ABCG2 p.Arg482His
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PMID: 14566825
[PubMed]
Miwa M et al: "Single amino acid substitutions in the transmembrane domains of breast cancer resistance protein (BCRP) alter cross resistance patterns in transfectants."
No.
Sentence
Comment
66
PA/R482Q and PA/R482H (Group 3) showed similar degrees of resistance to mitoxantrone and SN-38.
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ABCG2 p.Arg482His 14566825:66:16
status: VERIFIED165 Group 3 members (PA/R482Q and PA/R482H) showed similar degrees of resistance to mitoxantrone and SN-38.
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ABCG2 p.Arg482His 14566825:165:33
status: VERIFIED
PMID: 16815914
[PubMed]
Ejendal KF et al: "The nature of amino acid 482 of human ABCG2 affects substrate transport and ATP hydrolysis but not substrate binding."
No.
Sentence
Comment
7
Six of the mutants (R482G, R482H, R482K, R482P, R482T, and R482Y) and the wild-type protein (R482wt) were selected for studies of basal and stimulated ATPase activity and photoaffinity labeling with the substrate analog [125 I]iodoarylazidoprazosin.
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ABCG2 p.Arg482His 16815914:7:27
status: VERIFIED65 Like R482wt, the R482K mutant was also incapable of rhodamine 123 transport, and R482H, which also contains a basic side chain at position 482, was also impaired in rhodamine 123 transport.
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ABCG2 p.Arg482His 16815914:65:81
status: VERIFIED69 Transport of the fluorescent compound Bodipy FL prazosin followed a similar pattern to that observed for rhodamine 123, where the variants R482wt, R482K, R482H, and R482Y show the least transport (Fig. 3).
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ABCG2 p.Arg482His 16815914:69:154
status: VERIFIED71 Analysis of the substrate binding properties of wild-type and six mutant ABCG2 proteins In order to further investigate the effects of the R482X mutations, we studied the drug-binding ability of a selection of ABCG2 mutants (R482G, R482H, R482K, R482P, R482T, and R482Y) and the wild-type ABCG2 (R482wt).
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ABCG2 p.Arg482His 16815914:71:232
status: VERIFIED73 We selected mutants R482H, R482P, and R482Y because they are partially deficient in rhodamine 123 transport, whereas mitoxantrone transport is intact.
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ABCG2 p.Arg482His 16815914:73:20
status: VERIFIED75 Of these six ABCG2 mutants plus the wild-type protein, biochemical analyses of R482H and R482P have not been described previously.
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ABCG2 p.Arg482His 16815914:75:79
status: VERIFIED86 We analyzed expression of ABCG2 in the membranes using the monoclonal antibody BXP-21 (Fig. 5A), which shows that the R482G, R482wt, and R482T membranes used here express less ABCG2, compared with the membranes expressing the R482H, R482K, R482P, and R482Y variants.
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ABCG2 p.Arg482His 16815914:86:226
status: VERIFIED90 In contrast, the R482H, R482K, R482Y, and R482wt variants are not markedly affected by the addition of 20 mM prazosin.
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ABCG2 p.Arg482His 16815914:90:17
status: VERIFIED96 Specific [125 I]IAAP photoaffinity labeling of crude membranes derived from HeLa cells expressing wild-type ABCG2 (R482wt) and the ABCG2 variants R482G, R482H, R482K, R482P, R482T, and R482Y.
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ABCG2 p.Arg482His 16815914:96:153
status: VERIFIED106 Basal and drug-stimulated ATPase activity of wild-type ABCG2 (R482wt) and ABCG2 variants R482G, R482H, R482K, R482P, R482T, and R482Y.
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ABCG2 p.Arg482His 16815914:106:96
status: VERIFIED121 Our data demonstrate that the R482H mutant is able to efflux mitoxantrone to the same extent as the wild-type protein (data not shown), although it is somewhat deficient in rhodamine 123 and Bodipy FL prazosin transport.
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ABCG2 p.Arg482His 16815914:121:30
status: VERIFIED140 This hypothesis may also explain the differences in the ATPase activity seen for R482H and R482K mutants and the wild-type R482 protein.
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ABCG2 p.Arg482His 16815914:140:81
status: VERIFIED141 Moreover, several variants (R482H, R482K, R482wt, and R482Y) showed no prazosin-stimulated ATPase activity.
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ABCG2 p.Arg482His 16815914:141:28
status: VERIFIED