2001
DOI: 10.1016/s0022-2275(20)31693-x
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Apolipoprotein A-I conformation markedly influences HDL interaction with scavenger receptor BI

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Cited by 97 publications
(31 citation statements)
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“…The facts that HDL consists of particles of varying sizes and different lipid and protein compositions and densities (54), and that apoA-I is the principal component of HDL, are in accordance with observations that the physical characteristics of HDL as well as the conformation/organization of apoA-I in HDL particles are critical for optimal binding of HDL to SR-B1 (38). Indeed, it has been demonstrated that spherical -HDL particles, which are larger in size, cholesterol rich, and lower density, bind more strongly to SR-B1 as compared with high-density lipid-poor pre-HDL (55,56). Interestingly, reconstituted discoidal apoA-I complexes bind SR-B1 with even much greater affinity than native -HDL (55).…”
Section: Sr-b1 Ligandssupporting
confidence: 88%
“…The facts that HDL consists of particles of varying sizes and different lipid and protein compositions and densities (54), and that apoA-I is the principal component of HDL, are in accordance with observations that the physical characteristics of HDL as well as the conformation/organization of apoA-I in HDL particles are critical for optimal binding of HDL to SR-B1 (38). Indeed, it has been demonstrated that spherical -HDL particles, which are larger in size, cholesterol rich, and lower density, bind more strongly to SR-B1 as compared with high-density lipid-poor pre-HDL (55,56). Interestingly, reconstituted discoidal apoA-I complexes bind SR-B1 with even much greater affinity than native -HDL (55).…”
Section: Sr-b1 Ligandssupporting
confidence: 88%
“…The increased catabolism of medium HDL is likely explained by a unique conformation of apoA-I on the sur-face of the HDL particles or to an increase in the fluidity of the phospholipid surface. A recent study demonstrated that large HDL compared with small HDL were bound to scavenger receptor BI on the surface of CHO cells with higher affinity, and the authors concluded that HDL size and/or apoA-I conformation influences the binding of HDL subfractions to scavenger receptor BI (52). We have previously shown that recombinant HDL made with phosphatidylcholine containing n-3 fatty acids (docosahexanoic and eicosapentaenoic acid) in the sn-2 position have apoA-I that is in a different conformation and has a decreased stability compared with particles containing phosphatidylcholine with oleic acid in the sn-2 position (53).…”
Section: Discussionmentioning
confidence: 99%
“…The potential interaction of apoA-I with eNOS in cultured endothelial cells has been previously reported . However, lipid-free apoA-I failed to activate eNOS despite being the ligand for SR-BI, suggesting that other HDL components may be important or are required to support the conformation of apoA-I to allow its interaction with SR-BI and to stimulate eNOS (de Beer et al 2001). In isolated endothelial cell plasma membranes, anti-apoA-I antibody blocks eNOS activation by HDL in vitro .…”
Section: Mechanisms Under Physiological Conditionsmentioning
confidence: 99%