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Different Functional and Structural Characteristics between ApoA-I and ApoA-4 in Lipid-Free and Reconstituted HDL State: ApoA-4 Showed Less Anti-Atherogenic Activity

Authors
Yoo, Jeong-AhLee, Eun-YoungPark, Ji YoonLee, Seung-TaekHam, SihyunCho, Kyung-Hyun
Issue Date
Jun-2015
Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
Keywords
apolipoprotein A-I; apolipoprotein A-4; fructosylation; recombinant high-density lipoprotein
Citation
MOLECULES AND CELLS, v.38, no.6, pp 573 - 579
Pages
7
Journal Title
MOLECULES AND CELLS
Volume
38
Number
6
Start Page
573
End Page
579
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/10514
DOI
10.14348/molcells.2015.0052
ISSN
1016-8478
0219-1032
Abstract
Apolipoprotein A-I and A-IV are protein constituents of high-density lipoproteins although their functional difference in lipoprotein metabolism is still unclear. To compare anti-atherogenic properties between apoA-I and apoA-4, we characterized both proteins in lipid-free and lipid-bound state. In lipid-free state, apoA4 showed two distinct bands, around 78 and 67 angstrom on native gel electrophoresis, while apoA-I showed scattered band pattern less than 71 angstrom. In reconstituted HDL (rHDL) state, apoA-4 showed three major bands around 101 angstrom and 113 angstrom, while apoA-I-rHDL showed almost single band around 98 angstrom size. Lipid-free apoA-I showed 2.9-fold higher phospholipid binding ability than apoA-4. In lipid-free state, BS3-crosslinking revealed that apoA-4 showed less multimerization tendency upto dimer, while apoA-I showed pentamerization. In rHDL state (95: 1), apoA-4 was existed as dimer as like as apoA-I. With higher phospholipid content (255: 1), five apoA-I and three apoA-4 were required to the bigger rHDL formation. Regardless of particle size, apoA-I-rHDL showed superior LCAT activation ability than apoA-4-rHDL. Uptake of acetylated LDL was inhibited by apoA-I in both lipid-free and lipid-bound state, while apoA-4 inhibited it only lipid-free state. ApoA-4 showed less anti-atherogenic activity with more sensitivity to glycation. In conclusion, apoA-4 showed inferior physiological functions in lipid-bound state, compared with those of apoA-I, to induce more pro-atherosclerotic properties.
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