ライフサイエンスコーパス: ABCG2

1 3.4% explained by two major loci (SLC2A9 and ABCG2).

2 ing cassette protein, subfamily G, member 2 (ABCG2).

3 inst breast cancer resistance protein (BCRP, ABCG2).

4 viously unrecognized conformational cycle of ABCG2.

5 oro led to high inhibitory activities toward ABCG2.

6 in CYP2B6, NR1I3, CYP2A6, ABCB1, ABCB5, and ABCG2.

7 gulation of the multidrug resistance protein ABCG2.

8 , and 4e, displayed limited interaction with ABCG2.

9 th that can be restored by the inhibition of ABCG2.

10 ic drug efflux both in vitro and in vivo via ABCG2.

11 us drug-selected cancer cells overexpressing ABCG2.

12 fluorescent substrates for ABCB1, ABCC1, and ABCG2.

13 of the key transporters playing this role is ABCG2.

14 tabilizing the inward facing conformation of ABCG2.

15 hormone prolactin (PRL) in the regulation of ABCG2.

16 etric cellular division in CSP cells lacking Abcg2.

17 efly luciferase, is a specific substrate for ABCG2.

18 ted that CGamF export was mainly mediated by ABCG2.

19 s of the common Q141K polymorphic isoform of ABCG2.

20 kynurenine pathway into milk is mediated by ABCG2.

21 t 33342 transport but were not substrates of ABCG2.

22 persistent need for studies of inhibitors of ABCG2.

23 of drug transporter proteins MDR1, MRP1, and ABCG2.

24 bitory potency as well as selectivity toward ABCG2.

25 elective, potent, and nontoxic inhibitors of ABCG2.

26 xcretion, which may be mediated by ABCB1 and ABCG2.

27 hate-binding cassette subfamily G, member 2 [ABCG2]).

28 and breast cancer resistance protein (Bcrp), Abcg2].

29 have been revealed by demonstrating that for ABCG2 a single amino acid is essential for engaging and

30 y binding to the proximal promoter region of ABCG2, a CSC marker.

31 s associated with lowered gene expression of ABCG2, ABCB1 and AKR1C1.

32 ABCG2, ABCB1, and possibly other transporters influence

33 given the pronounced species differences in ABCG2/ABCB1 expression ratios at the BBB.

34 ted in significant down-regulation of BMI-1, ABCG2, ABCG5, and MDR1 expression and in a concomitant i

35 -cadherin expression and increased levels of ABCG2, ABCG5, and MDR1.

36 Seed coats of abcg2 abcg6 abcg20 triple mutant plants had increased pe

37 ive suberin barrier in roots and seed coats (ABCG2, ABCG6, and ABCG20) and for synthesis of an intact

38 trast, these mice display a severe defect in ABCG2 abundance and function in the intestinal tract.

39 tle alterations of renal urate excretion and ABCG2 abundance.

40 apeutic-dose oral erlotinib to inhibit ABCB1/ABCG2 activity at the human BBB.

41 ey characteristics of stem-like tumor cells, ABCG2 activity did not affect radiation resistance or tu

42 These results demonstrate that enhanced ABCG2 activity renders TNBC cell resistance to ALA-PDT a

43 self-renewal was enriched in cells with high ABCG2 activity, and could be specifically inhibited by p

44 ntibody fragments or inhibitors, the resting ABCG2 adopts a closed conformation.

45 e consumption were replicated (in/near GCKR, ABCG2, AHR, POR and CYP1A1/2).

46 es potentially involved in pharmacokinetics (ABCG2, AHR, POR and CYP1A2) and pharmacodynamics (BDNF a

47 Breast cancer resistance protein (BCRP/ABCG2), an ATP-binding cassette (ABC) membrane-associate

48 e have investigated the interactions between ABCG2 and 56 naturally-occurring phytochemicals includin

49 ly because of combined partial saturation of ABCG2 and ABCB1 activity.

50 duce DNA damage responses, and to upregulate ABCG2 and ABCB1 expression, which therefore increased th

51 549) to understand the physiological role of ABCG2 and find that participants with the Q141K ABCG2 va

52 croenvironment in maintaining high levels of ABCG2 and GLI1.

