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Journal articles on the topic 'Breas cancer resistance protein'

Author: Grafiati

Published: 28 June 2021

Last updated: 17 February 2022

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1

Horak, I. R., D. S. Gerashchenko, and L. B. Drobot. "Adaptor protein Ruk/CIN85 modulates resistance to doxorubicin of murine 4T1 breast cancer cells." Ukrainian Biochemical Journal 90, no. 3 (June 25, 2018): 94–100. http://dx.doi.org/10.15407/ubj90.03.094.

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2

Qadir, Misbah, Kieran L. O’Loughlin, Nicole A. Williamson, Hans Minderman, and Maria R. Baer. "Cyclosporine A Modulates the Multidrug Resistance Proteins P-Glycoprotein, Multidrug Resistance Protein, Breast Cancer Resistance Protein and Lung Resistance Protein." Blood 104, no. 11 (November 16, 2004): 1180. http://dx.doi.org/10.1182/blood.v104.11.1180.1180.

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Abstract Multidrug resistance (MDR) mediated by the ATP-binding cassette proteins P-glycoprotein (Pgp), multidrug resistance protein (MRP-1), breast cancer resistance protein (BCRP) and the vault protein lung resistance protein (LRP) is implicated in treatment failure in acute myeloid leukemia (AML). Pgp, MRP-1 and BCRP mediate energy-dependent cellular drug efflux, while LRP blocks cytoplasmic-nuclear drug transport. MDR modulators are non-cytotoxic drugs that block the activity of MDR proteins. In clinical trials, the Pgp modulator cyclosporine A (CsA) improved treatment outcome in AML, while its non-immunosuppressive, non-nephrotoxic analogue PSC-833 has not, despite being a potent Pgp modulator in preclinical models. CsA is known to also modulate MRP-1, and we hypothesized that a broad spectrum of MDR modulation might contribute to its clinical efficacy. We studied the effects of CsA and PSC-833 on in vitro drug uptake, retention and cytotoxicity in drug-selected and transfected resistant cell lines overexpressing Pgp, MRP-1 or BCRP, and on nuclear-cytoplasmic drug distribution and cytotoxicity in cell lines overexpressing LRP. Cellular drug content was measured by flow cytometry, and nuclear-cytoplasmic drug distribution was assessed by confocal microscopy. CsA enhanced uptake and retention of the substrate drug mitoxantrone in cells overexpressing Pgp (HL60/VCR), MRP-1 (HL60/ADR) and BCRP (8226/MR20) and increased cytotoxicity 7-, 4- and 4-fold, respectively. Moreover, CsA increased the nuclear content of doxorubicin in 8226/MR20 cells, which co-express LRP with BCRP, and increased doxorubicin cytotoxicity 12-fold. The effect of CsA on nuclear drug content and cytotoxicity in 8226/MR20 cells occurred without an effect on cellular doxorubicin content, consistent with the fact that 8226/MR20 cells co-express wild type BCRP (BCRPR482), which does not efflux doxorubicin. Moreover the BCRP modulator fumitremorgin C had no effect on 8226/MR20 content, nuclear uptake nor cytotoxicity of doxorubicin. CsA also enhanced nuclear doxorubicin content in a second cell line with LRP-mediated resistance, HT1080/DR4. PSC-833 enhanced mitoxantrone retention and cytotoxicity in cells overexpressing Pgp, but, in contrast to CsA, had no effect on mitoxantrone uptake, retention nor cytotoxicity in cells expressing MRP-1 nor BCRP, and had no effect on doxorubicin nuclear content nor cytotoxicity in cells expressing LRP. Thus CsA is a broad-spectrum MDR modulator, with activity against Pgp, MRP-1, BCRP and LRP, while PSC-833 only modulates Pgp. The broad-spectrum activity of CsA may contribute to its clinical efficacy. These findings support identification and testing of other broad-spectrum MDR modulators.

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3

McGrath, Eoghan, Susan Logue, Katarzyna Mnich, Shane Deegan, Richard Jäger, Adrienne Gorman, and Afshin Samali. "The Unfolded Protein Response in Breast Cancer." Cancers 10, no. 10 (September 21, 2018): 344. http://dx.doi.org/10.3390/cancers10100344.

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In 2018, in the US alone, it is estimated that 268,670 people will be diagnosed with breast cancer, and that 41,400 will die from it. Since breast cancers often become resistant to therapies, and certain breast cancers lack therapeutic targets, new approaches are urgently required. A cell-stress response pathway, the unfolded protein response (UPR), has emerged as a promising target for the development of novel breast cancer treatments. This pathway is activated in response to a disturbance in endoplasmic reticulum (ER) homeostasis but has diverse physiological and disease-specific functions. In breast cancer, UPR signalling promotes a malignant phenotype and can confer tumours with resistance to widely used therapies. Here, we review several roles for UPR signalling in breast cancer, highlighting UPR-mediated therapy resistance and the potential for targeting the UPR alone or in combination with existing therapies.

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4

Staud, Frantisek, and Petr Pavek. "Breast cancer resistance protein (BCRP/ABCG2)." International Journal of Biochemistry & Cell Biology 37, no. 4 (April 2005): 720–25. http://dx.doi.org/10.1016/j.biocel.2004.11.004.

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5

Wang, Ming-Yang, Hsin-Yi Huang, Yao-Lung Kuo, Chiao Lo, Hung-Yu Sun, Yu-Jhen Lyu, Bo-Rong Chen, Jie-Ning Li, and Pai-Sheng Chen. "TARBP2-Enhanced Resistance during Tamoxifen Treatment in Breast Cancer." Cancers 11, no. 2 (February 12, 2019): 210. http://dx.doi.org/10.3390/cancers11020210.

