Relevant bibliographies by topics / Cytochrome P450

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Cytochrome P450'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Cytochrome P450"

1

Bandiera, S. "Expression and catalysis of sex-specific cytochrome P450 isozymes in rat liver." Canadian Journal of Physiology and Pharmacology 68, no. 6 (June 1, 1990): 762–68. http://dx.doi.org/10.1139/y90-117.

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Research interest in the study of cytochromes P450 has recently been shifting to the characterization of "constitutively" expressed isozymes from that of the inducible forms. Several "constitutive" cytochrome P450 isozymes have been purified from rat liver including five immunochemically related proteins designated cytochromes P450f, P450g, P450h, P450i, and P450k. These hemoproteins have been identified as distinct isozymes on the basis of spectral, electrophoretic, and catalytic properties and NH2-terminal sequence analysis. Purification and immunoquantitation studies have indicated that these isozymes are expressed in a developmental as well as sex-related manner, and are relatively refractory to induction by xenobiotics. Cytochromes P450h and P450g are male-specific proteins, cytochrome P450i is a female-specific isozyme, while cytochromes P450f and P450k are present in both male and female adult rats. In addition, the expression of cytochrome P450g was shown to segregate into two phenotypes in outbred rats. Genetic studies utilizing inbred strains have indicated that the gene responsible for inheritance of high levels of cytochrome P450g is autosomal. Although considerable progress has been made in understanding the role of gonadal hormones and growth hormone in the hepatic regulation of cytochromes P450g, P450h, and P450i in particular, the physiological significance of the "constitutive" isozymes in the liver remains largely unresolved.Key words: cytochrome P450, regulation, constitutive, liver, sex differences.
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2

Ershov, P. V., Yu V. Mezentsev, E. O. Yablokov, L. A. Kalushskiy, A. V. Florinskaya, A. V. Svirid, A. A. Gilep, S. A. Usanov, A. E. Medvedev, and A. S. Ivanov. "Study specificity of isatin interactions with P450 cytochromes." Biomeditsinskaya Khimiya 64, no. 1 (January 2018): 61–65. http://dx.doi.org/10.18097/pbmc20186401061.

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Cytochrome P450-dependent monooxygenase systems exist basically in all living organisms, where they perform various important functions. The coordinated functioning of these systems involves many proteins participating in different protein-protein interactions (PPI). Previously, we have found that the endogenous non-peptide bioregulator isatin (indoledione-2,3), synthesized from indole by means of certain cytochromes P450 (e.g. P450 2E1, P450 2C19, P450 2A6) regulates affinity of some PPI. In this work, an attempt has been undertaken to register a direct interaction of isatin with a set of different proteins related to the functioning of cytochrome P450-dependent monooxygenase: five isoforms of cytochromes P450, two isoforms of cytochrome b5, cytochrome P450 reductase, adrenodoxin, adrenodoxin reductase and ferrochelatase. The study has shown that isatin binds specifically only to cytochromes P450 with high affinity (the equilibrium dissociation constant (Kd) is about 10-8 M).
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Godbole, Rucha C., Anupama A. Pable, and Vitthal T. Barvkar. "Transcriptome-wide identification, characterization, and phylogenomic analysis of cytochrome P450s from Nothapodytes nimmoniana reveal candidate genes involved in the camptothecin biosynthetic pathway." Genome 64, no. 1 (January 2021): 1–14. http://dx.doi.org/10.1139/gen-2020-0067.

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The plant Nothapodytes nimmoniana is an important source of camptothecin (CPT), an anticancer compound widely used in the treatment of colorectal, lung, and ovarian cancers. CPT is biosynthesized by the combination of the seco-iridoid and indole pathways in plants. The majority of the biosynthetic steps and associated genes still remain unknown. Certain reactions in the seco-iridoid pathway are catalyzed by cytochrome P450 enzymes. Hence, identifying transcriptionally active cytochrome P450 genes becomes essential in the elucidation of the CPT biosynthetic pathway. Here, we report the identification of 94 cytochrome P450s from the assembled transcriptomic data from leaf and root tissues of N. nimmoniana. The identified cytochrome P450 genes were full length and possessed all four conserved characteristic signature motifs of cytochrome P450 genes. Phylogenetic analysis of the protein sequences revealed their evolution and diversification and further categorized them into A-type (52.12%) and non-A-type (47.87%) cytochrome P450s. These 94 sequences represent 38 families and 63 subfamilies of cytochrome P450s. We also compared the transcriptional activity of identified cytochrome P450s with the expression of their homologs in the CPT-producing plant Ophiorrhiza pumila. Based on expression profiles and quantitative PCR validation, we propose NnCYP81CB1 and NnCYP89R1 as candidate cytochrome P450 genes involved in camptothecin biosynthesis in N. nimmoniana.
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4

Iwasaki, M., R. L. P. Lindberg, R. O. Juvonen, and M. Negishi. "Site-directed mutagenesis of mouse steroid 7α-hydroxylase (cytochrome P-4507α): role of residue-209 in determining steroid-cytochrome P-450 interaction." Biochemical Journal 291, no. 2 (April 15, 1993): 569–73. http://dx.doi.org/10.1042/bj2910569.

