ライフサイエンスコーパス: MRP1

1 MRP1 expression markedly increased upon macrophage activ

2 MRP1 inhibition prevented the decline in intracellular G

3 MRP1 mediated efficient ATP-dependent transport of LNO(2

4 MRP1 was expressed in 8 (50%) of 16 tumors, and MRP2 was

5 MRP1-dependent transport of leukotriene C(4) and estradi

6 1/ATP-binding cassette subfamily C member 1 (MRP1/ABCC1) and the PI3/AKT pathway.

7 Multidrug resistance protein 1 (MRP1) actively transports a wide variety of drugs out of

8 chopulmonary multidrug resistance protein 1 (MRP1) and permeability glycoprotein (P-gp) and assess th

9 p multidrug resistance-associated protein 1 (MRP1) and the transcription factor NFkappaB.

10 The multidrug resistance protein 1 (MRP1) encoded by ABCC1 was originally discovered as a ca

11 e multidrug resistance-associated protein 1 (MRP1) has been closely linked to poor treatment response

12 Multidrug resistance-associated protein 1 (MRP1) is a drug efflux transporter that has been implica

13 Multidrug resistance protein 1 (MRP1) is an ABC exporter that extrudes a variety of chem

14 t multidrug resistance-associated protein 1 (MRP1) is prevalent in many cancer types, the functional

15 e multidrug resistance-associated protein 1 (MRP1) transporter.

16 n multidrug resistance-associated protein 1 (MRP1) was mutated to either a different aromatic residue

17 , multidrug resistance-associated protein 1 (MRP1), and breast cancer resistance protein (BCRP), whic

18 , multidrug resistance-associated protein 1 (MRP1), and found that MSC EV suppressed MRP1 mRNA, prote

19 ilencing the multidrug resistance protein 1 (MRP1), before chemotherapeutic drug delivery in vivo wit

20 f multidrug resistance-associated protein 1 (MRP1), is regulated by yeast casein kinase 2alpha (Cka1p

21 , multidrug resistance-associated protein 1 (MRP1), mediates this release potentially as a dinitrosyl

22 d multidrug resistance-associated protein 1 (MRP1).

23 ting multidrug resistance-related protein 1 (MRP1).

24 ship between multidrug resistance protein 1 (MRP1, ABCC1) expression and cellular sensitivity to mito

25 , ABCB1) and multidrug resistance protein 1 (MRP1, ABCC1) to confirm the selectivity toward BCRP.

26 , multidrug resistance-associated protein 1 (MRP1, ABCC1), and breast cancer resistance protein (BCRP

27 d multidrug resistance-associated protein 1 (MRP1, ABCC1).

28 pic 5-domain multidrug resistance protein 1 (MRP1/ABCC1) extrudes a variety of drugs and organic anio

29 transporter multidrug resistance protein 1 (MRP1/ABCC1) is responsible for the cellular export of a

30 (ABCB1/Pgp), multidrug resistance protein 1 (MRP1/ABCC1), or multidrug resistance protein 2 (MRP2/ABC

31 transporter multidrug resistance protein 1 (MRP1/ABCC1).

32 ), multidrug-resistant-associated protein 1 (MRP1; ABCC1), MRP2 (ABCC2), and MRP4 (ABCC4).

33 e multidrug resistance-associated protein-1 (MRP1) and the reduction of substrate export by this tran

34 express the multidrug resistance protein-1 (MRP1) and use this as their major exporter of GSSG.

35 r extents of multidrug resistance protein-1 (MRP1) expression, and greater MRP1-mediated efflux of NO

36 substrate of multidrug resistance protein-1 (MRP1), into HEK-MRP1 cells, which overexpress MRP1, and

37 nzymes including GSTA2, GSTP1, CYP3A4, HO-1, MRP1, and MRP5.