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Tamoxifen is the most widely used hormone therapy in estrogen receptor-positive (ER+) breast cancer, which accounts for approximately 70% of all breast cancers. Although patients who receive tamoxifen therapy benefit with respect to an improved overall prognosis, resistance and cancer recurrence still occur and remain important clinical challenges. A recent study identified TAR (HIV-1) RNA binding protein 2 (TARBP2) as an oncogene that promotes breast cancer metastasis. In this study, we showed that TARBP2 is overexpressed in hormone therapy-resistant cells and breast cancer tissues, where it enhances tamoxifen resistance. Tamoxifen-induced TARBP2 expression results in the desensitization of ER+ breast cancer cells. Mechanistically, tamoxifen post-transcriptionally stabilizes TARBP2 protein through the downregulation of Merlin, a TARBP2-interacting protein known to enhance its proteasomal degradation. Tamoxifen-induced TARBP2 further stabilizes SOX2 protein to enhance desensitization of breast cancer cells to tamoxifen, while similar to TARBP2, its induction in cancer cells was also observed in metastatic tumor cells. Our results indicate that the TARBP2-SOX2 pathway is upregulated by tamoxifen-mediated Merlin downregulation, which subsequently induces tamoxifen resistance in ER+ breast cancer.

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6

JIA, P., S. WU, F. LI, Q. XU, M. WU, G. CHEN, G. LIAO, et al. "Breast cancer resistance protein-mediated topotecan resistance in ovarian cancer cells." International Journal of Gynecological Cancer 15, no. 6 (November 2005): 1042–48. http://dx.doi.org/10.1111/j.1525-1438.2005.00260.x.

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7

YUAN, Jian-Hui, Jin-Quan CHENG, Long-Yuan JIANG, Wei-Dong JI, Liang-Feng GUO, Jian-Jun LIU, Xing-Yun XU, Jing-Song HE, Xian-Ming WANG, and Zhi-Xiong ZHUANG. "Breast Cancer Resistance Protein Expression and 5-Fluorouracil Resistance." Biomedical and Environmental Sciences 21, no. 4 (August 2008): 290–95. http://dx.doi.org/10.1016/s0895-3988(08)60044-6.

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8

Natarajan, Karthika, Yi Xie, Maria R. Baer, and Douglas D. Ross. "Role of breast cancer resistance protein (BCRP/ABCG2) in cancer drug resistance." Biochemical Pharmacology 83, no. 8 (April 2012): 1084–103. http://dx.doi.org/10.1016/j.bcp.2012.01.002.

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9

WU, Xin-Gang, Shu-Bin PENG, and Qian HUANG. "Transcriptional regulation of breast cancer resistance protein." Hereditas (Beijing) 34, no. 12 (December 24, 2012): 1529–36. http://dx.doi.org/10.3724/sp.j.1005.2012.01529.

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10

Nooter, Kees, Guy Brutel de la Riviere, Jan Klijn, Gerrit Stoter, and John Foekens. "Multidrug resistance protein in recurrent breast cancer." Lancet 349, no. 9069 (June 1997): 1885–86. http://dx.doi.org/10.1016/s0140-6736(05)63876-7.

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11

Poguntke, Maren, Eszter Hazai, Martin F. Fromm, and Oliver Zolk. "Drug transport by breast cancer resistance protein." Expert Opinion on Drug Metabolism & Toxicology 6, no. 11 (September 27, 2010): 1363–84. http://dx.doi.org/10.1517/17425255.2010.519700.

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12

Kawabata, Shigeru, Mikio Oka, Ken Shiozawa, Kazuhiro Tsukamoto, Katsumi Nakatomi, Hiroshi Soda, Minoru Fukuda, et al. "Breast Cancer Resistance Protein Directly Confers SN-38 Resistance of Lung Cancer Cells." Biochemical and Biophysical Research Communications 280, no. 5 (February 2001): 1216–23. http://dx.doi.org/10.1006/bbrc.2001.4267.

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13

Hsu, Li-Han, Nei-Min Chu, Yung-Feng Lin, and Shu-Huei Kao. "G-Protein Coupled Estrogen Receptor in Breast Cancer." International Journal of Molecular Sciences 20, no. 2 (January 14, 2019): 306. http://dx.doi.org/10.3390/ijms20020306.

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The G-protein coupled estrogen receptor (GPER), an alternate estrogen receptor (ER) with a structure distinct from the two canonical ERs, being ERα, and ERβ, is expressed in 50% to 60% of breast cancer tissues and has been presumed to be associated with the development of tamoxifen resistance in ERα positive breast cancer. On the other hand, triple-negative breast cancer (TNBC) constitutes 15% to 20% of breast cancers and frequently displays a more aggressive behavior. GPER is prevalent and involved in TNBC and can be a therapeutic target. However, contradictory results exist regarding the function of GPER in breast cancer, proliferative or pro-apoptotic. A better understanding of the GPER, its role in breast cancer, and the interactions with the ER and epidermal growth factor receptor will be beneficial for the disease management and prevention in the future.

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14

Hazai, Eszter, and Zsolt Bikádi. "Homology modeling of breast cancer resistance protein (ABCG2)." Journal of Structural Biology 162, no. 1 (April 2008): 63–74. http://dx.doi.org/10.1016/j.jsb.2007.12.001.

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15

Plasschaert, Sabine LA, Dorina M. Van Der Kolk, Eveline SJM De Bont, Edo Vellenga, Willem A. Kamps, and Elisabeth GE De Vries. "Breast Cancer Resistance Protein (BCRP) in Acute Leukaemia." Leukemia & Lymphoma 45, no. 4 (April 2004): 649–54. http://dx.doi.org/10.1080/10428190310001597928.