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We have cloned a cDNA encoding mouse steroid 7 alpha-hydroxylase P450(7) alpha (cytochrome P-450(7) alpha) and expressed it in Saccharomyces cerevisiae. Mouse P450(7) alpha is 70% identical in its amino acid sequence with the mouse steroid 15 alpha-hydroxylase P450(15) alpha (2A4). The Leu at position 209 of P450(15) alpha is the most important residue to determine the steroid hydroxylase activity of the P450 [Lindberg and Negishi (1989) Nature (London) 339, 632-634]. The P450(7) alpha contains Asn at the position corresponding to the Leu-209 of P450(15) alpha, although both P450s hydroxylate testosterone. The CO-reduced P450(7) alpha complex is unstable, so that it is quickly converted into the inactive P420, whereas the P450(15) alpha is very stable. The P450(7) alpha, however, is stabilized either by addition of testosterone or by a mutation of Asn-209 to Leu. The mutant P450(7) alpha displays a 17-fold lower Vmax. value than the wild-type enzyme. Unexpectedly, it also has 3-fold lower Km and Kd values. Residue 209 in P450(7) alpha, therefore, appears to be located at a critical site of the haem-substrate-binding pocket. Corticosterone inhibits the testosterone 7 alpha-hydroxylase activity of the wild-type P450(7) alpha, whereas it does not inhibit the mutant P450(7) alpha. Conversely, the P450(15) alpha activity becomes inhibited by corticosterone upon the replacement of Leu-209 by Asn. In addition, this mutation increases the corticosterone 15 alpha-hydroxylase activity of P450(15) alpha at least 20-fold. Whereas the inhibition by corticosterone depends on the presence of Asn at position 209, deoxycorticosterone inhibits the activities of the P450s regardless of the type of residue at 209. The results indicate, therefore, that the identity of residue 209 determines the affinity as well as specificity of steroid binding to both P450(7) alpha and P450(15) alpha.
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5

Rwere, Freeborn, Sangchoul Im, and Lucy Waskell. "The FMN “140s Loop” of Cytochrome P450 Reductase Controls Electron Transfer to Cytochrome P450." International Journal of Molecular Sciences 22, no. 19 (September 30, 2021): 10625. http://dx.doi.org/10.3390/ijms221910625.

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Cytochrome P450 reductase (CYPOR) provides electrons to all human microsomal cytochrome P450s (cyt P450s). The length and sequence of the “140s” FMN binding loop of CYPOR has been shown to be a key determinant of its redox potential and activity with cyt P450s. Shortening the “140s loop” by deleting glycine-141(ΔGly141) and by engineering a second mutant that mimics flavo-cytochrome P450 BM3 (ΔGly141/Glu142Asn) resulted in mutants that formed an unstable anionic semiquinone. In an attempt to understand the molecular basis of the inability of these mutants to support activity with cyt P450, we expressed, purified, and determined their ability to reduce ferric P450. Our results showed that the ΔGly141 mutant with a very mobile loop only reduced ~7% of cyt P450 with a rate similar to that of the wild type. On the other hand, the more stable loop in the ΔGly141/Glu142Asn mutant allowed for ~55% of the cyt P450 to be reduced ~60% faster than the wild type. Our results reveal that the poor activity of the ΔGly141 mutant is primarily accounted for by its markedly diminished ability to reduce ferric cyt P450. In contrast, the poor activity of the ΔGly141/Glu142Asn mutant is presumably a consequence of the altered structure and mobility of the “140s loop”.
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6

Hodek, Petr, Tomáš Koblas, Helena Rýdlová, Božena Kubíčková, Miroslav Šulc, Jiří Hudeček, and Marie Stiborová. "Chicken Egg Yolk as an Excellent Source of Highly Specific Antibodies Against Cytochromes P450." Collection of Czechoslovak Chemical Communications 69, no. 3 (2004): 659–73. http://dx.doi.org/10.1135/cccc20040659.

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Using chicken antibodies IgY (purified from egg yolks) against mammalian cytochromes P450 and by means of cytochrome P450 marker substrates, we found for the first time the presence of hepatopancreatic cytochrome P450 in crayfishOrconectes limosus(an inducible cytochrome P450 2B-like enzyme) and we were able to detect and quantify cytochrome P450 1A1 in microsomes of human livers. Expression levels of cytochrome P450 1A1 in human livers constituted less than 0.6% of the total hepatic cytochrome P450 complement. The results obtained in our study are clear examples that chicken IgY are suitable for cytochrome P450 detection and quantification. Due to the evolutionary distance, chicken IgY reacts with more epitopes on a mammalian antigen, which gives an amplification of the signal. Moreover, this approach offers many advantages over common mammalian antibody production since chicken egg is an abundant source of antibodies (about 100 mg IgY/yolk) and the egg collection is a non-invasive technique. In the case of antibodies against cytochrome P450 2B4, we documented fast and steady production of highly specific immunoglobulins. Thus, chicken antibodies should be considered as a good alternative to and/or superior substitute for conventional polyclonal antibody produced in mammals.
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Munro, A. W., K. J. McLean, K. R. Marshall, A. J. Warman, G. Lewis, O. Roitel, M. J. Sutcliffe, et al. "Cytochromes P450: novel drug targets in the war against multidrug-resistant Mycobacterium tuberculosis." Biochemical Society Transactions 31, no. 3 (June 1, 2003): 625–30. http://dx.doi.org/10.1042/bst0310625.