38 ic parameters of As(GS)3 for HEK-Asn19/23Gln-MRP1 were similar to those of HeLa/HEK-SF-MRP1 and HeLa-

39 e-negative breast cancer model following 80% MRP1 silencing compared with the continuous tumor growth

40 C transporters such as P-glycoprotein/ABCB1, MRP1/ABCC1, and MXR/ABCG2 seems to be a major cause of f

41 teins ABCB1 (P-gp), ABCG2 (BCRP), and ABCC1 (MRP1), which are involved in the formation of multidrug

42 rters such as ABCB1 (P-glycoprotein), ABCC1 (MRP1), and ABCG2 (BCRP) are well known for their role in

43 s inhibited by MK571, an inhibitor of ABCC1 (MRP1), but not by inhibitors of ABCB1 (MDR-1, P-glycopro

44 ) expression and the drug-transporter ABCC1 (MRP1) were linked to thiopurine sensitivity, suggesting

45 idrug resistance-associated protein 1 (ABCC1/MRP1; herein referred to as ABCC1), we measured N1(IC) a

46 such as ABCB1/P-glycoprotein/MDR1 and ABCC1/MRP1 causes multidrug resistance in cancer chemotherapy.

47 r therapeutic development to sensitize ABCC1/MRP1-mediated drug resistance in cancer chemotherapy.

48 These findings suggest that ABCC1/MRP1 may exist and function as a dimer and that MSD0L0 l

49 the human full-length ABC transporter ABCC1/MRP1 using several biochemical approaches.

50 y the ATP-binding cassette transporter ABCC1/MRP1, and is then able to initialize cascades downstream

51 nction when coexpressed with wild-type ABCC1/MRP1.

52 In addition, MRP1 regulates redox homeostasis, inflammation, and horm

53 enic, a human carcinogen, is a high-affinity MRP1 substrate as arsenic triglutathione [As(GS)3].

54 y in the 4-position were more active against MRP1 than derivatives with amide functionality.

55 Moreover, mutation of Thr249 to alanine (MRP1-T249A) also resulted in decreased MRP1-dependent tr

56 es of Trypanosoma brucei apoMRP1/MRP2 and an MRP1/MRP2-gRNA complex.

57 , and they continue to efficiently efflux an MRP1 substrate.

58 P1 steady-state levels and fail to efflux an MRP1 substrate.

59 Membrane vesicles from an MRP1-transfected HeLa cell line lacking membrane-associa

60 lation of the cytotoxic drug vincristine, an MRP1 substrate, depleted virus from naturally latent CD1

61 tance of the combined effect of GST P1-1 and MRP1 in protecting cells from the cytotoxic effects of N

62 tand the role of glutathione, GSTP1a-1a, and MRP1 in NQO detoxification, we have characterized the ki

63 efflux pump P-glycoprotein (P-gp, ABCB1) and MRP1 (ABCC1).

64 ated drug-resistant cells (i.e. NCI/ADR) and MRP1-mediated resistant cells (i.e. MCF-7/VP).

65 l cell lines (e.g., wild-type HeLa cells and MRP1-overexpressing HeLa-R cells).

66 Indeed, CK2alpha and MRP1 interact physically, and recombinant CK2 phosphoryl

67 rubicin accumulation in MRP1 CK2alpha(-) and MRP1-T249A cells compared with MRP1 cells.

68 and LTC(4) from LTA(4) are competitive, and MRP1 is the efflux pump for LTC(4) Inhibition of MRP1 wi

69 lts suggest that glutathione conjugation and MRP1-mediated conjugate transport can attenuate LNO(2) b

70 gate the role of glutathione conjugation and MRP1-mediated efflux in the regulation of PPARgamma-depe

71 rly affected by nonenzymatic conjugation and MRP1-mediated efflux.

72 cin, suggesting that dual targeting EGFR and MRP1 could serve as a therapeutic approach to overcome T

73 Downregulating EGFR and MRP1 inhibits T-DM1R-JIMT1 cell growth and re-sensitizes

74 While nonenzymatic QO-SG formation and MRP1-mediated conjugate efflux result in low-level prote

75 selective for ABCG2 over P-glycoprotein and MRP1, appeared not to be transported by ABCG2, and was a

76 ased modulators targeting P-glycoprotein and MRP1.

77 ed sensitivity toward daunorubicin (P-gp and MRP1) and SN-38 (BCRP) in A2780/ADR (P-gp), H69AR (MRP1)

78 -sestamibi is a known substrate for P-gp and MRP1, which are established cellular drug efflux transpo

79 involved in drug resistance, namely GST and MRP1 (multidrug resistance-associated protein 1), are cr

80 Considering this, and because GSTP1 and MRP1 are up-regulated during macrophage activation, this

81 iability studies demonstrated that GSTP1 and MRP1 protect activated macrophages from NO cytotoxicity.