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16

Lage, Hermann, and Manfred Dietel. "Effect of the breast-cancer resistance protein on atypical multidrug resistance." Lancet Oncology 1, no. 3 (November 2000): 169–75. http://dx.doi.org/10.1016/s1470-2045(00)00032-2.

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17

Imai, Yasuo, Satomi Tsukahara, Sakiyo Asada, and Yoshikazu Sugimoto. "Phytoestrogens/Flavonoids Reverse Breast Cancer Resistance Protein/ABCG2-Mediated Multidrug Resistance." Cancer Research 64, no. 12 (June 15, 2004): 4346–52. http://dx.doi.org/10.1158/0008-5472.can-04-0078.

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18

Austin Doyle, L., and Douglas D. Ross. "Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2)." Oncogene 22, no. 47 (October 2003): 7340–58. http://dx.doi.org/10.1038/sj.onc.1206938.

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19

Ahmed-Belkacem, Abdelhakim, Alexandre Pozza, Sira Macalou, Jose?? M. Pe??rez-Victoria, Ahce`ne Boumendjel, and Attilio Di Pietro. "Inhibitors of cancer cell multidrug resistance mediated by breast cancer resistance protein (BCRP/ABCG2)." Anti-Cancer Drugs 17, no. 3 (March 2006): 239–43. http://dx.doi.org/10.1097/00001813-200603000-00001.

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20

Iseri, Ozlem. "Expression of Multidrug Resistance 1, Lung Resistance Protein and Breast Cancer Resistance Protein Genes in Chronic Leukemias." International Journal of Hematology and Oncology 21, no. 2 (June 1, 2011): 92–100. http://dx.doi.org/10.4999/uhod.10012.

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21

Bharthuar, A., T. Khoury, K. N. Haas, T. Mashtare, J. Black, M. Baer, G. Yang, N. Khushalani, and R. V. Iyer. "Expression of breast cancer resistance protein (BCRP) in esophageal cancers (EC)." Journal of Clinical Oncology 27, no. 15_suppl (May 20, 2009): e13529-e13529. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.e13529.

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e13529 Background: EC patients face a dismal outcome despite tri-modality management strategy. Median survival remains 15–18 months despite platinum, fluropyrimidine & irinotecan based therapy. BCRP is an ATP-dependent efflux protein associated with chemotherapy (CT) (e.g. irinotecan) resistance. Role of BCRP expression in EC and normal esophageal cells is not known. We examined the expression of this protein and correlate it with survival (OS) in patients receiving irinotecan-based CT. Methods: With IRB approval, 40 cases of EC diagnosed between 2004 and 2008 were stained for BCRP expression by IHC & scored by the pathologist blinded to clinical data. Baseline demographics, therapy given & OS data were collected and correlated with BCRP expression. BCRP score (membrane or cytoplasm) >/= 30 was considered positive (calculated by multiplying BCRP intensity and % staining). Fisher's exact test used to determine association between BCRP expression & demographics. Cox proportional hazards model used for association of BCRP & OS. Results: Baseline patient and tumor characteristics: Gender: M 35, F 5; Histology: 37 Adenoca & 3 SCC; Stage 1-III 27, Stage IV 10, unknown 3; CT: cisplatin+irinotecan (n=16), oxaliplatin+fluoropyrimidine (n=8), other (n=16); IHC: 30 of 40 cancers (75%) expressed BCRP [strong (n=28) & intermediate (n=3); membranous (n=17), cytoplasmic (n=27) & both (n=14)]. Down-regulation of BCRP expression in tumor compared to normal cells seen in 40% of patients. Median OS was 19 months with no difference in OS between BCRP positive and negative patients (p=0.13). Estimated hazard ratio (HR) of death for BCRP positive patients was 2.29 (95% CI 0.79 - 6.64).There was no association between BCRP expression and stage, age, gender or histology. For patients who received cisplatin and irinotecan as first line CT there was no difference in OS (p=0.39) of BCRP negative versus positive patients. Conclusions: BCRP expression is seen in a majority of EC & normal esophageal mucosa. Response rates to irinotecan based therapies are seen in 30–40 % of EC, whether the 40% with low tumor BCRP constitute a majority of the responders needs to be prospectively validated in a larger dataset & should include markers that predict response to 5-FU & platinum based CT to allow individualizing therapy for this cancer. No significant financial relationships to disclose.

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Bharthuar, A., T. Khoury, M. R. Baer, J. Black, A. Oseroff, N. Khushalani, M. M. Javle, H. Nava, and R. V. Iyer. "Expression of breast cancer resistance protein in upper gastro-intestinal cancers." Journal of Clinical Oncology 26, no. 15_suppl (May 20, 2008): 15599. http://dx.doi.org/10.1200/jco.2008.26.15_suppl.15599.

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23

Jiang, Huangyu, Jia Yu, Haihui Zheng, Jiamei Chen, Jinjun Wu, Xiaoxiao Qi, Ying Wang, et al. "Breast Cancer Resistance Protein and Multidrug Resistance Protein 2 Regulate the Disposition of Acacetin Glucuronides." Pharmaceutical Research 34, no. 7 (April 18, 2017): 1402–15. http://dx.doi.org/10.1007/s11095-017-2157-8.

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24

Li, Jun, Mingjie Lu, Jiao Jin, Xiyi Lu, Tongpeng Xu, and Shidai Jin. "miR-449a Suppresses Tamoxifen Resistance in Human Breast Cancer Cells by Targeting ADAM22." Cellular Physiology and Biochemistry 50, no. 1 (2018): 136–49. http://dx.doi.org/10.1159/000493964.