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Novel drug strategies are desperately needed to combat the global threat posed by multidrug-resistant strains of Mycobacterium tuberculosis (Mtb). The genome sequence of Mtb has revealed an unprecedented number of cytochrome P450 enzymes in a prokaryote, suggesting fundamental physiological roles for many of these enzymes. Several azole drugs (known inhibitors of cytochromes P450) have been shown to have potent anti-mycobacterial activity, and the most effective azoles have extremely tight binding constants for one of the Mtb P450s (CYP121). The structure of CYP121 has been determined at atomic resolution, revealing novel features of P450 structure, including mixed haem conformations and putative proton-relay pathways from protein surface to haem iron. The structure provides both a platform for investigation of structure/mechanism of cytochrome P450, and for design of inhibitor molecules as novel anti-tubercular agents.
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Hrubý, Kamil, Eva Anzenbacherová, Pavel Anzenbacher, and Milan Nobilis. "Biotransformation of Benfluron by Rat Hepatic Cytochrome P450. Identification of Individual CYP-Enzymes Involved in Biotransformation of Benfluron, Prospective Antineoplastic Based on Benzo[c]fluorene." Collection of Czechoslovak Chemical Communications 65, no. 8 (2000): 1374–86. http://dx.doi.org/10.1135/cccc20001374.

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Benfluron, 5-[2-(dimethylamino)ethoxy]-7H-benzo[c]fluoren-7-one hydrochloride, a prospective antineoplastic agent, is metabolised by cytochromes P450 to N-demethyl and 9-hydroxy derivatives. To prove the participation of individual cytochrome P450 isoforms in formation of these metabolites, selective induction of cytochromes P450, inhibition of benfluron biotransformation using inhibitors specific for individual cytochromes P450, and inhibition by benfluron of "marker" enzyme activities characteristic of certain cytochromes P450 were used. N-Demethylbenfluron appears to be formed mainly by the cytochromes P450 of the 3A, 2B and 2C subfamilies with possible participation of the isoform 2E1; 9-hydroxybenfluron is formed with participation of cytochromes P450 belonging to 1A, and most probably to 3A and 2E1 enzymes. The fact that benfluron is in this respect a relatively promiscuous substrate may be an advantage because its metabolism should not be influenced by the absence or low activity of some cytochrome P450 isoforms and by possible drug interactions.
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9

Shumyantseva, Victoria V., Tatiana V. Bulko, Polina I. Koroleva, Evgeniya V. Shikh, Anna A. Makhova, Maryia S. Kisel, Irina V. Haidukevich, and Andrei A. Gilep. "Human Cytochrome P450 2C9 and Its Polymorphic Modifications: Electroanalysis, Catalytic Properties, and Approaches to the Regulation of Enzymatic Activity." Processes 10, no. 2 (February 17, 2022): 383. http://dx.doi.org/10.3390/pr10020383.

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The electrochemical properties of cytochrome P450 2C9 (CYP2C9) and polymorphic modifications P450 2C9*2 (CYP2C9*2) and P450 2C9*3 (CYP2C9*3) were studied. To analyze the comparative electrochemical and electrocatalytic activity, the enzymes were immobilized on electrodes modified with a membrane-like synthetic surfactant (didodecyldimethylammonium bromide (DDAB)). An adequate choice of the type of modified electrode was confirmed by cyclic voltammetry of cytochromes P450 under anaerobic conditions, demonstrating well-defined peaks of reduction and oxidation of the heme iron. The midpoint potential, Emid, of cytochrome P450 2C9 is −0.318 ± 0.01 V, and Emid = −0.324 ± 0.01 V, and Emid = −0.318 ± 0.03 V for allelic variant 2C9*2 and allelic variant 2C9*3, respectively. In the presence of substrate diclofenac under aerobic conditions, cytochrome P450 2C9 and its polymorphic modifications P450 2C9*2 and P450 2C9*3 exhibit catalytic properties. Stimulation of the metabolism of diclofenac by cytochrome P450 2C9 in the presence of antioxidant medications mexidol and taurine was shown.
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Pratiwi, R. A., N. S. W. Yahya, and Y. Chi. "Bio function of Cytochrome P450 on fungus: a review." IOP Conference Series: Earth and Environmental Science 959, no. 1 (January 1, 2022): 012023. http://dx.doi.org/10.1088/1755-1315/959/1/012023.

