| Literature DB >> 29883800 |
Meng Zhang1, Xiaobo Zhai1, Jinping Li2, John J Albers3, Simona Vuletic4, Gang Ren5.
Abstract
Human phospholipid transfer protein (PLTP) mediates the transfer of phospholipids among atheroprotective high-density lipoproteins (HDL) and atherogenic low-density lipoproteins (LDL) by an unknown mechanism. Delineating this mechanism would represent the first step towards understanding PLTP-mediated lipid transfers, which may be important for treating lipoprotein abnormalities and cardiovascular disease. Here, using various electron microscopy techniques, PLTP is revealed to have a banana-shaped structure similar to cholesteryl ester transfer protein (CETP). We provide evidence that PLTP penetrates into the HDL and LDL surfaces, respectively, and then forms a ternary complex with HDL and LDL. Insights into the interaction of PLTP with lipoproteins at the molecular level provide a basis to understand the PLTP-dependent lipid transfer mechanisms for dyslipidemia treatment.Entities:
Keywords: Electron microscopy; HDL; Liposome; PLTP; PLTP bound to HDL; PLTP bound to liposome; Phospholipid transfer protein
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Year: 2018 PMID: 29883800 PMCID: PMC6114099 DOI: 10.1016/j.bbalip.2018.06.001
Source DB: PubMed Journal: Biochim Biophys Acta Mol Cell Biol Lipids ISSN: 1388-1981 Impact factor: 4.698