The molecular structure of apolipoprotein A-II modulates the capacity of HDL to promote cell cholesterol efflux |
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Affiliation: | 1. Institut für Archäologie, Lehrbereich Klassische Archäologie, Humboldt-Universität zu Berlin, Unter den Linden 6, D - 10099 Berlin, Germany;2. Deutsches Bergbau-Museum Bochum, Abteilung Forschung, Herner Straße 45, D - 44787 Bochum, Germany;3. Institute of Nanoscience and Nanotechnology, N.C.S.R. “Demokritos”, GR - 15310, Aghia Paraskevi, Attiki, Greece |
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Abstract: | The influence of apolipoprotein A-II (apoA-II) molecular structure on the capacity of high density lipoproteins (HDL) to promote cellular cholesterol efflux was investigated in cultured mouse peritoneal macrophages (MPM). Conversion by reduction and carboxamidomethylation of the naturally occurring dimeric apoA-II to its monomeric form in both native or reconstituted HDL did not change apolipoprotein secondary structure and lipoprotein size/composition. All particles containing monomeric apoA-II, i.e., native HDL3 or reconstituted HDL with or without apoA-I, showed a higher ability to promote cholesterol efflux originating from plasma membrane and intracellular stores, compared to particles containing dimeric apoA-II. These findings indicate that apolipoprotein molecular structure is a major determinant of HDL capacity to promote cholesterol efflux from cells. |
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