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Abstract Cytochrome P450 is the superfamily of proteins involved in the metabolism of organisms, including fungi. Fungal have more diverse P450 families than plants, animals, or bacteria. Research on fungal P450 has blossomed and become an important area in biology and ecology. Cytochrome P450 could be detoxifying natural and environmental contaminants to survive in several ecological niches. Furthermore, the presence of the fungal Cytochrome P450 as an antifungal drug target is a promising approach for the controlling of pest and plant pathogenic fungi. To date, numerous studies have revealed the annotation of diverse P450 followed by an elucidation of P450 functions. This mini-review starts with some basic information of P450s on fungi, then discusses the incredible bio function of characterized fungal P450.
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Dissertations / Theses on the topic "Cytochrome P450"

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Skinner, Michael Stephen. "Olfactory cytochrome P450." Thesis, University of Warwick, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.307349.

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2

Farooq, Yassar. "Mechanisms of electron transfer from cytochrome P450 reductase to cytochrome P450 3A4." Thesis, University of Leicester, 2010. http://hdl.handle.net/2381/8597.

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The study demonstrates that CPR and P450 3A4 can be prepared to highly pure state by the use of detergent CHAPS. Optimisation of published methods led to pure flavoprotein, ~90% full-length with a small amount of truncated CPR. The reconstitution of CPR and P450 3A4 into liposomes using CHAPS and Superose 6 column purification has achieved a homogenous highly functional proteoliposomes with good catalytic activity and almost completely reducible P450 3A4 in a simple controllable system. The spectroscopic data has shown that reduction of P450 3A4 in proteoliposomes was at least 10 fold higher than in the simple reconstituted system suggesting that isolation of proteoliposomes from unbound protein aggregates had marked effect on the catalytic activity of P450. Negative staining electron microscopy has revealed proteoliposomes of having mean diameter of 200 ±15 nm in size; the lipid:protein ratio indicated that they incorporated 350 proteins per liposome. Type 1 difference spectral changes were observed upon binding of testosterone and erythromycin. Measurements of the first electron transfer have shown that the reduction of P450 3A4 is highly dependent on the presence of substrate. P450 3A4 reduction in proteoliposomes in the presence of testosterone was rapid and biphasic, with 90% of the P450 reduced in the fast phase, whereas reduction in the presence of erythromycin was monophasic, but substantially slower. Changes in the CPR:P450 molar ratio did not alter the rate of reduction and thus the data strongly indicates that first electron transfer occurs through preformed CPR:P450 complexes in the proteoliposomes that have a lifetime of about order of hundreds of milliseconds. The origin of the slow phase of reduction of P450 is not conclusive from our experiments, but it may be due to P450 heterogeneity. NADPH oxidation and 6β-hydroxytestosterone formation results have revealed that P450 3A4 is highly uncoupled enzyme with rates limited by CPR to P450 3A4 ratio. Hyperbolic plots of rates of NADPH consumption and 6β hydroxytestosterone formation vs CPR concentration indicate apparent Ks of 0.4 μM. This suggests that CPR:P450 complex can dissociate and reform between first and second electron transfer, which in turn indicates that second electron transfer occurs by diffusion mechanism.
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Al-Anizy, Mohammed. "Studies on cytochrome P450 4X1." Thesis, University of Nottingham, 2005. http://eprints.nottingham.ac.uk/10404/.

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Antisera raised against recombinant human CYP4Z1 (4Z1), mouse Aryl hydrocarbon receptor (AhR), and C.elegans Latrophilin (LpH) proteins were titred over the course of several bleeds. The sensitivity of the antibodies shows an increase over the course of several immunizations, with the minimum amount detected being 1 ng of 4Z1, 0.3 ng of AhR, and 0.3 ng of LpH. Terminal bleeds were taken for the AhR and LpH antisera. The AhR antisera detects proteins in rat and mouse liver cytosol consistent with previous reports of the AhR. LpH is predicted to be localized in a membrane compartment on the basis of its primary structure, so sub-cellular fractions of C.elegans were isolated and tested, revealing a protein of ~113 kDa in a crude membrane preparation. This protein was not solubilized in < 1% Emulgen 913, but was soluble in 2% dodecylmaltoside. A fresh 15k supernatant treated with 2% dodecylmaltoside showed a strong band of LpH protein at ~113 kDa. However, 66 kDa band was detected when the samples were stored overnight at 4 degrees centigrade due to presence of a G protein coupled receptor proteolysis site (GPS) between position M536 and C547 of LpH, which is a characteristic feature in the LpH protein family. In order to study the expression of the CYP 4X1 in mouse tissues, RNase protection assays were performed. Different tissues were assayed at the same time and the same riboprobe was used to hybridise all the samples. The CYP 4\x1 probe was shown to be full length (-ve control). However, the +ve control (RNase positive) shows an absence of signal when hybridised to the yeast tRNA demonstrating the specificity of the signal in the samples. Several RNA samples were hybridised with mouse cyp4X1 gene probe, such as aorta, brain and heart and liver. The mouse cyp4X1 gene appears to have 12 exon from the genomic sequence and encodes a protein which high identity with the human and rat cyp4X1 gene. The full-length of the probe was 424 b.p and the protected fragments were 177 b.p. The murine cyp4X1 was not expressed in control liver, but is expressed in brain at high level. Cyp4X1 gene was also investigated in aorta tissue and found to be expressed at low levels. Known inducers of hepatic cytochrome P450 were used (Ciprofibrate, TCDD, PB, and dexamethasone), but had no induction effect in the samples. Western blotting of brain confirmed that the cyp4X1 protein is expressed in brain, and quantification showed that this is a major cytochrome P450 in brain.
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Bell, Stephen Graham. "The use of active site mutants of cytochrome P450(cam) in chemical synthesis." Thesis, University of Oxford, 1999. http://ora.ox.ac.uk/objects/uuid:7f48cf79-37b0-45cd-a40e-e971af466cff.

