ライフサイエンスコーパス: ABCG2

1 marker (CXCR4) and a drug resistance marker (ABCG2).

2 ransporter breast cancer resistance protein (ABCG2).

3 ) and breast cancer resistance protein (BCRP/ABCG2).

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

5 3.4% explained by two major loci (SLC2A9 and ABCG2).

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

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

8 us drug-selected cancer cells overexpressing ABCG2.

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

10 fluorescent substrates for ABCB1, ABCC1, and ABCG2.

11 of the key transporters playing this role is ABCG2.

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

13 etric cellular division in CSP cells lacking Abcg2.

14 bitory potency as well as selectivity toward ABCG2.

15 efly luciferase, is a specific substrate for ABCG2.

16 ted that CGamF export was mainly mediated by ABCG2.

17 s of the common Q141K polymorphic isoform of ABCG2.

18 persistent need for studies of inhibitors of ABCG2.

19 ivatives are exported by the ABC transporter ABCG2.

20 elective, potent, and nontoxic inhibitors of ABCG2.

21 strongly expressed the stem cell-associated ABCG2.

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

23 oro led to high inhibitory activities toward ABCG2.

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

25 gulation of the multidrug resistance protein ABCG2.

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

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

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

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

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

31 ABCG2, ABCB1, and possibly other transporters influence

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

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

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

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

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

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

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

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

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

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

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

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

44 , in DLBCL tumor samples, significantly high ABCG2 and GLI1 levels were found in DLBCL tumors with ly

45 croenvironment in maintaining high levels of ABCG2 and GLI1.

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

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

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

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

50 le side population (SP) cells, which express Abcg2 and may participate in muscle regeneration or may

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

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

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

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

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

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

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

58 mation, and increased expression of CD44 and ABCG2, and PHA665752 treatment suppressed tumor sphere f

59 or the stem cells markers, nestin, vimentin, ABCG2, and Sca-1.

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

61 th serum uric acid concentrations, GLUT9 and ABCG2 appeared to be important modulators of uric acid l

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

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

64 ABCC4) and breast cancer resistance protein (ABCG2), are important for protecting the brain from circ

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

66 resulted in increased expression of BCL2 and ABCG2 associated with increased chemotolerance.

67 ated ABCB1 ATPase activities while inhibited ABCG2 ATPase activities.

68 (IAAP), whereas it only slightly stimulated ABCG2 ATPase activity and inhibited photolabeling of ABC

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

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

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

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

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

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

75 y decreases the efflux activity of ABCB1 and ABCG2, but has no significant effects on ABCC1.

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

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

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

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

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

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

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

83 Functional determination that GLUT9 and ABCG2 can transport urate at the apical border of proxim

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

85 In addition to ABCG2, co-culture of DLBCL cells with HS-5 cells also re

86 Upregulation of ABCG2 coincided with increased occupancy of aryl hydroca

87 human breast cancer resistance protein (BCRP/ABCG2) confers multidrug resistance and mediates the act

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

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

90 xpression levels of the putative LSC markers ABCG2, DeltaNp63alpha, and cytokeratin (K)14 were signif

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

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

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

94 ABCG2 effects were Notch-independent and mediated by div

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

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

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

98 The use of an ABCG2 inhibitor confirmed that ABCG2 export of clofarabine is maximal when dCK levels a

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

100 Thus, the ABCG2 expressing side population demonstrates multipoten

101 tracing, we demonstrate that the progeny of Abcg2-expressing cells contributed to multiple cell type

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

103 In contrast, 2',5'-DHC treatment of ABCG2-expressing yeast increased extracellular GSH level

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

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

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

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

108 ignaling pathway as a key factor behind high ABCG2 expression in DLBCL through direct upregulation of

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

116 duced lung tumorigenesis, KLF5 regulation of ABCG2 expression may be important for chemotherapeutic r

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

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

122 h a role for the extended TXXXGXXXG motif in ABCG2 folding, processing, and/or dimerization.

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 sion in DLBCL through direct upregulation of ABCG2 gene transcription.

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

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

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

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

137 iphosphate-binding cassette drug transporter ABCG2 in DLBCL correlated inversely with disease- and fa

138 and we show substantial variation in dCK and ABCG2 in myeloid leukemia, we hypothesized that the acti

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

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

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

142 We show that cells expressing Abcg2 increased upon injury and that muscle regeneration

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

144 We show that ABCG2 influence on clofarabine cytotoxicity was markedly

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

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

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

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

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

150 lly inhibited by pharmacological and genetic ABCG2 inhibition.

