Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers

Apolipoprotein A-I (apoA-I) interaction with specific cell lipid domains was suggested to trigger cholesterol and phospholipid efflux. We analyzed here apoA-I interaction with dimyristoylphosphatidylcholine/ distearoylphosphatidylcholine (DMPC/DSPC) bilayers at a temperature showing phase coexistenc...

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Detalles Bibliográficos
Autores principales:	Tricerri, María Alejandra, Toledo, Juan Domingo, Sánchez, Susana A., Hazlett, Theodore L., Gratton, Enrico, Jonas, Ana, Garda, Horacio Alberto
Formato:	Articulo
Lenguaje:	Inglés
Publicado:	2005
Materias:	Ciencias Médicas Giant unilamellar vesicles Lipid-phase coexistence Lipid-protein interactions Small unilamellar vesicles
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/83147
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-83147
record_format	dspace
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Ciencias Médicas Giant unilamellar vesicles Lipid-phase coexistence Lipid-protein interactions Small unilamellar vesicles
spellingShingle	Ciencias Médicas Giant unilamellar vesicles Lipid-phase coexistence Lipid-protein interactions Small unilamellar vesicles Tricerri, María Alejandra Toledo, Juan Domingo Sánchez, Susana A. Hazlett, Theodore L. Gratton, Enrico Jonas, Ana Garda, Horacio Alberto Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers
topic_facet	Ciencias Médicas Giant unilamellar vesicles Lipid-phase coexistence Lipid-protein interactions Small unilamellar vesicles
description	Apolipoprotein A-I (apoA-I) interaction with specific cell lipid domains was suggested to trigger cholesterol and phospholipid efflux. We analyzed here apoA-I interaction with dimyristoylphosphatidylcholine/ distearoylphosphatidylcholine (DMPC/DSPC) bilayers at a temperature showing phase coexistence. Solid and liquid-crystalline domains were visualized by two-photon fluorescence microscopy on giant unilamellar vesicles (GUVs) labeled with 6-dodecanoyl-2-dimethylamino-naphthalene (Laurdan). A decrease of vesicle size was detected as long as they were incubated with lipid-free apoA-I, together with a shape deformation and a relative enrichment in DSPC. Selective lipid removal mediated by apoA-I from different domains was followed in real time by changes in the Laurdan generalized polarization. The data show a selective interaction of apoA-I with liquid-crystalline domains, from which it removes lipids, at a molar ratio similar to the domain compositions. Next, apoA-I was incubated with DMPC/DSPC small unilamellar vesicles, and products were isolated and quantified. Protein solubilized both lipids but formed complexes relatively enriched in the liquid component. We also show changes in the GUV morphology when cooling down. Our results suggest that the most efficient reaction between apoA-I and DMPC/DSPC occurs in particular bilayer conditions, probably when small fluid domains are nucleated within a continuous gel phase and interfacial packing defects are maximal.
format	Articulo Articulo
author	Tricerri, María Alejandra Toledo, Juan Domingo Sánchez, Susana A. Hazlett, Theodore L. Gratton, Enrico Jonas, Ana Garda, Horacio Alberto
author_facet	Tricerri, María Alejandra Toledo, Juan Domingo Sánchez, Susana A. Hazlett, Theodore L. Gratton, Enrico Jonas, Ana Garda, Horacio Alberto
author_sort	Tricerri, María Alejandra
title	Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers
title_short	Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers
title_full	Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers
title_fullStr	Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers
title_full_unstemmed	Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers
title_sort	visualization and analysis of apolipoprotein a-i interaction with binary phospholipid bilayers
publishDate	2005
url	http://sedici.unlp.edu.ar/handle/10915/83147
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bdutipo_str	Repositorios
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Visualization and analysis of apolipoprotein A-I interaction with binary phospholipid bilayers

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