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

Author: Grafiati

Published: 14 March 2023

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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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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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11

Arai, Yuki, Satoshi Endo, Namiki Miyagi, et al. "Structure–activity relationship of flavonoids as potent inhibitors of carbonyl reductase 1 (CBR1)." Fitoterapia 101 (March 2015): 51–56. http://dx.doi.org/10.1016/j.fitote.2014.12.010.

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12

Gonzalez-Covarrubias, Vanessa, Jianping Zhang, James L. Kalabus, Mary V. Relling, and Javier G. Blanco. "Pharmacogenetics of Human Carbonyl Reductase 1 (CBR1) in Livers from Black and White Donors." Drug Metabolism and Disposition 37, no. 2 (2008): 400–407. http://dx.doi.org/10.1124/dmd.108.024547.

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13

Jang, Miran, and Sung Soo Kim. "Inhibition of Carbonyl Reductase 1(CBR1) Enhances Arsenic Trioxide-mediated Apoptosis in Leukemia Cells." Free Radical Biology and Medicine 49 (January 2010): S63. http://dx.doi.org/10.1016/j.freeradbiomed.2010.10.148.

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Quiñones-Lombraña, Adolfo, Qiuying Cheng, Daniel C. Ferguson, and Javier G. Blanco. "Transcriptional regulation of the canine carbonyl reductase 1 gene ( cbr1 ) by the specificity protein 1 (Sp1)." Gene 592, no. 1 (2016): 209–14. http://dx.doi.org/10.1016/j.gene.2016.08.005.

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15

Gonzalez-Covarrubias, Vanessa, James L. Kalabus, and Javier G. Blanco. "Inhibition of Polymorphic Human Carbonyl Reductase 1 (CBR1) by the Cardioprotectant Flavonoid 7-monohydroxyethyl Rutoside (monoHER)." Pharmaceutical Research 25, no. 7 (2008): 1730–34. http://dx.doi.org/10.1007/s11095-008-9592-5.

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16

Cheng, Q., C. Sanborn, D. Ferguson, and J. G. Blanco. "Short Communication DNA sequence variants in the carbonyl reductase 1 (cbr1) gene in seven breeds of Canis lupus familiaris." Genetics and Molecular Research 11, no. 2 (2012): 1109–16. http://dx.doi.org/10.4238/2012.april.27.10.

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Gonzalez-Covarrubias, Vanessa, Debashis Ghosh, Sukhwinder S. Lakhman, Lakshmi Pendyala, and Javier G. Blanco. "A Functional Genetic Polymorphism on Human Carbonyl Reductase 1 (CBR1 V88I) Impacts on Catalytic Activity and NADPH Binding Affinity." Drug Metabolism and Disposition 35, no. 6 (2007): 973–80. http://dx.doi.org/10.1124/dmd.107.014779.

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18

Kalabus, James L., Qiuying Cheng, and Javier G. Blanco. "MicroRNAs Differentially Regulate Carbonyl Reductase 1 (CBR1) Gene Expression Dependent on the Allele Status of the Common Polymorphic Variant rs9024." PLoS ONE 7, no. 11 (2012): e48622. http://dx.doi.org/10.1371/journal.pone.0048622.

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Lakhman, Sukhwinder S., Xiaomin Chen, Vanessa Gonzalez-Covarrubias, Erin G. Schuetz, and Javier G. Blanco. "Functional Characterization of the Promoter of Human Carbonyl Reductase 1 (CBR1). Role of XRE Elements in Mediating the Induction of CBR1 by Ligands of the Aryl Hydrocarbon Receptor." Molecular Pharmacology 72, no. 3 (2007): 734–43. http://dx.doi.org/10.1124/mol.107.035550.

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Seliger, Jan Moritz, Hans-Jörg Martin, Edmund Maser, and Jan Hintzpeter. "Potent inhibition of human carbonyl reductase 1 (CBR1) by the prenylated chalconoid xanthohumol and its related prenylflavonoids isoxanthohumol and 8-prenylnaringenin." Chemico-Biological Interactions 305 (May 2019): 156–62. http://dx.doi.org/10.1016/j.cbi.2019.02.031.