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Background/Aims: Most of estrogen receptor positive breast cancer patients respond well initially to endocrine therapies, but often develop resistance during treatment with selective estrogen receptor modulators (SERMs) such as tamoxifen. Altered expression and functions of microRNAs (miRNAs) have been reportedly associated with tamoxifen resistance. Thus, it is necessary to further elucidate the function and mechanism of miRNAs in tamoxifen resistance. Methods: Tamoxifen sensitivity was validated by using Cell Counting Kit-8 in tamoxifen-sensitive breast cancer cells (MCF-7, T47D) and tamoxifen-resistant cells (MCF-7/TAM, T47D/ TAM). Quantitative real-time polymerase chain reaction (qRT-PCR) was performed to detect the expression level of miR-449a in tamoxifen-sensitive/-resistant cells and patient serums. Dual-luciferase assay was used to identify the binding of miR-449a and predicted gene ADAM22. The expression level of ADAM22 was determined by qRT-PCR and western blotting in miR-449a +/- breast cancer cells. Subsequently, rescue experiments were carried out to identify the function of ADAM22 in miR-449a-reduced tamoxifen resistance. Finally, Gene ontology (GO) and Protein-protein interaction analyses were performed to evaluate the potential mechanisms of ADAM22 in regulating tamoxifen resistance. Results: MiR-449a levels were downregulated significantly in tamoxifen-resistant breast cancer cells when compared with their parental cells, as well as in clinical breast cancer serum samples. Overexpression of miR-449a re-sensitized the tamoxifen-resistant breast cancer cells, while inhibition of miR-449a conferred tamoxifen resistance in parental cells. Luciferase assay identified ADAM22 as a direct target gene of miR-449a. Additionally, silencing of ADAM22 could reverse tamoxifen resistance induced by miR-449a inhibition in ER-positive breast cancer cells. GO analysis results showed ADAM22 was mainly enriched in the biological processes of cell adhesion, cell differentiation, gliogenesis and so on. Protein-protein interaction analyses appeared that ADAM22 might regulate tamoxifen resistance through PPARG, LGI1, KRAS and LYN. Conclusion: Decreased miR-449a causes the upregulation of ADAM22, which induces tamoxifen resistance of breast cancer cells. These results suggest that miR-449a, functioning by targeting ADAM22, contributes to the mechanisms underlying breast cancer endocrine resistance, which may provide a potential therapeutic strategy in ER-positive breast cancers.

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Wu, Minhua, Jinhua Ding, Limu Wen, Yuxin Zhou, and Weizhu Wu. "Molecular Mechanism of Secondary Endocrine Resistance in Luminal Breast Cancer." BioMed Research International 2021 (March 16, 2021): 1–7. http://dx.doi.org/10.1155/2021/6618519.

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Objective. The molecular mechanism of secondary resistance in Luminal breast cancer was studied to provide new ideas for the treatment of breast cancer. Methods. The sensitivity of the downregulation of myeloid leukemia factor 1-interacting proteins (MLF1IP) to Tamoxifen (TAM) was tested by the Cell Counting Kit-8 (CCK-8). The apoptosis of MLF1IP-mediated resistance was analyzed by flow cytometry (FCM) with/without TAM. Western blot was used in detecting various kinds of apoptosis and the expression of the protein related to the phosphatidylinositol 3-kinase (PI3K)/AKT signaling pathway to study the molecular mechanism of secondary endocrine resistance in Luminal breast cancer. Results. The downregulation of MLF1IP could significantly increase the drug sensitivity of Michigan Cancer Foundation-7 (MCF-7) cells and also inhibit the proliferation of MCF-7 cells under the stimulation of drugs. Western blot results showed that the expression of Bcl-2-associated X (BAX), Caspase3, Caspase7, and Caspase9 proteins increased when MLF1IP was downregulated. The results of the PI3K/AKT signaling pathway revealed that the phosphatase and tensin homolog deleted on chromosome ten (PTEN) protein expression of MCF7-shRNA was higher than that of MCF7-NC cells, while the expression of p-AKT was lower than that of MCF7-NC cells. Conclusions. (1) MLF1IP-related apoptosis resistance plays an essential role in MLF1IP-mediated secondary resistance of breast cancer cells. (2) MLF1IP promotes AKT phosphorylation by inhibiting the PTEN expression, thus activating the PI3K/AKT signaling pathway and causing the secondary resistance of Luminal breast cancer. (3) MLF1IP can be used as a factor to predict the endocrine resistance of Luminal breast cancer.

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Samanta, Sanjoy, Bryan Pursell, and Arthur M. Mercurio. "IMP3 Protein Promotes Chemoresistance in Breast Cancer Cells by Regulating Breast Cancer Resistance Protein (ABCG2) Expression." Journal of Biological Chemistry 288, no. 18 (March 28, 2013): 12569–73. http://dx.doi.org/10.1074/jbc.c112.442319.

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Grossman, H. Barton. "Expression of multidrug resistance proteins P-glycoprotein, multidrug resistance protein 1, breast cancer resistance protein and lung resistance related protein in locally advanced bladder cancer treated with neoadjuvant chemotherapy: biological and clinical implications." Urologic Oncology: Seminars and Original Investigations 22, no. 3 (May 2004): 266–67. http://dx.doi.org/10.1016/j.urolonc.2004.03.004.