53 ced chemotolerance suggesting that targeting ABCG2 and Hh signaling may have therapeutic value in ove

54 flammation" schizophrenia subgroup had lower ABCG2 and higher ICAM1, VE-cadherin, occludin and interf

55 t clinical use of mithramycin for repressing ABCG2 and inhibiting stem cell signaling in thoracic mal

56 Variants in ABCG2 and LPA were associated with change in statin-indu

57 hange in Lp-PLA(2) activity were observed in ABCG2 and LPA, likely because of their impact on statin-

58 rogen strongly altered the high affinity for ABCG2 and the complete inhibition of mitoxantrone efflux

59 ling both drug efflux and ATPase activity of ABCG2 and to elucidate their molecular mechanism of inte

60 Variants at 2p24 (in GCKR), 4q22 (in ABCG2) and 7q11.23 (near POR) that were previously assoc

61 resistance protein (humans, ABCG2; rodents, Abcg2) and P-glycoprotein (humans, ABCB1; rodents, Abcb1

62 to the brain was restricted by Abcb1a/b and Abcg2, and CLuptake into the brain was only significantl

63 n the ABCG2 promoter, markedly downregulated ABCG2, and inhibited proliferation and tumorigenicity of

64 d more keratin 14, N-Cadherin, DeltaNp63 and ABCG2, and less keratin 12, consistent with their less d

65 and MRP1, appeared not to be transported by ABCG2, and was at least as active on various drug-select

66 The more pronounced role that ABCG2 appears to play at the human blood-brain barrier a

67 ABCB1) and breast cancer resistance protein (ABCG2) are 2 efflux transporters at the blood-brain barr

68 and breast cancer resistance protein (BCRP, ABCG2) are the three major ABC transport proteins confer

69 umor stem cells are separable, and highlight ABCG2 as a potential driver of glioma stemness.

70 ated ABCB1 ATPase activities while inhibited ABCG2 ATPase activities.

71 Furthermore, the E2F1-ABCG2 axis suppresses chemotherapy-induced cell death th

72 Compound 1p stimulated the ABCG2 basal ATPase activity by contrast to a chromone le

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

74 membrane transporter proteins ABCB1 (P-gp), ABCG2 (BCRP), and ABCC1 (MRP1), which are involved in th

75 report that the major multidrug transporter ABCG2 (BCRP/MXR) is directly and specifically activated

76 The breast cancer resistance protein (BCRP, ABCG2) belongs to the superfamily of ATP binding-cassett

77 THZ1-resistant cells upregulated ABCG2 but remained sensitive to ICEC0942.

78 inhibit the breast cancer resistance protein ABCG2 but with totally different structure-activity rela

79 nhibitors, we found that xanthines decreased ABCG2 by inducing its rapid internalization and lysosome

80 ays significantly decreased the induction of ABCG2 by PRL without altering STAT5 recruitment to the G

81 tion-5 (STAT5) also blunted the induction of ABCG2 by PRL, suggesting a role for the JAK2/STAT5 pathw

82 ired but not sufficient for the induction of ABCG2 by PRL.

83 om last dose, SLCO1B1 c.521T>C (P<0.001) and ABCG2 c.421C>A (P<0.01) were important to rosuvastatin c

84 Here, we show that ABCG2 can actively drive expression of stem cell markers

85 substrate and inhibitor (ligands) binding to ABCG2 can be differentiated quantitatively by the number

86 To overcome this mechanism, inhibitors of ABCG2 can be used.

87 the exciting possibility that by inhibiting ABCG2, cancer stem cells and other cancers may be target

88 nked to the drug transporter genes ABCC2 and ABCG2 caused chemo-resistance.

89 Upregulation of ABCG2 coincided with increased occupancy of aryl hydroca

90 and breast cancer resistance protein (i.e., ABCG2) consistently being shown to be key effectors of M

91 ed stem/progenitor cell marker (p63alpha and ABCG2) content and clonogenic capacity in the explants b

92 Similar results were seen in ABCG2(+) CSCs versus ABCG2(-) non-CSCs from primary huma

93 We generated a new Abcg2-driven lineage-tracing mouse model with efficient

94 Finally, functional inhibition of ABCG2 drug efflux activity with fumitremorgin C or inhib

95 ane of CD44, the EGF receptor, the ABCB1 and ABCG2 drug transporters, and the MCT4 monocarboxylate tr

96 ance (MDR) mediated by the ABCB1, ABCC1, and ABCG2 drug-efflux transporters.

