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dc.contributor.author
Ale, Elisa Carmen  
dc.contributor.author
Maggio, Bruno  
dc.contributor.author
Fanani, Maria Laura  
dc.date.available
2023-03-17T01:29:56Z  
dc.date.issued
2012-04  
dc.identifier.citation
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  
dc.identifier.issn
0005-2736  
dc.identifier.uri
http://hdl.handle.net/11336/190839  
dc.description.abstract
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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
BREWSTER ANGLE MICROSCOPY  
dc.subject
LIPID DOMAIN BORDER  
dc.subject
LIQUID-EXPANDED PHASE  
dc.subject
LIQUID-ORDERED DOMAIN  
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SPHINGOMYELIN  
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TIE LINE  
dc.subject.classification
Biofísica  
dc.subject.classification
Ciencias Biológicas  
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS  
dc.title
Ordered-disordered domain coexistence in ternary lipid monolayers activates sphingomyelinase by clearing ceramide from the active phase  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2023-03-15T20:35:25Z  
dc.journal.volume
1818  
dc.journal.number
11  
dc.journal.pagination
2767-2776  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
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  
dc.description.fil
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  
dc.description.fil
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  
dc.journal.title
Biochimica et Biophysica Acta - Biomembranes  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbamem.2012.06.017  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273612002155