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21

Jordheim, Lars-Petter, Vincent Ribrag, Herve Ghesquieres, et al. "Single Nucleotide Polymorphisms in ABCB1 and CBR1 Predict Toxicity to R-CHOP Type Regimens in Patients with Diffuse Non Hodgkin's Lymphoma." Blood 120, no. 21 (2012): 1616. http://dx.doi.org/10.1182/blood.v120.21.1616.1616.

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Abstract Abstract 1616 We analyzed single nucleotide polymorphisms (SNPs) in patients with diffuse large B-cell lymphoma treated in the prospective GELA LNH 2003 studies. Peripheral blood DNA samples collected at diagnosis before chemotherapy were obtained from 760 patients (among a total of 1367 accrued) including 441 randomized to received R-CHOP or modified R-CHOP (LNH 03–7B) and 319 who received R-ACVBP. The median age was 59 years (range 18–93) and there were 441 males and 319 females. 429 were IPI 0–2 (56.4%) and 331 were IPI 3–5 (43.6%). 119 patients had an ECOG performance status >1

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Kalabus, James L., Qiuying Cheng, Raqeeb G. Jamil, Erin G. Schuetz, and Javier G. Blanco. "Induction of carbonyl reductase 1 (CBR1) expression in human lung tissues and lung cancer cells by the cigarette smoke constituent benzo[a]pyrene." Toxicology Letters 211, no. 3 (2012): 266–73. http://dx.doi.org/10.1016/j.toxlet.2012.04.006.

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23

Docherty, Anna R., Arden Moscati, Tim B. Bigdeli, et al. "Pathway-based polygene risk for severe depression implicates drug metabolism in CONVERGE." Psychological Medicine 50, no. 5 (2019): 793–98. http://dx.doi.org/10.1017/s0033291719000618.

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AbstractBackgroundThe Psychiatric Genomics Consortium (PGC) has made major advances in the molecular etiology of MDD, confirming that MDD is highly polygenic. Pathway enrichment results from PGC meta-analyses can also be used to help inform molecular drug targets. Prior to any knowledge of molecular biomarkers for MDD, drugs targeting molecular pathways (MPs) proved successful in treating MDD. It is possible that examining polygenicity within specific MPs implicated in MDD can further refine molecular drug targets.MethodsUsing a large case–control GWAS based on low-coverage whole genome sequen

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24

Fan, L., J. Y. Guo, C. I. Wong, et al. "Genetic variants in human carbonyl reductase 3 (CBR3) and their influence on doxorubicin pharmacokinetics in Asian breast cancer patients." Journal of Clinical Oncology 25, no. 18_suppl (2007): 2505. http://dx.doi.org/10.1200/jco.2007.25.18_suppl.2505.

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2505 Background: Human carbonyl reductase 3 (CBR3) is one of the main metabolizing enzymes to extensively reduce doxorubicin to its major active metabolite, doxorubicinol in normal and tumor tissues. Recently, the CBR3 958G>A (V244M) genetic variant has been described to alter function in vitro. We postulate that CBR3 genetic variants could contribute to the inter-individual variability of doxorubicin pharmacokinetics in breast cancer patients. Methods: We studied 101 female breast cancer patients (66 Chinese, 26 Malay, 7 Indian and 2 of other ethnic origins) who were treated with doxorubic

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25

Santana, Sanzio, Thassila Nogueira Pitanga, Jeanne Machado de Santana, et al. "Hydroxyurea Exhibits Antioxidant Activity Via the Nrf2 Pathway- Antioxidant/Electrophile Response Element Regulated By p62/ SQSTM1." Blood 132, Supplement 1 (2018): 3648. http://dx.doi.org/10.1182/blood-2018-99-117220.

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Abstract Introduction: The pathophysiology of sickle cell anemia (HF) is characterized by hemolytic and intermittent vasoconstrictive events with increased redox status in the vascular microenvironment that favors the chronic inflammation. Objectives: To investigate whether hydroxyurea (HU) acts in the inhibition/minimization of reactive oxygen/nitrogen species (ROS/RNS) and in the modulation of in vitro the antioxidant genes expression. Methods: DPPH (1,1-diphenyl-2-picrylhydrazyl) radical scavenging assay was performed to determine the antioxidant activity of HU using L-ascorbate (L-Asc) and

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26

Budik, S., I. Walter, R. Ertl, and C. Aurich. "Detection of Carbonyl Reductase-1 (CBR-1) enzyme in pre-implantation equine conceptuses and its putative role in embryo mobility." Journal of Equine Veterinary Science 89 (June 2020): 103065. http://dx.doi.org/10.1016/j.jevs.2020.103065.

