Relevant bibliographies by topics / Carbonyl reductase 1 (CBR1)

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

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Published: 14 March 2023

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

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Varatharajan, Savitha, Ajay Abraham, Shaji R. Velayudhan, Rayaz Ahmed, Aby Abraham, Biju George, Mammen Chandy, Alok Srivastava, Vikram Mathews, and Poonkuzhali Balasubramanian. "Carbonyl Reductase 1 Expression and Polymorphisms Influence Daunorubicin Metabolism in AML." Blood 118, no. 21 (November 18, 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 expression of Dnr metabolising enzymes (CBR1 and CBR3) on the in vitro cytotoxicity of Dnr in primary AML cells and ii) effect of Single nucleotide polymorphisms (SNPs) in CBR1 and CBR3 on the plasma pharmacokinetics of Dnr and Daunorubicinol (DOL) in AML patients. Ninety patients with AML (excluding AML-M3) at diagnosis before the initiation of therapy were included. Bone marrow (BM) was collected at diagnosis and blast percentage in our cohort of patients ranged from 20–100%. Mononuclear cells (MNCs) were isolated by density gradient centrifugation. Total RNA was extracted from BMMNCs and cDNA was prepared. CBR1 and CBR3 mRNA expression was measured using Taqman based quantitative RT-PCR normalized to GAPDH. In-vitro cytotoxicity of Dnr was determined by MTT cell viability assay. Intracellular levels of Dnr and DOL was estimated by HPLC coupled with Fluorescence detector (FD). SNPs in CBR1 and CBR3 were screened by PCR followed by sequencing. In addition, plasma samples during Dnr infusion was collected at 0, 1, 2, 4, 6 and 24hrs from 24 of the 90 AML patients. Levels of Dnr and DOL in the plasma samples were estimated by HPLC coupled with FD and Area under Curve (AUC) for Dnr and DOL were calculated. CBR1 (range: 0.02–253.15) and CBR3 (range: 8.24– 29296.67) mRNA expression showed wide inter-individual variation. Intracellular levels of Dnr (range: 17.98–1718ng/3×106cells) and DOL (range: 2.76–62.07ng/3×106cells) showed 95 and 22 fold variation respectively. IC50 of Dnr in these samples ranged from 0.05 to 3.15 μM. Based on the IC50, samples were categorized as sensitive (IC50<0.5μM), intermediate (IC50: 0.5–1.0μM) and resistant (IC50>1.0μM) to Dnr. CBR1 expression was significantly higher in resistant samples (median-102.99: range: 7.18–253.15) compared to intermediate (median- 29.73: range: 0.02–224.23) and sensitive samples (median-18.67: range: 0.34–105.40 p=0.0154) [Figure 1]. In addition, significant correlation between CBR1 expression and intracellular DOL levels was observed (r= 0.52; p<0.0001), as samples with higher CBR1 expression had increased DOL levels. CBR3 expression did not show any significant association with invitro cytotoxicity or intracellular DOL levels. Five SNPs in CBR1 and 3 in CBR3 were identified. CBR1 SNPs, rs20572, rs9024 and rs25678 were in complete linkage disequilibrium (LD). Variant of rs25678 and rs20572/rs9024 had an allelic frequency of 0.244 and 0.20 respectively. Among CBR3 SNPs, variants of two non-synonymous polymorphisms rs8133502 and rs1056892 showed allelic frequency of 0.31 and 0.51 respectively. AUC of Dnr and DOL in plasma samples ranged from 22–2474ng*h/ml and 37–2027 ng*h/ml respectively while clearance of Dnr ranged from 0.04 to 3.34 L/h. Plasma DOL AUC, unlike in vitro intracellular DOL, did not show any significant association with CBR1 and CBR3 expression. In patients with variant rs25678 genotype, Dnr AUC was higher and clearance was lower compared to the wild type genotype, reaching a trend to statistical significance (p=0.0537 and 0.1184 for Dnr AUC and clearance). Influence of Dnr and DOL plasma levels on clinical outcome, if any, remains to be evaluated. This is the first report showing the influence of CBR1 and CBR3 in in-vitro cytotoxicity of Dnr and role of SNPs in CBR1 and CBR3 in plasma pharmacokinetics of Dnr in AML patients. To conclude, higher expression of CBR1 confers resistance to Dnr in primary AML cells and polymorphisms of this gene may influence the pharmacokinetics of Dnr. Disclosures: No relevant conflicts of interest to declare.
