Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase

Autores
Ale, Elisa Carmen; Maggio, Bruno; Fanani, Maria Laura
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
We explored the action of sphingomyelinase (SMase) on ternary monolayers containing phosphatidylcholine, sphingomyelin (SM) and dihydrocholesterol, which varied along a single tie line of phase coexistence. SMase activity exhibited a higher rate and extent of hydrolysis when the film is within the liquid-expanded (LE)/liquid-ordered (LO) coexistence range, compared to monolayers in the full LO phase. Since Alexa-SMase preferably adsorbs to the LE phase and there was no direct correlation found between enzymatic activity and domain borders, we postulate that the LE phase is the active phase for ceramide (Cer) generation. The enzymatically generated Cer was organized in different ways depending on the initial LE/LO ratio. The action of SMase in Chol-poor monolayers led to the formation of Cer-enriched domains, while in Chol-rich monolayers it resulted in the incorporation of Cer in the LO phase and the formation of new Chol- and Cer-enriched domains. The following novel mechanism is proposed to provide an explanation for the favored action of SMase on interfaces that exhibit an LE-LO phase coexistence: the LO phase sequesters the product Cer causing its depletion from the more enzyme-susceptible LE phase, thus decreasing inhibition by the reaction product. Furthermore, LO domains function as a substrate reservoir by allowing a rapid exchange of the substrate from this phase to the SM-depleted LE phase.
Fil: Ale, Elisa Carmen. 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: Maggio, Bruno. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Fanani, Maria Laura. 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
BREWSTER ANGLE MICROSCOPY
LIPID DOMAIN BORDER
LIQUID-EXPANDED PHASE
LIQUID-ORDERED DOMAIN
SPHINGOMYELIN
TIE LINE
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:11336/190839
Acceder
id CONICETDig_1bdd8a8d4ba3c3c73df992075295e8cc
oai_identifier_str oai:ri.conicet.gov.ar:11336/190839
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phaseAle, Elisa CarmenMaggio, BrunoFanani, Maria LauraBREWSTER ANGLE MICROSCOPYLIPID DOMAIN BORDERLIQUID-EXPANDED PHASELIQUID-ORDERED DOMAINSPHINGOMYELINTIE LINEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1We explored the action of sphingomyelinase (SMase) on ternary monolayers containing phosphatidylcholine, sphingomyelin (SM) and dihydrocholesterol, which varied along a single tie line of phase coexistence. SMase activity exhibited a higher rate and extent of hydrolysis when the film is within the liquid-expanded (LE)/liquid-ordered (LO) coexistence range, compared to monolayers in the full LO phase. Since Alexa-SMase preferably adsorbs to the LE phase and there was no direct correlation found between enzymatic activity and domain borders, we postulate that the LE phase is the active phase for ceramide (Cer) generation. The enzymatically generated Cer was organized in different ways depending on the initial LE/LO ratio. The action of SMase in Chol-poor monolayers led to the formation of Cer-enriched domains, while in Chol-rich monolayers it resulted in the incorporation of Cer in the LO phase and the formation of new Chol- and Cer-enriched domains. The following novel mechanism is proposed to provide an explanation for the favored action of SMase on interfaces that exhibit an LE-LO phase coexistence: the LO phase sequesters the product Cer causing its depletion from the more enzyme-susceptible LE phase, thus decreasing inhibition by the reaction product. Furthermore, LO domains function as a substrate reservoir by allowing a rapid exchange of the substrate from this phase to the SM-depleted LE phase.Fil: Ale, Elisa Carmen. 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: Maggio, Bruno. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; ArgentinaFil: Fanani, Maria Laura. 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; ArgentinaElsevier Science2012-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/190839Ale, Elisa Carmen; Maggio, Bruno; Fanani, Maria Laura; Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 11; 4-2012; 2767-27760005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.06.017info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273612002155info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:24:13Zoai:ri.conicet.gov.ar:11336/190839instacron: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 14:24:13.668CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
title Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
spellingShingle Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
Ale, Elisa Carmen
BREWSTER ANGLE MICROSCOPY
LIPID DOMAIN BORDER