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This thesis describes a study of the substrate selectivity of active site mutants of the monooxygenase cytochrome P450cam. A range of mutants was constructed which replaced the phenolic side-chain at the Tyr-96 position by various hydrophobic amino acid residues. These 'hydrophobic mutants' were then combined with other mutations around the active site (Val-247, Phe-87, Ile-395 and Phe-193) which altered the space available at different positions in the active site. These mutants were then tested with an in vitro reconstituted P450cam system with a range of substrates related to diphenylmethane and phenylcylcohexane. All of these large compounds were poor substrates for the wild-type enzyme. It was found that it was necessary to increase both the space available in the active site and the active site hydrophobicity to achieve substrate turnover. The substrates were oxidised preferentially on the aliphatic cyclohexyl ring over the more constrained phenyl ring suggesting that the active site is predisposed to binding the cyclohexyl ring close to the haem. Hydroxylation using the in vitro reconstituted P450cam system is limited by catalyst lifetime and the need for the expensive cofactor NADH. For P450cam hydroxylation to become a viable synthetic method it is necessary to find ways to bypass the use of NADH. For this reason various self-sufficient P450cam system were constructed and expressed in E. coli. The best of these, despite limited protein expression, was found to turnover camphor with the wild-type P450cam enzyme and other substrates with the Y96A mutant. The in vivo catalytic system was then used to screen many P450cam mutants for the oxidation of natural products, monoterpenes and sesquiterpenes (e.g. limonene, pinene and valencene). Most of the target substrates are not oxidised by the wild-type enzyme but all are hydroxylated by some if not all of the P450cam mutants with different degrees of selectivity. Some of the products identified so far are important compounds in the field of flavour and fragrance chemistry (e.g. verbenol and nookatone).
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Sideri, Anastasia. "Directed evolution of cytochrome P450 BM3." Thesis, Imperial College London, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.435931.

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Marsh, Rachael. "Cytochrome P450 studies in Aspergillus fumigatus." Thesis, University of Sheffield, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364267.

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Maughan, Juanita Amanda. "Molecular investigations of plant cytochrome P450." Thesis, University College London (University of London), 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388204.

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Papagiannidou, Eleni. "Cytochrome P450-mediated metabolism of melatonin." Thesis, University of Surrey, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.422928.

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Tyzack, Jonathan David. "Prediction of cytochrome P450 xenobiotic metabolism." Thesis, University of Cambridge, 2014. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708289.

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Busi, Florent. "Pharmacogénétique du cytochrome P450 humain CYP3A5." Paris 5, 2005. http://www.theses.fr/2005PA05P621.

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Les CYP3A sont les P450 les plus abondants dans le foie où ils métabolisent plus de 50 % des médicaments. Le CYP3A5 n'est exprimé que dans 25 % de la population caucasienne. Une mutation (CYP3A5*3) entraînant un épissage alternatif a été associée à un faible niveau de CYP3A5. Un niveau d'ARNm CYP3A5 plus élevé chez les individus *1/*3 par rapport aux homozygotes *3/*3 nous a amené à rechercher les causes de cette variation. L'ARN *3 est plus instable et sa dégradation est réalisée par la NMD (nonsense mediated mRNA decay). Le génotype CYP3A5 a des conséquences en clinique. Nous avons mis au point une technique de génotypage informationnel basé sur la PCR quantitative permettant de déterminer en une seule réaction le génotype et le phénotype CYP3A5. Cette technique permettrait d'ajuster les doses de molécules de faible index thérapeutique lorsque leur pharmacocinétique dépend du CYP3A5. Cette technique peut être généralisée à l'étude des gènes épissés alternativement
CYP3A are the most abundant P450 in the human liver where they metabolize more than 50% of drugs. CYP3A5 is found in only 25% of the Caucasian population. A SNP (CYP3A5*3) yielding to alternative splicing was associated with low CYP3A5 protein content. A higher CYP3A5 mRNA level found in *1/*3 as compared to *3/*3 individuals led us to investigate the mechanism underlying this difference. CYP3A5*3 mRNA was unstable and its degradation was mediated by nonsense mediated mRNA decay (NMD). CYP3A5 genotype has consequences in clinics. We describe a new informative genotyping assay based on quantitative real-time PCR, allowing the determination of CYP3A5 genotype and phenotype in one single step. This assay could be used to improve the dosage of drugs metabolized by CYP3A5 having a narrow therapeutic window. This assay can be generalized to the study of alternatively spliced genes
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Books on the topic "Cytochrome P450"

1

R, Waterman Michael, and Johnson Eric F, eds. Cytochrome P450. San Diego: Academic Press, 1991.

