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-Ah; Lee, Eun-Young; Park, Ji Yoon; Lee, Seung-Taek; Ham, Sihyun; Cho, 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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