97 ABCG2 effects were Notch-independent and mediated by div

98 truded from the brain and spinal cord by the Abcg2 efflux transporter.

99 ABCB1) and breast cancer resistance protein (ABCG2) efflux transporters.

100 ed that HNF4A transactivated the promoter of ABCG2, encoding a major urate transporter, in kidney cel

101 ells), coexpression of rat Oatp1a1 and human ABCG2 enhanced the uptake and efflux, respectively, of C

102 lular clofarabine metabolites suggested that ABCG2 exported clofarabine more readily than clofarabine

103 Thus, the ABCG2 expressing side population demonstrates multipoten

104 candidate for in vivo chemosensitization of ABCG2-expressing tumors.

105 , particularly in those lines with low basal ABCG2 expression (p<0.01).

106 Thus, the down-regulation of ABCG2 expression and/or function has been proposed as pa

107 At 24 degrees C, reduced ABCG2 expression coincided with increased mitochondrial

108 High ABCG2 expression has also been found in a variety of sol

109 ficant correlation between elevated E2F1 and ABCG2 expression in human lung cancers.

110 Since data on ABCG2 expression in liver malignances are scanty, here w

111 E2F1 regulates ABCG2 expression in multiple cell systems, and, importan

112 PRL dose-dependently induced ABCG2 expression in T-47D human breast cancer cells.

113 Compared to non-stored cells, ABCG2 expression increased between temperatures 8-16 deg

114 Furthermore, ABCG2 expression is a characteristic feature of cancer s

115 SN22 inhibited NB cell growth regardless of ABCG2 expression levels.

116 important role in MDR, where their inherent ABCG2 expression may allow them to survive chemotherapy

117 hat activates the apoptotic pathway, reduced ABCG2 expression to increase intracellular irinotecan le

118 ABCG2 expression was found to be highest in the most und

119 ABCG2 expression was sensitive to antineoplastic drugs s

120 related with ICEC0942 and THZ1 response, and ABCG2 expression with THZ2 response, in a panel of cance

121 le for the JAK2/STAT5 pathway in PRL-induced ABCG2 expression.

122 ancer drug-resistant cell subline) levels of ABCG2 expression.

123 and ABCC1 yielded a high selectivity toward ABCG2 for the quinazoline compounds.

124 We hypothesized that ABCG2 function at the BBB could be evaluated by using bi

125 This method for imaging ABCG2 function at the BBB will facilitate understanding

126 lities, no specific probe exists for imaging ABCG2 function in vivo.

127 Our results suggest a correlation of ABCG2 gene expression and differentiation stage both in

128 derived from human hepatocellular carcinoma, ABCG2 gene expression was assessed by reverse transcript

129 ABCG2 gene expression was higher in HCC than both cirrho

130 ivity of a luciferase reporter driven by the ABCG2 gene promoter and 5'-flanking region containing th

131 ome proliferator response element within the ABCG2 gene promoter.

132 The pathophysiological nature of the common ABCG2 gout and hyperuricemia associated variant Q141K (r

133 ctural insights, no anticancer drug bound to ABCG2 has been resolved, and the mechanisms of multidrug

134 inding cassette, subfamily G, member 2 gene (ABCG2) has been shown to be associated with serum uric a

135 e key properties of ligands interacting with ABCG2 have been disovered.

136 d ATP-binding cassette-sub-family G-member2 (ABCG2) have important roles in neuroplasticity.

137 sidue(s) had extraordinary potencies against ABCG2 (IC(50) < 150 nM).