151 The use of an ABCG2 inhibitor confirmed that ABCG2 export of clofarabi

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

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

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

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

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

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

158 Potent ABCG2 inhibitors were recently identified as asymmetric

159 Potent and selective ABCG2 inhibitors with low cytotoxicity were investigated

160 Therefore, we propose that addition of ABCG2 inhibitors would effectively increase the antitumo

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

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

163 ther were also identified as novel flavonoid ABCG2 inhibitors.

164 Our data indicate that ABCG2 is a novel GSH transporter.

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

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

167 ABCG2 is an ATP-binding cassette half-transporter import

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

169 plasmic domains of the nonsterol transporter ABCG2 is both targeted to endosomes and functional, and

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

171 ABCG2 is involved in epithelial transport/barrier functi

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

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

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

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

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

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

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

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

180 Furthermore, Abcg2-labeled cells increased significantly upon injury

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

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

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

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

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

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

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

188 ABCG2-mediated bile acid transport was inhibited by estr

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

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

191 Conversely, dCK overexpression blunted ABCG2-mediated efflux of clofarabine by increasing the f

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

193 ytotoxicity was strongly reduced by enhanced ABCG2-mediated efflux.

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

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

196 esized that the activity of dCK may modulate ABCG2-mediated resistance to clofarabine by regulating t

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

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

199 acid demonstrated significant inhibition of ABCG2-mediated transport.

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

201 +/- 0.005 mL/min/g of tissue; Abcb1a/b((-/-))Abcg2((-/-)) mice, 0.0095 +/- 0.001 mL/min/g of tissue;

202 +/- 0.004 mL/min/g of tissue; Abcb1a/b((-/-))Abcg2((-/-)) mice, 0.079 +/- 0.013 mL/min/g of tissue; P

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

204 Abcg2 modulates CSP cell cycle progression and asymmetri

205 e elements leads to a major increase in both ABCG2 mRNA and protein expression.

206 LBCL cells with HS-5 stromal cells increased ABCG2 mRNA and protein levels by paracrine activation of

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

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

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

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

211 and that muscle regeneration was impaired in Abcg2-null mice, resulting in fewer centrally nucleated

212 In Abcg2-null mice, the SP fraction is lost in skeletal mus

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

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

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

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

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

218 lter the sensitivity of parental, ABCB1-, or ABCG2-overexpressing cells to non-ABCB1 and non-ABCG2 su

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

220 irmed by HPLC analysis of drug exported from ABCG2-overexpressing cells.

221 ppression of ABCG2 with short hairpin RNA or ABCG2 overexpression in human epithelial cells decreased

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

223 ABCG2, p63, and Hes1 immunostaining were significantly d

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

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

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

227 Homology modeling of ABCG2 places the TXXXGXXXG motif at the dimer interface.

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

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

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

231 That ABCG2 primarily effluxes clofarabine, but not chlorfarab

232 After injury, Abcg2 progeny made a minor contribution to regenerated m

233 ng site for GLI transcription factors in the ABCG2 promoter and established its functionality using l

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 In addition to expressing stem cell genes ABCG2, Six2, Notch1, and Pax6, SSPCs were able to differ

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

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

247 G2-overexpressing cells to non-ABCB1 and non-ABCG2 substrate drugs, nor did sildenafil affect the fun

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

249 L/G406L/G410L mutant when incubated with the ABCG2 substrate MX showed a shift on immunoblot analysis

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 e ABC transporters such as ABCB1, ABCC1, and ABCG2 that modulate intracompartmental and intracellular

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

272 -induced export of S1P mediated by ABCC1 and ABCG2 transporters and consequent activation of S1P rece

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

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

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

276 stant cells selectively over cells that lack ABCG2 transporters.

277 cytoplasmic structures bearing ATP-dependent ABCG2 transporters.

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

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

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

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

282 Because the level and function of dCK and ABCG2 vary substantially among other types of cancer, th

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

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

285 y lower expression of ABCB1 but not ABCC4 or ABCG2 was found following exposure to Abeta(1-42) peptid

286 ABCG2 was identified as the only gene in the array that

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

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

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

293 me-wide scans found that genetic variants of ABCG2 were associated with higher SUA concentrations and

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

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

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

299 Pase activity and inhibited photolabeling of ABCG2 with [(125)I]-IAAP.

300 In addition, suppression of ABCG2 with short hairpin RNA or ABCG2 overexpression in

301 hibits the transporter function of ABCB1 and ABCG2, with a stronger effect on ABCB1.