ABCC1 p.Pro235Ala
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PMID: 12948592
[PubMed]
Ito K et al: "Mutation of proline residues in the NH(2)-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function."
No.
Sentence
Comment
50
MRP1-P235/255A was generated by introducing P255A into the MRP1-P235A construct.
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ABCC1 p.Pro235Ala 12948592:50:64
status: NEW107 The seven single (P196A, P205A, P207A, P209A, P235A, P255A, and P272A) and two multiply substituted CL3 mutants (P196/205/207/209A and P235/255A) could also be stably expressed in HeLa cells.
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ABCC1 p.Pro235Ala 12948592:107:46
status: NEW147 GFP-tagged MRP1 proteins are shown in green; nuclei were stained with propidium iodide and are shown in red. (C) HeLa cells stably expressing wild-type MRP1, MRP1-P235A, MRP1-P255A, MRP1-P235/255A, and MRP1-P196/205/207/209A were cultured and processed for immunofluorescence and confocal microscopy as described in panel A.
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ABCC1 p.Pro235Ala 12948592:147:163
status: NEW149 Duplicate immunoblots of the P235A, P255A, P235/255A, and P272A MRP1 mutants probed with MAb QCRL-1 and MAb MRPr1 indicated that detection of the P255A and P235/P255A mutant MRP1 proteins relative to wild-type MRP1 by MAb MRPr1 was lower than that by MAb QCRL-1 (not shown).
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ABCC1 p.Pro235Ala 12948592:149:29
status: NEW151 When MRP1-P235A was detected with MAb QCRL-1, the signal intensity was approximately 1.8-fold higher than that for wild-type MRP1, while the signal intensity for MRP1-P235/P255A was approximately 2.3-fold higher (Fig. 5A).
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ABCC1 p.Pro235Ala 12948592:151:10
status: NEW152 When MRP1-P235A was detected with MAb MRPr1, the signal intensity was also higher than that of wild-type MRP1 (approximately 1.4-fold) but the signal intensity for P235/255A was less than that of wild-type MRP1 (approximately 75%) (Fig. 5B).
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ABCC1 p.Pro235Ala 12948592:152:10
status: NEW153 Thus, MRP1-P235A Fig. 5.
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ABCC1 p.Pro235Ala 12948592:153:11
status: NEWX
ABCC1 p.Pro235Ala 12948592:153:94
status: NEW154 Dot blot analyses of MRP1 expression in membranes from HeLa cells expressing CL3 mutants MRP1-P235A, MRP1-P255A, and MRP1-P235/255A.
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ABCC1 p.Pro235Ala 12948592:154:94
status: NEW156 MRP1-P235A and MRP1-P235/255A mutants probed with (A) MAb QCRL-1 and (B) MAb MRPr1.
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ABCC1 p.Pro235Ala 12948592:156:5
status: NEW159 (A and B) Wild-type MRP1 (n); MRP1-P235A (E); MRP1-P235/255A (z).
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ABCC1 p.Pro235Ala 12948592:159:35
status: NEW167 Plasma membrane localization of CL3 MRP1-Pro mutants is unchanged in transfected HeLa cells The changes in immunoreactivity of the MRP1-P255A and MRP1-P235/255A mutant proteins suggested that the Pro255 to Ala substitution introduced a conformation change in CL3.
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ABCC1 p.Pro235Ala 12948592:167:160
status: NEW168 To determine whether this change might also affect plasma membrane trafficking of MRP1-P255A, transfected HeLa cells expressing this mutant as well as the MRP1-P235A and MRP1-P235/255A mutants were examined by confocal microscopy as before.
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ABCC1 p.Pro235Ala 12948592:168:48
status: NEWX
ABCC1 p.Pro235Ala 12948592:168:160
status: NEW169 Like wild-type MRP1, MRP1-P255A as well as MRP1-P235A and MRP1-P235/ 255A localized mostly to the plasma membrane of confluent HeLa cells (Fig. 4C).
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ABCC1 p.Pro235Ala 12948592:169:48
status: NEW188 Results were expressed relative to wild-type Table 1 Kinetic parameters of [3 H]LTC4 uptake by membrane vesicles prepared from transfected HeLa cells expressing MRP1-Pro mutants Transfected cell line Km (nM) Vmax (pmol minÀ 1 mgÀ 1 ) Normalized Vmax MSD1 mutants WT-MRP1 128 80 80 P42A 139 35 41 P51A 109 55 50 P42/51A 103 15 48 P69A 142 46 42 P110A 150 73 124 CL3 mutants WT-MRP1 88 57 57 P196A 143 25 52 P205A 63 14 88 P207A 81 75 110 P209A 112 121 85 P196/205/207/209A 90 87 94 P235A 91 45 30 P255A 99 110 67 P235/255A 97 81 35 P272A 80 59 109 The kinetic parameters of [3 H]LTC4 uptake were determined by regression analysis of the Eadie-Hofstee transformed data.
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ABCC1 p.Pro235Ala 12948592:188:491
status: NEW146 GFP-tagged MRP1 proteins are shown in green; nuclei were stained with propidium iodide and are shown in red. (C) HeLa cells stably expressing wild-type MRP1, MRP1-P235A, MRP1-P255A, MRP1-P235/255A, and MRP1-P196/205/207/209A were cultured and processed for immunofluorescence and confocal microscopy as described in panel A.
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ABCC1 p.Pro235Ala 12948592:146:163
status: NEW148 Duplicate immunoblots of the P235A, P255A, P235/255A, and P272A MRP1 mutants probed with MAb QCRL-1 and MAb MRPr1 indicated that detection of the P255A and P235/P255A mutant MRP1 proteins relative to wild-type MRP1 by MAb MRPr1 was lower than that by MAb QCRL-1 (not shown).
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ABCC1 p.Pro235Ala 12948592:148:29
status: NEW150 When MRP1-P235A was detected with MAb QCRL-1, the signal intensity was approximately 1.8-fold higher than that for wild-type MRP1, while the signal intensity for MRP1-P235/P255A was approximately 2.3-fold higher (Fig. 5A).
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ABCC1 p.Pro235Ala 12948592:150:10
status: NEW155 MRP1-P235A and MRP1-P235/255A mutants probed with (A) MAb QCRL-1 and (B) MAb MRPr1.
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ABCC1 p.Pro235Ala 12948592:155:5
status: NEW158 (A and B) Wild-type MRP1 (n); MRP1-P235A (E); MRP1-P235/255A (z).
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ABCC1 p.Pro235Ala 12948592:158:35
status: NEW187 Results were expressed relative to wild-type Table 1 Kinetic parameters of [3 H]LTC4 uptake by membrane vesicles prepared from transfected HeLa cells expressing MRP1-Pro mutants Transfected cell line Km (nM) Vmax (pmol min 1 mg 1 ) Normalized Vmax MSD1 mutants WT-MRP1 128 80 80 P42A 139 35 41 P51A 109 55 50 P42/51A 103 15 48 P69A 142 46 42 P110A 150 73 124 CL3 mutants WT-MRP1 88 57 57 P196A 143 25 52 P205A 63 14 88 P207A 81 75 110 P209A 112 121 85 P196/205/207/209A 90 87 94 P235A 91 45 30 P255A 99 110 67 P235/255A 97 81 35 P272A 80 59 109 The kinetic parameters of [3 H]LTC4 uptake were determined by regression analysis of the Eadie-Hofstee transformed data.
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ABCC1 p.Pro235Ala 12948592:187:479
status: NEW