138 are scanty, here we report the expression of ABCG2 in adult human hepatocellular carcinoma (HCC) in b

139 rs resulted in significant up-regulations of ABCG2 in all cell lines, particularly in those lines wit

140 understanding of the transporters URAT1 and ABCG2 in particular would appear to provide opportunitie

141 er, these data suggest an important role for Abcg2 in positively regulating skeletal muscle regenerat

142 e present single-particle cryo-EM studies of ABCG2 in the apo state, and bound to the three structura

143 or the subcellular distribution of ABCB1 and ABCG2 in the cells exposed to 3 muM of bafetinib.

144 Q141K variant, support an important role for ABCG2 in urate excretion in both the human kidney and in

145 lements and/or Sp1 sites markedly attenuated ABCG2 induction.

146 -binding cassette G-subfamily transporter 2 (Abcg2) influences the proliferation of cardiac side popu

147 scaffold, contributed to both the potency of ABCG2 inhibition and the cytotoxicity.

148 clinical applicability for continuous ABCB1/ABCG2 inhibition at the BBB may be limited by safety con

149 lastoma tumorspheres in vitro, we found that Abcg2 inhibition could potentiate responses to the clini

150 We successfully implemented ABCB1/ABCG2 inhibition protocols in nonhuman primates resultin

151 studies in vivo in this model confirmed that Abcg2 inhibition was sufficient to enhance antiprolifera

152 lly inhibited by pharmacological and genetic ABCG2 inhibition.

153 mg/kg) or after pretreatment with the ABCB1/ABCG2 inhibitor elacridar (10 mg/kg).

154 to investigate the effects of the ABCB1 and ABCG2 inhibitor elacridar on brain uptake using (11)C-er

155 affold, potent CK2 inhibitors into selective ABCG2 inhibitors and vice versa.

156 tment of brain tumors, but no marketed ABCB1/ABCG2 inhibitors are currently available.

157 Only a few potent and selective ABCG2 inhibitors have been discovered, i.e., fumitremorg

158 it as one of the ten best triple ABCC1/ABCB1/ABCG2 inhibitors in the literature.

159 mice increased with coadministration of the ABCG2 inhibitors Ko143, gefitinib, and nilotinib, but no

160 assessed the efficacy of two different ABCB1/ABCG2 inhibitors to enhance brain distribution of (11)C-

161 Potent ABCG2 inhibitors were recently identified as asymmetric

162 Potent and selective ABCG2 inhibitors with low cytotoxicity were investigated

163 The best ABCG2 inhibitors, such as 4c, 4h, 4i, 4j, and 4k, behave

164 In addition, some of the best ABCG2 inhibitors, which displayed a very low cytotoxicit

165 ther were also identified as novel flavonoid ABCG2 inhibitors.

166 imidines were revealed as triple ABCB1/ABCC1/ABCG2 inhibitors.

167 The inhibition of ABCB1 and ABCG2 is a promising approach to enhance brain distribut

168 In conclusion, ABCG2 is able to transport bile acids.

169 ABCG2 is an ABC transporter that extrudes a variety of c

170 ABCG2 is an ATP-binding-cassette (ABC) transporter that

171 Physiologically, ABCG2 is highly expressed in areas such as the blood-bra

172 ABCG2 is involved in epithelial transport/barrier functi

173 ATP-binding cassette sub-family G member 2 (ABCG2) is a homodimeric ATP-binding cassette (ABC) trans

174 ng cassette, subfamily G, isoform 2 protein (ABCG2) is an important member of the ABC transporter sup

175 ATP-binding cassette transporter G2 (ABCG2) is involved in the secretion of several compounds

176 The Breast Cancer Resistance Protein (BCRP/ABCG2) is one member of ABC transporters proteins super

177 ansporter, breast cancer resistance protein, ABCG2, is up-regulated in certain chemoresistant cancer

178 )C-erlotinib was 2.6-fold higher in Abcb1a/b;Abcg2 knockout mice than in WT mice, measured as percent

179 Wild-type and Abcb1a/b or Abcg2 knockout mice underwent (11)C-erlotinib PET/MR sca

180 using CSP cells isolated from wild-type and Abcg2 knockout mice, we found that Abcg2 regulates G1-S

181 stered orally to wild-type (WT) and Abcb1a/b;Abcg2 knockout mice.

