ABCB1 p.Phe343Ala
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PMID: 23104431
[PubMed]
Gozalpour E et al: "Interaction of digitalis-like compounds with p-glycoprotein."
No.
Sentence
Comment
10
The uptake of [3 H]-N-methyl-quinidine (NMQ), the P-gp substrate in vesicular transport assays, was determined.The mutations I306A, F343A, F728A,T945A, and L975A abolished NMQ transport activity of P-gp.
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ABCB1 p.Phe343Ala 23104431:10:132
status: NEW45 Removal of the side chain resulted in loss of NMQ transport activity of five human P-gp mutants: I306A, F343A, F728A, T945A, and L975A, which seem to have key role in the transport of NMQ.
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ABCB1 p.Phe343Ala 23104431:45:104
status: NEW62 Ten different P-gp mutants were produced: L65A, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A and all mutations were confirmed by sequencing of full-length P-gp cDNA.
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ABCB1 p.Phe343Ala 23104431:62:69
status: NEW122 All the indicated amino acids were replaced by alanine to remove the side chain of the residue (L65A, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A).
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ABCB1 p.Phe343Ala 23104431:122:123
status: NEW132 NMQ transport activity of mutants L65A, F336A, I340A, F942A, andV982A as compared with wild-type P-gp ranged from 60 to 150%, whereas NMQ transport activity of I306A, F343A, F728A, T945A, and L975A varied between 8 and 30%.
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ABCB1 p.Phe343Ala 23104431:132:167
status: NEW180 Fig. 5.ߓ Western blot analysis (A) and NMQ transport activity of wild type and L65A, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A mutant P-gp (B).
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ABCB1 p.Phe343Ala 23104431:180:112
status: NEW190 The first group of mutants (I306A, F343A, F728A, T945A, and L975A) exhibited a significantly lower NMQ transport activity (8-30% of wild-type P-gp).
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ABCB1 p.Phe343Ala 23104431:190:35
status: NEW
No.
Sentence
Comment
56
Nine different P-gp mutants, I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A, were produced and sequencing of full-length P-gp cDNA was used to confirm all mutations (Gozalpour et al., 2013).
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ABCB1 p.Phe343Ala 25264938:56:50
status: NEW154 Nine amino acids were replaced by alanine (I306A, F336A, I340A, F343A, F728A, F942A, T945A, L975A, and V982A) and P-gp mutants were expressed in HEK293 cells to produce membrane vesicles.
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ABCB1 p.Phe343Ala 25264938:154:64
status: NEW167 NMQ transport activity of P-gp mutants I306A, F343A and F728A was less than 40% of wild type.
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ABCB1 p.Phe343Ala 25264938:167:46
status: NEW170 Convallatoxin and NMQ transport activity were not significantly different for I306A, F336A, I340A, F728A, F942A, T945A, and L975A (Fig. 5C), whereas they differed significantly for F343A and V982A (Fig. 5D and E).
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ABCB1 p.Phe343Ala 25264938:170:181
status: NEW172 The data clearly demonstrates that transport activity of F343A for NMQ was abolished due to the mutagenesis, whereas it was partially preserved for convallatoxin.
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ABCB1 p.Phe343Ala 25264938:172:57
status: NEW212 The transport activity of F343A and V982A mutants for NMQ and convallatoxin were compared using an unpaired Student's t-test: nnn Po0.0001 (D and E).
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ABCB1 p.Phe343Ala 25264938:212:26
status: NEW253 The P-gp mutants, I306A, F343A and F728A exhibited a NMQ transport activity that was less than 30% of the wild type activity.
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ABCB1 p.Phe343Ala 25264938:253:25
status: NEW259 The transport activities of NMQ and convallatoxin were significantly different for the F343A and V982A mutant (Fig. 5D and E).
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ABCB1 p.Phe343Ala 25264938:259:87
status: NEW260 NMQ transport activity of F343A was completely diminished, whereas convallatoxin transport activity was conserved.
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ABCB1 p.Phe343Ala 25264938:260:26
status: NEW