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[Role of apolipoprotein AI on nascent high-density lipoprotein particle formation].

Authors :
Wu JF
Tang YY
Zeng GF
Tang CK
Source :
Sheng li ke xue jin zhan [Progress in physiology] [Sheng Li Ke Xue Jin Zhan] 2014 Apr; Vol. 45 (2), pp. 81-6.
Publication Year :
2014

Abstract

Apolipoprotein AI (apoA-I) is the major protein component of high-density lipoprotein (HDL), and apoA-I can stabilize the structure of HDL. Whereas the amphipathic alpha-helix is the structural motif for apoA-I to complete the corresponding functionality. In the lipid-free state, the N-terminal of apoA-I molecule is a dynamic four-helix bundle structure, most amino acid residues of the C-terminal domain is the formation of a disordered structure, which is the initial domain that mediates bingding to phospholipid surface. Two molecules of apoA-I are arranged in an anti-parallel, double-belt conformation around the surface of the discoidal HDL particles. However, the apoA-I molecule forms a trefoil scaffold structure, which can adapt to the surface of spherical HDL particles. ATP-binding cassette transporter A1 (ABCA1) can mediate phospholipid and cholesterol efflux from intracellular and interact with apoA-I to generate nascent HDL particles. Overall, apoA-I and HDL as an anti-atherosclerotic effect of primary target, we focus on the molecular structure of apoA-I, which determines the structure and function of different size of HDL particles, as well as the conformational changes after interaction with lipids, in order to learn more about the relationship of apolipoprotein and lipids metabolism against atherosclerosis.

Details

Language :
Chinese
ISSN :
0559-7765
Volume :
45
Issue :
2
Database :
MEDLINE
Journal :
Sheng li ke xue jin zhan [Progress in physiology]
Publication Type :
Academic Journal
Accession number :
25069300