182 pe mice, obstructive cholestasis in pregnant Abcg2(-/-) knockout mice induced similar bile acid accum

183 The absence of Abcb1a/b and Abcg2 led to a 2.6-fold decrease in CLbile (wild-type mi

184 Key molecular features of diverse ABCG2 ligands using the pai-pai clamp along with structu

185 Transporters such as ABCB1 and ABCG2 limit the exposure of several anticancer drugs to

186 No variants in the 3 genes (ABCG2, LPA, and APOE) that previously showed genome-wide

187 reduction on rosuvastatin were identified at ABCG2, LPA, and APOE, and a further association at PCSK9

188 teractions necessary for the dimerization of ABCG2: Lys-473 (K473) and Phe-142 (F142).

189 nd the lower potency of elacridar to inhibit ABCG2 may be an explanation of these interspecies differ

190 Pharmacologic inhibition of ABCB1/ABCG2 may improve the efficacy of dual-substrate drugs f

191 Thus, ABCG2 may play a key role in bile acid transport in plac

192 ABCG2-mediated bile acid transport was inhibited by estr

193 , this work expands the current knowledge on ABCG2-mediated CS and provides a potential strategy for

194 e, nontoxic, and nontransported inhibitor of ABCG2-mediated drug efflux.

195 Pharmacologic strategies to inhibit ABCB1/ABCG2-mediated efflux transport at the BBB have been suc

196 The compounds competitively inhibited ABCG2-mediated Hoechst 33342 transport but were not subs

197 indicated that bafetinib reversed ABCB1- and ABCG2-mediated MDR by blocking the drug efflux function

198 o have inhibitory effects on both ABCB1- and ABCG2-mediated MDR in this in-vitro investigation.

199 h for highly effective modulators addressing ABCG2-mediated MDR, 23 pyrimidines were synthesized and

200 e, compound 37, reversed ABCB1-, ABCC1-, and ABCG2-mediated MDR, making it one of the three most pote

201 cein AM, and noncompetitive inhibitor of the ABCG2-mediated pheophorbide A transport.

202 Furthermore, they are able to reverse the ABCG2-mediated resistance toward SN-38 and inhibit the A

203 wild-type levels, yielding a restoration of ABCG2-mediated specific drug efflux activity.

204 acid demonstrated significant inhibition of ABCG2-mediated transport.

205 brain to levels comparable to Abcb1a/b((-/-))Abcg2((-/-)) mice (0.090 +/- 0.007 mL/min/g of tissue, P

206 +/- 0.005 mL/min/g of tissue; Abcb1a/b((-/-))Abcg2((-/-)) mice, 0.0095 +/- 0.001 mL/min/g of tissue;

207 +/- 0.004 mL/min/g of tissue; Abcb1a/b((-/-))Abcg2((-/-)) mice, 0.079 +/- 0.013 mL/min/g of tissue; P

208 ometry in milk and plasma from wild-type and Abcg2(-/-) mice as well as dairy cows carrying the ABCG2

209 c acid were higher in wild-type mice than in Abcg2(-/-) mice.

210 des a framework for further investigation of ABCG2-modulated phytochemical bioavailability, MDR, and

211 Abcg2 modulates CSP cell cycle progression and asymmetri

212 ter explants decreased (P < 0.001) ABCB1 and ABCG2 mRNA and protein levels.

213 KT, PPARgamma), and drug efflux transporter (ABCG2, MRP3, MRP4) genes.

214 Here we explore the Q141K ABCG2 mutation using a comparative approach, contrasting

215 ar results were seen in ABCG2(+) CSCs versus ABCG2(-) non-CSCs from primary human T-cell lymphoma.

216 l isolated cells expressed stem cell markers ABCG2, Notch1, OCT-3/4, AnkG, and MUC1 but not TM marker

217 ed expression of SC-renewal genes, including ABCG2, OCT-4, and WNT-3, also occurred in NSCs during on

218 to that of Ko143, and they are selective for ABCG2 over ABCB1.

219 st derivative, namely, 1p, was selective for ABCG2 over P-glycoprotein and MRP1, appeared not to be t

220 entages of drug-resistant ALDH+ cells, MDR-1/ABCG2 overexpressing cells, and cancer stem-like cells.

