ABCA1 p.Lys2031Arg
| Predicted by SNAP2: | A: D (53%), C: D (53%), D: D (66%), E: D (63%), F: D (66%), G: D (59%), H: N (57%), I: N (53%), L: D (59%), M: N (53%), N: N (53%), P: D (75%), Q: D (59%), R: N (87%), S: N (72%), T: N (53%), V: D (63%), W: D (80%), Y: D (71%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, L: D, M: D, N: D, P: D, Q: D, R: N, S: D, T: D, V: D, W: D, Y: D, |
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[hide] The effects of neurological disorder-related codon... Biosci Biotechnol Biochem. 2012;76(12):2289-93. Epub 2012 Dec 7. Tomioka M, Toda Y, Kurisu J, Kimura Y, Kengaku M, Ueda K
The effects of neurological disorder-related codon variations of ABCA13 on the function of the ABC protein.
Biosci Biotechnol Biochem. 2012;76(12):2289-93. Epub 2012 Dec 7., [PMID:23221702]
Abstract [show]
Rare coding variants of ATP-binding cassette protein A13 (ABCA13) contribute to the risk of neurological disorders, but little is known about the physiological function of ABCA13 and how single nucleotide polymorphisms (SNPs) affect it. Here, we examined the effects of neurological disorder-related SNPs ABCA13, T4031A and R4843C in the context of ABCA1, and found that the former SNP (T1088A in ABCA1) severely impaired the ABCA1 functions of apolipoprotein A-I (apoA-I) binding and cholesterol efflux. The antibody against mouse ABCA13 reacted with neurons in the cerebral cortex, hippocampus, and cerebellum. These results suggest that the T4031A replacement affects the function of ABCA13 in the brain.
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No. Sentence Comment
66 Hence we established HEK293 cells that stably expressed ABCA1 containing ABCA13 SNPs, ABCA1-T1088A, ABCA1- K2031C, and ABCA1-K2031R (as control).
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ABCA1 p.Lys2031Arg 23221702:66:125
status: NEW70 However, the K2031C SNP did not significantly affect cholesterol efflux as compared to the wild type or K2031R (Fig. 2A).
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ABCA1 p.Lys2031Arg 23221702:70:104
status: NEW71 ApoA-I binding of HEK/ABCA1-SNP mutants at the plasma membrane We have reported that the first step in high-density lipoprotein (HDL) formation is apoA-I binding to the extracellular domains of ABCA1.13) Hence we examined to determine whether the loss in the cholesterol efflux ability of T1088A was due to a change in apoA-I binding.
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ABCA1 p.Lys2031Arg 23221702:71:104
status: NEW79 For K2031C and wild-type K2031R, most of the protein was resistant to EndoH, but 50% or more of ABCA1-T1088 was sensitive to EndoH (Fig. 4), suggesting that the T1088A mutation caused improper folding of the protein.
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ABCA1 p.Lys2031Arg 23221702:79:25
status: NEW67 Hence we established HEK293 cells that stably expressed ABCA1 containing ABCA13 SNPs, ABCA1-T1088A, ABCA1- K2031C, and ABCA1-K2031R (as control).
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ABCA1 p.Lys2031Arg 23221702:67:125
status: NEW80 For K2031C and wild-type K2031R, most of the protein was resistant to EndoH, but 50% or more of ABCA1-T1088 was sensitive to EndoH (Fig. 4), suggesting that the T1088A mutation caused improper folding of the protein.
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ABCA1 p.Lys2031Arg 23221702:80:25
status: NEW