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27

Zhou, Yumin, Man Wang, Weiyan Yang, et al. "Environmental and Genetic Factors in the Pathogenesis of COPD in the Road-Working Population." Disease Markers 2021 (April 29, 2021): 1–10. http://dx.doi.org/10.1155/2021/9953234.

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Background. Chronic obstructive pulmonary disease (COPD) is a typical heterogeneous condition caused by environmental and genetic risk factors. Objectives. We investigated extrinsic (environmental) and intrinsic (genetic) factors contributing to the development of COPD in a nonsmoker road-working population in Northeast China. Method. The target population was divided into a COPD group and an exposed control group. Another healthy nonroad working nonsmoker control group was also included for environmental factor comparison. Peripheral blood was collected and analyzed using inductively coupled

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Gaudy, Allison, Gerald J. Fetterly, Alex A. Adjei, et al. "Investigation of the pharmacogenetic influences of carbonyl reductase on doxorubicin and doxorubicinol in breast cancer patients." Journal of Clinical Oncology 31, no. 15_suppl (2013): 2594. http://dx.doi.org/10.1200/jco.2013.31.15_suppl.2594.

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2594 Background: The anthracycline doxorubicin (DOX) is widely used to treat breast cancer. Doxorubicin is associated with pharmacokinetic and pharmacodynamic variability and despite its use for several years there is limited understanding behind it. Hepatic carbonyl reductases (CBR1 and CBR3) catalyze the reduction of DOX into its main circulating C-13 metabolite doxorubicinol (DOXOL). Polymorphisms in CBR1 and CBR3 influence synthesis of DOXOL, and could potentially play a role in the pharmacokinetic (PK) variability seen with doxorubicin treatment. In this study, we examined the influence o

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Elsayed, Abdelrahman H., Huiyun Wu, Xueyuan Cao, et al. "A 5-Gene Ara-C, Daunorubicin and Etoposide (ADE) Drug Response Score As a Prognostic Tool to Predict AML Treatment Outcome." Blood 134, Supplement_1 (2019): 1429. http://dx.doi.org/10.1182/blood-2019-128787.

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Introduction: Cytarabine, daunorubicin and etoposide (ADE) are commonly used for remission and intensification of pediatric acute myeloid leukemia (AML). However, development of drug resistance is a major cause of treatment failure. In this study, we performed a comprehensive evaluation of expression levels of genes of pharmacological significance (pharmacokinetic /pharmacodynamic) to ADE and derived a drug response score predictive of treatment outcomes in pediatric AML patients. Methods: This study included 163 cases (median age=8.79 year, range= (0.013-21.1)) with AML enrolled in the multic

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Larkin, Trisha, Abdelrahman H. Elsayed, Roya Rafiee, et al. "Identification of Pharmacogenomic Single Nucleotide Polymorphism Variants As Contributors to Toxicity Phenotype in the Treatment of Acute Childhood Leukemia." Blood 136, Supplement 1 (2020): 25–26. http://dx.doi.org/10.1182/blood-2020-143195.

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Introduction: Despite more than 80% long-term survival in acute lymphoblastic leukemia (ALL), morbidity due to drug-related toxicities remains high. Treatment interruptions and omissions from these toxicities may affect survivorship outcomes and morbidities in pediatric cancer. Although multiple factors contribute to a patient's risk of toxicity pharmacogenetic factors have been shown to play critical roles. Genetic variation within genes involved in pharmacokinetic and pharmacodynamic pathways of chemotherapies can influence gene expression and/or activity resulting in inter-patient variation

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31

Bateman, Raynard L., Daniel Rauh, Brandon Tavshanjian, and Kevan M. Shokat. "Human Carbonyl Reductase 1 Is anS-Nitrosoglutathione Reductase." Journal of Biological Chemistry 283, no. 51 (2008): 35756–62. http://dx.doi.org/10.1074/jbc.m807125200.

