4 edition of Bioactivation of doxorubicin by human NADPH-cytochrome P450 reductase found in the catalog.
Bioactivation of doxorubicin by human NADPH-cytochrome P450 reductase
Thesis (M.Sc.) -- University of Toronto, 1998.
|Series||Canadian theses = -- Thèses canadiennes|
|The Physical Object|
|Pagination||2 microfiches : negative. --|
The reductive activation of the antitumor drug RH1 to its semiquinone free radical by NADPH cytochrome P reductase and by HCT human colon cancer cells October Free Radical Research 40(9. Up-Regulation of Carbonyl Reductase 1 Renders Development of Doxorubicin Resistance in Human Gastrointestinal Cancers Cellular reductases such as cytochrome P reductase 4) Metzger A, Meineke I, Brockmöller J, Klein K, Zanger UM, Maser E, Wojnowski L. Carbonyl reductase 1 is a predominant doxorubicin reductase in the human by: 8.
Nitric oxide synthases (NOSs) play a crucial role in the control of blood flow, memory formation, and the immune response. These proteins can be structurally divided into oxygenase and reductase domains. The reductase domain shares a high degree of sequence homology with P reductase, which is thought to be the major enzyme responsible for the one-electron reduction of Cited by: Drug metabolism is the metabolic breakdown of drugs by living organisms, usually through specialized enzymatic systems. More generally, xenobiotic metabolism (from the Greek xenos "stranger" and biotic "related to living beings") is the set of metabolic pathways that modify the chemical structure of xenobiotics, which are compounds foreign to an organism's normal biochemistry, such as any drug.
Whilst non-parenchymal liver cells may play a role in catalysing Pmediated bioactivation of ellipticine in HRN and HBRN mice, the presence of ellipticine-DNA adducts in the livers of HRN and HBRN mice suggests the involvement of a Pindependent bioactivation by: 1. A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P monooxygenases (e.g. EC , unspecific monooxygenase) by stabilizing the one-electron reduced form of .
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Doxorubicin (DOX) is a useful antineopIastic dmg with multiple mechanisms of cytotoxicity. One such mechanism involves the reductive bioactivation of the quinone ring to a semi-quinone radical, and subsequent redox-cycling.
It is known that rat NADPH- cytochrome P reductase (CYPRED) catdyzes DOX reduction and sensitizes humanAuthor: Shairoj Ramji. We hypothesized that human NADPH-cytochrome P reductase (CYPRED) catalyzes doxorubicin reduction and that overexpression of this enzyme sensitizes human breast cancer cell lines to the aerobic cytotoxicity of doxorubicin.
cDNA-expressed human CYPRED catalyzed doxorubicin reduction, measured as the rate of doxorubicin-stimulated NADPH by: We hypothesized that human NADPH-cytochrome p reductase (CYPRED) catalyzes doxorubicin reduction and that overexpression of this enzyme sensitizes human breast cancer cell lines to.
Doxorubicin is a useful antineoplastic drug with multiple mechanisms of cytotoxicity. One such mechanism involves the reductive bioactivation of the quinone ring to a semiquinone radical, which can exert direct toxic effects and/or undergo redox cycling.
We hypothesized that human NADPH-cytochrome P reductase (CYPRED) catalyzes doxorubicinCited by: One electron bioactivation caused by the NADPH‐cytochrome P‐ reductase (P‐ reductase) is responsible for the toxic effect of the cytostatic, doxorubicin, and the herbicide, paraquat.
Although the target organs for these compounds are different, the mechanism of toxicity is the by: Ramji S, Lee C, Inaba T, Patterson AV, Riddick DS () Human NADPH-cytochrome p reductase overexpression does not enhance the aerobic cytotoxicity of doxorubicin in human breast cancer cell lines.
Cancer Res – View Article PubMed/NCBI Google Scholar Human cytochrome P (P) Family 4 enzymes are involved in the metabolism of fatty acids and the bioactivation of carcinogenic arylamines and toxic natural products, e.g.
4-ipomeanol. We evaluated the role of hepatic versus extra-hepatic metabolism of ellipticine, using the HRN (Hepatic Cytochrome P Reductase Null) mouse model, in which cytochrome P oxidoreductase (POR) is deleted in hepatocytes, resulting in the loss of essentially all hepatic CYP by: Request PDF | Role of hepatic cytochromes P in bioactivation of the anticancer drug ellipticine: Studies with the hepatic NADPH: Cytochrome P reductase null mouse | Ellipticine is an.