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DIESTRA, JULIO E., ENRIC CONDOM, XAVIER GARCÍA DEL MURO, GEORGE L. SCHEFFER, JAVIER PÉREZ, AMADO J. ZURITA, JOSÉ MUÑOZ-SEGUÍ, et al. "Expression of Multidrug Resistance Proteins P-Glycoprotein, Multidrug Resistance Protein 1, Breast Cancer Resistance Protein and Lung Resistance Related Protein in Locally Advanced Bladder Cancer Treated With Neoadjuvant Chemotherapy: Biological and Clinical Implications." Journal of Urology 170, no. 4 Part 1 (October 2003): 1383–87. http://dx.doi.org/10.1097/01.ju.0000074710.96154.c9.

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29

Gregorj, Chiara, Agostino Tafuri, Maria T. Petrucci, Maria C. Scerpa, Fabiana De Cave, Maria R. Ricciardi, Antonella Vitale, Francesca Paoloni, and Robin Foa. "Breast Cancer Resistance Protein (BCRP) in Adult Acute Lymphoblastic Leukemia Patients." Blood 104, no. 11 (November 16, 2004): 1897. http://dx.doi.org/10.1182/blood.v104.11.1897.1897.

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Abstract The transporter breast cancer resistance protein (BCRP) is a member of the ATP-binding cassette which has been recently described as a protein involved in the multidrug resistance (MDR) phenotype. There are currently no reports concerning the role of this protein in adult acute lymphoblastic leukemia (ALL). The aim of this study was to evaluate the frequency of BCRP expression, its correlation with other MDR-related proteins and their prognostic role in 93 untreated adult ALL patients enrolled in the GIMEMA protocols LAL 0496 and LAL 2000. BCRP protein expression was detected by flow cytometry using the monoclonal antibody BXP-34 (Kamiya, Seattle, WA) and the analysis was performed by the Kolmogorov-Smirnov (KS) statistic test (D-value). Detection of BCRP in the cell lines MCF7 pcDNA3 and MDA231 pcDNA3 showed a D-value of 0.12 ± 0.11 and 0.09 ± 0.06, respectively (negative controls). In contrast, the cell lines MCF7 pcDNA3 clone 8 and MDA231 pcDNA3 clone 23 overexpressed BCRP with a D-value of 0.44 ± 0.21 and 0.33 ± 0.11, respectively (positive controls). Analysis of primary ALL samples showed a BCRP expression (D-value >0.20) in 70/93 (75.3%) cases, with a mean value of 0.33 ± 0.19 (range 0.00-0.87, median 0.33) in the overall population analyzed. BCRP expression resulted higher (mean 0.34 ± 0.03) in samples from patients with WBC counts ≥100 x 109/L compared to the values (mean 0.26 ± 0.13) found in those with lower WBC counts (P=0.06). No significant difference was found between BCRP expression and the clinical characteristics of the patients. The analysis was then extended to the Multidrug Resistance Associated protein (MRP1) and to the MDR1/P-glycoprotein-170 (MDR1). A D-value ≥0.20 and ≥0.05 was found in 53.4% (39/73) and 30.2% (26/86) of cases, respectively. Samples analyzed for both BCRP and MRP1 expression (73/93) showed a significant correlation (R2 = 0.25; P=0.0001): 12.3% of samples were negative for both proteins, while 43.8% expressed both BCRP and MRP1 proteins. In addition, MRP1 negative samples showed lower BCRP levels (mean 0.30, range 0–0.60) compared to MRP1 positive cases (mean 0.38, range 0–0.87) (P=0.017). BCRP expression did not correlate with MDR1 expression. None of these MDR markers correlated separately with achievement of complete remission (CR). In contrast, BCRP/MRP1 co-expression correlated significantly (P=0.034) with failure to respond to induction treatment: 47.8% (11/23) of BCRP+/MRP1+ patients failed to achieve CR, while 78.4% (29/37) of cases negative for only one protein (BCRP-/MRP1+ or BCRP+/MRP1−) or for both (BCRP-/MRP1-) responded to induction treatment. Multivariate analysis (Backward method) confirmed the unfavorable prognostic role on CR of these two proteins concomitantly expressed (P=0.029; OR 0.27, 95% CI, 0.081–0.87). In conclusion, our study shows that BCRP is expressed in a significant proportion of adult ALL. The co-expression of BCRP and MRP1 plays an unfavorable prognostic role on achievement of CR in ALL. These data suggest that the resistance phenotype may be the result of the combined effects of several transporter proteins involved in the MDR process and therefore detection of all these proteins may better predict clinical response to induction treatment.

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Imai, Yasuo, Satomi Tsukahara, Etsuko Ishikawa, Takashi Tsuruo, and Yoshikazu Sugimoto. "Estrone and 17β-Estradiol Reverse Breast Cancer Resistance Protein-mediated Multidrug Resistance." Japanese Journal of Cancer Research 93, no. 3 (March 2002): 231–35. http://dx.doi.org/10.1111/j.1349-7006.2002.tb02162.x.

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Woehlecke, Holger, Hiroyuki Osada, Andreas Herrmann, and Hermann Lage. "Reversal of breast cancer resistance protein-mediated drug resistance by tryprostatin A." International Journal of Cancer 107, no. 5 (October 14, 2003): 721–28. http://dx.doi.org/10.1002/ijc.11444.

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32

WANG, MIN, XIANMING WANG, JIANHUI YUAN, and LIANGFENG GUO. "Expression of the breast cancer resistance protein and 5-fluorouracil resistance in clinical breast cancer tissue specimens." Molecular and Clinical Oncology 1, no. 5 (July 4, 2013): 853–57. http://dx.doi.org/10.3892/mco.2013.143.

