyl ether linkage. The aim of this study was to gain information about the supramolecular structural organization of these atypical lipids and their changes in the segregation, topological and thermodynamic coexistence during cooling. After isolation of these SM species and CGP subclasses from ram sperm by a combination of chromatographic techniques, large and giant unilamellar vesicles (LUVs and GUVs) were prepared and examined by fluorescence spectroscopy and microscopy. Whereas the 3 subclasses of CGP remained in the liquid crystalline state, the SM species 30:6 SM, 32:6 SM and 34:6 SM showed gel-liquid crystalline transition temperatures within the 40 °C - 5 °C range (5, 15 y 29 °C, respectively). In ternary PC:Cholesterol:SM systems, 32:6 SM and 34:6 SM showed propensity to promote cholesterol-SM domain formation during cooling, although at different temperatures and rates from those of 16:0 SM, here used as a positive control. In GUVs containing 32:6 SM, the lateral lipid segregation and the process of dye efflux started at comparable temperatures. This coincidence did not occur in GUVs containing 16:0 SM. Thus, whereas at physiological temperatures VLCPUFA containing SM molecular species are in a fluid state and are not involved in cholesterol rich domains, this state is deeply altered at the low temperatures at which these gametes are usually preserved, thereby affecting their membrane stability.Fil: Peñalva, Daniel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Hozbor, Federico Andrés. Instituto Nacional de Tecnología Agropecuaria; ArgentinaFil: Aveldaño, Marta Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaXLVIII Reunión Anual de la Sociedad Argentina de BiofísicaSan LuisArgentinaSociedad Argentina de BiofísicaUniversidad Nacional de San LuisSociedad Argentina de BiofísicaAndujar, Sebastian Antonio2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/157367Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 51-51CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:38:51Zoai:ri.conicet.gov.ar:11336/157367instacron: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:34982025-09-29 09:38:51.802CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
title Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
spellingShingle Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
Peñalva, Daniel Alejandro
sperm
cholesterol
sphingomyelin
GUVs
title_short Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
title_full Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
title_fullStr Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
title_full_unstemmed Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
title_sort Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling
dc.creator.none.fl_str_mv Peñalva, Daniel Alejandro
Hozbor, Federico Andrés
Aveldaño, Marta Isabel
Antollini, Silvia Susana
author Peñalva, Daniel Alejandro
author_facet Peñalva, Daniel Alejandro
Hozbor, Federico Andrés
Aveldaño, Marta Isabel
Antollini, Silvia Susana
author_role author
author2 Hozbor, Federico Andrés
Aveldaño, Marta Isabel
Antollini, Silvia Susana
author2_role author
author
author
dc.contributor.none.fl_str_mv Andujar, Sebastian Antonio
dc.subject.none.fl_str_mv sperm
cholesterol
sphingomyelin
GUVs
topic sperm
cholesterol
sphingomyelin
GUVs
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Although the molecular changes that affect the spermatozoa of economically important animals, such as bull and ram, are of great research interest, changes regarding plasma membrane lipid organization as temperature decreases are still poorly understood. Gametes from these mammals contain sphingomyelin (SM) species very long chain n-3 polyunsaturated fatty acids (VLCPUFA). (e.g., 30:6 SM, 32:6 SM and 34:6 SM in ram), while in most mammalian cells SM typically contains saturated and monounsaturated acyl chains (C14 to C24). Also, these spermatozoa have three subclasses of choline glycerophospholipids (CGP) with docosahexaenoic acid (22:6n-3) ester-bound at the sn-2 position of glycerol, the sn-1 position being occupied by a C16 hydrophobic chain bound by an ester, ether o vinyl ether linkage. The aim of this study was to gain information about the supramolecular structural organization of these atypical lipids and their changes in the segregation, topological and thermodynamic coexistence during cooling. After isolation of these SM species and CGP subclasses from ram sperm by a combination of chromatographic techniques, large and giant unilamellar vesicles (LUVs and GUVs) were prepared and examined by fluorescence spectroscopy and microscopy. Whereas the 3 subclasses of CGP remained in the liquid crystalline state, the SM species 30:6 SM, 32:6 SM and 34:6 SM showed gel-liquid crystalline transition temperatures within the 40 °C - 5 °C range (5, 15 y 29 °C, respectively). In ternary PC:Cholesterol:SM systems, 32:6 SM and 34:6 SM showed propensity to promote cholesterol-SM domain formation during cooling, although at different temperatures and rates from those of 16:0 SM, here used as a positive control. In GUVs containing 32:6 SM, the lateral lipid segregation and the process of dye efflux started at comparable temperatures. This coincidence did not occur in GUVs containing 16:0 SM. Thus, whereas at physiological temperatures VLCPUFA containing SM molecular species are in a fluid state and are not involved in cholesterol rich domains, this state is deeply altered at the low temperatures at which these gametes are usually preserved, thereby affecting their membrane stability.
Fil: Peñalva, Daniel Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Hozbor, Federico Andrés. Instituto Nacional de Tecnología Agropecuaria; Argentina
Fil: Aveldaño, Marta Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Antollini, Silvia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
XLVIII Reunión Anual de la Sociedad Argentina de Biofísica
San Luis
Argentina
Sociedad Argentina de Biofísica
Universidad Nacional de San Luis
description Although the molecular changes that affect the spermatozoa of economically important animals, such as bull and ram, are of great research interest, changes regarding plasma membrane lipid organization as temperature decreases are still poorly understood. Gametes from these mammals contain sphingomyelin (SM) species very long chain n-3 polyunsaturated fatty acids (VLCPUFA). (e.g., 30:6 SM, 32:6 SM and 34:6 SM in ram), while in most mammalian cells SM typically contains saturated and monounsaturated acyl chains (C14 to C24). Also, these spermatozoa have three subclasses of choline glycerophospholipids (CGP) with docosahexaenoic acid (22:6n-3) ester-bound at the sn-2 position of glycerol, the sn-1 position being occupied by a C16 hydrophobic chain bound by an ester, ether o vinyl ether linkage. The aim of this study was to gain information about the supramolecular structural organization of these atypical lipids and their changes in the segregation, topological and thermodynamic coexistence during cooling. After isolation of these SM species and CGP subclasses from ram sperm by a combination of chromatographic techniques, large and giant unilamellar vesicles (LUVs and GUVs) were prepared and examined by fluorescence spectroscopy and microscopy. Whereas the 3 subclasses of CGP remained in the liquid crystalline state, the SM species 30:6 SM, 32:6 SM and 34:6 SM showed gel-liquid crystalline transition temperatures within the 40 °C - 5 °C range (5, 15 y 29 °C, respectively). In ternary PC:Cholesterol:SM systems, 32:6 SM and 34:6 SM showed propensity to promote cholesterol-SM domain formation during cooling, although at different temperatures and rates from those of 16:0 SM, here used as a positive control. In GUVs containing 32:6 SM, the lateral lipid segregation and the process of dye efflux started at comparable temperatures. This coincidence did not occur in GUVs containing 16:0 SM. Thus, whereas at physiological temperatures VLCPUFA containing SM molecular species are in a fluid state and are not involved in cholesterol rich domains, this state is deeply altered at the low temperatures at which these gametes are usually preserved, thereby affecting their membrane stability.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/157367
Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 51-51
CONICET Digital
CONICET
url http://hdl.handle.net/11336/157367
identifier_str_mv Changes in biophysical properties of membranes containing sphingomyelins with very long chain PUFA during cooling; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 51-51
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://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/
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.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
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 13.070432

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