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Blanco, Javier G., Can-Lan Sun, Wendy Landier, Lu Chen, Diego Esparza-Duran, Wendy Leisenring, Allison Mays, 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 (May 1, 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 follow-up, and race/ethnicity) using conditional logistic regression techniques. Results A dose-dependent association was observed between cumulative anthracycline exposure and cardiomyopathy risk (0 mg/m2: reference; 1 to 100 mg/m2: odds ratio [OR], 1.65; 101 to 150 mg/m2: OR, 3.85; 151 to 200 mg/m2: OR, 3.69; 201 to 250 mg/m2: OR, 7.23; 251 to 300 mg/m2: OR, 23.47; > 300 mg/m2: OR, 27.59; Ptrend < .001). Among individuals carrying the variant A allele (CBR1:GA/AA and/or CBR3:GA/AA), exposure to low- to moderate-dose anthracyclines (1 to 250 mg/m2) did not increase the risk of cardiomyopathy. Among individuals with CBR3 V244M homozygous G genotypes (CBR3:GG), exposure to low- to moderate-dose anthracyclines increased cardiomyopathy risk when compared with individuals with CBR3:GA/AA genotypes unexposed to anthracyclines (OR, 5.48; P = .003), as well as exposed to low- to moderate-dose anthracyclines (OR, 3.30; P = .006). High-dose anthracyclines (> 250 mg/m2) were associated with increased cardiomyopathy risk, irrespective of CBR genotype status. Conclusion This study demonstrates increased anthracycline-related cardiomyopathy risk at doses as low as 101 to 150 mg/m2. Homozygosis for G allele in CBR3 contributes to increased cardiomyopathy risk associated with low- to moderate-dose anthracyclines, such that there seems to be no safe dose for patients homozygous for the CBR3 V244M G allele. These results suggest a need for targeted intervention for those at increased risk of cardiomyopathy.
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Hu, Dawei, Namiki Miyagi, Yuki Arai, Hiroaki Oguri, Takeshi Miura, Toru Nishinaka, Tomoyuki Terada, 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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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 determined using immunoblotting. Remarkable age-related decrease in specific activities of CYP2B, CYP3A, and UDP-glucuronosyl transferase was observed, whereas no changes in activities of CYP1A2, flavine monooxygenase, aldo-keto reductase 1C, and antioxidant enzymes with advancing age were found. On the other hand, specific activity of CBR1 and GST was 2.4 folds and 5.6 folds higher in the senescent rats compared with the young ones, respectively. Interindividual variability in CBR1 activity increased significantly with rising age. We suppose that elevated activities of GST and CBR1 may protect senescent rats against xenobiotic as well as eobiotic electrophiles and reactive carbonyls, but they may alter metabolism of drugs, which are CBR1 and especially GSTs substrates.
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Bell, Rachel, Elisa Villalobos, Mark Nixon, Allende Miguelez-Crespo, Matthew Sharp, Martha Koerner, Emma Allan, 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 (May 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 which retains GR activity. CBR1 is abundant in adipose tissue and increased in obese adipose of mice and humans1 and increased Cbr1 expression is associated with increased fasting glucose1. We hypothesised that increased Cbr1/20β-DHB in obese adipose contributes to excessive GR activation and worsens glucose tolerance. We generated a novel murine model of adipose-specific Cbr1 over-expression (R26-Cbr1Adpq) by crossing conditional knock-in mice with Adiponectin-Cre mice. CBR1 protein and activity were doubled in subcutaneous adipose tissue of male and female R26-Cbr1Adpq mice compared with floxed controls; corresponding to a two-fold increase 20β-DHB (1.6 vs. 4.2ng/g adipose; P=0.0003; n=5-7/group). There were no differences in plasma 20β-DHB or corticosterone. Bodyweight, lean or fat mass, did not differ between male or female R26-Cbr1Adpq mice and floxed controls. Lean male R26-Cbr1Adpq mice had higher fasting glucose (9.5±0.3 vs. 8.4±0.3mmol/L; P=0.04) and worsened glucose