221 lls; mitoxantrone and [(3)H]-mitoxantrone in ABCG2 overexpressing cells, respectively.

222 Bafetinib significantly sensitized ABCB1 and ABCG2 overexpressing MDR cells to their anticancer subst

223 idine could also sensitize ABCB1- as well as ABCG2-overexpressing cells toward daunorubicin and SN-38

224 Similarly, in ABCG2-overexpressing cells, sildenafil inhibited resista

225 ATP-binding cassette subfamily G member 2 (ABCG2), p63, and hairy enhancer of split 1 (Hes1) were c

226 ABCG2, p63, and Hes1 immunostaining were significantly d

227 Similarly, the expression levels of ABCG2, p63, K15, Hes1, and N-cadherin transcripts were a

228 ) maintained their characteristic phenotype (ABCG2, Pax6, CD90, p63-alpha, CD45, CD73, CD105, Vimenti

229 sed the stem cell markers nestin, Musashi 1, ABCG2, Pax6, Chx 10, DeltaN p63, and Sox 2.

230 genetic associations were also observed for ABCG2, PKD2, the dentin/bone SCPP sub-family, EDNRA, TJF

231 BCC1), and breast cancer resistance protein (ABCG2) play an important role in anticancer drug resista

232 ABCG2 plays a major role in anticancer-drug efflux and r

233 Breast cancer resistance protein (BCRP/ABCG2) plays an important role in determining the absorp

234 drocarbon receptor, Sp1, and Nrf2 within the ABCG2 promoter, and deletion of xenobiotic response elem

235 ases in AhR, Sp1, and Nrf2 levels within the ABCG2 promoter, markedly downregulated ABCG2, and inhibi

236 sistance protein (BCRP, official gene symbol ABCG2) protect the conceptus from exposure to toxins and

237 ne, and dyphylline can dramatically decrease ABCG2 protein in cells that have either moderate (BeWo,

238 In the mouse model, Abcg2 protein was expressed at the plasma membrane where

239 bitory activity of dietary phytochemicals on ABCG2 provides a framework for further investigation of

240 Mechanistic investigations revealed that the ABCG2 Q141K variant was fully processed but retained in

241 -type and Abcg2 knockout mice, we found that Abcg2 regulates G1-S cell cycle transition by fluorescen

242 hment of limbal stem cell (DeltaNp63alpha(+)/ABCG2(+)) reserve.

243 rs breast cancer resistance protein (humans, ABCG2; rodents, Abcg2) and P-glycoprotein (humans, ABCB1

244 associated loci (except ALDH16A1), including ABCG2, SLC2A9, GCKR, ALDH2 and CNIH2, were replicated.

245 of SU conditional on significant SLC2A9 and ABCG2 SNPs revealed new loci, nucleobindin 1 (NUCB1) and

246 y be used to enhance brain delivery of ABCB1/ABCG2 substrate anticancer drugs, but its clinical appli

247 ng cells, sildenafil inhibited resistance to ABCG2 substrate anticancer drugs, for example, increasin

248 ly restrict brain distribution of dual ABCB1/ABCG2 substrate drugs, such as tyrosine kinase inhibitor

249 ly increased the retention of an established ABCG2 substrate in MCF-7/MX100 cells but not in parental

250 ct on the transport of mitoxantrone, a known ABCG2 substrate.

251 ve the efficacy of anticancer drugs that are ABCG2 substrates.

252 Inhibitors of ABCG2, such as tyrosine kinase inhibitors, phosphodieste

253 s one of the most frequent variants in human ABCG2, the polymorphism Q141K impairs expression, locali

254 r for breast cancer resistance protein (BCRP/ABCG2), there is a persistent need for studies of inhibi

255 ABCB1) and breast cancer resistance protein (ABCG2), thereby limiting its utility in the treatment of

256 st 33342 as fluorescent dye and substrate of ABCG2 to elucidate the compounds binding modes.

257 The ability of ABCG2 to export these bile acids was confirmed by microi

258 The rapid up-regulation of ABCG2 to exposure to doxorubicin emphasizes the importan

259 ) element at -434 base pairs upstream of the ABCG2 transcription start site.

