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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.

Yoo JA, Lee EY, Park JY, Lee ST, Ham S, Cho KH - Mol. Cells (2015)

Bottom Line: Regardless of particle size, apoA-I-rHDL showed superior LCAT activation ability than apoA-4-rHDL.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.

View Article: PubMed Central - PubMed

Affiliation: School of Biotechnology, Yeungnam University, Gyeongsan 712-749, Korea.

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 Å on native gel electrophoresis, while apoA-I showed scattered band pattern less than 71 Å. In reconstituted HDL (rHDL) state, apoA-4 showed three major bands around 101 Å and 113 Å, while apoA-I-rHDL showed almost single band around 98 Å 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.

No MeSH data available.


Kinetics of LCAT reaction with POPC-rHDL substrates. The rHDLs were prepared at a molar ratio of 95:5:1:150 (POPC:FC: apoA-I:Na-cholate) with 4-[14C]-cholesterol. After the reaction, esterified products (CE) were isolated via thin-layer chromatography and quantitated via scintillation counting.
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f4-molce-38-6-573: Kinetics of LCAT reaction with POPC-rHDL substrates. The rHDLs were prepared at a molar ratio of 95:5:1:150 (POPC:FC: apoA-I:Na-cholate) with 4-[14C]-cholesterol. After the reaction, esterified products (CE) were isolated via thin-layer chromatography and quantitated via scintillation counting.

Mentions: For apoA-I-rHDL, smaller rHDL (molar ratio 95:5:1, POPC: FC:apoA-I) substrate showed the highest LCAT activation activeity (around 47% conversion rate), whereas larger rHDL (255:13:1) showed a 10% conversion rate (Fig. 4). For apoA4-rHDL, smaller rHDL showed 22% LCAT activation ability, whereas larger rHDL showed almost loss of LCAT activation. This result suggests that apoA-I has stronger LCAT activation ability than apoA-4 and smaller rHDL showed higher LCAT activation activity than larger rHDL in both apoA-I and apoA-4.


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.

Yoo JA, Lee EY, Park JY, Lee ST, Ham S, Cho KH - Mol. Cells (2015)

Kinetics of LCAT reaction with POPC-rHDL substrates. The rHDLs were prepared at a molar ratio of 95:5:1:150 (POPC:FC: apoA-I:Na-cholate) with 4-[14C]-cholesterol. After the reaction, esterified products (CE) were isolated via thin-layer chromatography and quantitated via scintillation counting.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4469915&req=5

f4-molce-38-6-573: Kinetics of LCAT reaction with POPC-rHDL substrates. The rHDLs were prepared at a molar ratio of 95:5:1:150 (POPC:FC: apoA-I:Na-cholate) with 4-[14C]-cholesterol. After the reaction, esterified products (CE) were isolated via thin-layer chromatography and quantitated via scintillation counting.
Mentions: For apoA-I-rHDL, smaller rHDL (molar ratio 95:5:1, POPC: FC:apoA-I) substrate showed the highest LCAT activation activeity (around 47% conversion rate), whereas larger rHDL (255:13:1) showed a 10% conversion rate (Fig. 4). For apoA4-rHDL, smaller rHDL showed 22% LCAT activation ability, whereas larger rHDL showed almost loss of LCAT activation. This result suggests that apoA-I has stronger LCAT activation ability than apoA-4 and smaller rHDL showed higher LCAT activation activity than larger rHDL in both apoA-I and apoA-4.

Bottom Line: Regardless of particle size, apoA-I-rHDL showed superior LCAT activation ability than apoA-4-rHDL.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.

View Article: PubMed Central - PubMed

Affiliation: School of Biotechnology, Yeungnam University, Gyeongsan 712-749, Korea.

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 Å on native gel electrophoresis, while apoA-I showed scattered band pattern less than 71 Å. In reconstituted HDL (rHDL) state, apoA-4 showed three major bands around 101 Å and 113 Å, while apoA-I-rHDL showed almost single band around 98 Å 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.

No MeSH data available.