Academic literature on the topic 'Cytochrome P450 3A'

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Journal articles on the topic "Cytochrome P450 3A"

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de Wildt, Saskia N., Gregory L. Kearns, J. Steven Leeder, and John N. van den Anker. "Cytochrome P450 3A." Clinical Pharmacokinetics 37, no. 6 (1999): 485–505. http://dx.doi.org/10.2165/00003088-199937060-00004.

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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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de Leon, Jose, and Jayme Bork. "Risperidone and Cytochrome P450 3A." Journal of Clinical Psychiatry 58, no. 10 (October 15, 1997): 450. http://dx.doi.org/10.4088/jcp.v58n1010b.

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Geist, Marcus, Hubert Bardenheuer, Juergen Burhenne, and Gerd Mikus. "Alteration of drug-metabolizing enzyme activity in palliative care patients: Microdosed assessment of cytochrome P450 3A." Palliative Medicine 33, no. 7 (April 26, 2019): 850–55. http://dx.doi.org/10.1177/0269216319843629.

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Background: Cytochrome P450 3A is the most relevant drug-metabolizing enzyme in humans as it is involved in the elimination of 50% of marketed drugs. Nothing is known about the activity of cytochrome P450 3A in palliative care patients who have complicated symptoms often associated with a terminal illness. Aim: In order to improve drug dosing in end-of-life care and to avoid drug interactions, cytochrome P450 3A activity was determined in patients of a palliative care unit under real-life clinical conditions. Design: As midazolam is an established marker substance for cytochrome P450 3A activity, this single-arm prospective trial was designed to obtain a 4-h pharmacokinetic profile of midazolam after oral administration of a 10-µg dose from each enrolled patient. Plasma concentrations of midazolam and its primary metabolite 1′-hydroxy-midazolam were quantified by mass spectrometry techniques. Cytochrome P450 3A activity was calculated as partial metabolic clearance from a limited sampling area under the curve. All other drugs taken by the participating patients were considered, as well as recent blood test results and patients’ diagnoses. The trial was registered at German Clinical Trials Register ( www.drks.de ): DRKS00011753. Setting/participants: The trial was carried out at a university palliative care unit under real-life clinical conditions. Every patient admitted to the ward was screened for possible participation, independent of the individual performance status. Results: Partial metabolic clearance of midazolam in palliative care patients was 31.7 ± 32.1 L/h. This was a highly significant 40% reduction ( p < 0.0001) in comparison with the cytochrome P450 3A activity of healthy subjects. Conclusion: Dosing of cytochrome P450 3A substrate drugs (e.g. macrolide antibiotics, benzodiazepines, calcium channel blockers) needs to be adjusted in palliative care patients; otherwise, escalation of debilitating symptoms due to drug interactions might occur.
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Burk, Oliver, and Leszek Wojnowski. "Cytochrome P450 3A and their regulation." Naunyn-Schmiedeberg's Archives of Pharmacology 369, no. 1 (January 1, 2004): 105–24. http://dx.doi.org/10.1007/s00210-003-0815-3.

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Zangar, Richard C., Marissa Hernandez, and Raymond F. Novak. "Posttranscriptional Elevation of Cytochrome P450 3A Expression." Biochemical and Biophysical Research Communications 231, no. 1 (February 1997): 203–5. http://dx.doi.org/10.1006/bbrc.1997.6054.

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Thervet, Eric, Christopher Legendre, Philippe Beaune, and Dany Anglicheau. "Cytochrome P450 3A polymorphisms and immunosuppressive drugs." Pharmacogenomics 6, no. 1 (January 2005): 37–47. http://dx.doi.org/10.1517/14622416.6.1.37.

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Tydén, E., L. Olsén, J. Tallkvist, H. Tjälve, and P. Larsson. "Cytochrome P450 3A, NADPH cytochrome P450 reductase and cytochrome b5 in the upper airways in horse." Research in Veterinary Science 85, no. 1 (August 2008): 80–85. http://dx.doi.org/10.1016/j.rvsc.2007.09.012.

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Correia, Maria Almira, Sheila Sadeghi, and Eduardo Mundo-Paredes. "CYTOCHROME P450 UBIQUITINATION: Branding for the Proteolytic Slaughter?" Annual Review of Pharmacology and Toxicology 45, no. 1 (September 22, 2005): 439–64. http://dx.doi.org/10.1146/annurev.pharmtox.45.120403.100127.

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The hepatic cytochromes P450 (P450s) are monotopic endoplasmic reticulum (ER)-anchored hemoproteins engaged in the enzymatic oxidation of a wide variety of endo- and xenobiotics. In the course of these reactions, the enzymes generate reactive O2 species and/or reactive metabolic products that can attack the P450 heme and/or protein moiety and structurally and functionally damage the enzyme. The in vivo conformational unraveling of such a structurally damaged P450 signals its rapid removal via the cellular sanitation system responsible for the proteolytic disposal of structurally aberrant, abnormal, and/or otherwise malformed proteins. A key player in this process is the ubiquitin (Ub)-dependent 26S proteasome system. Accordingly, the structurally deformed P450 protein is first branded for recognition and proteolytic removal by the 26S proteasome with an enzymatically incorporated polyUb tag. P450s of the 3A subfamily such as the major human liver enzyme CYP3A4 are notorious targets for this process, and they represent excellent prototypes for the understanding of integral ER protein ubiquitination. Not all the participants in hepatic CYP3A ubiquitination and subsequent proteolytic degradation have been identified. The following discussion thus addresses the various known and plausible events and/or cellular participants involved in this multienzymatic P450 ubiquitination cascade, on the basis of our current knowledge of other eukaryotic models. In addition, because the detection of ubiquitinated P450s is technically challenging, the critical importance of appropriate methodology is also discussed.
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von Moltke, Lisa L., David J. Greenblatt, Jürgen Schmider, Jerold S. Harmatz, and Richard I. Shader. "Metabolism of Drugs by Cytochrome P450 3A Isoforms." Clinical Pharmacokinetics 29, Supplement 1 (1995): 33–44. http://dx.doi.org/10.2165/00003088-199500291-00007.