82 Considering this and that GSTs and MRP1 form an integrated detoxification unit with chemoth

83 that glutathione conjugation of NO(2)-LA and MRP1-mediated efflux of the conjugates were associated w

84 n-transporting polypeptide) mRNA levels, and MRP1 protein levels; however, differences existed in MRP

85 ral other transporters (e.g. OAT2, OAT3, and MRP1) have also been proposed as important PAH transport

86 notypes of SNPs in the ALOX5 (rs2115819) and MRP1 (rs119774) genes and changes in FEV(1) (p < 0.05),

87 rimidines using the doxorubicin selected and MRP1 overexpressing small cell lung cancer cell line H69

88 ibited by several conjugated organic anions (MRP1 substrates) as well as the metalloid antimonite (K(

89 ensitive space and was inhibited by the anti-MRP1 antibody QCRL3.

90 or P-glycoprotein) and ABCC1 (also known as MRP1) whose inhibition remains a priority to circumvent

91 wn as MDR1 or P-gp) and ABCC1 (also known as MRP1), whose inhibition remains a priority to circumvent

92 lpha results in decreased phosphorylation at MRP1-Thr249.

93 S)3 transport kinetics were observed between MRP1-enriched membrane vesicles prepared from human embr

94 , these data suggest that cross-talk between MRP1 glycosylation and phosphorylation occurs and that p

95 ATP analogs bind MRP1 with reduced apparent affinity, inducing a partiall

96 o track the conformational changes of bovine MRP1 (bMRP1) in real time.

97 etermined the molecular structures of bovine MRP1 in two conformations: an apo form at 3.5 A without

98 prevented by the MRP1 inhibitor MK571 and by MRP1 small interfering RNA.

99 reducing their transport out of the cell by MRP1.

100 nt with the interpretation that MX efflux by MRP1 involves cotransport of MX and glutathione.

101 ss MRP1, and monitored the calcein efflux by MRP1.

102 ivated metabolite of PABA/NO was effluxed by MRP1 in a GSH-dependent manner.

103 key physiological organic anions effluxed by MRP1, and an ever growing body of evidence indicates tha

104 GSSG export by MRP1 leads to a perturbation of endothelial redox state

105 ing by cytotoxic agents normally exported by MRP1.

106 by MDR1 Pgp and, to a much lesser extent, by MRP1, but not MRP2-MRP6 or BCRP/MXR.

107 mon currency for NO transport and storage by MRP1 and GST P1-1, respectively.

108 As(GS)(3) transport by MRP1 was osmotically sensitive and was inhibited by seve

109 NQO was not transported by MRP1 either alone or in the presence of S-methyl glutath

110 confirmed that thiodione was transported by MRP1, and that glutathione is an essential substrate for

111 In Jurkat cells, MRP1 was largely localized to the plasma membrane, and t

112 in MRP1 cells, but not in MRP1 CK2alpha(-), MRP1-T249A, or MRP1-T249E cells, suggesting that CK2alph

113 lts demonstrate the utility of the two-color MRP1 construct for investigating ATP-binding cassette tr

114 Two-color MRP1 transport activity was normal, as shown by vesicula

115 uctural dynamics, we engineered a "two-color MRP1" construct by fusing green fluorescent protein (GFP

116 In conclusion, MRP1 transports inorganic arsenic as a tri-GSH conjugate

117 n the brain and hence form the corresponding MRP1 substrate tracers in situ.

118 protein Ycf1p and its mammalian counterpart, MRP1, belong to the ABCC subfamily of ATP-binding casset

119 a noncompetitive inhibitor of daunorubicin (MRP1), calcein AM (P-gp), and pheophorbide A (BCRP) tran

120 nine (MRP1-T249A) also resulted in decreased MRP1-dependent transport, whereas a phosphomimicking mut

121 er cell lines where CK2 inhibition decreased MRP1-mediated efflux of doxorubicin and increased doxoru

122 e short isoform of UL138 also show decreased MRP1 levels, but the magnitude of the decrease is not th

123 ing the long isoform of UL138 show decreased MRP1 steady-state levels and fail to efflux an MRP1 subs

124 d 2-related factor 2 (Nrf2), which decreased MRP1 and GSTP1 expression, concomitant with reduced (59)

125 across the cell membrane via the ATP-driven MRP1 pump.