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32

Miura, Takeshi, Toru Nishinaka, and Tomoyuki Terada. "Different functions between human monomeric carbonyl reductase 3 and carbonyl reductase 1." Molecular and Cellular Biochemistry 315, no. 1-2 (2008): 113–21. http://dx.doi.org/10.1007/s11010-008-9794-5.

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Aplenc, R., J. Blanco, W. Leisenring, et al. "Polymorphisms in candidate genes in patients with congestive heart failure (CHF) after childhood cancer: A Report from the Childhood Cancer Survivor Study (CCSS)." Journal of Clinical Oncology 24, no. 18_suppl (2006): 9004. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.9004.

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9004 Background: In cancer survivors, CHF associated with the use of anthracyclines is an important clinical complication. Risk factors for anthracycline associated cardiac toxicity, including cumulative dose, gender, and age, have been described. However, these risk factors do not fully explain the observed clinical variability. Notably, the potential role of genetic risk factors has not been studied. A recent “unifying hypothesis” postulates that the early cardiac damage is mediated mostly by oxidative stress while the more chronic type of toxicity is induced by anthracycline alcohol metabol

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34

Wayne, Laura L., and John Browse. "Homologous electron transport components fail to increase fatty acid hydroxylation in transgenic Arabidopsis thaliana." F1000Research 2 (October 4, 2013): 203. http://dx.doi.org/10.12688/f1000research.2-203.v1.

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Ricinoleic acid, a hydroxylated fatty acid (HFA) present in castor (Ricinus communis) seeds, is an important industrial commodity used in products ranging from inks and paints to polymers and fuels. However, due to the deadly toxin ricin and allergens also present in castor, it would be advantageous to produce ricinoleic acid in a different agricultural crop. Unfortunately, repeated efforts at heterologous expression of the castor fatty acid hydroxylase (RcFAH12) in the model plant Arabidopsis thaliana have produced only 17-19% HFA in the seed triacylglycerols (TAG), whereas castor seeds accum

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Wayne, Laura L., and John Browse. "Homologous electron transport components fail to increase fatty acid hydroxylation in transgenic Arabidopsis thaliana." F1000Research 2 (November 13, 2013): 203. http://dx.doi.org/10.12688/f1000research.2-203.v2.

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Ricinoleic acid, a hydroxylated fatty acid (HFA) present in castor (Ricinus communis) seeds, is an important industrial commodity used in products ranging from inks and paints to polymers and fuels. However, due to the deadly toxin ricin and allergens also present in castor, it would be advantageous to produce ricinoleic acid in a different agricultural crop. Unfortunately, repeated efforts at heterologous expression of the castor fatty acid hydroxylase (RcFAH12) in the model plant Arabidopsis thaliana have produced only 17-19% HFA in the seed triacylglycerols (TAG), whereas castor seeds accum

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Boušová, Iva, Lenka Skálová, Pavel Souček, and Petra Matoušková. "The modulation of carbonyl reductase 1 by polyphenols." Drug Metabolism Reviews 47, no. 4 (2015): 520–33. http://dx.doi.org/10.3109/03602532.2015.1089885.

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Carlquist, Magnus, Torbjörn Frejd, and Marie F. Gorwa-Grauslund. "Flavonoids as inhibitors of human carbonyl reductase 1." Chemico-Biological Interactions 174, no. 2 (2008): 98–108. http://dx.doi.org/10.1016/j.cbi.2008.05.021.

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Kassner, Nina, Klaus Huse, Hans-Jörg Martin, et al. "Carbonyl Reductase 1 Is a Predominant Doxorubicin Reductase in the Human Liver." Drug Metabolism and Disposition 36, no. 10 (2008): 2113–20. http://dx.doi.org/10.1124/dmd.108.022251.

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Tang, Xianqing, Peiqiang Mu, Jun Wu, et al. "Carbonyl Reduction of Mequindox by Chicken and Porcine Cytosol and Cloned Carbonyl Reductase 1." Drug Metabolism and Disposition 40, no. 4 (2012): 788–95. http://dx.doi.org/10.1124/dmd.111.043547.

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Moschini, Roberta, Rossella Rotondo, Giovanni Renzone, et al. "Kinetic features of carbonyl reductase 1 acting on glutathionylated aldehydes." Chemico-Biological Interactions 276 (October 2017): 127–32. http://dx.doi.org/10.1016/j.cbi.2017.03.003.

