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Difference in lipid packing sensitivity of exchangeable apolipoproteins apoA-I and apoA-II: an important determinant for their distinctive role in lipid metabolism.
Chièze, Lionel; Bolanos-Garcia, Victor Martin; Le Caër, Gérard; Renault, Anne; Vié, Véronique; Beaufils, Sylvie.
Afiliación
  • Chièze L; Institut de Physique de Rennes, UMR-CNRS 6251 Université de Rennes 1, Campus de Beaulieu, Rennes cedex, France.
Biochim Biophys Acta ; 1818(11): 2732-41, 2012 Nov.
Article en En | MEDLINE | ID: mdl-22627110
Exchangeable apolipoproteins A-I and A-II play distinct roles in reverse cholesterol transport. ApoA-I interacts with phospholipids and cholesterol of the cell membrane to make high density lipoprotein particles whereas apolipoprotein A-II interacts with high density lipoprotein particles to release apolipoprotein A-I. The two proteins show a high activity at the aqueous solution/lipid interface and are characterized by a high content of amphipathic α-helices built upon repetition of the same structural motif. We set out to investigate to what extent the number of α-helix repeats of this structural motif modulates the affinity of the protein for lipids and the sensitivity to lipid packing. To this aim we have compared the insertion of apolipoproteins A-I and A-II in phospholipid monolayers formed on a Langmuir trough in conditions where lipid packing, surface pressure and charge were controlled. We also used atomic force microscopy to obtain high resolution topographic images of the surface at a resolution of several nanometers and performed statistical image analysis to calculate the spatial distribution and geometrical shape of apolipoproteins A-I and A-II clusters. Our data indicate that apolipoprotein A-I is sensitive to packing of zwitterionic lipids but insensitive to the packing of negatively charged lipids. Interestingly, apolipoprotein A-II proved to be insensitive to the packing of zwitterionic lipids. The different sensitivity to lipid packing provides clues as to why apolipoprotein A-II barely forms nascent high density lipoprotein particles while apolipoprotein A-I promotes their formation. We conclude that the different interfacial behaviors of apolipoprotein A-I and apolipoprotein A-II in lipidic monolayers are important determinants of their distinctive roles in lipid metabolism.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfolípidos / Apolipoproteína A-II / Apolipoproteína A-I Tipo de estudio: Diagnostic_studies Idioma: En Revista: Biochim Biophys Acta Año: 2012 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Fosfolípidos / Apolipoproteína A-II / Apolipoproteína A-I Tipo de estudio: Diagnostic_studies Idioma: En Revista: Biochim Biophys Acta Año: 2012 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Países Bajos