126 erly decorated for the preparation of either MRP1 or P-gp highly selective inhibitors.

127 Endothelial MRP1 may provide a novel therapeutic target for preventi

128 ed by increased drug resistance and enhanced MRP1-mediated drug efflux.

129 favor a mechanism for glutathione-enhanced, MRP1-mediated QO-SG transport that does not involve cotr

130 n parental control cells that do not express MRP1.

131 of CK2alpha in MCF7-derived cells expressing MRP1 [MRP1 CK2alpha(-)] resulted in increased doxorubici

132 The apparent K(m) of As(GS)(3) for MRP1 was 0.32 microM, suggesting a remarkably high relat

133 lkyl side chains proved to be beneficial for MRP1 inhibition.

134 dentifying the regions of UL138 required for MRP1 downregulation and predicting genetic variants that

135 lation in macrophages, indicating a role for MRP1 in transporting DNICs out of cells.

136 at glutathione is an essential substrate for MRP1-mediated transport.

137 ed the genetic requirements within UL138 for MRP1 downregulation.

138 Furthermore, luciferase activity from MRP1 promoter/luciferase gene reporter constructs was si

139 eta-d-glucuronide into vesicles derived from MRP1 CK2alpha(-) cells was decreased compared with MRP1

140 gi sorting motif are required for functional MRP1 downregulation.

141 microM and a V(max) comparable to other good MRP1 substrates.

142 nce protein-1 (MRP1) expression, and greater MRP1-mediated efflux of NO2-OA-glutathione conjugates.

143 and SN-38 (BCRP) in A2780/ADR (P-gp), H69AR (MRP1), and MDCK II BCRP (BCRP) cells.

144 tidrug resistance protein-1 (MRP1), into HEK-MRP1 cells, which overexpress MRP1, and monitored the ca

145 Structural analysis of human MRP1-NBD1 revealed that the Walker A S685 forms a hydrog

146 ions were examined for their effect on human MRP1-mediated uptake of tritiated estradiol glucuronide

147 d was not observed in aortas of hypertensive MRP1-/- mice.

148 ted in increased doxorubicin accumulation in MRP1 cells, but not in MRP1 CK2alpha(-), MRP1-T249A, or

149 ed intracellular doxorubicin accumulation in MRP1 CK2alpha(-) and MRP1-T249A cells compared with MRP1

150 inhibitor that increased MX accumulation in MRP1-expressing MCF7 cells but had no effect on MRP-poor

151 on caused by hypertension was ameliorated in MRP1-/- mice.

152 dispensable for a UL138-mediated decrease in MRP1 protein levels, is necessary for a functional inhib

153 tein levels; however, differences existed in MRP1 localization and function.

154 ion (MRP1-T249E) led to dramatic increase in MRP1-dependent transport.

155 bicin accumulation in MRP1 cells, but not in MRP1 CK2alpha(-), MRP1-T249A, or MRP1-T249E cells, sugge

156 tiopronin led to a significant reduction in MRP1 protein.

157 ction in human NB cells results in increased MRP1 mRNA and protein levels, which in turn is accompani

158 ecular nanoswitch triggered by the increased MRP1 expression within the tumor tissue microenvironment

159 domain, have different abilities to inhibit MRP1 function.

160 the presence of glutathione, but uptake into MRP1-containing vesicles was entirely attributable to it

161 In contrast, Taxotere selectively killed MRP1-expressing leukemia cells, which did not undergo G2

162 In contrast, Raji cells had little MRP1 at the plasma membrane and did not export calcein u

163 wenty-eight SNPs in the ALOX5, LTA4H, LTC4S, MRP1, and cysLT1R genes, and an ALOX5 repeat polymorphis

164 the stably transduced MCF7 derivative, MCF7/MRP1-10, resulted in strong inhibition of LNO(2)-induced

165 xpression of drug transporter proteins MDR1, MRP1, and ABCG2.