tolerance (AUC 1819±66 vs. 1392±14; P=0.03). Female R26-Cbr1Adpq mice also had a worsened glucose tolerance but fasting glucose was not altered with genotype. There were no differences in fasting insulin or non-esterified fatty acid between genotypes in either sex. Expression of GR-induced genes Pnpla2, Gilz and Per1, were increased in adipose of R26-Cbr1Adpq mice. Following high-fat diet induced obesity, no differences in bodyweight, lean or fat mass, with genotype were observed in male and female mice, and genotype differences in fasting glucose and glucose tolerance were abolished. In conclusion, adipose-specific over-expression of Cbr1 in lean male and female mice led to increased levels of 20β-DHB in adipose but not plasma, and both sexes having worsened glucose tolerance. The influence of adipose CBR1/20β-DHB on glucose tolerance was not associated with altered fat mass or bodyweight and was attenuated by high-fat diet-induced obesity. These metabolic consequences of Cbr1 manipulation require careful consideration given the wide variation in CBR1 expression in the human population, the presence of inhibitors and enhancers in many foodstuffs and the proposed use of inhibitors as an adjunct for cancer treatment regimens. Reference: Morgan et al., Scientific Reports. 2017; 7.
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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 (September 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 converts PGE2 into PGF2α, and the PGE2/PGF2α ratios were investigated in porcine peri- and post-implantation conceptuses. Furthermore, expression of CBR1 was examined in the endometrium. PGHS-2 and mPGES-1 were upregulated, and PGHS-1, PGFS, and CBR1 were downregulated in conceptuses during trophoblastic elongation. A second increase of mPGES-1 mRNA occurred after days 20–21 of pregnancy. After initiation of implantation, expression of PGHS-1, PGFS, and CBR1 in conceptuses increased and remained higher until days 24–25 of pregnancy. Comparison of the endometrial CBR1 protein expression in cyclic and pregnant gilts revealed upregulation on days 16–17 of the cycle and downregulation on days 10–11 of pregnancy. In conclusion, reciprocal expression of PGHS-2, mPGES-1, PGFS, and CBR1 in day 10–13 conceptuses and decrease of endometrial CBR1 may be important in increasing the PGE2/PGF2α ratio during maternal recognition of pregnancy. This study indicates that PGE2 produced via PGHS-2 and mPGES-1 in conceptus may be involved in corpus luteum control. Moreover, high expression of conceptus PGHS-1, mPGES-1, PGFS, and CBR1 after initiation of implantation suggests their significant role in placentation.
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Guo, Chunming, Wangsheng Wang, Chao Liu, Leslie Myatt, and Kang Sun. "Induction of PGF2α Synthesis by Cortisol Through GR Dependent Induction of CBR1 in Human Amnion Fibroblasts." Endocrinology 155, no. 8 (August 1, 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 production in a concentration-dependent manner, in parallel with elevation of CBR1 levels. Either siRNA-mediated knockdown of glucocorticoid receptor (GR) expression or GR antagonist RU486 attenuated the induction of CBR1 by cortisol. Chromatin immunoprecipitation (ChIP) showed an increased enrichment of both GR and RNA polymerase II to CBR1 promoter. Knockdown of CBR1 expression with siRNA or inhibition of CBR1 activity with rutin decreased both basal and cortisol-stimulated PGF2α production in human amnion fibroblasts. In conclusion, CBR1 may play a critical role in PGF2α synthesis in human amnion fibroblasts, and cortisol promotes the conversion of PGE2 into PGF2α via GR-mediated induction of CBR1 in human amnion fibroblasts. This stimulatory effect of cortisol on CBR1 expression may partly explain the concurrent increases of cortisol and PGF2α in human amnion tissue with labor, and these findings may account for the increased production of PGF2α in the fetal membranes prior to the onset of labor.
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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 (April 27, 2015): 922–27. http://dx.doi.org/10.1124/dmd.115.064295.

