ABCMdb

ABCC1 p.Glu1089Gln

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Publications

PMID: 11278596 [PubMed] Zhang DW et al: "Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines."

No. Sentence Comment

7 The mutation E1089D showed the same phenotype as MRP1, while the E1089Q substitution markedly decreased resistance to anthracyclines without affecting LTC4 and E217betaG transport. Login to comment
112 In contrast, conversion of glutamate 1089 to glutamine, as it is in the murine protein, essentially eliminated the ability of MRP1 to confer resistance to doxorubicin, daunorubicin, and epirubicin, as did mutations MRP1E1089A, MRP1E1089L, and MRP1E1089K (Table II). Login to comment
113 In addition, mutation of glutamate 1089 to glutamine, alanine, and leucine decreased the relative resistance to vincristine by 55-65%, while mutation to lysine essentially eliminated resistance to this drug. Login to comment
116 Typical survival curves for transfectants expressing wild type MRP1 and the mutant proteins E1089Q, E1089D, and E1089K are shown in Fig. 4. Login to comment
146 In view of the effect of mutations of glutamate 1089 in the human protein on resistance to vincristine and VP-16 in addition to the anthracyclines, we also examined LTC4 and E217betaG transport by wild type and mutant human MRP1, including MRP1, E1089Q, E1089D, and E1089K. Login to comment
223 Mutation of glutamate 1089 to glutamine essentially eliminated anthracycline resistance, confirming the crucial role of this residue. Login to comment

PMID: 11429411 [PubMed] Zhang DW et al: "Identification of a nonconserved amino acid residue in multidrug resistance protein 1 important for determining substrate specificity: evidence for functional interaction between transmembrane helices 14 and 17."

No. Sentence Comment

196 Consequently, a double mutation of MRP1 was also made, in which Glu1089 was replaced with Gln and Thr1242 was substituted with Ala (E1089Q/T1242A). Login to comment
203 Similarly, introduction of the E1089Q mutation into MRP1T1242A increased resistance to vincristine and VP-16 despite the fact that the single TM14 mutation in the human protein has been shown to decrease resistance to both of these drugs (29). Login to comment
204 However, the E1089Q mutation eliminated the ability of MRP1T1242A to confer resistance to anthracyclines (Table III), as observed previously when this amino acid substitution was introduced into wild type MRP1 as a single mutation (29). Login to comment

PMID: 12042670 [PubMed] Conrad S et al: "A naturally occurring mutation in MRP1 results in a selective decrease in organic anion transport and in increased doxorubicin resistance."

No. Sentence Comment

154 Moreover, substitution of the acidic Glu residue at position 1089 with Gln can selectively alter the ability of MRP1 to confer resistance to anthracycline antibiotics, but has no effect on its ability to transport E217âG or LTC4 [39]. Login to comment

PMID: 12138119 [PubMed] Qian YM et al: "Photolabeling of human and murine multidrug resistance protein 1 with the high affinity inhibitor [125I]LY475776 and azidophenacyl-[35S]glutathione."

No. Sentence Comment

159 The extent of [125 I]LY475776 labeling of E1089Q MRP1 was decreased severalfold relative to that of wild type protein, whereas [125 I]LY475776 labeling of Q1086E mrp1 was slightly enhanced when compared with wild type mrp1 (Fig. 6A, left panel). Login to comment

PMID: 12867490 [PubMed] Nunoya K et al: "Molecular cloning and pharmacological characterization of rat multidrug resistance protein 1 (mrp1)."

No. Sentence Comment

301 Previously, we showed that the hMRP1 TM 14 mutations E1089Q and E1089K, which either reduce or completely eliminate resistance to doxorubicin and vincristine, had no effect on estrone 3-sulfate transport (Zhang et al., 2001b). Login to comment

PMID: 14754409 [PubMed] Karwatsky JM et al: "Drug binding domains of MRP1 (ABCC1) as revealed by photoaffinity labeling."

No. Sentence Comment

234 Previous studies [67] showed that this residue is required for efficient transport of E217βG. In addition, a mutation of Glu1089 to Gln, the corresponding amino acid in mrp1, abolished MRP1-mediated anthracyclin resistance [68]. Login to comment
237 The extent of MRP1 Glu1089 to Gln photolabeling was reduced, whereas labeling of mrp1 Gln1089 to Glu was enhanced slightly. Login to comment

PMID: 14965249 [PubMed] Haimeur A et al: "The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulation."