260 ability to inhibit mitoxantrone efflux from ABCG2-transfected HEK293 cells.

261 y multidrug-resistant cells that express the ABCG2 transporter (also called breast cancer resistance

262 preclinical proof of concept for blockade of ABCG2 transporter activity as a strategy to empower chem

263 )/CD24(low), and increased expression of the ABCG2 transporter and increased aldehyde dehydrogenase (

264 Treatment of TNBC cells with ABCG2 transporter inhibitor Ko143 significantly increase

265 BC cell resistance to ALA-PDT and inhibiting ABCG2 transporter is a promising approach for targeting

266 e kinetics at the single-cell level, such as ABCG2 transporter-mediated efflux and DNA binding, are r

267 sport of E(2)17betaG and methotrexate by the ABCG2 transporter.

268 r mRNA expression and functional activity of ABCG2 transporter; and have a higher proliferation index

269 tidrug ATP-binding cassette, subfamily G, 2 (ABCG2) transporter was recently identified as an importa

270 chanisms, including ATP-binding cassette G2 (ABCG2) transporter-mediated irinotecan efflux from cells

271 (MCF-7/FLV1), exploits the overexpression of ABCG2 transporters and induces caspase-dependent apoptot

272 on specific stimulation of ATP hydrolysis by ABCG2 transporters with subtoxic doses of curcumin combi

273 oth pathways inhibits the efflux activity of ABCG2 transporters, leads to depletion of intracellular

274 stant cells selectively over cells that lack ABCG2 transporters.

275 cytoplasmic structures bearing ATP-dependent ABCG2 transporters.

276 The breast cancer resistance protein (ABCG2) transports chemotherapeutic drugs out of cells, w

277 ding cassette (ABC) transport proteins, like ABCG2, triggering active efflux of various structurally

278 nce to ICEC0942 and THZ1, and confirmed that ABCG2 upregulation is a mechanism of resistance to THZ1.

279 le role of sex hormones in the regulation of ABCG2 urate transporter and its potential implications f

280 x capability mediated by the ABC transporter ABCG2 using the side population assay, and their charact

281 ating a mouse model of the orthologous Q140K Abcg2 variant and find male mice have significant hyperu

282 G2 and find that participants with the Q141K ABCG2 variant display elevated serum urate, unaltered FE

283 e chromone derivative specifically inhibited ABCG2 versus other multidrug ABC transporters and was no

284 ABCG2 was also found to confer high levels of resistance

285 among this class of drug transporters, only ABCG2 was expressed at highly increased levels in human

286 Interaction of the compounds with ABCG2 was investigated by a colorimetric ATPase assay.

287 No induction of ABCG2 was observed.

288 the breast cancer resistance protein (BCRP, ABCG2) was confirmed by TaqMan real-time RT-PCR assay.

289 ABC transporter G2 (ABCG2) was expressed in recombinants from side populatio

290 the breast cancer resistance protein (BCRP; ABCG2) was tested using uptake assays in cells overexpre

291 An efflux transporter, ABCG2, was lower, while mRNAs encoding VE-cadherin and I

292 CB1, ABCB11, ABCC2, ABCC3, ABCC4, ABCC6, and ABCG2 We showed that IS increases the expression and act

293 gnificantly increased when both Abcb1a/b and Abcg2 were absent (wild-type mice, 0.017 +/- 0.004 mL/mi

294 When Abcb1 and Abcg2 were disrupted in mice, brain uptake of (11)C-erlo

295 alues below 0.5 muM and high selectivity for ABCG2 were identified.

296 ons between tryptophan-related compounds and ABCG2 were investigated.

297 of the chemotherapy drug efflux transporter ABCG2, which contributes to normal tissue protection.

298 ) led to upregulation of the xenobiotic pump ABCG2, which is expressed in cancer stem cells and confe

299 In rat placenta, the expression of Abcg2, which was much higher than that of Bsep, was not

300 -/-) mice as well as dairy cows carrying the ABCG2 Y581S polymorphism (Y/S) and noncarrier animals (Y