Post-Transcriptional Regulation of Breast Cancer Resistance Protein after Intestinal Ischemia-Reperfusion

Ogura, Jiro; Kobayashi, Masaki; Itagaki, Shirou; Hirano, Takeshi; Iseki, Ken

doi:10.1248/bpb.31.1032

Cited by 7 publications

(5 citation statements)

References 23 publications

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“…A possible explanation for this discrepancy is that ABCG2 is post- transcriptionally and/or -translationally regulated in GBM cells such that RNA and protein levels do not correlate. Previous studies have reported that ABCG2 is post-transcriptionally regulated [26, 27]. In addition, others have reported that ABCG2 activity was predicted by its protein abundance and not by its mRNA expression [28].…”

Section: Discussionmentioning

confidence: 99%

Expression and function of ABCG2 and XIAP in glioblastomas

et al. 2017

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Despite multimodal treatment that includes surgery, radiation and chemotherapy, virtually all glioblastomas (GBM) recur, indicating that these interventions are insufficient to eradicate all malignant cells. To identify potential new therapeutic targets in GBMs, we examined the expression and function of proteins that are associated with therapy resistance and cancer cell survival. We measured the expression of eight such proteins in 50 GBM samples by immunohistochemistry and analyzed patient survival. We report that GBM patients with high expression of ABCG2 (also called BCRP) or XIAP at the protein level had worse survival than those with low expression. The adjusted hazard ratio for ABCG2 was 2.35 and for XIAP was 2.65. Since glioma stem cells (GSCs) have been shown to be more resistant than bulk tumor cells to anti-cancer therapies and to express high levels of these proteins, we also sought to determine if ABCG2 and XIAP have functional roles in GSCs. We used small molecule inhibitors to treat patient-derived GBM tumorspheres in vitro and observed that inhibitors of ABCG2, Ko143 and fumitremorgin, significantly reduced self-renewal. These results suggest that ABCG2 and XIAP proteins may be useful indicators of patient survival and that inhibition of ABCG2 may be a promising therapeutic target in GBMs.

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Section: Discussionmentioning

confidence: 99%

Expression and function of ABCG2 and XIAP in glioblastomas

et al. 2017

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“…We previously reported that Bcrp expression level in the apical membrane in the ileum after intestinal I/R was significantly decreased (25). These findings suggest that the decrease in BCRP expression at the apical membrane after intestinal I/R is caused by suppression of BCRP S-S bond formation.…”

Section: Discussionmentioning

confidence: 78%

Intestinal Ischemia-Reperfusion Increases Efflux for Uric Acid Via Paracellular Route in the Intestine, but Decreases that Via Transcellular Route Mediated by BCRP

Ogura¹,

Kuwayama²,

Takaya³

et al. 2012

J Pharm Pharm Sci

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-Purpose. Uric acid is thought to be one of the most important antioxidants in human biological fluids. Intestinal ischemia-reperfusion (I/R) is an important factor associated with high rates of morbidity and mortality. Reactive oxygen species (ROS) are responsible for intestinal I/R injury. The aim of this study was to clarify the efflux for uric acid from the intestine after intestinal I/R. Methods. We used intestinal ischemia-reperfusion (I/R) model rats. Serosal to mucosal flux for [14 C]-uric acid was assessed by using Ussing-type diffusion chambers. BCRP/Bcrp expression was assessed by Western blot analysis. Caco-2 cells were used for a model of the intestinal epithelium, and rotenone was used as a mitochondrial dysfunction inducer. Results. Serosal to mucosal flux for uric acid was increased after intestinal I/R, and that for mannitol was also increased. Ko143, which is a BCRP inhibitor, did not affect the uric acid transport. The decreasing uric acid transport mediated by Bcrp was caused by decrease in the level of Bcrp homodimer, bridged by an S-S bond. The suppression of Bcrp S-S bond formation was associated with mitochondrial dysfunction. Moreover, BCRP S-S bond formation activity was decreased by rotenone in Caco-2 cells. Conclusions. Serosal to mucosal flux for uric acid is significantly increased via the paracelluler route, but that via the transcellular route mediated by Bcrp is decreased after intestinal I/R. The decreasing uric acid flux mediated by Bcrp is caused by suppression of Bcrp S-S bond formation. This suppression of Bcrp S-S bond formation may be related to mitochondrial dysfunction.

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“…In another study, the expression of Ab-cc2 in the liver was controlled by nuclear receptor activation, which is impaired during cholestasis (41). Abcg2 was found to play a role during oxidative stress, and its expression levels changed after IR injury in the kidney, liver, heart, cerebral vascular tissue, and intestines (42)(43)(44)(45)(46)(47). The levels of Abcc2 (Mrp2) expression in the rat liver decreased after IR injury, and endocytosis of Mrp2 developing in the canalicular membrane following IR caused impaired bile function (48).…”

Section: Discussionmentioning

confidence: 98%

4-phenyl butyric acid improves hepatic ischemia/reperfusion and affects gene expression of ABC transporter Abcc5 in rats

Güven,

Tanoglu,

Ozcelik

et al. 2023

Croat Med J

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Aim To assess the effects of 4-phenyl butyric acid (PBA) on oxidative stress, inflammation, liver histology, endoplasmic (ER) reticulum stress, and the expression levels of ATP-binding cassette transporter family members in a hepatic ischemia-reperfusion (IR) model. Methods Thirty-five rats were randomly divided into five groups: sham, IR, IR + 100 mg kg −1 PBA, IR + 200 mg kg −1 PBA, and IR + placebo. After sacrifice, we assessed serum biochemical variables, myeloperoxidase (MPO), malondialdehyde (MDA), total antioxidant status (TAS), and total oxidant status (TOS). The expression levels of Abcc (2 and 5), Abcg2, Abcf2, Ire1-α, and Perk genes were measured with a quantitative real-time polymerase chain reaction. ResultsSerum biochemical variables, MPO, MDA, TAS, and TOS levels of the PBA groups (especially in the low dose group) were lower than in the IR and placebo group (P < 0.05). Histological tissue damage in the IR group was more severe than in the PBA groups. Ire1-α and Perk expression levels were significantly lower in the PBA groups than the IR group (P < 0.001). Abcc (2 and 5) and Abcg2 expression levels were significantly lower in the IR group than in the sham and PBA groups (P < 0.001, P < 0.035, and P < 0.009, respectively). ConclusionsThe use of PBA significantly positively affected IR injury, which makes PBA a candidate treatment to reduce liver IR.

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Post-Transcriptional Regulation of Breast Cancer Resistance Protein after Intestinal Ischemia-Reperfusion

Cited by 7 publications

References 23 publications

Expression and function of ABCG2 and XIAP in glioblastomas

Expression and function of ABCG2 and XIAP in glioblastomas

Intestinal Ischemia-Reperfusion Increases Efflux for Uric Acid Via Paracellular Route in the Intestine, but Decreases that Via Transcellular Route Mediated by BCRP

4-phenyl butyric acid improves hepatic ischemia/reperfusion and affects gene expression of ABC transporter Abcc5 in rats

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