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41

Shi, Sophia M., and Li Di. "The role of carbonyl reductase 1 in drug discovery and development." Expert Opinion on Drug Metabolism & Toxicology 13, no. 8 (2017): 859–70. http://dx.doi.org/10.1080/17425255.2017.1356820.

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42

Varatharajan, Savitha, Ajay Abraham, Wei Zhang, et al. "Carbonyl reductase 1 expression influences daunorubicin metabolism in acute myeloid leukemia." European Journal of Clinical Pharmacology 68, no. 12 (2012): 1577–86. http://dx.doi.org/10.1007/s00228-012-1291-9.

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43

Ramsden, Diane, Dustin Smith, Raquel Arenas, Kosea Frederick, and Matthew A. Cerny. "Identification and Characterization of a Selective Human Carbonyl Reductase 1 Substrate." Drug Metabolism and Disposition 46, no. 10 (2018): 1434–40. http://dx.doi.org/10.1124/dmd.118.082487.

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44

Moschini, Roberta, Giovanni Renzone, Vito Barracco, et al. "A new role for Carbonyl Reductase 1 on 4-hydroxynonenal detoxification." Free Radical Biology and Medicine 124 (August 2018): 572. http://dx.doi.org/10.1016/j.freeradbiomed.2018.05.047.

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45

Hintzpeter, Jan, Jan Hornung, Bettina Ebert, Hans-Jörg Martin, and Edmund Maser. "Curcumin is a tight-binding inhibitor of the most efficient human daunorubicin reductase – Carbonyl reductase 1." Chemico-Biological Interactions 234 (June 2015): 162–68. http://dx.doi.org/10.1016/j.cbi.2014.12.019.

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46

Barracco, Vito, Roberta Moschini, Giovanni Renzone, et al. "Dehydrogenase/reductase activity of human carbonyl reductase 1 with NADP(H) acting as a prosthetic group." Biochemical and Biophysical Research Communications 522, no. 1 (2020): 259–63. http://dx.doi.org/10.1016/j.bbrc.2019.11.090.

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47

Biswas, Md Sanaullah, Ryota Terada, and Jun’ichi Mano. "Inactivation of Carbonyl-Detoxifying Enzymes by H2O2 Is a Trigger to Increase Carbonyl Load for Initiating Programmed Cell Death in Plants." Antioxidants 9, no. 2 (2020): 141. http://dx.doi.org/10.3390/antiox9020141.

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H2O2-induced programmed cell death (PCD) of tobacco Bright Yellow-2 (BY-2) cells is mediated by reactive carbonyl species (RCS), degradation products of lipid peroxides, which activate caspase-3-like protease (C3LP). Here, we investigated the mechanism of RCS accumulation in the H2O2-induced PCD of BY-2 cells. The following biochemical changes were observed in 10-min response to a lethal dose (1.0 mM) of H2O2, but they did not occur in a sublethal dose (0.5 mM) of H2O2. (1) The C3LP activity was increased twofold. (2) The intracellular levels of RCS, i.e., 4-hydroxy-(E)-hexenal and 4-hydroxy-(

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Alshogran, Osama, Bradley Urquhart, and Thomas Nolin. "Downregulation of Hepatic Carbonyl Reductase Type 1 in End-Stage Renal Disease." Drug Metabolism Letters 9, no. 2 (2015): 111–18. http://dx.doi.org/10.2174/1872312809666150818111626.

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Lu, Yuan, Wen Liu, Ting Lv, et al. "Aidi injection reduces doxorubicin-induced cardiotoxicity by inhibiting carbonyl reductase 1 expression." Pharmaceutical Biology 60, no. 1 (2022): 1616–24. http://dx.doi.org/10.1080/13880209.2022.2110127.

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OSAWA, YUKI, YOSHIHITO YOKOYAMA, TATSUHIKO SHIGETO, MASAYUKI FUTAGAMI, and HIDEKI MIZUNUMA. "Decreased expression of carbonyl reductase 1 promotes ovarian cancer growth and proliferation." International Journal of Oncology 46, no. 3 (2014): 1252–58. http://dx.doi.org/10.3892/ijo.2014.2810.

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