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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 (April 6, 2018): 227–36. http://dx.doi.org/10.12991/mpj.2018.60.

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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 (February 2013): 126–35. http://dx.doi.org/10.1016/j.cbi.2012.11.023.

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Dissertations / Theses on the topic "Carbonyl reductase 1 (CBR1)"

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ROTONDO, ROSSELLA. "New enzymatic pathway(s) in 4-hydroxynonenal metabolism." Doctoral thesis, Università di Siena, 2017. http://hdl.handle.net/11365/1007903.

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The main effect of lipid peroxidation, which often occurs in response to oxidative stress, is the production of different toxic aldehydes. In particular, over the years, the lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE) has received much attention for its dual role in the pathogenesis of several diseases and as signaling molecule. HNE metabolism is reported to mainly occur through its conjugation with glutathione (GSH) and the subsequent formation of 3-glutathionyl-4-hydroxynonanal (GSHNE) [1, 2]. This molecule is susceptible to both oxidative and reductive transformations, which occur through the action of either the NADPH-dependent activity of aldose reductase (AKR1B1) [1] or through the NAD(P)+ -dependent activity of aldehyde dehydrogenase, respectively [3, 4]. Recently, we have demonstrated the implication of a new NADP+-dependent enzymatic activity able to oxidize GSHNE to its corresponding acid 3-glutathionyl-nonanoic-γ-lactone (GSHNA-γ-lactone) [5]. The enzyme was purified from a human astrocytoma cells line (ADF) to electrophoretic homogeneity as protein doublet in SDS-PAGE, with an apparent molecular weight of 31-32 kDa. Proteomic analysis identified both proteins as human CBR1, also known as NADP+ 15-hydroxyprostaglandine dehydrogenase with 74% of homology and proved their migration differences due to the occurrence of a carboxyethyl moiety at Lys239 [5]. This modification has been already described for the human enzyme and has been demonstrated to have no effect on the protein activity and specificity [6, 7]. The enzyme efficiently catalyzes the oxidation of GSHNE, while it is practically inactive towards 4-hydroxy trans-2-nonenal and other HNE-S-thiolated adducts containing an incomplete glutathionyl moiety [5]. Nucleotide sequence analysis of hCBR1 cDNA from ADF cells completely matched with the human wild type counterpart [5], excluding any gain-of-function mutations in the cDNA-derived protein sequence of hCBR1 [8, 9]. Highly purified human recombinant carbonyl reductase 1 (E.C. 1.1.1.184, hCBR1), which preserves its ability to oxidize specifically GSHNE, is also shown to efficiently act as aldehyde reductase on glutathionylated alkanals, namely 3-glutathionyl-4-hydroxynonanal (GSHNE), 3-glutathionyl-nonanal, 3-glutathionyl-hexanal and 3-glutathionyl-propanal [10]. The presence of the glutathionyl moiety appears as a necessary requirement for the susceptibility of these compounds to the NADPH-dependent reduction by hCBR1. In fact the corresponding alkanals and alkenals, and the cysteinyl and γ-glutamyl-cysteinyl alkanals adducts were either ineffective or very poorly active as CBR1 substrates [10]. Mass spectrometry analysis reveals the ability of hCBR1 to reduce GSHNE to the corresponding 3-glutathionyl-1,4-dihydroxynonane (GSDHN) and at the same time to catalyze the oxidation of the hemiacetal form of GSHNE, generating the 3-glutathionylnonanoic-γ-lactone. These data are indicative of the ability of the enzyme to catalyze a disproportion reaction of the substrate through the redox recycle of the pyridine cofactor [10]. A rationale for the observed preferential activity of hCBR1 on different GSHNE diastereoisomers is given by molecular modelling. These results evidence the potential of hCBR1 acting on GSHNE to accomplish a dual role, both in terms of HNE detoxification and, through the production of GSDHN, in terms of involvement into the signalling cascade of the cellular inflammatory response.
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Klafke, Jonatas Zeni. "Efeitos da Campomanesia xanthocarpa em parâmetros bioquímicos, hematológicos e de estresse oxidativo em pacientes hipercolestrolêmicos." Universidade Federal de Santa Maria, 2009. http://repositorio.ufsm.br/handle/1/11116.