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1951-, Phillips Ian R., and Shephard Elizabeth A. 1950-, eds. Cytochrome P450 protocols. 2nd ed. Totowa, N.J: Humana Press, 2005.

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Yan, Zhengyin, and Gary W. Caldwell, eds. Cytochrome P450. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1542-3.

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Schenkman, John B., and Helmut Greim, eds. Cytochrome P450. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77763-9.

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Ortiz de Montellano, Paul R., ed. Cytochrome P450. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12108-6.

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Ortiz de Montellano, Paul R., ed. Cytochrome P450. Boston, MA: Springer US, 2005. http://dx.doi.org/10.1007/b139087.

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de Montellano, Paul R. Ortiz, ed. Cytochrome P450. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5.

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F, Johnson Eric, and Waterman Michael R, eds. Cytochrome P450. San Diego: Academic Press, 1996.

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Emel, Arinç, Schenkman John B, and Greim Helmut, eds. Cytochrome P450. Berlin: Springer-Verlag, 1993.

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Paul R. Ortiz de Montellano, Ian R. Phillips, and Elizabeth A. Shephard. Cytochrome P450 protocols. 3rd ed. New York: Humana, 2013.

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Book chapters on the topic "Cytochrome P450"

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Girhard, Marco, Patrick J. Bakkes, Osama Mahmoud, and Vlada B. Urlacher. "P450 Biotechnology." In Cytochrome P450, 451–520. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12108-6_8.

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Groves, John T., and Yuan-Zhang Han. "Models and Mechanisms of Cytochrome P450 Action." In Cytochrome P450, 3–48. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_1.

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Whitlock, James P., and Michael S. Denison. "Induction of Cytochrome P450 Enzymes That Metabolize Xenobiotics." In Cytochrome P450, 367–90. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_10.

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Waxman, David J., and Thomas K. H. Chang. "Hormonal Regulation of Liver Cytochrome P450 Enzymes." In Cytochrome P450, 391–417. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_11.

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Kagawa, Norio, and Michael R. Waterman. "Regulation of Steroidogenic and Related P450s." In Cytochrome P450, 419–42. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_12.

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Capdevila, Jorge H., Darryl Zeldin, Keiko Makita, Armando Karara, and John R. Falck. "Cytochrome P450 and the Metabolism of Arachidonic Acid and Oxygenated Eicosanoids." In Cytochrome P450, 443–71. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_13.

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Guengerich, F. Peter. "Human Cytochrome P450 Enzymes." In Cytochrome P450, 473–535. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_14.

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Mansuy, Daniel, and Jean-Paul Renaud. "Heme-Thiolate Proteins Different from Cytochromes P450 Catalyzing Monooxygenations." In Cytochrome P450, 537–74. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_15.

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Marnett, Lawrence J., and Todd A. Kennedy. "Comparison of the Peroxidase Activity of Hemoproteins and Cytochrome P450." In Cytochrome P450, 49–80. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_2.

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Mueller, Ernest J., Paul J. Loida, and Stephen G. Sligar. "Twenty-five Years of P450cam Research." In Cytochrome P450, 83–124. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2391-5_3.

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Conference papers on the topic "Cytochrome P450"

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Burris-Hiday, Sarah, Mengqi Chai, Michael L. Gross, and Emily Scott. "Human Cytochrome P450 Interactions with Redox Partner Cytochrome P450 Reductase." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.267650.

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"Cytochrome P450 Enzymes and Microbial Drug Preparation." In 2017 International Conference on Materials Science and Biological Engineering. Francis Academic Press, 2017. http://dx.doi.org/10.25236/icmsbe.2017.14.

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Seguin, Ryan P., Libin Xu, and Ryan Nguyen. "Unusual Metabolism of Benzethonium by Cytochrome P450." In ASPET 2023 Annual Meeting Abstracts. American Society for Pharmacology and Experimental Therapeutics, 2023. http://dx.doi.org/10.1124/jpet.122.564180.

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Tian, Haijin, Paul Quehl, Joel Hollender, and Joachim Jose. "Surface display of human cytochrome P450 enzymes 3A4, 1A2, 2C9, 2C19 and 2D6 with cytochrome P450 reductase for drug metabolism studies." In 5th International Electronic Conference on Medicinal Chemistry. Basel, Switzerland: MDPI, 2019. http://dx.doi.org/10.3390/ecmc2019-06333.

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Баранова, Надежда Ивановна, Людмила Андреевна Ащина, and Александра Игоревна Болгова. "ROLE OF CYTOKINES AND CYTOCHROMES P450 IN METABOLISM OF ANTIVIRAL DRUGS FROM COVID-19." In Вопросы фундаментальных и прикладных научных исследований: сборник статей международной научной конференции (Омск, Март 2023). Crossref, 2023. http://dx.doi.org/10.37539/230310.2023.78.67.003.

