ABCA1 p.Leu268Ala
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PMID: 18246469
[PubMed]
Zannis VI et al: "Discrete roles of apoA-I and apoE in the biogenesis of HDL species: lessons learned from gene transfer studies in different mouse models."
No.
Sentence
Comment
149
A triple substitution (apoE4[Leu261Ala/Trp264Ala/Phe265Ala]) or five residue substitutions (apoE4[Leu261Ala/Trp264Ala/ Phe265Ala/Leu268Ala/Val269Ala]) did not induce hypertriglyceridemia and both were associated with greatly increased HDL cholesterol levels (Figure 8A III, B III and A IV, B IV, respectively) (19,20).
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ABCA1 p.Leu268Ala 18246469:149:129
status: NEW150 EM analysis of the HDL fractions showed that apoE4[Leu261Ala/Trp264Ala/Phe265Ala] and the apoE4[Leu261Ala/Trp264Ala/Phe265Ala/Leu268Ala/ Val269Ala] formed spherical HDL (Figure 8C III, IV), apoE4[Phe265Ala] formed discoidal HDL (Figure 8CI), and the apoE4[Leu261Ala/Trp264Ala] formed mostly spherical and few discoidal HDL particles (Figure 8C II) (20).
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ABCA1 p.Leu268Ala 18246469:150:126
status: NEW
PMID: 17206937
[PubMed]
Kypreos KE et al: "Pathway of biogenesis of apolipoprotein E-containing HDL in vivo with the participation of ABCA1 and LCAT."
No.
Sentence
Comment
30
It is important to note that infection of apoA-I-/- mice with adenovirus expressing a recently described apoE4 (L261A/ W264A/F265A/L268A/V269A) mutant designated apoE4mut1 [17] did not induce dyslipidaemia and promoted the formation of spherical apoE-containing HDL particles, suggesting that this mutant has improved functions in lipoprotein clearance as well as in the biogenesis of apoE-containing HDL.
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ABCA1 p.Leu268Ala 17206937:30:131
status: NEW117 Substitution of alanine for hydrophobic residues in the region 261-269 enhances formation of spherical HDL and does not induce dyslipidaemia in apoA-I-/- mice In another set of experiments, apoA-I-/- mice were infected with 2 × 109 pfu of an adenovirus expressing the apoE4 mutant (L261A/W264A/F265A/L268A/V269A) mutant designated apoE4mut1 [17].
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ABCA1 p.Leu268Ala 17206937:117:305
status: NEW137 These experiments indicated that, under conditions of apoE overexpression, the endogenous Figure 4 Cholesterol FPLC profile, apoE distribution and electron microscopy analysis of HDL fraction of apoE-/- mice infected with recombinant adenoviruses expressing apoE4mut1 (A) FPLC profiles of total, free and esterified cholesterol of apoE-/- mice infected with 2 × 109 pfu of adenoviruses expressing apoE4mut1 (AdGFRP-E4[L261A,T264A,F265A, L268A,V269A]).
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ABCA1 p.Leu268Ala 17206937:137:445
status: NEW29 It is important to note that infection of apoA-I-/- mice with adenovirus expressing a recently described apoE4 (L261A/ W264A/F265A/L268A/V269A) mutant designated apoE4mut1 [17] did not induce dyslipidaemia and promoted the formation of spherical apoE-containing HDL particles, suggesting that this mutant has improved functions in lipoprotein clearance as well as in the biogenesis of apoE-containing HDL.
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ABCA1 p.Leu268Ala 17206937:29:131
status: NEW115 Substitution of alanine for hydrophobic residues in the region 261-269 enhances formation of spherical HDL and does not induce dyslipidaemia in apoA-I-/- mice In another set of experiments, apoA-I-/- mice were infected with 2 &#d7; 109 pfu of an adenovirus expressing the apoE4 mutant (L261A/W264A/F265A/L268A/V269A) mutant designated apoE4mut1 [17].
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ABCA1 p.Leu268Ala 17206937:115:304
status: NEW135 These experiments indicated that, under conditions of apoE overexpression, the endogenous Figure 4 Cholesterol FPLC profile, apoE distribution and electron microscopy analysis of HDL fraction of apoE-/- mice infected with recombinant adenoviruses expressing apoE4mut1 (A) FPLC profiles of total, free and esterified cholesterol of apoE-/- mice infected with 2 &#d7; 109 pfu of adenoviruses expressing apoE4mut1 (AdGFRP-E4[L261A,T264A,F265A, L268A,V269A]).
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ABCA1 p.Leu268Ala 17206937:135:444
status: NEW