Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane

Autores
Rodi, Pablo Marcelo; Cabeza, Matías Sebastián; Gennaro, Ana Maria
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Early works have shown that when biomembranes are extracted with the non-ionic detergent Triton X-100 at 4°C, only a subset of the components is solubilized. The aim of this paper was to investigate the solubilization of a cell membrane at different Triton concentrations, and to compare the lipid composition and acyl chain order/mobility of the insoluble material with those of the original membrane. We choose bovine erythrocytes, because they have an uncommon composition, as they have a huge amount of sphingomyelin and phosphatidylcholine is almost absent. We determined the degree of order/mobility of the lipid acyl chains by EPR spectroscopy, using liposoluble spin labels. Incubation of bovine erythrocytes with increasing Triton X-100 concentrations yields decreasing amounts of insoluble material which is enriched in sphingomyelin and depleted in cholesterol. Complete lipid solubilization is achieved at a detergent/lipid ratio of about 60, which is much higher than the values reported for human erythrocytes, but is in line with results obtained in model systems. An insoluble pellet is still obtained at higher Triton concentrations, which seems to consist mainly of protein. A very high correlation is found between lipid chain mobility restrictions and sphingomyelin content in the lipid structures. The human erythrocyte membrane also fits well in this correlation, suggesting a significant role of sphingomyelin in determining acyl chain organization. The analogies and differences between our insoluble material and the detergent-resistant membranes (DRM) are discussed.
Fil: Rodi, Pablo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Cabeza, Matías Sebastián. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Materia
Erythrocyte
Membrane
Detergent
Epr
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:11336/26360
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membraneRodi, Pablo MarceloCabeza, Matías SebastiánGennaro, Ana MariaErythrocyteMembraneDetergentEprhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Early works have shown that when biomembranes are extracted with the non-ionic detergent Triton X-100 at 4°C, only a subset of the components is solubilized. The aim of this paper was to investigate the solubilization of a cell membrane at different Triton concentrations, and to compare the lipid composition and acyl chain order/mobility of the insoluble material with those of the original membrane. We choose bovine erythrocytes, because they have an uncommon composition, as they have a huge amount of sphingomyelin and phosphatidylcholine is almost absent. We determined the degree of order/mobility of the lipid acyl chains by EPR spectroscopy, using liposoluble spin labels. Incubation of bovine erythrocytes with increasing Triton X-100 concentrations yields decreasing amounts of insoluble material which is enriched in sphingomyelin and depleted in cholesterol. Complete lipid solubilization is achieved at a detergent/lipid ratio of about 60, which is much higher than the values reported for human erythrocytes, but is in line with results obtained in model systems. An insoluble pellet is still obtained at higher Triton concentrations, which seems to consist mainly of protein. A very high correlation is found between lipid chain mobility restrictions and sphingomyelin content in the lipid structures. The human erythrocyte membrane also fits well in this correlation, suggesting a significant role of sphingomyelin in determining acyl chain organization. The analogies and differences between our insoluble material and the detergent-resistant membranes (DRM) are discussed.Fil: Rodi, Pablo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaFil: Cabeza, Matías Sebastián. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaElsevier Science2006-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/26360Rodi, Pablo Marcelo; Cabeza, Matías Sebastián; Gennaro, Ana Maria; Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane; Elsevier Science; Biophysical Chemistry; 122; 2; 7-2006; 114-1220301-4622CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2006.03.005info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0301462206000780info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-17T10:44:42Zoai:ri.conicet.gov.ar:11336/26360instacron: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:34982025-09-17 10:44:42.727CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
title Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
spellingShingle Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
Rodi, Pablo Marcelo
Erythrocyte
Membrane
Detergent
Epr
title_short Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
title_full Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
