Bovine apolipoprotein (apo)A-I displays more enhanced antioxidant and anti-atherosclerotic activity in lipid-free and lipid-bound states than human and porcine apoA-I

Title
Bovine apolipoprotein (apo)A-I displays more enhanced antioxidant and anti-atherosclerotic activity in lipid-free and lipid-bound states than human and porcine apoA-I
Author(s)
조경현김성민박가영최인호
Keywords
HIGH-DENSITY-LIPOPROTEINS; A-I; HUMAN-PLASMA; MEMBRANE; V156K; MICE; HDL; DIMYRISTOYLPHOSPHATIDYLCHOLINE; ATHEROSCLEROSIS; CHOLESTEROL
Issue Date
201310
Publisher
SPANDIDOS PUBL LTD
Citation
INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE, v.32, no.4, pp.843 - 850
Abstract
Apolipoprotein A-I (apoA-I) is a major component of high-density lipoprotein (HDL), which displays anti-atherosclerotic activity in plasma. In the current study, we compared the functional and structural characteristics of human, bovine and porcine apoA-I as regards their antioxidant ability and protein stability. In the lipid-free state, the immunoreactivity of bovine and porcine apoA-I differed from that of human apoA-I and bovine and porcine apoA-I exhibited greater resistance to denaturation induced by urea treatment. Bovine apoA-I showed the weakest binding ability of dimyristoyl phosphatidylcholine; however, bovine apoA-I formed slightly larger reconstituted HDL (rHDL) particles with palmitoyl oleoyl phosphatidylcholine, with a higher number of apoA-I-containing particles. Bovine and porcine apoA-I comprised of pentameric structures, whereas human apoA-I in the rHDL state consisted of trimeric structures. Although apoA-I from all three species showed a similar content of alpha-helicity in the lipid-free state (approximately 53%), bovine apoA-I showed a lower alpha-helicity content (approximately 66%) compared with human apoA-I (approximately 74%) in the rHDL state. Bovine apoA-I was more resistant to denaturation and glycation upon treatment with urea and fructose, respectively. Furthermore, bovine apoA-I showed a greater inhibition of cupric ion-mediated low-density lipoprotein (LDL) oxidation and uptake of acetylated LDL by macrophages compared with human or porcine apoA-I in the lipid-free and lipid-bound states. In conclusion, bovine apoA-I has unique functional properties in the lipid-free and lipid-bound states, and displays significantly enhanced anti-atherosclerotic activity.
URI
http://hdl.handle.net/YU.REPOSITORY/28851http://dx.doi.org/10.3892/ijmm.2013.1473
ISSN
1107-3756
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