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Представлен обзор данных о возможном влиянии фармакогенетических маркеров на эффективность и безопасность этиотропной терапии COVID-19. Рассматриваются клинические исследования ремдесивира, фавипиравира, молнупиравира. Описываются потенциальные фармакогенетические маркеры цитокинов, влияющие на гены семейства цитохромов P450. A review of the data on the possible influence of pharmacogenetic markers on the efficacy and safety of COVID-19 etiotropic therapy is presented. Clinical trials of remdesivir, favipiravir, and molnupiravir are reviewed. Potential pharmacogenetic markers of cytokines affecting cytochrome P450 family genes are described.
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Özgen, İlker Tolga, Esra Kutlu, Hatice Nursoy, Yaşar Cesur, and Gözde Yeşil. "P94 Cytochrome P450 oxidoreductase enzyme deficiency: a case report." In Faculty of Paediatrics of the Royal College of Physicians of Ireland, 9th Europaediatrics Congress, 13–15 June, Dublin, Ireland 2019. BMJ Publishing Group Ltd and Royal College of Paediatrics and Child Health, 2019. http://dx.doi.org/10.1136/archdischild-2019-epa.449.

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Wu, Huan, Yun-Qiang Di, Chun-Hou Zheng, and Junfeng Xia. "Prediction of cytochrome P450 inhibition using ensemble of extreme learning machine." In 2013 IEEE International Conference on Bioinformatics and Biomedicine (BIBM). IEEE, 2013. http://dx.doi.org/10.1109/bibm.2013.6732515.

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Casper, Jessica A., Diane R. Bielenberg, Jennifer Cheng, Birgitta Schmidt, Bruce D. Hammock, Darryl C. Zeldin, Mark W. Kieran, and Dipak Panigrahy. "Abstract 3952: Cytochrome P450-derived eicosanoids regulate pancreatic cancer and metastasis." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-3952.

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Abraham, JE, M. Maranian, K. Driver, D. Greenberg, MN Shah, HM Earl, AM Dunning, PP Pharoah, and C. Caldas. "Cytochrome P450 2D6 variants and their association with breast cancer survival." In CTRC-AACR San Antonio Breast Cancer Symposium: 2008 Abstracts. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/0008-5472.sabcs-3089.

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Hirakawa, Hidehiko, and Teruyuki Nagamune. "Nanoarchitechture of cytochrome P450 system using a ring-shaped protein complex." In 2010 IEEE 10th Conference on Nanotechnology (IEEE-NANO). IEEE, 2010. http://dx.doi.org/10.1109/nano.2010.5698070.

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Reports on the topic "Cytochrome P450"

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Ahsan, Habibul. Cytochrome P450-17alpha Polymorphism and Risk of Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada390825.

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Arnold, Frances H. Structural and Kinetic Studies of Novel Cytochrome P450 Small-Alkane Hydroxylases. Office of Scientific and Technical Information (OSTI), February 2012. http://dx.doi.org/10.2172/1035499.

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Loper, J. C. Third international symposium: Cytochrome P450 biodiversity. Final report, January 1, 1995--December 31, 1995. Office of Scientific and Technical Information (OSTI), March 1997. http://dx.doi.org/10.2172/508155.

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Sherr, David H. The Aryl Hydrocarbon (Dioxin) Receptor/Transcription Factor and Cytochrome P450 1B1 as Targets for Breast Cancer Immunotherapy. Fort Belvoir, VA: Defense Technical Information Center, September 2002. http://dx.doi.org/10.21236/ada413137.

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Alworth, William L., and David A. Mullin. Use of Genetic Engineering to Produce a Mutated Cytochrome P450 Enzyme Capable of Both Oxidizing and Reductively Dechlorinating Hazardous Organic Chemicals. Fort Belvoir, VA: Defense Technical Information Center, November 2000. http://dx.doi.org/10.21236/ada391816.

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Amir, Rachel, David J. Oliver, Gad Galili, and Jacline V. Shanks. The Role of Cysteine Partitioning into Glutathione and Methionine Synthesis During Normal and Stress Conditions. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7699850.bard.

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The objective of this research is to study the nature of the competition for cysteine (Cys), the first organic sulfur-containing compound, between its two main metabolites, glutathione (GSH) and methionine (Met). GSH plays a central role in protecting plants during various stresses, while Met, an essential amino acid, regulates essential processes and metabolites in plant cells through its metabolite S-adenosyl-Met. Our results, which are based on flux analysis and measurements of Met- metabolites, show that the flux towards Met synthesis is high during non-stress conditions, however the flux is significantly reduced under stress conditions, when there is high synthesis of GSH. Under oxidative stress the expression level of the regulatory enzyme of Met synthesis, cystathionine g-synthase (CGS) was reduced. By using three different systems, we have found that that GSH down regulates the expression level of CGS, thus reducing Met synthesis. We have found that this regulation occurs at the post-transcriptional level, and further studies have shown that it occurs at post-translationaly. To reveal how oxidative stress affects the flux towards Met and GSH, flux analysis was performed. We have found that the level of Met is significantly reduced, while the level of glutathione significantly increases during stress. Under stress conditions most of the glutathione is converted from GSH to GSSG (the oxidised form of glutathione). These results suggest that under normal growth conditions, Cys is channelled towards both pathways to support GSH accumulation and the synthesis of growth-essential Met metabolites. However, during oxidative stress, when a high level of GSH is required to protect the plants, the levels of GSH increase while those of CGS are reduced. This reduction leaves more Cys available for GSH synthesis under stress conditions. In addition we have also studied the effects of high GSH level on the transcriptome profile. The analysis revealed that GSH affects the expression level of many major genes coding to enzymes or proteins associated with photosynthesis, starch degradation, hormone metabolism (especially genes associated with jasmonate), biotic stress (especially genes associated with PR-proteins), cytochrome P450 genes, regulation of transcription and signaling (especially genes associated with receptor kinases and calcium). These results suggest that indeed GSH levels affect different pathways and metabolites in plants.
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Meidan, Rina, and Robert Milvae. Regulation of Bovine Corpus Luteum Function. United States Department of Agriculture, March 1995. http://dx.doi.org/10.32747/1995.7604935.bard.

