ABCC1 p.Lys1092Met
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PMID: 12954620
[PubMed]
Zhang DW et al: "Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding state."
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51
They are as follows: T1082A (5Ј-C TCC AAG GAG CTC GAC GCA GTG GAC TCC-3Ј), D1084N (5Ј-CTG GAC ACA GTG AAT TCC ATG ATC CCG-3Ј), D1084A (5Ј-CTG GAC ACA GTG AAA TCG ATG ATC CCG-3Ј), D1084E (5Ј-CTG GAC ACA GTG GAC TCG ATG ATC CCG-3Ј), D1084V (5Ј-CTG GAC ACA GTG GTA TCG ATG ATC CCG-3Ј), S1085A (5Ј-CTG GAC ACA GTC GAC GCC ATG ATC CCG G-3Ј), K1092M (5Ј-C CCG GAG GTC ATC ATG ATG TTC ATG GGC-3Ј), K1092A (5Ј-C CCG GAG GTC ATC GCG ATG TTC ATG GGC-3Ј), K1092E (5Ј-C CCG GAG GTC ATC GAG ATG TTC ATG GGC-3Ј), K1092R (5Ј-C CCG GAG GTC ATC AGG ATG TTC ATG GGC-3Ј), S1097A (5Ј-G ATG TTC ATG GGC GCC CTG TTC AAC-3Ј), N1100A (5Ј-TTC ATG GGC TCG CTC TTC GCC GTC ATT GGT G-3Ј), N1100S (5Ј-TTC ATG GGC TCG CTC TTC AGT GTC ATT GGT G-3Ј).
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ABCC1 p.Lys1092Met 12954620:51:409
status: NEW118 RESULTS Expression of Mutant MRP1 in Stably Transfected HEK293 Cells-To examine the functional importance of charged and polar residues in TM14 of MRP1, we generated a series of six mutant proteins in which Thr1082 , Ser1085 , Ser1097 , and Asn1100 were replaced with Ala, Asp1084 was replaced with Asn, and Lys1092 was mutated to Met (Fig. 1).
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ABCC1 p.Lys1092Met 12954620:118:308
status: NEW136 The levels of LTC4 uptake by vesicles prepared from HEK transfectants expressing either wild type MRP1 or mutations T1082A, S1085A, K1092M, S1097A, and N1100A were proportional to the relative expression levels of the wild type and mutant proteins.
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ABCC1 p.Lys1092Met 12954620:136:132
status: NEW138 ATP-dependent transport of [3 H]E217betaG was unaffected by the T1082A, S1085A and K1092M mutations (Fig. 3, D-F), but substitution of Ser1097 with Ala and conversion of Asp1084 to Asn both dramatically decreased transport.
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ABCC1 p.Lys1092Met 12954620:138:83
status: NEW145 In contrast, although substitution of Lys1092 with Met had no detectable effect on resistance to the electroneutral drug VP-16, the mutation increased resistance to the cationic drugs, vincristine and doxorubicin.
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ABCC1 p.Lys1092Met 12954620:145:38
status: NEW147 Transport of [3 H]GSH by Wild Type and Mutant MRP1-The studies described above indicated that mutations S1097A and D1084N affected the ability of MRP1 to confer drug resistance and to transport conjugated organic anions, whereas the K1092M mutation influenced only the drug resistance profile of MRP1.
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ABCC1 p.Lys1092Met 12954620:147:233
status: NEW164 Other mutations, including mutations S1097A and K1092M that altered the drug resistance profile of MRP1, had no effect.
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ABCC1 p.Lys1092Met 12954620:164:48
status: NEW165 These findings suggest that the effects of mutations S1097A and K1092M on MRP1-mediated drug resistance appear to result primarily from changes in the ability to interact with the drug substrate rather than GSH.
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ABCC1 p.Lys1092Met 12954620:165:64
status: NEW229 Mutational and Functional Analysis of Mutant Human MRP146058 addition, because of the effect of the K1092M mutation on the drug resistance profile of MRP1, Lys1092 was converted to Ala, Glu, and Arg.
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ABCC1 p.Lys1092Met 12954620:229:101
status: NEW248 The mutation K1092R also showed the same phenotype as wild type MRP1, whereas mutations K1092A and K1092E, like K1092M, increased the ability of MRP1 to confer resistance to vincristine and doxorubicin but not to VP-16.
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ABCC1 p.Lys1092Met 12954620:248:112
status: NEW