Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins

Protein and protein-lipid interactions, with and within specific areas in the cell membrane, are critical in order to modulate the cell signaling events required to maintain cell functions and viability. Biological bilayers are complex, dynamic platforms, and thus in vivo observations usually need t...

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Detalles Bibliográficos
Autores principales: Sánchez, Susana A., Tricerri, María Alejandra, Ossato, Giulia, Gratton, Enrico
Formato: Articulo
Lenguaje:Inglés
Publicado: 2010
Materias:
Ciencias Médicas
ApoA-I
Fluorescence microscopy
GUV
Laurdan GP
RHDL
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/82444
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-82444
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
ApoA-I
Fluorescence microscopy
GUV
Laurdan GP
RHDL
spellingShingle Ciencias Médicas
ApoA-I
Fluorescence microscopy
GUV
Laurdan GP
RHDL
Sánchez, Susana A.
Tricerri, María Alejandra
Ossato, Giulia
Gratton, Enrico
Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
topic_facet Ciencias Médicas
ApoA-I
Fluorescence microscopy
GUV
Laurdan GP
RHDL
description Protein and protein-lipid interactions, with and within specific areas in the cell membrane, are critical in order to modulate the cell signaling events required to maintain cell functions and viability. Biological bilayers are complex, dynamic platforms, and thus in vivo observations usually need to be preceded by studies on model systems that simplify and discriminate the different factors involved in lipid-protein interactions. Fluorescence microscopy studies using giant unilamellar vesicles (GUVs) as membrane model systems provide a unique methodology to quantify protein binding, interaction, and lipid solubilization in artificial bilayers. The large size of lipid domains obtainable on GUVs, together with fluorescence microscopy techniques, provides the possibility to localize and quantify molecular interactions. Fluorescence Correlation Spectroscopy (FCS) can be performed using the GUV model to extract information on mobility and concentration. Two-photon Laurdan Generalized Polarization (GP) reports on local changes in membrane water content (related to membrane fluidity) due to protein binding or lipid removal from a given lipid domain. In this review, we summarize the experimental microscopy methods used to study the interaction of human apolipoprotein A-I (apoA-I) in lipid-free and lipid-bound conformations with bilayers and natural membranes. Results described here help us to understand cholesterol homeostasis and offer a methodological design suited to different biological systems.
format Articulo
Articulo
author Sánchez, Susana A.
Tricerri, María Alejandra
Ossato, Giulia
Gratton, Enrico
author_facet Sánchez, Susana A.
Tricerri, María Alejandra
Ossato, Giulia
Gratton, Enrico
author_sort Sánchez, Susana A.
title Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
title_short Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
title_full Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
title_fullStr Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
title_full_unstemmed Lipid packing determines protein-membrane interactions: Challenges for apolipoprotein A-I and high density lipoproteins
title_sort lipid packing determines protein-membrane interactions: challenges for apolipoprotein a-i and high density lipoproteins
publishDate 2010
url http://sedici.unlp.edu.ar/handle/10915/82444
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AT tricerrimariaalejandra lipidpackingdeterminesproteinmembraneinteractionschallengesforapolipoproteinaiandhighdensitylipoproteins
AT ossatogiulia lipidpackingdeterminesproteinmembraneinteractionschallengesforapolipoproteinaiandhighdensitylipoproteins
AT grattonenrico lipidpackingdeterminesproteinmembraneinteractionschallengesforapolipoproteinaiandhighdensitylipoproteins
bdutipo_str Repositorios
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