Factors determining detergent resistance of erythrocyte membranes

Autores
Rodi, Pablo Marcelo; Trucco, Verónica Milagros; Gennaro, Ana Maria
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The degree of detergent insolubility of cell membranes is a useful parameter to test the strength of lipid–lipid interactions relative to lipid–detergent interactions. Thus, solubility studies could give insights about lipid–lipid interactions relevant in domain formation. In this work we perform a detailed study of the solubilization of four different erythrocyte membrane systems: intact human and bovine erythrocytes, and human and bovine erythrocytes depleted in cholesterol with methyl-â-cyclodextrin. Each system was incubated with different concentrations of the non-ionic detergent Triton X-100, and the insoluble fraction was characterized by determining cholesterol and phosphorus content. A distinct solubilization behavior was obtained for the four systems, which was quantified by a “detergent resistance parameter” obtained from the fit of the solubility curves. In order to correlate these findings with membrane structural parameters, we quantify the degree of acyl chain order/rigidity of the original membranes by EPR spectroscopy, finding that detergent resistance is higher when acyl chains are more rigid. Regarding compositional properties, we found a good correlation between detergent resistance parameters and the total amount of cholesterol plus sphingomyelin in the original membranes. Our results suggest that a high degree of acyl chain packing is the determinant membrane factor for resistance to the action of Triton X-100 in erythrocytes.
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: Trucco, Verónica Milagros. Universidad Nacional del Litoral; 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
Triton X-100
Membrane Solubility
Spin Labels
Acyl Chain Packing
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:11336/24825
Acceder
id CONICETDig_6f67728d9d0134711c26c41ec3b5b933
oai_identifier_str oai:ri.conicet.gov.ar:11336/24825
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Factors determining detergent resistance of erythrocyte membranesRodi, Pablo MarceloTrucco, Verónica MilagrosGennaro, Ana MariaTriton X-100Membrane SolubilitySpin LabelsAcyl Chain Packinghttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1The degree of detergent insolubility of cell membranes is a useful parameter to test the strength of lipid–lipid interactions relative to lipid–detergent interactions. Thus, solubility studies could give insights about lipid–lipid interactions relevant in domain formation. In this work we perform a detailed study of the solubilization of four different erythrocyte membrane systems: intact human and bovine erythrocytes, and human and bovine erythrocytes depleted in cholesterol with methyl-â-cyclodextrin. Each system was incubated with different concentrations of the non-ionic detergent Triton X-100, and the insoluble fraction was characterized by determining cholesterol and phosphorus content. A distinct solubilization behavior was obtained for the four systems, which was quantified by a “detergent resistance parameter” obtained from the fit of the solubility curves. In order to correlate these findings with membrane structural parameters, we quantify the degree of acyl chain order/rigidity of the original membranes by EPR spectroscopy, finding that detergent resistance is higher when acyl chains are more rigid. Regarding compositional properties, we found a good correlation between detergent resistance parameters and the total amount of cholesterol plus sphingomyelin in the original membranes. Our results suggest that a high degree of acyl chain packing is the determinant membrane factor for resistance to the action of Triton X-100 in erythrocytes.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: Trucco, Verónica Milagros. Universidad Nacional del Litoral; 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 Science2008-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24825Rodi, Pablo Marcelo; Trucco, Verónica Milagros; Gennaro, Ana Maria; Factors determining detergent resistance of erythrocyte membranes; Elsevier Science; Biophysical Chemistry; 135; 1-3; 4-2008; 14-180301-4622CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpc.2008.02.015info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0301462208000513info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:58:25Zoai:ri.conicet.gov.ar:11336/24825instacron: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:34982025-10-15 14:58:26.113CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Factors determining detergent resistance of erythrocyte membranes
title Factors determining detergent resistance of erythrocyte membranes
spellingShingle Factors determining detergent resistance of erythrocyte membranes
Rodi, Pablo Marcelo
Triton X-100
Membrane Solubility
Spin Labels
Acyl Chain Packing