166 the genetic requirements for UL138-mediated MRP1 downregulation and anticipates the possible evoluti

167 alpha in MCF7-derived cells expressing MRP1 [MRP1 CK2alpha(-)] resulted in increased doxorubicin sens

168 Mutant MRP1 lacking N-linked glycosylation [Asn19/23/1006Gln; s

169 nsport, whereas a phosphomimicking mutation (MRP1-T249E) led to dramatic increase in MRP1-dependent t

170 In addition, administration of a nonspecific MRP1 inhibitor (MK-571) reduced LTC(4) and subsequently

171 Reversan represents a new class of nontoxic MRP1 inhibitor, which may be clinically useful for the t

172 mmunohistochemical assessment (grade 0-3) of MRP1 and P-gp expression in the lung by using parametric

173 storage function of GST P1-1 and ability of MRP1 to efflux DNICs are vital in protection against NO

174 tional studies showed that in the absence of MRP1, PABA/NO activated the extracellular-regulated and

175 ally determine intracellular accumulation of MRP1 substrates using a p53-responsive reporter as an in

176 Expression and functional activity of MRP1 were determined using flow cytometry and SECM, and

177 required for proper folding and assembly of MRP1 into a fully transport competent native structure.

178 e tracer can allow noninvasive assessment of MRP1 activity in vivo.

179 Structural comparison of MRP1 and P-glycoprotein advances our understanding of th

180 a illustrates how different conformations of MRP1 are temporally linked and how substrate and ATP alt

181 sential for UL138-mediated downregulation of MRP1 steady-state levels and inhibition of MRP1 efflux a

182 complex role of CL5 for stable expression of MRP1 at the plasma membrane and more specifically show t

183 o TM10 are critical for stable expression of MRP1 at the plasma membrane.

184 However, expression of MRP1 in the stably transduced MCF7 derivative, MCF7/MRP1

185 he most effective at restoring expression of MRP1 mutants K513A, K516A, E521A, and E535A.

186 nt to Adriamycin due to either expression of MRP1 or lack of G2 checkpoints.

187 mational change in the COOH-proximal half of MRP1.

188 is necessary for a functional inhibition of MRP1 activity.

189 f MRP1 steady-state levels and inhibition of MRP1 efflux activity.

190 ed the effect of MSC EV on the inhibition of MRP1 in vitro and the antimicrobial effect in vivo.

191 is the efflux pump for LTC(4) Inhibition of MRP1 will increase LTB(4) production.

192 are responsible for altering the kinetics of MRP1-mediated As(GS)3 transport.

193 aster in patients (n = 6) with low levels of MRP1 expression (grade 0-1) and mean T1/2 of 105 minutes

194 ), compared with those with higher levels of MRP1 expression (grade 2-3, n = 7) and mean T1/2 of 149

195 Latency-associated loss of MRP1 and accumulation of the cytotoxic drug vincristine,

196 The UL138-mediated loss of MRP1 provides a marker for detecting latent HCMV infecti

197 To enable measurement of MRP1 function in the living brain, a series of 6-halopur

198 Herein, we report the measurement of MRP1 functional activity in individual cancer cells usin

199 u(521), and Glu(535) all cause misfolding of MRP1 and target the protein for proteasome-mediated degr

200 Overexpression of MRP1 conferred the most significant degree of resistance

201 ed the kinetics and cofactor requirements of MRP1-mediated transport of QO-SG and NQO.

202 xicity can be ascertained; thus, the role of MRP1 in MX resistance remains controversial.

203 upon macrophage activation, and the role of MRP1 in NO-induced (59)Fe release was demonstrated by Mr

204 Previously, the structures of MRP1 were determined in an inward-facing (IF) or outward

205 sefulness of SECM in quantitative studies of MRP1 inhibitors and suggests that monoclonal antibodies

206 , inhibitors, or transportable substrates of MRP1.

207 Treatment of MRP1-overexpressing cells with tiopronin led to a signif

208 understanding of efflux mechanisms based on MRP1.

209 Differences in their effects on MRP1 and P-gp activity were noted, and a second set of t

210 t cells, disulfiram reverses either MDR1- or MRP1-mediated efflux of fluorescent drug substrates.

211 but not in MRP1 CK2alpha(-), MRP1-T249A, or MRP1-T249E cells, suggesting that CK2alpha regulates MRP

212 for the treatment of neuroblastoma and other MRP1-overexpressing drug-refractory tumors by increasing

213 RP1), into HEK-MRP1 cells, which overexpress MRP1, and monitored the calcein efflux by MRP1.

214 or metabolites, because cells overexpressing MRP1 were less sensitive to the drug and had reduced lev

215 The present study, using paired parental, MRP1-poor, and transduced MRP1-overexpressing MCF7 cells

216 ysically, and recombinant CK2 phosphorylates MRP1-derived peptide in vitro in a Thr249-dependent mann

217 es as a prominent structural class of potent MRP1 inhibitors.

