ABCC4 p.Glu378Gln
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PMID: 18612080
[PubMed]
El-Sheikh AA et al: "Functional role of arginine 375 in transmembrane helix 6 of multidrug resistance protein 4 (MRP4/ABCC4)."
No.
Sentence
Comment
61
Twelve mutants of the human MRP4 were generated: FF/L- (F368L and F369-), ERE/ SSQ (E374S, R375S, and E378Q), FFERE/L-SSQ (F368L, F369-, E374S, R375S, and E378Q), F368L, F369-, E374S, R375S, R375A, R375K, R375E, E378Q, and R998A.
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ABCC4 p.Glu378Gln 18612080:61:102
status: NEWX
ABCC4 p.Glu378Gln 18612080:61:155
status: NEWX
ABCC4 p.Glu378Gln 18612080:61:212
status: NEW91 Each experi- Fig. 3. Western blot analysis (A), 0.5 M [3 H]MTX (B), and 1 M [3 H]cGMP (C) transport activity of wild-type, F368L, F369-, E374S, R375S, and E378Q MRP4 transporter proteins.
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ABCC4 p.Glu378Gln 18612080:91:171
status: NEW92 A, top, Western blot of membrane vesicles isolated from HEK293 cells overexpressing MRP4 or MRP4 mutants F368L, F369-, E374S, R375S, and E378Q, as well as negative control detected by polyclonal anti-human MRP4 (representative of three).
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ABCC4 p.Glu378Gln 18612080:92:137
status: NEW95 Concentration-dependent uptake of [3 H]MTX and [3 H]cGMP in membrane vesicles expressing human MRP4 mutants. Control (Œ), wild-type (f), F368L (F), F369- (Ⅺ), E374S (᭛), R375S (E), and E378Q (x) MRP4 membrane vesicles were incubated with [3 H]MTX (top) or [3 H]cGMP (bottom) concentrations indicated in the figure.
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ABCC4 p.Glu378Gln 18612080:95:205
status: NEW142 To investigate the substitution of the amino acids of the previous mutants in more detail, we constructed the single mutants F368L, F369-, E374S, R375S, and E378Q.
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ABCC4 p.Glu378Gln 18612080:142:157
status: NEW144 The transport activity of both [3 H]MTX and [3 H]cGMP (0.5 and 1 M, respectively) was significantly reduced in mutants F368L, F369-, E374S, and E378Q compared with wild-type MRP4 (Fig. 3).
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ABCC4 p.Glu378Gln 18612080:144:152
status: NEW148 Mutants F368L, F369-, E374S, and E378Q showed transport activity levels that were comparable with that of the negative control at all concentrations tested for both MTX and cGMP.
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ABCC4 p.Glu378Gln 18612080:148:33
status: NEW188 Nevertheless, several MRP4 mutants (FF/L-, ERE/SSQ, FFERE/L-SSQ, F368L, F369-, E374S, R375A, R375E, E378Q, and R998A) showed significantly diminished transport activity of either MTX or cGMP compared with that of wild-type MRP4.
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ABCC4 p.Glu378Gln 18612080:188:100
status: NEW