title_short Factors determining detergent resistance of erythrocyte membranes
title_full Factors determining detergent resistance of erythrocyte membranes
title_fullStr Factors determining detergent resistance of erythrocyte membranes
title_full_unstemmed Factors determining detergent resistance of erythrocyte membranes
title_sort Factors determining detergent resistance of erythrocyte membranes
dc.creator.none.fl_str_mv Rodi, Pablo Marcelo
Trucco, Verónica Milagros
Gennaro, Ana Maria
author Rodi, Pablo Marcelo
author_facet Rodi, Pablo Marcelo
Trucco, Verónica Milagros
Gennaro, Ana Maria
author_role author
author2 Trucco, Verónica Milagros
Gennaro, Ana Maria
author2_role author
author
dc.subject.none.fl_str_mv Triton X-100
Membrane Solubility
Spin Labels
Acyl Chain Packing
topic Triton X-100
Membrane Solubility
Spin Labels
Acyl Chain Packing
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.3
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The degree of detergent insolubility of cell membranes is a useful parameter to test the strength of lipid–lipid interactions relative to lipid–detergent interactions. Thus, solubility studies could give insights about lipid–lipid interactions relevant in domain formation. In this work we perform a detailed study of the solubilization of four different erythrocyte membrane systems: intact human and bovine erythrocytes, and human and bovine erythrocytes depleted in cholesterol with methyl-â-cyclodextrin. Each system was incubated with different concentrations of the non-ionic detergent Triton X-100, and the insoluble fraction was characterized by determining cholesterol and phosphorus content. A distinct solubilization behavior was obtained for the four systems, which was quantified by a “detergent resistance parameter” obtained from the fit of the solubility curves. In order to correlate these findings with membrane structural parameters, we quantify the degree of acyl chain order/rigidity of the original membranes by EPR spectroscopy, finding that detergent resistance is higher when acyl chains are more rigid. Regarding compositional properties, we found a good correlation between detergent resistance parameters and the total amount of cholesterol plus sphingomyelin in the original membranes. Our results suggest that a high degree of acyl chain packing is the determinant membrane factor for resistance to the action of Triton X-100 in erythrocytes.
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: Trucco, Verónica Milagros. Universidad Nacional del Litoral; 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 The degree of detergent insolubility of cell membranes is a useful parameter to test the strength of lipid–lipid interactions relative to lipid–detergent interactions. Thus, solubility studies could give insights about lipid–lipid interactions relevant in domain formation. In this work we perform a detailed study of the solubilization of four different erythrocyte membrane systems: intact human and bovine erythrocytes, and human and bovine erythrocytes depleted in cholesterol with methyl-â-cyclodextrin. Each system was incubated with different concentrations of the non-ionic detergent Triton X-100, and the insoluble fraction was characterized by determining cholesterol and phosphorus content. A distinct solubilization behavior was obtained for the four systems, which was quantified by a “detergent resistance parameter” obtained from the fit of the solubility curves. In order to correlate these findings with membrane structural parameters, we quantify the degree of acyl chain order/rigidity of the original membranes by EPR spectroscopy, finding that detergent resistance is higher when acyl chains are more rigid. Regarding compositional properties, we found a good correlation between detergent resistance parameters and the total amount of cholesterol plus sphingomyelin in the original membranes. Our results suggest that a high degree of acyl chain packing is the determinant membrane factor for resistance to the action of Triton X-100 in erythrocytes.
publishDate 2008
dc.date.none.fl_str_mv 2008-04
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/11336/24825
Rodi, Pablo Marcelo; Trucco, Verónica Milagros; Gennaro, Ana Maria; Factors determining detergent resistance of erythrocyte membranes; Elsevier Science; Biophysical Chemistry; 135; 1-3; 4-2008; 14-18
0301-4622
CONICET Digital
CONICET
url http://hdl.handle.net/11336/24825
identifier_str_mv Rodi, Pablo Marcelo; Trucco, Verónica Milagros; Gennaro, Ana Maria; Factors determining detergent resistance of erythrocyte membranes; Elsevier Science; Biophysical Chemistry; 135; 1-3; 4-2008; 14-18
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.2008.02.015
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0301462208000513
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.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
_version_ 1846083124724760576
score 13.22299

Publicaciones similares