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Lv, Qing, Shiming Guan, Mingjie Zhu, Hu Huang, Junqiang Wu, and Xiaofeng Dai. "FGFR1 Is Associated With Tamoxifen Resistance and Poor Prognosis of ER-Positive Breast Cancers by Suppressing ER Protein Expression." Technology in Cancer Research & Treatment 20 (January 1, 2021): 153303382110049. http://dx.doi.org/10.1177/15330338211004935.

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Fibroblast growth factor receptor 1 (FGFR1) is widely recognized as a key player in mammary carcinogenesis and associated with the prognosis and therapeutic response of breast cancers. With the aim of investigating the correlation between FGFR1 expression and estrogen receptor (ER) and exploring the effect of FGFR1 on endocrine therapy response and ER+ breast cancer prognosis, we examined the FGFR1 protein expression among 184 ER-positive breast cancers by the immunohistochemistry (IHC) method, analyzed the association between FGFR1 expression and disease characters using the Pearson’s chi-square test, and assessed the prognostic role of FGFR1 among breast cancers using Cox regression and Kaplan-Meier analyses. Moreover, in vitro assays were conducted to confirm the correlation between FGFR1 and ER expression and investigate the effect of FGFR1 on tamoxifen (TAM) sensitivity in ER+breast cancer. The results showed that ER expression was negatively correlated with FGFR1 expression ( P = 0.011, r = -0.221). Moreover, FGFR1 expression was one of the prognostic factors of ER-positive breast cancer (OR = 1.974, 95% CI = 1.043-3.633), and high FGFR1 expression was correlated with decreased breast cancer overall survival. In addition, knocking down FGFR1 inhibited cell proliferation and enhanced TAM sensitivity in TAM-resistant cells. In conclusion, we found that there was a significant negative correlation between FGFR1 and ER levels in ER+breast cancers, high FGFR1 protein expression was associated with poor breast cancer prognosis, down-regulating FGFR1 could elevate ER expression and is associated with enhanced TAM sensitivity in ER+breast cancers.

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Yang, Liu, Mingli Jin, and Kwang Won Jeong. "Histone H3K4 Methyltransferases as Targets for Drug-Resistant Cancers." Biology 10, no. 7 (June 25, 2021): 581. http://dx.doi.org/10.3390/biology10070581.

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The KMT2 (MLL) family of proteins, including the major histone H3K4 methyltransferase found in mammals, exists as large complexes with common subunit proteins and exhibits enzymatic activity. SMYD, another H3K4 methyltransferase, and SET7/9 proteins catalyze the methylation of several non-histone targets, in addition to histone H3K4 residues. Despite these structural and functional commonalities, H3K4 methyltransferase proteins have specificity for their target genes and play a role in the development of various cancers as well as in drug resistance. In this review, we examine the overall role of histone H3K4 methyltransferase in the development of various cancers and in the progression of drug resistance. Compounds that inhibit protein–protein interactions between KMT2 family proteins and their common subunits or the activity of SMYD and SET7/9 are continuously being developed for the treatment of acute leukemia, triple-negative breast cancer, and castration-resistant prostate cancer. These H3K4 methyltransferase inhibitors, either alone or in combination with other drugs, are expected to play a role in overcoming drug resistance in leukemia and various solid cancers.

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35

Zhan, Ting, Xiaoli Chen, Xia Tian, Zheng Han, Meng Liu, Yanli Zou, Shasha Huang, et al. "MiR-331-3p Links to Drug Resistance of Pancreatic Cancer Cells by Activating WNT/β-Catenin Signal via ST7L." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382094580. http://dx.doi.org/10.1177/1533033820945801.

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Background: Pancreatic cancer is an aggressive type of cancer with poor prognosis, short survival rate, and high mortality. Drug resistance is a major cause of treatment failure in the disease. MiR-331-3p has been reported to play an important role in several cancers. We previously showed that miR-331-3p is upregulated in pancreatic cancer and promotes pancreatic cancer cell proliferation and epithelial-to-mesenchymal transition–mediated metastasis by targeting ST7L. However, it is uncertain whether miR-331-3p is involved in drug resistance. Methods: We investigated the relationship between miR-331-3p and pancreatic cancer drug resistance. As part of this, microRNA mimics or inhibitors were transfected into pancreatic cancer cells. Quantitative polymerase chain reaction was used to detect miR-331-3p expression, and flow cytometry was used to detect cell apoptosis. The Cell Counting Kit-8 assay was used to measure the IC50 values of gemcitabine in pancreatic cancer cells. The expression of multidrug resistance protein 1, multidrug resistance-related protein 1, breast cancer resistance protein, β-Catenin, c-Myc, Cyclin D1, Bcl-2, and Caspase-3 was evaluated by Western blotting. Results: We confirmed that miR-331-3p is upregulated in gemcitabine-treated pancreatic cancer cells and plasma from chemotherapy patients. We also confirmed that miR-331-3p inhibition decreased drug resistance by regulating cell apoptosis and multidrug resistance protein 1, multidrug resistance-related protein 1, and breast cancer resistance protein expression in pancreatic cancer cells, whereas miR-331-3p overexpression had the opposite effect. We further demonstrated that miR-331-3p effects in drug resistance were partially reversed by ST7L overexpression. In addition, overexpression of miR-331-3p activated Wnt/β-catenin signaling in pancreatic cancer cells, and ST7L overexpression restored activation of Wnt/β-catenin signaling. Conclusions: Taken together, our data demonstrate that miR-331-3p contributes to drug resistance by activating Wnt/β-catenin signaling via ST7L in pancreatic cancer cells. These data provide a theoretical basis for new targeted therapies in the future.

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Cherigo, Lilia, Dioxelis Lopez, and Sergio Martinez-Luis. "Marine Natural Products as Breast Cancer Resistance Protein Inhibitors." Marine Drugs 13, no. 4 (April 3, 2015): 2010–29. http://dx.doi.org/10.3390/md13042010.