218 hese novel templates gave a number of potent MRP1 modulators with great selectivity against Pgp.

219 Mutation of 19 potential MRP1 phosphorylation sites revealed that HEK-Tyr920Phe/S

220 pports a model in which CK2alpha potentiates MRP1 function via direct phosphorylation of Thr249.

221 In this process, MRP1/MRP2 serves as a matchmaker by binding to guide RNA

222 The multidrug resistance protein MRP1 is an ATP-binding cassette (ABC) transporter that c

223 The multidrug resistance protein MRP1 is an ATP-driven pump that confers resistance to ch

224 the multidrug resistance-associated protein (MRP1) gene is strongly correlated with expression of the

225 the multidrug resistance-associated protein (MRP1, ABCC1) was identified in small cell lung cancer fo

226 sette protein, multidrug resistance protein (MRP1/ABCC1), transports conjugated organic anions (e.g.

227 ce protein, mitoxantrone-resistant protein), MRP1-mediated MX transport is dependent upon the presenc

228 The mitochondrial RNA binding proteins MRP1 and MRP2 form a heteromeric complex that functions

229 we showed that multidrug resistance proteins MRP1 and MRP3 attenuate cytotoxic and transactivating ac

230 p, multidrug resistance-associated proteins (MRP1-MRP6), or the breast cancer resistance protein (BCR

231 To quantify MRP1 structural dynamics, we engineered a "two-color MRP

232 The recombinant MRP1 protein expressed and trafficked normally to the pl

233 9E cells, suggesting that CK2alpha regulates MRP1 function via phosphorylation of Thr249.

234 lpha), the human homolog of Cka1p, regulates MRP1 by phosphorylation at the semiconserved site Thr249

235 The role of CK2 in regulating MRP1 was confirmed in other cancer cell lines where CK2

236 , while ATP hydrolysis per se does not reset MRP1 to the resting state.

237 Results MRP1 expression was seen in 12 of 13 patients, while P-g

238 rates in all cells and was unable to reverse MRP1-mediated MDR and had no effect on the parental cell

239 rrolopyrimidine (4) as a novel and selective MRP1 inhibitor.

240 eas individual HEK-Tyr920Phe- and -Ser921Ala-MRP1 mutants were similar to HEK-WT-MRP1.

241 sites revealed that HEK-Tyr920Phe/Ser921Ala-MRP1 transported As(GS)3 like HeLa-WT-MRP1, whereas indi

242 osylation [Asn19/23/1006Gln; sugar-free (SF)-MRP1] expressed in either HEK293 or HeLa cells had low K

243 e of phosphatase inhibitors, both WT- and SF-MRP1-enriched membrane vesicles had a high Km value for

244 ln-MRP1 were similar to those of HeLa/HEK-SF-MRP1 and HeLa-WT-MRP1, whereas those of single glycosyla

245 by forming a single bipartite binding site, MRP1 can recognize a spectrum of substrates with differe

246 clinical trials, the development of specific MRP1 inhibitors is still in its infancy.

247 As such, MRP1 is a multitasking transporter that likely influence

248 In summary, MSC EV suppressed MRP1 activity through transfer of miR-145, thereby resul

249 n 1 (MRP1), and found that MSC EV suppressed MRP1 mRNA, protein, and pump function in LPS-stimulated

250 sphorylation of Tyr920 and Ser921 can switch MRP1 to a lower-affinity, higher-capacity As(GS)3 transp

251 However, it is now clear that MRP1 serves a broader role than simply mediating the ATP

252 We conclude that MRP1 supports detoxification of NQO via efficient, gluta

253 MCF7 cells, unequivocally demonstrates that MRP1 confers resistance to MX cytotoxicity and that resi

254 c conditions, providing direct evidence that MRP1 is involved in GSH export.

