Academic literature on the topic 'Carbonyl reductase 1 (CBR1)'

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Journal articles on the topic "Carbonyl reductase 1 (CBR1)"

1

Varatharajan, Savitha, Ajay Abraham, Shaji R. Velayudhan, et al. "Carbonyl Reductase 1 Expression and Polymorphisms Influence Daunorubicin Metabolism in AML." Blood 118, no. 21 (2011): 2484. http://dx.doi.org/10.1182/blood.v118.21.2484.2484.

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Abstract Abstract 2484 Treatment failure in AML can be attributed to resistance to chemotherapeutic drugs. Induction chemotherapy of AML involves combination of Daunorubicin (Dnr) and Cytarabine. Up-regulation in the expression of efflux transporters such as ABCB1 and ABCG2 has been shown to be one of the causes of Dnr resistance in AML. Apart from efflux transporters, increased expression of the Dnr metabolising enzymes (Carbonyl reductase 1 (CBR1) and CBR3) also can influence the cytotoxic activity of Dnr against leukemic cells. Aim of the present study is to investigate: i) the role of mRNA
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2

Blanco, Javier G., Can-Lan Sun, Wendy Landier, et al. "Anthracycline-Related Cardiomyopathy After Childhood Cancer: Role of Polymorphisms in Carbonyl Reductase Genes—A Report From the Children's Oncology Group." Journal of Clinical Oncology 30, no. 13 (2012): 1415–21. http://dx.doi.org/10.1200/jco.2011.34.8987.

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Purpose Carbonyl reductases (CBRs) catalyze reduction of anthracyclines to cardiotoxic alcohol metabolites. Polymorphisms in CBR1 and CBR3 influence synthesis of these metabolites. We examined whether single nucleotide polymorphisms in CBR1 (CBR1 1096G>A) and/or CBR3 (CBR3 V244M) modified the dose-dependent risk of anthracycline-related cardiomyopathy in childhood cancer survivors. Patients and Methods One hundred seventy survivors with cardiomyopathy (patient cases) were compared with 317 survivors with no cardiomyopathy (controls; matched on cancer diagnosis, year of diagnosis, length of
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3

Hu, Dawei, Namiki Miyagi, Yuki Arai, et al. "Synthesis of 8-hydroxy-2-iminochromene derivatives as selective and potent inhibitors of human carbonyl reductase 1." Organic & Biomolecular Chemistry 13, no. 27 (2015): 7487–99. http://dx.doi.org/10.1039/c5ob00847f.

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Human carbonyl reductase 1 (CBR1), a member of the short-chain dehydrogenase/reductase superfamily, reduces anthracycline anticancer drugs to their less potent anticancer C-13 hydroxy metabolites, which are linked with pathogenesis of cardiotoxicity, a side effect of the drugs.
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4

Vyskočilová, Erika, Barbora Szotáková, Lenka Skálová, Hana Bártíková, Jitka Hlaváčová, and Iva Boušová. "Age-Related Changes in Hepatic Activity and Expression of Detoxification Enzymes in Male Rats." BioMed Research International 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/408573.

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Process of aging is accompanied by changes in the biotransformation of xenobiotics and impairment of normal cellular functions by free radicals. Therefore, this study was designed to determine age-related differences in the activities and/or expressions of selected drug-metabolizing and antioxidant enzymes in young and old rats. Specific activities of 8 drug-metabolizing enzymes and 4 antioxidant enzymes were assessed in hepatic subcellular fractions of 6-week-old and 21-month-old male Wistar rats. Protein expressions of carbonyl reductase 1 (CBR1) and glutathioneS-transferase (GST) were deter
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5

Bell, Rachel, Elisa Villalobos, Mark Nixon, et al. "Carbonyl Reductase 1 Overexpression in Adipose Amplifies Local Glucocorticoid Action and Impairs Glucose Tolerance in Lean Mice." Journal of the Endocrine Society 5, Supplement_1 (2021): A806. http://dx.doi.org/10.1210/jendso/bvab048.1639.

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Abstract Glucocorticoids play a critical role in metabolic homeostasis. Chronic or excessive activation of the glucocorticoid receptor (GR) in adipose tissue contributes to metabolic disorders such as glucose intolerance and insulin resistance. Steroid-metabolising enzymes in adipose, such as 11β-HSD1 or 5α-reductase, modulate the activation of GR by converting primary glucocorticoids into more or less potent ligands. Carbonyl reductase 1 (CBR1) is a novel regulator of glucocorticoid metabolism, converting corticosterone/cortisol to 20β-dihydrocorticosterone/cortisol (20β-DHB/F); a metabolite
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6

Waclawik, Agnieszka, and Adam J. Ziecik. "Differential expression of prostaglandin (PG) synthesis enzymes in conceptus during peri-implantation period and endometrial expression of carbonyl reductase/PG 9-ketoreductase in the pig." Journal of Endocrinology 194, no. 3 (2007): 499–510. http://dx.doi.org/10.1677/joe-07-0155.

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Prostaglandins (PGs) play a pivotal role in luteolysis, maternal recognition of pregnancy, and implantation. In many species, including pigs, both conceptus (embryo and associated membranes) and endometrium synthesize PGE2, which may antagonize PGF2α by playing a luteotropic/antiluteolytic role. Previously, we have reported expression profiles of PG G/H synthases (PGHS-1 and PGHS-2), PGE synthase (mPGES-1), and PGF synthase (PGFS) in the endometrium of cyclic and pregnant pigs. In the present study, expression of above-mentioned PG synthesis enzymes and PG 9-ketoreductase (CBR1), which convert
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7

Guo, Chunming, Wangsheng Wang, Chao Liu, Leslie Myatt та Kang Sun. "Induction of PGF2α Synthesis by Cortisol Through GR Dependent Induction of CBR1 in Human Amnion Fibroblasts". Endocrinology 155, № 8 (2014): 3017–24. http://dx.doi.org/10.1210/en.2013-1848.

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Abundant evidence indicates a pivotal role of prostaglandin F2α (PGF2α) in human parturition. Both the fetal and maternal sides of the fetal membranes synthesize PGF2α. In addition to the synthesis of PGF2α from PGH2 by PGF synthase (PGFS), PGF2α can also be converted from PGE2 by carbonyl reductase 1 (CBR1). Here, we showed that there was concurrent increased production of cortisol and PGF2α in association with the elevation of CBR1 in human amnion obtained at term with labor versus term without labor. In cultured primary human amnion fibroblasts, cortisol (0.01–1μM) increased PGF2α productio
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8

Ferguson, Daniel C., Qiuying Cheng, and Javier G. Blanco. "Characterization of the Canine Anthracycline-Metabolizing Enzyme Carbonyl Reductase 1 (cbr1) and the Functional Isoform cbr1 V218." Drug Metabolism and Disposition 43, no. 7 (2015): 922–27. http://dx.doi.org/10.1124/dmd.115.064295.

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9

Madadi Mahani, Nosrat, Alireaza Mohadesi Zarandi, and Azra Horzadeh. "QSAR studies of novel iminochromene derivatives as as carbonyl reductase 1 (CBR1) inhibito." Marmara Pharmaceutical Journal 22, no. 2 (2018): 227–36. http://dx.doi.org/10.12991/mpj.2018.60.

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10

Miura, Takeshi, Ayako Taketomi, Toru Nishinaka, and Tomoyuki Terada. "Regulation of human carbonyl reductase 1 (CBR1, SDR21C1) gene by transcription factor Nrf2." Chemico-Biological Interactions 202, no. 1-3 (2013): 126–35. http://dx.doi.org/10.1016/j.cbi.2012.11.023.

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