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37

Kalyoncu, U., and I. Ertenli. "The breast cancer resistance protein: gatekeeper to the synovium?" International Journal of Clinical Rheumatology 5, no. 5 (October 2010): 509–11. http://dx.doi.org/10.2217/ijr.10.46.

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Xia, Cindy Q., Ning Liu, Gerald T. Miwa, and Liang-Shang Gan. "Interactions of Cyclosporin A with Breast Cancer Resistance Protein." Drug Metabolism and Disposition 35, no. 4 (January 12, 2007): 576–82. http://dx.doi.org/10.1124/dmd.106.011866.

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39

Shimizu, Takuya, Tomoko Sugiura, Tomohiko Wakayama, Ai Kijima, Noritaka Nakamichi, Shoichi Iseki, David L. Silver, and Yukio Kato. "PDZK1 Regulates Breast Cancer Resistance Protein in Small Intestine." Drug Metabolism and Disposition 39, no. 11 (August 4, 2011): 2148–54. http://dx.doi.org/10.1124/dmd.111.040295.

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40

Deng, Feng-Lian, Li Li, and Zan-Song Huang. "Role of breast cancer resistance protein in gastrointestinal tumors." World Chinese Journal of Digestology 27, no. 6 (March 28, 2019): 395–401. http://dx.doi.org/10.11569/wcjd.v27.i6.395.

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Sim, Hong-May, Chong-Yew Lee, Pui Lai Rachel Ee, and Mei-Lin Go. "Dimethoxyaurones: Potent inhibitors of ABCG2 (breast cancer resistance protein)." European Journal of Pharmaceutical Sciences 35, no. 4 (November 2008): 293–306. http://dx.doi.org/10.1016/j.ejps.2008.07.008.

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42

Pick, Anne, Werner Klinkhammer, and Michael Wiese. "Specific Inhibitors of the Breast Cancer Resistance Protein (BCRP)." ChemMedChem 5, no. 9 (July 14, 2010): 1498–505. http://dx.doi.org/10.1002/cmdc.201000216.

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43

Wright, Griffin, Manoj Sonavane, and Natalie R. Gassman. "Activated STAT3 Is a Novel Regulator of the XRCC1 Promoter and Selectively Increases XRCC1 Protein Levels in Triple Negative Breast Cancer." International Journal of Molecular Sciences 22, no. 11 (May 22, 2021): 5475. http://dx.doi.org/10.3390/ijms22115475.

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Base Excision Repair (BER) addresses base lesions and abasic sites induced by exogenous and endogenous stressors. X-ray cross complementing group 1 (XRCC1) functions as a scaffold protein in BER and single-strand break repair (SSBR), facilitating and coordinating repair through its interaction with a host of critical repair proteins. Alterations of XRCC1 protein and gene expression levels are observed in many cancers, including colorectal, ovarian, and breast cancer. While increases in the expression level of XRCC1 are reported, the transcription factors responsible for this up-regulation are not known. In this study, we identify the signal transducer and activator of transcription 3 (STAT3) as a novel regulator of XRCC1 through chromatin immunoprecipitation. Activation of STAT3 through phosphorylation at Y705 by cytokine (IL-6) signaling increases the expression of XRCC1 and the occupancy of STAT3 within the XRCC1 promoter. In triple negative breast cancer, the constitutive activation of STAT3 upregulates XRCC1 gene and protein expression levels. Increased expression of XRCC1 is associated with aggressiveness and resistance to DNA damaging chemotherapeutics. Thus, we propose that activated STAT3 regulates XRCC1 under stress and growth conditions, but constitutive activation in cancers results in dysregulation of XRCC1 and subsequently BER and SSBR.

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Jordan, V. Craig, and Bert W. O'Malley. "Selective Estrogen-Receptor Modulators and Antihormonal Resistance in Breast Cancer." Journal of Clinical Oncology 25, no. 36 (December 20, 2007): 5815–24. http://dx.doi.org/10.1200/jco.2007.11.3886.

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Selective estrogen-receptor (ER) modulators (SERMs) are synthetic nonsteroidal compounds that switch on and switch off target sites throughout the body. Tamoxifen, the pioneering SERM, blocks estrogen action by binding to the ER in breast cancers. Tamoxifen has been used ubiquitously in clinical practice during the last 30 years for the treatment of breast cancer and is currently available to reduce the risk of breast cancer in high-risk women. Raloxifene maintains bone density (estrogen-like effect) in postmenopausal osteoporotic women, but at the same time reduces the incidence of breast cancer in both high- and low-risk (osteoporotic) postmenopausal women. Unlike tamoxifen, raloxifene does not increase the incidence of endometrial cancer. Clearly, the simple ER model of estrogen action can no longer be used to explain SERM action at different sites around the body. Instead, a new model has evolved on the basis of the discovery of protein partners that modulate estrogen action at distinct target sites. Coactivators are the principal players that assemble a complex of functional proteins around the ligand ER complex to initiate transcription of a target gene at its promoter site. A promiscuous SERM ER complex creates a stimulatory signal in growth factor receptor–rich breast or endometrial cancer cells. These events cause drug-resistant, SERM-stimulated growth. The sometimes surprising pharmacology of SERMs has resulted in a growing interest in the development of new selective medicines for other members of the nuclear receptor superfamily. This will allow the precise treatment of diseases that was previously considered impossible.