255 lung cancer cell line, H69AR, we found that MRP1 transports arsenite (As(III)) only in the presence

256 th copies of wild-type MRP1, indicating that MRP1 plays a significant role in the drug resistance in

257 using inside-out membrane vesicles show that MRP1 supports ATP-dependent, osmotically sensitive uptak

258 Results show that MRP1 supports efficient transport of QO-SG with a K(m) o

259 The structures show that MRP1/MRP2 is a heterotetramer and, despite little sequen

260 These prior studies also showed that MRP1 and GSTP1 protect tumor cells against NO cytotoxici

261 The results suggest that MRP1-like the alternative MX transporters ABCG2 and ABCB

262 cogene in primary NB tumors, suggesting that MRP1 may be a target for MYCN-mediated gene regulation.

263 lease was demonstrated by Mrp1 siRNA and the MRP1 inhibitor, MK571, which inhibited NO-mediated iron

264 ust export of GSSG that was prevented by the MRP1 inhibitor MK571 and by MRP1 small interfering RNA.

265 Using membrane vesicles prepared from the MRP1-overexpressing lung cancer cell line, H69AR, we fou

266 e expression was less than expression of the MRP1 and 2 genes in HepG2 cells but similar to MRP3 gene

267 ANCE HCMV UL138 curtails the activity of the MRP1 drug transporter by reducing its steady-state level

268 Homozygous deletion of the MRP1 gene in primary murine neuroblastoma tumors resulte

269 dy QCRL-4, a selective blocking agent of the MRP1 pumps.

270 similar to or greater than expression of the MRP1, 2 and 3 genes in CWR22Rv1 and TSU-PR1 cells.

271 Selective inhibition of these MRP1 pumps inside live HeLa cells by MK571 produced a lo

272 This MRP1-associated reduced accumulation of MX was partially

273 Three (MRP1, MRP2, and MRP3) of the four members that have this

274 Thus, MRP1/MRP2 acts as an RNA matchmaker by stabilizing the R

275 tumors resulted in increased sensitivity to MRP1 substrate drugs (vincristine, etoposide, and doxoru

276 reen fluorescent protein (GFP) and TagRFP to MRP1 nucleotide-binding domains NBD1 and NBD2, respectiv

277 ubicin or paclitaxel); (3) siRNA targeted to MRP1 mRNA as a suppressor of pump drug resistance; (4) s

278 ucer, antisense oligonucleotides targeted to MRP1 mRNA as a suppressor of pump resistance and to BCL2

279 d remarkable affinity and selectivity toward MRP1.

280 g paired parental, MRP1-poor, and transduced MRP1-overexpressing MCF7 cells, unequivocally demonstrat

281 ase and the ATP-binding cassette transporter MRP1.

282 otency against P-gp and another transporter (MRP1), for their apparent permeability (Papp) and for th

283 ysiologically significant ABCC transporters (MRP1, SUR1, and CFTR), determined by using single-partic

284 ox double point mutations, while a truncated MRP1 promoter lacking all three E-boxes exhibited only b

285 h tumors containing both copies of wild-type MRP1, indicating that MRP1 plays a significant role in t

286 r LTC4 transport activity than the wild-type MRP1, indicating that the hydroxyl group at this positio

287 Furthermore, when MRP1 expression was decreased with RNA interference, GSH

288 cells adapt to the underlying surface, while MRP1 functional activity increases once the dimensions o

289 tly enhanced by coexpression of GSTP1-1 with MRP1.

290 2alpha(-) and MRP1-T249A cells compared with MRP1 cells.

291 K2alpha(-) cells was decreased compared with MRP1 vesicles.

292 From comparison with MRP1, a feature distinguishing CFTR from all other ABC t

293 e show that EGFR positively coordinates with MRP1 in T-DM1R-JIMT1 cells to contribute to cross-resist

294 e demonstrating significant correlation with MRP1 expression in the lungs.

295 for As(GS)3, similar to HeLa wild-type (WT) MRP1.

296 n/Tyr920Glu/Ser921Glu were similar to HEK-WT-MRP1, indicating that the phosphorylation-mimicking subs

297 er921Ala-MRP1 mutants were similar to HEK-WT-MRP1.

298 cosylation mutants were like those of HEK-WT-MRP1.

299 921Ala-MRP1 transported As(GS)3 like HeLa-WT-MRP1, whereas individual HEK-Tyr920Phe- and -Ser921Ala-M

300 lar to those of HeLa/HEK-SF-MRP1 and HeLa-WT-MRP1, whereas those of single glycosylation mutants were