Comparison of in Vitro Bioactivation of Flutamide and Its Cyano Analogue: Evidence for Reductive Activation by Human NADPH:Cytochrome P Reductase Article Jan The cytochrome P (P) enzymes first attracted interest because of their relevance to the metabolism of drugs, steroids, and carcinogens.
Collectively, the 57 human Cited by: Cytochrome P Structure, Mechanism, and Biochemistry, third edition is a revision of a review that summarizes the current state of research in the field of drug metabolism.
The emphasis is on structure, mechanism, biochemistry, and regulation. Coverage is interdisciplinary, ranging from bioinorganic chemistry of cytochrome P to its relevance in human medicine. International Journal of Molecular Sciences, an international, peer-reviewed Open Access journal.
Drug Metabolism, Bioactivation and Biodiversity NADPH-cytochrome P reductase (CPR) is the unique redox partner of microsomal cytochrome Ps (CYPs). Treatment of MCF-7 cells with doxorubicin in the presence of purified rat NADPH cytochrome P reductase (Pred) and NADPH resulted in a marked enhancement of drug by: Based on immunoblot analysis and NADPH-cytochrome c reductase activity experiments, we have estimated the content of NADPH-cytochrome P reductase to represent between and % of aortic microsomal protein.
The content of NADPH-cytochrome P reductase in aortic microsomes appears to be 5- to fold less than that found in hepatic microsomes, as determined by immunoblot Cited by: In our recent study, we have evidenced the important role of bioreductive activation of DOX by exogenously added NADPH cytochrome P reductase (CPR) from human liver and NADPH in cytotoxic activity against human promyelocytic sensitive leukaemia HL60 cell line as well as its MDR sublines exhibiting two different phenotypes of MDR related to the overexpression of P-glycoprotein Cited by: MDA breast cancer cells were transfected with the cDNA for human PR and stable clones were isolated.
These high PR-expressing clones were used to determine the aerobic and hypoxic toxicity of EO9 and the two analogues that lacked functionality at either C-2 or CCited by: Flutamide (FLU), a nonsteroidal antiandrogen drug widely used in the treatment of prostate cancer, has been associated with idiosyncratic hepatotoxicity in patients.
It is proposed that bioactivation of FLU and subsequent binding of reactive metabolite(s) to cellular proteins play a causative role.
A toxicogenomic study comparing FLU and its nitro to cyano analogue (CYA) showed that the Cited by: Deletion of the NADPH-cytochrome P reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity Cheng Fang, Jun Gu, Fang Xie, Melissa Behr, Weizhu Yang, E.
Dale Abel, and Xinxin DingCited by: Cytochrome P Oxidoreductase Influences CYP2B6 Activity in Cyclophosphamide Bioactivation.
Competing Interests: The authors assure that Dr. Ylva Terelius, who is employed at Department of Discovery Research, Medivir AB, Huddinge, Sweden, has no conflict of interest in the present by:.
Microsomal cytochrome P (CYP) metabolism requires a coupled supply of electrons, which are donated by the auxiliary protein NADPH cytochrome P oxidoreductase (CPR).
CPR, encoded by the POR gene, is a ~kDa electron-transferring diflavin enzyme anchored to the membrane of the endoplasmic reticulum [ 1 ].Cited by: 1.It also plays a critical role in the bioactivation and detoxification of one-electron acceptors such as the therapeutically important anticancer agents mitomicin c and tirapazepine.
I identified a novel NADPH-dependent flavin reductase in C. elegans (FRE-1) with high similarity to cytochrome P reductase and the nitric oxide synthases (NOS).Author: Dorota Anna Kwasnicka.NADPH-cytochrome P reductase (CPR) is the unique redox partner of microsomal cytochrome Ps (CYPs).
CPR exists in a conformational equilibrium between open and closed conformations throughout its electron transfer (ET) function.
Previously, we have shown that electrostatic and flexibility properties of the hinge segment of CPR are critical for ET. Three mutants of human CPR were Cited by: 1.