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Sayer, R., J. Turner, D. Sullivan, J. Fiorica, and J. Lancaster. "Characterization of breast cancer resistance protein (BCRP) in epithelial ovarian cancer (EOC)." Journal of Clinical Oncology 23, no. 16_suppl (June 2005): 2020. http://dx.doi.org/10.1200/jco.2005.23.16_suppl.2020.

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Andrade, Daniel, Meghna Mehta, James Griffith, Sangphil Oh, Joshua Corbin, Anish Babu, Supriyo De, et al. "HuR Reduces Radiation-Induced DNA Damage by Enhancing Expression of ARID1A." Cancers 11, no. 12 (December 13, 2019): 2014. http://dx.doi.org/10.3390/cancers11122014.

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Tumor suppressor ARID1A, a subunit of the chromatin remodeling complex SWI/SNF, regulates cell cycle progression, interacts with the tumor suppressor TP53, and prevents genomic instability. In addition, ARID1A has been shown to foster resistance to cancer therapy. By promoting non-homologous end joining (NHEJ), ARID1A enhances DNA repair. Consequently, ARID1A has been proposed as a promising therapeutic target to sensitize cancer cells to chemotherapy and radiation. Here, we report that ARID1A is regulated by human antigen R (HuR), an RNA-binding protein that is highly expressed in a wide range of cancers and enables resistance to chemotherapy and radiation. Our results indicate that HuR binds ARID1A mRNA, thereby increasing its stability in breast cancer cells. We further find that ARID1A expression suppresses the accumulation of DNA double-strand breaks (DSBs) caused by radiation and can rescue the loss of radioresistance triggered by HuR inhibition, suggesting that ARID1A plays an important role in HuR-driven resistance to radiation. Taken together, our work shows that HuR and ARID1A form an important regulatory axis in radiation resistance that can be targeted to improve radiotherapy in breast cancer patients.

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Sun, Ruipu, Ying Ying, Zhimin Tang, Ting Liu, Fuli Shi, Huixia Li, Taichen Guo, Shibo Huang, and Ren Lai. "The Emerging Role of the SLCO1B3 Protein in Cancer Resistance." Protein & Peptide Letters 27, no. 1 (December 10, 2019): 17–29. http://dx.doi.org/10.2174/0929866526666190926154248.

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Currently, chemotherapy is one of the mainstays of oncologic therapies. But the efficacy of chemotherapy is often limited by drug resistance and severe side effects. Consequently, it is becoming increasingly important to investigate the underlying mechanism and overcome the problem of anticancer chemotherapy resistance. The solute carrier organic anion transporter family member 1B3 (SLCO1B3), a functional transporter normally expressed in the liver, transports a variety of endogenous and exogenous compounds, including hormones and their conjugates as well as some anticancer drugs. The extrahepatic expression of SLCO1B3 has been detected in different cancer cell lines and cancer tissues. Recently, accumulating data indicates that the abnormal expression and function of SLCO1B3 are involved in resistance to anticancer drugs, such as taxanes, camptothecin and its analogs, SN-38, and Androgen Deprivation Therapy (ADT) in breast, prostate, lung, hepatic, and colorectal cancer, respectively. Thus, more investigations have been implemented to identify the potential SLCO1B3-related mechanisms of cancer drug resistance. In this review, we focus on the emerging roles of SLCO1B3 protein in the development of cancer chemotherapy resistance and briefly discuss the mechanisms of resistance. Elucidating the function of SLCO1B3 in chemoresistance may bring out novel therapeutic strategies for cancer treatment.

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Sugimoto, Yoshikazu, Satomi Tsukahara, Etsuko Ishikawa, and Junko Mitsuhashi. "Breast cancer resistance protein: Molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics." Cancer Science 96, no. 8 (August 2005): 457–65. http://dx.doi.org/10.1111/j.1349-7006.2005.00081.x.

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Choi, Hoo Kyun, Jin Won Yang, Sang Hee Roh, Chang Yeob Han, and Keon Wook Kang. "Induction of multidrug resistance associated protein 2 in tamoxifen-resistant breast cancer cells." Endocrine-Related Cancer 14, no. 2 (June 2007): 293–303. http://dx.doi.org/10.1677/erc-06-0016.

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Acquired resistance to tamoxifen (TAM) is a serious therapeutic problem in breast cancer patients. The transition from chemotherapy-responsive breast cancer cells to chemotherapy-resistant cancer cells is mainly accompanied by the increased expression of multidrug resistance-associated proteins (MRPs). In this study, it was found that TAM-resistant MCF-7 (TAMR-MCF-7) cells expressed higher levels of MRP2 than control MCF-7 cells. Molecular analyses using MRP2 gene promoters supported the involvement of the pregnane X receptor (PXR) in MRP2 overexpression in TAMR-MCF-7 cells. Although CCAAT/enhancer-binding protein β was overexpressed continuously in TAMR-MCF-7 cells, this might not be responsible for the transcriptional activation of the MRP2 gene. In addition, the basal activities of phosphatidylinositol 3-kinase (PI3-kinase) were higher in the TAMR-MCF-7 cells than in the control cells. The inhibition of PI3-kinase significantly reduced both the PXR activity and MRP2 expression in TAMR-MCF-7 cells. Overall, MRP2 induction plays a role in the additional acquisition of chemotherapy resistance in TAM-resistant breast cancer.

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Yoshida, Naoko, Tappei Takada, Yoshikazu Yamamura, Isao Adachi, Hiroshi Suzuki, and Junichi Kawakami. "Inhibitory Effects of Terpenoids on Multidrug Resistance-Associated Protein 2- and Breast Cancer Resistance Protein-Mediated Transport." Drug Metabolism and Disposition 36, no. 7 (April 24, 2008): 1206–11. http://dx.doi.org/10.1124/dmd.107.019513.

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