Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states

Autores
Pusterla, Julio Martín; Schneck, Emanuel; Oliveira, Rafael Gustavo
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Purified myelin membranes (PMMs) are the starting material for biochemical studies, from individual components up to the isolation of detergent-resistant membrane (DRM) fractions or detergent-insoluble glycosphingolipid (DIG) fractions, which are commonly believed to resemble physiological lipid rafts. The normal DIG isolation protocol involves the extraction of lipids under moderate cooling. The isolation of PMMs also involves the cooling of myelin as well as exposure to low ionic strength (IS). Here, we addressed the combined influence of cooling and IS on the structure of PMMs. The phase behaviour was investigated by small angle X-ray diffraction. Analysis of the diffraction peaks revealed the lamellar periodicity ( d ), the number of periodically correlated bilayers ( N ), and the relatives fractions of each phase. Departure from physiological conditions induced a phase separation in myelin. The effect of monovalent and divalent ions was also compared at equivalent IS, showing a differential effect, and phase diagrams for both ion types were established-Ca2+ induced the well-known over-compacted phase, but additionally we also found an expanded phase at low IS. Na+ promoted phase separation, and also induced over-compaction at sufficiently high IS. Finally, exploring the whole phase diagram, we found evidence for the direct isothermal transformation from the expanded to the compacted phase, suggesting that both phases could in fact originate from the identical primary lateral phase separation, whereas the apparent difference lies in the inter-bilayer interaction that is modulated by the ionic milieu.
Fil: Pusterla, Julio Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Schneck, Emanuel. Universitat Technische Darmstadt; Alemania
Fil: Oliveira, Rafael Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Materia
DETERGENT-INSOLUBLE GLYCOSPHINGOLIPID
DOMAIN PHASE SEGREGATION
LIPID–PROTEIN DOMAINS
MEMBRANE HETEROGENEITY
SMALL-ANGLE X-RAY DIFFRACTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/143970
Acceder
id CONICETDig_a65ee02a0264f9fc1ad2ef0f242b6926
oai_identifier_str oai:ri.conicet.gov.ar:11336/143970
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar statesPusterla, Julio MartínSchneck, EmanuelOliveira, Rafael GustavoDETERGENT-INSOLUBLE GLYCOSPHINGOLIPIDDOMAIN PHASE SEGREGATIONLIPID–PROTEIN DOMAINSMEMBRANE HETEROGENEITYSMALL-ANGLE X-RAY DIFFRACTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Purified myelin membranes (PMMs) are the starting material for biochemical studies, from individual components up to the isolation of detergent-resistant membrane (DRM) fractions or detergent-insoluble glycosphingolipid (DIG) fractions, which are commonly believed to resemble physiological lipid rafts. The normal DIG isolation protocol involves the extraction of lipids under moderate cooling. The isolation of PMMs also involves the cooling of myelin as well as exposure to low ionic strength (IS). Here, we addressed the combined influence of cooling and IS on the structure of PMMs. The phase behaviour was investigated by small angle X-ray diffraction. Analysis of the diffraction peaks revealed the lamellar periodicity ( d ), the number of periodically correlated bilayers ( N ), and the relatives fractions of each phase. Departure from physiological conditions induced a phase separation in myelin. The effect of monovalent and divalent ions was also compared at equivalent IS, showing a differential effect, and phase diagrams for both ion types were established-Ca2+ induced the well-known over-compacted phase, but additionally we also found an expanded phase at low IS. Na+ promoted phase separation, and also induced over-compaction at sufficiently high IS. Finally, exploring the whole phase diagram, we found evidence for the direct isothermal transformation from the expanded to the compacted phase, suggesting that both phases could in fact originate from the identical primary lateral phase separation, whereas the apparent difference lies in the inter-bilayer interaction that is modulated by the ionic milieu.Fil: Pusterla, Julio Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Schneck, Emanuel. Universitat Technische Darmstadt; AlemaniaFil: Oliveira, Rafael Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaMDPI2020-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/143970Pusterla, Julio Martín; Schneck, Emanuel; Oliveira, Rafael Gustavo; Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states; MDPI; Cells; 9; 3; 3-2020; 1-122073-4409CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2073-4409/9/3/670info:eu-repo/semantics/altIdentifier/doi/10.3390/cells9030670info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:37:45Zoai:ri.conicet.gov.ar:11336/143970instacron: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 15:37:45.801CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
title Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
spellingShingle Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
Pusterla, Julio Martín
DETERGENT-INSOLUBLE GLYCOSPHINGOLIPID
DOMAIN PHASE SEGREGATION
LIPID–PROTEIN DOMAINS
MEMBRANE HETEROGENEITY
SMALL-ANGLE X-RAY DIFFRACTION
