Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells

Autores
Santiago Valtierra, Florencia Ximena; Oresti, Gerardo Martin; Mateos, Melina Valeria; Aveldaño, Marta Isabel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
SP hingomyelins (SM) and ceramides (Cer) with nonhydroxy and 2-hydroxy very_ long-chain PUFA (n-V and h-V) are specific components of rat spermatogenic cells, including pachytene spermatocytes and round spermatids. Here we evaluated how these Iipids distribute among membrane fractions prepared from these germ cells in comparison with glycerophospholipids (GPL) and cholesterol. A small light (L) and a large heavy (H) membrane fractions, both derived from the cell plasma membrane, were isolated a detergent-free procedure, as well as a fraction containing intracellular membranes, used for comparison. Flotillin-1, a protein typical of raft membrane domains, was highly concentrated in the L fraction. Additionally, by using Triton X-100, detergent¬resistant and detergent-soluble membrane (DRM and DSM, respectively) fractions were obtained in order to compare results. The small L and DRM fractions were similar in that both displayed a higher percentage of SM and cholesterol than the corresponding H and DSM fractions. The SM from the L and DRM fractions was rich in saturated fatty acids (SFA), whereas that of H and DSM fractions contained most of the n-V and h-V. The GPL followed the same trend, as the L and DRM fractions contained mostly SFA and mostly PUFA, respectively. Interestingly, DRM, but not L, contained Cer with high proportion of n-V and h-V, suggesting detergent-resistant properties of these unusual lipids. Thus, the L and DRM fractions from germ Gens exhibit biochemical similarities in that they exclude SM with n-V and h-V, indicating that these species are not components of raft membrane domains_ The intracellular membrane fraction in the detergent-free method contained most of the n-V and h-V Cer species of the cells, likely precursors of the SM that in due course will be biosynthesized and transferred to the H fraction of the plasma membrane.
Fil: Santiago Valtierra, Florencia Ximena. 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: Oresti, Gerardo Martin. 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: Mateos, Melina Valeria. 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: 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
56th Meeting of the International Conference on the Bioscience of Lipids (ICBL).
Iguazú
Argentina
International Conference on the Bioscience of Lipids
Materia
LIPID DOMAINS
VLCPUFA
SPHINGOLIPIDS
DRMS
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:11336/251222

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cellsSantiago Valtierra, Florencia XimenaOresti, Gerardo MartinMateos, Melina ValeriaAveldaño, Marta IsabelLIPID DOMAINSVLCPUFASPHINGOLIPIDSDRMShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1SP hingomyelins (SM) and ceramides (Cer) with nonhydroxy and 2-hydroxy very_ long-chain PUFA (n-V and h-V) are specific components of rat spermatogenic cells, including pachytene spermatocytes and round spermatids. Here we evaluated how these Iipids distribute among membrane fractions prepared from these germ cells in comparison with glycerophospholipids (GPL) and cholesterol. A small light (L) and a large heavy (H) membrane fractions, both derived from the cell plasma membrane, were isolated a detergent-free procedure, as well as a fraction containing intracellular membranes, used for comparison. Flotillin-1, a protein typical of raft membrane domains, was highly concentrated in the L fraction. Additionally, by using Triton X-100, detergent¬resistant and detergent-soluble membrane (DRM and DSM, respectively) fractions were obtained in order to compare results. The small L and DRM fractions were similar in that both displayed a higher percentage of SM and cholesterol than the corresponding H and DSM fractions. The SM from the L and DRM fractions was rich in saturated fatty acids (SFA), whereas that of H and DSM fractions contained most of the n-V and h-V. The GPL followed the same trend, as the L and DRM fractions contained mostly SFA and mostly PUFA, respectively. Interestingly, DRM, but not L, contained Cer with high proportion of n-V and h-V, suggesting detergent-resistant properties of these unusual lipids. Thus, the L and DRM fractions from germ Gens exhibit biochemical similarities in that they exclude SM with n-V and h-V, indicating that these species are not components of raft membrane domains_ The intracellular membrane fraction in the detergent-free method contained most of the n-V and h-V Cer species of the cells, likely precursors of the SM that in due course will be biosynthesized and transferred to the H fraction of the plasma membrane.Fil: Santiago Valtierra, Florencia Ximena. 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: Oresti, Gerardo Martin. 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: Mateos, Melina Valeria. 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: 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; Argentina56th Meeting of the International Conference on the Bioscience of Lipids (ICBL).IguazúArgentinaInternational Conference on the Bioscience of LipidsUniversidad Nacional de Córdoba2015info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectConferenciaBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/251222Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells; 56th Meeting of the International Conference on the Bioscience of Lipids (ICBL).; Iguazú; Argentina; 2015; 1-1CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.icbl.info/category/conferences/Internacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:09:15Zoai:ri.conicet.gov.ar:11336/251222instacron: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:34982025-09-10 13:09:15.982CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
title Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
spellingShingle Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
Santiago Valtierra, Florencia Ximena
LIPID DOMAINS
VLCPUFA
SPHINGOLIPIDS
DRMS
title_short Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
