ABCA1 p.Ala594Thr
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PMID: 23087442
[PubMed]
Sorrenson B et al: "Functional rescue of mutant ABCA1 proteins by sodium 4-phenylbutyrate."
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16
Nine different ABCA1 mutants (p.A594T, p.I659V, p.R1068H, p.T1512M, p.Y1767D, p.N1800H, p.R2004K, p.A2028V, p.Q2239N) expressed in HEK293 cells, displaying different degrees of mislocalization to the plasma membrane and discrete impacts on cholesterol efflux, were subject to treatment with 4-PBA.
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ABCA1 p.Ala594Thr 23087442:16:32
status: NEW54 We identified a further three novel mutations, p.A594T, p.Y1767D, and p.Q2239N, and these were also included in this study. We hypothesized that efflux function would be improved for mutants that are dysfunctional as a result of protein mislocation.
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ABCA1 p.Ala594Thr 23087442:54:49
status: NEW73 Both media were RESULTS ABCA1 mutants with impaired localization have reduced cholesterol efflux function We identified three novel ABCA1 variants, p.A594T, p.Y1767D, and p.Q2239N, in heterozygote form in three individuals with HDL-C levels of 0.61, 0.17, and 0.37 mmol/L, respectively.
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ABCA1 p.Ala594Thr 23087442:73:153
status: NEW77 Investigation of the six uncharacterized mutations in transfected HEK293 cells showed the p.A594T, p.I659V, p.Y1767D, p.R2004K, and p.A2028V mutants to have various degrees of mislocalization (Fig. 2A).
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ABCA1 p.Ala594Thr 23087442:77:92
status: NEW112 Treatment with 4-PBA induced a significant increase in colocalization for the p.A594T, p.R1068H, p.T1512M, p.Y1767D, p.N1800H, and p.R2004K mutants. Treatment with 4-PBA did not affect the colocalization of the wild-type ABCA1-GFP protein (supplementary Fig. II).
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ABCA1 p.Ala594Thr 23087442:112:80
status: NEW196 This is in contrast with our results where the majority of the mutants showed significant improvements in function, including the p.A594T mutant, which is of a similar location to p.Q597R.
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ABCA1 p.Ala594Thr 23087442:196:132
status: NEW