title_short Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
title_full Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
title_fullStr Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
title_full_unstemmed Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
title_sort Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states
dc.creator.none.fl_str_mv Pusterla, Julio Martín
Schneck, Emanuel
Oliveira, Rafael Gustavo
author Pusterla, Julio Martín
author_facet Pusterla, Julio Martín
Schneck, Emanuel
Oliveira, Rafael Gustavo
author_role author
author2 Schneck, Emanuel
Oliveira, Rafael Gustavo
author2_role author
author
dc.subject.none.fl_str_mv DETERGENT-INSOLUBLE GLYCOSPHINGOLIPID
DOMAIN PHASE SEGREGATION
LIPID–PROTEIN DOMAINS
MEMBRANE HETEROGENEITY
SMALL-ANGLE X-RAY DIFFRACTION
topic DETERGENT-INSOLUBLE GLYCOSPHINGOLIPID
DOMAIN PHASE SEGREGATION
LIPID–PROTEIN DOMAINS
MEMBRANE HETEROGENEITY
SMALL-ANGLE X-RAY DIFFRACTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Purified myelin membranes (PMMs) are the starting material for biochemical studies, from individual components up to the isolation of detergent-resistant membrane (DRM) fractions or detergent-insoluble glycosphingolipid (DIG) fractions, which are commonly believed to resemble physiological lipid rafts. The normal DIG isolation protocol involves the extraction of lipids under moderate cooling. The isolation of PMMs also involves the cooling of myelin as well as exposure to low ionic strength (IS). Here, we addressed the combined influence of cooling and IS on the structure of PMMs. The phase behaviour was investigated by small angle X-ray diffraction. Analysis of the diffraction peaks revealed the lamellar periodicity ( d ), the number of periodically correlated bilayers ( N ), and the relatives fractions of each phase. Departure from physiological conditions induced a phase separation in myelin. The effect of monovalent and divalent ions was also compared at equivalent IS, showing a differential effect, and phase diagrams for both ion types were established-Ca2+ induced the well-known over-compacted phase, but additionally we also found an expanded phase at low IS. Na+ promoted phase separation, and also induced over-compaction at sufficiently high IS. Finally, exploring the whole phase diagram, we found evidence for the direct isothermal transformation from the expanded to the compacted phase, suggesting that both phases could in fact originate from the identical primary lateral phase separation, whereas the apparent difference lies in the inter-bilayer interaction that is modulated by the ionic milieu.
Fil: Pusterla, Julio Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Schneck, Emanuel. Universitat Technische Darmstadt; Alemania
Fil: Oliveira, Rafael Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
description Purified myelin membranes (PMMs) are the starting material for biochemical studies, from individual components up to the isolation of detergent-resistant membrane (DRM) fractions or detergent-insoluble glycosphingolipid (DIG) fractions, which are commonly believed to resemble physiological lipid rafts. The normal DIG isolation protocol involves the extraction of lipids under moderate cooling. The isolation of PMMs also involves the cooling of myelin as well as exposure to low ionic strength (IS). Here, we addressed the combined influence of cooling and IS on the structure of PMMs. The phase behaviour was investigated by small angle X-ray diffraction. Analysis of the diffraction peaks revealed the lamellar periodicity ( d ), the number of periodically correlated bilayers ( N ), and the relatives fractions of each phase. Departure from physiological conditions induced a phase separation in myelin. The effect of monovalent and divalent ions was also compared at equivalent IS, showing a differential effect, and phase diagrams for both ion types were established-Ca2+ induced the well-known over-compacted phase, but additionally we also found an expanded phase at low IS. Na+ promoted phase separation, and also induced over-compaction at sufficiently high IS. Finally, exploring the whole phase diagram, we found evidence for the direct isothermal transformation from the expanded to the compacted phase, suggesting that both phases could in fact originate from the identical primary lateral phase separation, whereas the apparent difference lies in the inter-bilayer interaction that is modulated by the ionic milieu.
publishDate 2020
dc.date.none.fl_str_mv 2020-03
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/11336/143970
Pusterla, Julio Martín; Schneck, Emanuel; Oliveira, Rafael Gustavo; Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states; MDPI; Cells; 9; 3; 3-2020; 1-12
2073-4409
CONICET Digital
CONICET
url http://hdl.handle.net/11336/143970
identifier_str_mv Pusterla, Julio Martín; Schneck, Emanuel; Oliveira, Rafael Gustavo; Phase diagram of purified CNS myelin reveals continuous transformation between expanded and compacted lamellar states; MDPI; Cells; 9; 3; 3-2020; 1-12
2073-4409
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://www.mdpi.com/2073-4409/9/3/670
info:eu-repo/semantics/altIdentifier/doi/10.3390/cells9030670
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
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 13.22299

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