title_full Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
title_fullStr Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
title_full_unstemmed Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
title_sort Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells
dc.creator.none.fl_str_mv Santiago Valtierra, Florencia Ximena
Oresti, Gerardo Martin
Mateos, Melina Valeria
Aveldaño, Marta Isabel
author Santiago Valtierra, Florencia Ximena
author_facet Santiago Valtierra, Florencia Ximena
Oresti, Gerardo Martin
Mateos, Melina Valeria
Aveldaño, Marta Isabel
author_role author
author2 Oresti, Gerardo Martin
Mateos, Melina Valeria
Aveldaño, Marta Isabel
author2_role author
author
author
dc.subject.none.fl_str_mv LIPID DOMAINS
VLCPUFA
SPHINGOLIPIDS
DRMS
topic LIPID DOMAINS
VLCPUFA
SPHINGOLIPIDS
DRMS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv SP hingomyelins (SM) and ceramides (Cer) with nonhydroxy and 2-hydroxy very_ long-chain PUFA (n-V and h-V) are specific components of rat spermatogenic cells, including pachytene spermatocytes and round spermatids. Here we evaluated how these Iipids distribute among membrane fractions prepared from these germ cells in comparison with glycerophospholipids (GPL) and cholesterol. A small light (L) and a large heavy (H) membrane fractions, both derived from the cell plasma membrane, were isolated a detergent-free procedure, as well as a fraction containing intracellular membranes, used for comparison. Flotillin-1, a protein typical of raft membrane domains, was highly concentrated in the L fraction. Additionally, by using Triton X-100, detergent¬resistant and detergent-soluble membrane (DRM and DSM, respectively) fractions were obtained in order to compare results. The small L and DRM fractions were similar in that both displayed a higher percentage of SM and cholesterol than the corresponding H and DSM fractions. The SM from the L and DRM fractions was rich in saturated fatty acids (SFA), whereas that of H and DSM fractions contained most of the n-V and h-V. The GPL followed the same trend, as the L and DRM fractions contained mostly SFA and mostly PUFA, respectively. Interestingly, DRM, but not L, contained Cer with high proportion of n-V and h-V, suggesting detergent-resistant properties of these unusual lipids. Thus, the L and DRM fractions from germ Gens exhibit biochemical similarities in that they exclude SM with n-V and h-V, indicating that these species are not components of raft membrane domains_ The intracellular membrane fraction in the detergent-free method contained most of the n-V and h-V Cer species of the cells, likely precursors of the SM that in due course will be biosynthesized and transferred to the H fraction of the plasma membrane.
Fil: Santiago Valtierra, Florencia Ximena. 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: Oresti, Gerardo Martin. 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: Mateos, Melina Valeria. 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: 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
56th Meeting of the International Conference on the Bioscience of Lipids (ICBL).
Iguazú
Argentina
International Conference on the Bioscience of Lipids
description SP hingomyelins (SM) and ceramides (Cer) with nonhydroxy and 2-hydroxy very_ long-chain PUFA (n-V and h-V) are specific components of rat spermatogenic cells, including pachytene spermatocytes and round spermatids. Here we evaluated how these Iipids distribute among membrane fractions prepared from these germ cells in comparison with glycerophospholipids (GPL) and cholesterol. A small light (L) and a large heavy (H) membrane fractions, both derived from the cell plasma membrane, were isolated a detergent-free procedure, as well as a fraction containing intracellular membranes, used for comparison. Flotillin-1, a protein typical of raft membrane domains, was highly concentrated in the L fraction. Additionally, by using Triton X-100, detergent¬resistant and detergent-soluble membrane (DRM and DSM, respectively) fractions were obtained in order to compare results. The small L and DRM fractions were similar in that both displayed a higher percentage of SM and cholesterol than the corresponding H and DSM fractions. The SM from the L and DRM fractions was rich in saturated fatty acids (SFA), whereas that of H and DSM fractions contained most of the n-V and h-V. The GPL followed the same trend, as the L and DRM fractions contained mostly SFA and mostly PUFA, respectively. Interestingly, DRM, but not L, contained Cer with high proportion of n-V and h-V, suggesting detergent-resistant properties of these unusual lipids. Thus, the L and DRM fractions from germ Gens exhibit biochemical similarities in that they exclude SM with n-V and h-V, indicating that these species are not components of raft membrane domains_ The intracellular membrane fraction in the detergent-free method contained most of the n-V and h-V Cer species of the cells, likely precursors of the SM that in due course will be biosynthesized and transferred to the H fraction of the plasma membrane.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Conferencia
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/11336/251222
Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells; 56th Meeting of the International Conference on the Bioscience of Lipids (ICBL).; Iguazú; Argentina; 2015; 1-1
CONICET Digital
CONICET
url http://hdl.handle.net/11336/251222
identifier_str_mv Sphingomyelins and ceramides with very-long-chain PUFA in membrane fractions and domains from rat spermatogenic cells; 56th Meeting of the International Conference on the Bioscience of Lipids (ICBL).; Iguazú; Argentina; 2015; 1-1
CONICET Digital
CONICET
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language eng
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https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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dc.coverage.none.fl_str_mv Internacional
dc.publisher.none.fl_str_mv Universidad Nacional de Córdoba
publisher.none.fl_str_mv Universidad Nacional de Córdoba
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