title_fullStr Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
title_full_unstemmed Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
title_sort Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane
dc.creator.none.fl_str_mv Rodi, Pablo Marcelo
Cabeza, Matías Sebastián
Gennaro, Ana Maria
author Rodi, Pablo Marcelo
author_facet Rodi, Pablo Marcelo
Cabeza, Matías Sebastián
Gennaro, Ana Maria
author_role author
author2 Cabeza, Matías Sebastián
Gennaro, Ana Maria
author2_role author
author
dc.subject.none.fl_str_mv Erythrocyte
Membrane
Detergent
Epr
topic Erythrocyte
Membrane
Detergent
Epr
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Early works have shown that when biomembranes are extracted with the non-ionic detergent Triton X-100 at 4°C, only a subset of the components is solubilized. The aim of this paper was to investigate the solubilization of a cell membrane at different Triton concentrations, and to compare the lipid composition and acyl chain order/mobility of the insoluble material with those of the original membrane. We choose bovine erythrocytes, because they have an uncommon composition, as they have a huge amount of sphingomyelin and phosphatidylcholine is almost absent. We determined the degree of order/mobility of the lipid acyl chains by EPR spectroscopy, using liposoluble spin labels. Incubation of bovine erythrocytes with increasing Triton X-100 concentrations yields decreasing amounts of insoluble material which is enriched in sphingomyelin and depleted in cholesterol. Complete lipid solubilization is achieved at a detergent/lipid ratio of about 60, which is much higher than the values reported for human erythrocytes, but is in line with results obtained in model systems. An insoluble pellet is still obtained at higher Triton concentrations, which seems to consist mainly of protein. A very high correlation is found between lipid chain mobility restrictions and sphingomyelin content in the lipid structures. The human erythrocyte membrane also fits well in this correlation, suggesting a significant role of sphingomyelin in determining acyl chain organization. The analogies and differences between our insoluble material and the detergent-resistant membranes (DRM) are discussed.
Fil: Rodi, Pablo Marcelo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Cabeza, Matías Sebastián. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
description Early works have shown that when biomembranes are extracted with the non-ionic detergent Triton X-100 at 4°C, only a subset of the components is solubilized. The aim of this paper was to investigate the solubilization of a cell membrane at different Triton concentrations, and to compare the lipid composition and acyl chain order/mobility of the insoluble material with those of the original membrane. We choose bovine erythrocytes, because they have an uncommon composition, as they have a huge amount of sphingomyelin and phosphatidylcholine is almost absent. We determined the degree of order/mobility of the lipid acyl chains by EPR spectroscopy, using liposoluble spin labels. Incubation of bovine erythrocytes with increasing Triton X-100 concentrations yields decreasing amounts of insoluble material which is enriched in sphingomyelin and depleted in cholesterol. Complete lipid solubilization is achieved at a detergent/lipid ratio of about 60, which is much higher than the values reported for human erythrocytes, but is in line with results obtained in model systems. An insoluble pellet is still obtained at higher Triton concentrations, which seems to consist mainly of protein. A very high correlation is found between lipid chain mobility restrictions and sphingomyelin content in the lipid structures. The human erythrocyte membrane also fits well in this correlation, suggesting a significant role of sphingomyelin in determining acyl chain organization. The analogies and differences between our insoluble material and the detergent-resistant membranes (DRM) are discussed.
publishDate 2006
dc.date.none.fl_str_mv 2006-07
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/11336/26360
Rodi, Pablo Marcelo; Cabeza, Matías Sebastián; Gennaro, Ana Maria; Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane; Elsevier Science; Biophysical Chemistry; 122; 2; 7-2006; 114-122
0301-4622
CONICET Digital
CONICET
url http://hdl.handle.net/11336/26360
identifier_str_mv Rodi, Pablo Marcelo; Cabeza, Matías Sebastián; Gennaro, Ana Maria; Detergent solubilization of bovine erythrocytes. Comparison between the insoluble material and the intact membrane; Elsevier Science; Biophysical Chemistry; 122; 2; 7-2006; 114-122
0301-4622
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2006.03.005
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0301462206000780
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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 13.001348

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