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Conselho Nacional de Desenvolvimento Científico e Tecnológico
In Southern Brazil, the plant Campomanesia xanthocarpa Berg. (Myrtaceae), popularly known as guavirova , has been empirically used for its potential effect in reducing blood cholesterol levels. Since there are no scientific data confirming its popular use, the aim of the present study was to investigate the effect of C. xanthocarpa on biochemical, hematological, anthropometrical and oxidative stress parameters in hypercholesterolemic patients. Thirty three patients were selected according to total cholesterol (TC) levels: 200-240 mg/dL, undesirable level (UL), and >240 mg/dL, hypercholesterolemic level (HL). UL or HL patients were randomly divided into control group (CG), which received placebo capsules, and experimental group 250 (EG 250) or 500 (EG 500), which received either 250 or 500 mg of encapsulated C. xanthocarpa. All groups received a cholesterol restriction diet and capsules once a day. The biochemical (TC, triglycerides, HDL, LDL and VLDL), hematological (hematocrit and hemoglobin), anthropometrical (weight and abdominal circumference) and oxidative stress (protein carbonyl) parameters were measured before, 45 and 90 days after the treatment started. There was no alteration on biochemical, hematological, anthropometric or oxidative stress parameters in UL patients of all groups. However, a significant decrease in TC and LDL levels was observed in HL patients from EG 500 group (reduction of 28±3 and 45±4% to levels before treatment) in relation to CG group patients (reduction of 12±2 and 29±4%). Moreover, a significant reduction in oxidative stress was observed in HL patients of EG 250 (51±12%) and EG 500 groups (34±18%) when compared to levels before treatment. A positive correlation between plasma oxidative stress PC and TC levels was observed. Finally, was demonstrated that C. xanthocarpa extract possesses anti-oxidant properties and 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitory activity in vitro. Confirming its popular use, the treatment with C. xanthocarpa encapsulated reduced blood TC and LDL levels in hypercholesterolemic patients. Besides its effect on cholesterol levels, this plant reduced the oxidative stress in plasma of hypercholesterolemic patients as well.
No Sul do Brasil, a planta Campomanesia xanthocarpa Berg. (Myrtaceae), popularmente conhecida como guavirova , tem sido empiricamente usada por seu efeito potencial em reduzir os níveis de colesterol sanguíneo. Uma vez que não há dados científicos confirmando seu uso popular, o alvo do presente estudo foi investigar os efeitos da C. xanthocarpa nos parâmetros bioquímicos, hematológicos, antropométricos e de estresse oxidativo em pacientes hipercolesterolêmicos. Trinta e três pacientes foram selecionados de acordo com os níveis de colesterol total (CT): 200-240 mg/dL, níveis indesejáveis (NI), e > 240 mg/dL, níveis hipercolesterolêmicos (NH). Os pacientes NI e NH foram randomicamente divididos em grupo controle (GC), que recebeu cápsulas placebo, e grupo experimental 250 (GE 250) ou 500 (GE 500), que recebeu 250 ou 500 mg de C. xanthocarpa encapsulada. Todos os grupos receberam uma dieta com restrição a colesterol e cápsulas diariamente. Os parâmetros bioquímicos (CT, triacilgliceróis, HDL, LDL e VLDL), hematológicos (hematócrito e hemoglobina), antropométricos (peso e circunferência abdominal) e de estresse oxidativo (proteína carbonilada) foram mensurados antes, 45 e 90 dias depois do tratamento. Não houve nenhum alteração significativa nos parâmetros bioquímico, hematológico, antropométrico e de estresse oxidativo em pacientes NI de todos os grupos. Entretanto, uma redução significativa nos níveis de CT e LDL foi observada em pacientes NH do GE 500 (redução de 28±3 e 45±4% para os níveis antes do tratamento) em relação aos pacientes do GC (redução de 12±2 e 29±4%). Além disso, uma redução significante no estresse oxidativo foi observada em pacientes NH do GE 250 (51±12%) e GE 500 (34±18%) quando comparado com os níveis antes do tratamento. Uma correlação positiva entre os níveis de proteína carbonilada e CT foi observada. Finalmente, foi demonstrado que o extrato de C. xanthocarpa possui propriedade antioxidante e atividade inibitória da 3-hidroxi-3-metilglutaril coenzima A redutase in vitro. Confirmando seu uso popular, o tratamento com C. xanthocarpa reduziu os níveis de CT e LDL sanguíneos em pacientes hipercolesterolêmicos. Além dos seus efeitos nos níveis de colesterol, esta planta reduziu o estresse oxidativo no plasma de pacientes hipercolesterolêmicos.
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Gonzalez, Covarrubias Mirelle Vanessa. "Pharmacogenetics of human carbonyl reductase 1 (CBR1) in liver from black and white donors." 2008. http://proquest.umi.com/pqdweb?did=1597613551&sid=17&Fmt=2&clientId=39334&RQT=309&VName=PQD.