No. Sentence Comment

204 More NH2-proximal regions of MSD3 also appear to be involved in LY475776 binding since tryptic fragments corresponding to TM12/13 and TM14/15 are photolabeled, and photolabeling is reduced in the TM14 Glu1089Gln MRP1 mutant [162, 165]. Login to comment

PMID: 16684361 [PubMed] Wang Z et al: "Nucleotide sequence analyses of the MRP1 gene in four populations suggest negative selection on its coding region."

No. Sentence Comment

156 It has been reported that an artificial mutation E1089Q created in MRP1 markedly affected the ability of MRP1 protein to confer resistance without affecting its ability to transport organic anions [52]. Login to comment

PMID: 17295059 [PubMed] Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."

No. Sentence Comment

114 E1089Q, E1089A, E1089L or E1089N mutations in TM14 markedly decreased resistance to anthracyclines without affecting LTC4 and E217βG transport [81]. Login to comment
142 Consistent with these results, converting human E1089 to mouse Q at the corresponding position (human MRP1/E1089Q) markedly decreased resistance to anthracycline, but without affecting LTC4 and E217βG transport [81], suggesting that anthracycline, LTC4 and E217βG might bind to slightly different regions within MRP1 protein. Login to comment
146 Introduction of a second mutation based on mouse Mrp1 sequence into human MRP1/T1242A to generate a double mutant MRP1/ E1089Q/T1242A created a protein similar to mouse wild-type Mrp1 that restored resistance to vicristine and VP-16 but not to doxorubicin and epirubicin [85]. Login to comment

PMID: 18691054 [PubMed] Zhou SF et al: "Substrates and inhibitors of human multidrug resistance associated proteins and the implications in drug development."

No. Sentence Comment

568 More NH2-proximal regions of TMD2 also appear to be involved in LY475776 binding since tryptic fragments corresponding to TM12/13 and TM14/15 are photolabeled, and photolabeling is reduced in the TM14 Glu1089Gln MRP1/ABCC1 mutant [252,253]. Login to comment

PMID: 19949927 [PubMed] Chang XB et al: "Molecular mechanism of ATP-dependent solute transport by multidrug resistance-associated protein 1."

No. Sentence Comment

104 Mutations of C43S in TM1 (112); P343A, K332L and K332D in TM6 (113, 114); W445A and P448A in TM8 (113, 115); T550A, T556A and P557A in TM10 (113, 116); N590A, F594A, P595A, N597A, S604A and S605A in TM11 (113, 117, 118); E1089Q, E1089A, E1089L, E1089N, K1092, S1097 and N1100 in TM14 (119, 120); R1197K in TM16 (121); Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y or R1249K in TM17 (121-124) significantly affect MRP1 function. Login to comment
110 In consistent with these results, converting human E1089 to mouse Q at the corresponding position (human MRP1/ E1089Q) markedly decreased resistance to anthracycline, but without affecting LTC4 and E2 17bG transport (119), suggesting that anthracycline and hydrophobic portion of LTC4 or E2 17bG might bind to slightly different regions within MRP1 protein. Login to comment

PMID: 21143116 [PubMed] He SM et al: "Structural and functional properties of human multidrug resistance protein 1 (MRP1/ABCC1)."

No. Sentence Comment

711 More NH2-proximal regions of TMD1 also appear to be involved in LY475776 binding since tryptic fragments corresponding to TM12/13 and TM14/15 are photolabeled, and photolabeling is reduced in the Glu1089Gln mutant of TM14 [270, 271]. Login to comment

PMID: 11557126 [PubMed] Leslie EM et al: "Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters."

No. Sentence Comment

36 Thus substitution of a glutamate at position 1089 with glutamine as found in the murine protein results in a marked decrease in anthracycline resistance, while transport of LTC4 and E217bG remain unchanged (Zhang et al., 2001). Login to comment

PMID: 12706887 [PubMed] Grailles M et al: "The Drosophila melanogaster multidrug-resistance protein 1 (MRP1) homolog has a novel gene structure containing two variable internal exons."

No. Sentence Comment

155 Site directed mutagenesis was used to change Glu 1089 to Gln, Asp, Ala, Leu or Lys. Login to comment
153 Site directed mutagenesis was used to change Glu 1089 to Gln, Asp, Ala, Leu or Lys. Login to comment