LIQUID-EXPANDED PHASE
LIQUID-ORDERED DOMAIN
SPHINGOMYELIN
TIE LINE
title_short Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
title_full Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
title_fullStr Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
title_full_unstemmed Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
title_sort Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase
dc.creator.none.fl_str_mv Ale, Elisa Carmen
Maggio, Bruno
Fanani, Maria Laura
author Ale, Elisa Carmen
author_facet Ale, Elisa Carmen
Maggio, Bruno
Fanani, Maria Laura
author_role author
author2 Maggio, Bruno
Fanani, Maria Laura
author2_role author
author
dc.subject.none.fl_str_mv BREWSTER ANGLE MICROSCOPY
LIPID DOMAIN BORDER
LIQUID-EXPANDED PHASE
LIQUID-ORDERED DOMAIN
SPHINGOMYELIN
TIE LINE
topic BREWSTER ANGLE MICROSCOPY
LIPID DOMAIN BORDER
LIQUID-EXPANDED PHASE
LIQUID-ORDERED DOMAIN
SPHINGOMYELIN
TIE LINE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv We explored the action of sphingomyelinase (SMase) on ternary monolayers containing phosphatidylcholine, sphingomyelin (SM) and dihydrocholesterol, which varied along a single tie line of phase coexistence. SMase activity exhibited a higher rate and extent of hydrolysis when the film is within the liquid-expanded (LE)/liquid-ordered (LO) coexistence range, compared to monolayers in the full LO phase. Since Alexa-SMase preferably adsorbs to the LE phase and there was no direct correlation found between enzymatic activity and domain borders, we postulate that the LE phase is the active phase for ceramide (Cer) generation. The enzymatically generated Cer was organized in different ways depending on the initial LE/LO ratio. The action of SMase in Chol-poor monolayers led to the formation of Cer-enriched domains, while in Chol-rich monolayers it resulted in the incorporation of Cer in the LO phase and the formation of new Chol- and Cer-enriched domains. The following novel mechanism is proposed to provide an explanation for the favored action of SMase on interfaces that exhibit an LE-LO phase coexistence: the LO phase sequesters the product Cer causing its depletion from the more enzyme-susceptible LE phase, thus decreasing inhibition by the reaction product. Furthermore, LO domains function as a substrate reservoir by allowing a rapid exchange of the substrate from this phase to the SM-depleted LE phase.
Fil: Ale, Elisa Carmen. 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: Maggio, Bruno. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Fanani, Maria Laura. 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 We explored the action of sphingomyelinase (SMase) on ternary monolayers containing phosphatidylcholine, sphingomyelin (SM) and dihydrocholesterol, which varied along a single tie line of phase coexistence. SMase activity exhibited a higher rate and extent of hydrolysis when the film is within the liquid-expanded (LE)/liquid-ordered (LO) coexistence range, compared to monolayers in the full LO phase. Since Alexa-SMase preferably adsorbs to the LE phase and there was no direct correlation found between enzymatic activity and domain borders, we postulate that the LE phase is the active phase for ceramide (Cer) generation. The enzymatically generated Cer was organized in different ways depending on the initial LE/LO ratio. The action of SMase in Chol-poor monolayers led to the formation of Cer-enriched domains, while in Chol-rich monolayers it resulted in the incorporation of Cer in the LO phase and the formation of new Chol- and Cer-enriched domains. The following novel mechanism is proposed to provide an explanation for the favored action of SMase on interfaces that exhibit an LE-LO phase coexistence: the LO phase sequesters the product Cer causing its depletion from the more enzyme-susceptible LE phase, thus decreasing inhibition by the reaction product. Furthermore, LO domains function as a substrate reservoir by allowing a rapid exchange of the substrate from this phase to the SM-depleted LE phase.
publishDate 2012
dc.date.none.fl_str_mv 2012-04
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/11336/190839
Ale, Elisa Carmen; Maggio, Bruno; Fanani, Maria Laura; Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 11; 4-2012; 2767-2776
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/190839
identifier_str_mv Ale, Elisa Carmen; Maggio, Bruno; Fanani, Maria Laura; Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 11; 4-2012; 2767-2776
0005-2736
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.bbamem.2012.06.017
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273612002155
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
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_ 1846082661890654208
score 13.22299

Publicaciones similares