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The main goal of this research plan was to elucidate regulatory mechanisms controlling the development, function of the bovine corpus luteum (CL). The CL contains two different sterodigenic cell types and therefore it was necessary to obtain pure cell population. A system was developed in which granulosa and theca interna cells, isolated from a preovulatory follicle, acquired characteristics typical of large (LL) and small (SL) luteal cells, respectively, as judged by several biochemical and morphological criteria. Experiments were conducted to determine the effects of granulosa cells removal on subsequent CL function, the results obtained support the concept that granulosa cells make a substaintial contribution to the output of progesterone by the cyclic CL but may have a limited role in determining the functional lifespan of the CL. This experimental model was also used to better understand the contribution of follicular granulosa cells to subsequent luteal SCC mRNA expression. The mitochondrial cytochrome side-chain cleavage enzyme (SCC), which converts cholesterol to pregnenolone, is the first and rate-limiting enzyme of the steroidogenic pathway. Experiments were conducted to characterize the gene expression of P450scc in bovine CL. Levels of P450scc mRNA were higher during mid-luteal phase than in either the early or late luteal phases. PGF 2a injection decreased luteal P450scc mRNA in a time-dependent manner; levels were significantly reduced by 2h after treatment. CLs obtained from heifers on day 8 of the estrous cycle which had granulosa cells removed had a 45% reduction in the levels of mRNA for SCC enzymes as well as a 78% reduction in the numbers of LL cells. To characterize SCC expression in each steroidogenic cell type we utilized pure cell populations. Upon luteinization, LL expressed 2-3 fold higher amounts of both SCC enzymes mRNAs than SL. Moreover, eight days after stimulant removal, LL retained their P4 production capacity, expressed P450scc mRNA and contained this protein. In our attempts to establish the in vitro luteinization model, we had to select the prevulatory and pre-gonadotropin surge follicles. The ratio of estradiol:P4 which is often used was unreliable since P4 levels are high in atretic follicles and also in preovulatory post-gonadotropin follicles. We have therefore examined whether oxytocin (OT) levels in follicular fluids could enhance our ability to correctly and easily define follicular status. Based on E2 and OT concentrations in follicular fluids we could more accurately identify follicles that are preovulatory and post gonadotropin surge. Next we studied OT biosynthesis in granulosa cells, cells which were incubated with forskolin contained stores of the precursor indicating that forskolin (which mimics gonadotropin action) is an effective stimulator of OT biosynthesis and release. While studying in vitro luteinization, we noticed that IGF-I induced effects were not identical to those induced by insulin despite the fact that megadoses of insulin were used. This was the first indication that the cells may secrete IGF binding protein(s) which regonize IGFs and not insulin. In a detailed study involving several techniques, we characterized the species of IGF binding proteins secreted by luteal cells. The effects of exogenous polyunsaturated fatty acids and arachidonic acid on the production of P4 and prostanoids by dispersed bovine luteal cells was examined. The addition of eicosapentaenoic acid and arachidonic acid resulted in a dose-dependent reduction in basal and LH-stimulated biosynthesis of P4 and PGI2 and an increase in production of PGF 2a and 5-HETE production. Indomethacin, an inhibitor of arachidonic acid metabolism via the production of 5-HETE was unaffected. Results of these experiments suggest that the inhibitory effect of arachidonic acid on the biosynthesis of luteal P4 is due to either a direct action of arachidonic acid, or its conversion to 5-HETE via the lipoxgenase pathway of metabolism. The detailed and important information gained by the two labs elucidated the mode of action of factors crucially important to the function of the bovine CL. The data indicate that follicular granulosa cells make a major contribution to numbers of large luteal cells, OT and basal P4 production, as well as the content of cytochrome P450 scc. Granulosa-derived large luteal cells have distinct features: when luteinized, the cell no longer possesses LH receptors, its cAMP response is diminished yet P4 synthesis is sustained. This may imply that maintenance of P4 (even in the absence of a Luteotropic signal) during critical periods such as pregnancy recognition, is dependent on the proper luteinization and function of the large luteal cell.
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