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Thesis (Ph.D.)--State University of New York at Buffalo, 2008.
Title from PDF title page (viewed on Feb. 11, 2009) Available through UMI ProQuest Digital Dissertations. Thesis adviser: Blanco, Javier G. Includes bibliographical references.
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Books on the topic "Carbonyl reductase 1 (CBR1)"

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Henry, Weiner, ed. Enzymology and molecular biology of carbonyl metabolism 10: Proceedings of the 10th Conference, Taos, New Mexico, July 1-5, 2000. Amsterdam: Elsevier, 2001.

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Geoffrey, Flynn T., Weiner Henry, and International Workshop on Aldehyde Dehydrogenase/Aldehyde Reductase/Alcohol Dehydrogenase (2nd : 1984 : Kingston, Ont.), eds. Enzymology of carbonyl metabolism 2: Aldehyde dehydrogenase, aldo-keto reductase, and alcohol dehydrogenase : proceedings of an international workshop, held in Kingston, Ontario, Canada, July 1-4, 1984. New York: A.R. Liss, 1985.

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Book chapters on the topic "Carbonyl reductase 1 (CBR1)"

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Schaller, Micheline, and Bendicht Wermuth. "Rat Carbonyl Reductase." In Advances in Experimental Medicine and Biology, 523–27. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4735-8_66.

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Mizoguchi, Tadashi, Hiroyuki Itabe, and Peter F. Kador. "Reactivity of Enzyme Modification Reagents with Aldose Reductase and Aldehyde Reductase." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 205–16. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_23.

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Wermuth, Bendicht. "Inhibition of Aldehyde Reductase by Carboxylic Acids." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 197–204. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_22.

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Nishimura, Chihiro, Yoshiharu Matsuura, Tsuyoshi Tanimoto, Takashi Yamaoka, Tai Akera, and T. Geoffrey Flynn. "cDNA Cloning and Expression of Human Aldose Reductase." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 119–27. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_15.

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Hohman, Thomas C., Deborah Carper, Sarmila Dasgupta, and Masayuki Kaneko. "Osmotic Stress Induces Aldose Reductase in Glomerular Endothelial Cells." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 139–52. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_17.

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Grimshaw, Charles E. "A Kinetic Perspective on the Peculiarity of Aldose Reductase." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 217–28. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_24.

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Wermuth, Bendicht. "Expression of Human and Rat Carbonyl Reductase in E. Coli." In Advances in Experimental Medicine and Biology, 203–9. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1965-2_26.

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Carper, Deborah, Sanai Sato, Susan Old, Stephen Chung, and Peter F. Kador. "In Vitro Expression of Human Placental Aldose Reductase in Escherichia Coli." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 129–38. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_16.

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Rondeau, Jean-Michel, Dino Moras, Frédérique Tête, Alberto Podjarny, Alain Van Dorsselaer, Jean-Marc Reymann, Patrick Barth, and Jean-François Biellmann. "Structural Studies of Pig Lens Aldose Reductase: Reversible Dimerization of the Enzyme." In Enzymology and Molecular Biology of Carbonyl Metabolism 3, 113–18. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5901-2_14.

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Maser, Edmund, and Udo C. T. Oppermann. "Molecular Cloning and Sequencing of Mouse Hepatic 11ß-Hydroxysteroid Dehydrogenase/Carbonyl Reductase." In Advances in Experimental Medicine and Biology, 211–21. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1965-2_27.

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Conference papers on the topic "Carbonyl reductase 1 (CBR1)"

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Marozkina, Nadzeya, W. G. Teague, Denise Thompson-Batt, Serpil C. Erzurum, and Benjamin Gaston. "Carbonyl Reductase 1 Expression And Activity Are Increased In Human Asthma." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2066.

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You might also be interested in the extended bibliographies on the topic 'Carbonyl reductase 1 (CBR1)' for particular source types:
Journal articles
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