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Dissertations / Theses on the topic "Cytochrome P450 3A"

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Givens, Raymond Carlos Maeda Nobuyo. "Physiologic effects of cytochrome P450 3A activity." Chapel Hill, N.C. : University of North Carolina at Chapel Hill, 2007. http://dc.lib.unc.edu/u?/etd,1371.

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Thesis (Ph. D.)--University of North Carolina at Chapel Hill, 2007.
Title from electronic title page (viewed Apr. 25, 2008). "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Nutrition, School of Public Health." Discipline: Nutrition; Department/School: Public Health.
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Westlind, Johnsson Anna. "Pharmacogenetics of human cytochrome P450 3A (CYP3A) enzymes /." Stockholm, 2003. http://diss.kib.ki.se/2003/91-7349-688-x.

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Johnson, Trevor Nigel. "Developmental and pathological changes in intestinal cytochrome P450 3A." Thesis, University of Sheffield, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.482841.

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Tydén, Eva. "Cytochrome P450 3A and ABC-transport proteins in horse /." Uppsala : Department of Biomedical Sciences and Veterinary Public Health, Swedish University of Agricultural Sciences, 2008. http://epsilon.slu.se/200893.pdf.

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Curi, Pedrosa Rozangela. "Effet de quelques anti-secrétoires gastriques sur l'expression des cytochromes P450 1A et 3A hépatiques humains : implication des cytochromes P450 3A dans le métabolisme de l'omeprazole." Montpellier 1, 1992. http://www.theses.fr/1992MON13519.

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Engman, Helena. "Intestinal barriers to oral drug absorption : cytochrome P450 3A and ABC-transport proteins /." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis, 2003. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3599.

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Mugundu, Ganesh. "Pharmacogenetic Impact on Metabolism and Cytochrome P450 (CYP)3A Inductive Effect of Tamoxifen." University of Cincinnati / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1266596002.

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Zerilli, Alain. "Cytochromes P450 2E1 et 3A : spécificité de l'induction tissulaire chez le rat, spécificité des substrats du P450 2E1." Brest, 1997. http://www.theses.fr/1997BRES3102.

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Swales, Karen Elizabeth. "An investigation of host cell effects on the xenobiotic induction of cytochrome P450 3A." Thesis, University of Surrey, 2002. http://epubs.surrey.ac.uk/843184/.

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Species differences exist in the induction response of CYP3A genes to xenobiotics, and these are proposed to be due, in part, to host cell differences. These host cell effects were investigated functionally by trans-species transfections of alkaline phosphatase reporter genes containing ~1.5 kb of the CYP3A23 or CYP3A4 5' flanking regions into human HepG2 and rat FaO and H4IIEC3 hepatoma cells. HepG2 and FaO cells were demonstrated to support induction of the activity of both CYP3A constructs by 50 muM dexamethasone but H4IIEC3 cells could not. The receptor mRNA complement (CAR, GRa, HNF4a, PXR and RXRa) of the rat and human cell lines were characterised in comparison to rat and human liver using semi-quantitative RT-PCR to identify any differences. Principal component analysis (PCA) of the receptor mRNA levels was scattered indicating that rat liver does not resemble human liver and that hepatoma cell lines do not resemble their liver counterparts in terms of individual receptor mRNA levels. Increasing knowledge of nuclear receptor interactions with response elements led to consideration that response to xenobiotics may be due to relative receptor abundance in the cells, as opposed to individual receptor expression levels. PCA on comparison ratios showed clustering of human and HepG2 receptor ratios, supporting the observation that CYP3A reporter gene induction responses in HepG2 cells mimic those in vivo. From this data we hypothesise that relative receptor expression levels are key to determining CYP3A responsiveness to xenobiotics. However this hypothesis could not be further examined at the protein level, as Western blotting experiments were equivocal. The latter hypothesis was further examined through the use of TaqMan, expanding the receptor cohort to include COUPTFI and RXRs and gamma, plus CYP3A mRNA expression levels. In addition the effects of xenobiotics, dexamethasone, rifampicin, PCN and phenobarbital at a range of concentrations, were tested. The hepatoma cell lines did not have the same endogenous CYP3A mRNA expression or induction profiles as liver. The TaqMan results suggested that in human CYP3A regulation, the relative abundance of PXR heterodimerisation partners or accessory factors were more important than the level of PXR, whereas in rats, PXR was dominant in determining induction of CYP3A, indicating a further species difference. In conclusion, host cell effects on CYP3A regulation are dependent on receptor abundance and interactions, as well as differential receptor activation.
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Salphati, Laurent. "P-glycoproteine et cytochrome p450 3a : interactions potentielles et roles complementaires dans l'absorption et la disposition des drogues." Paris 11, 1998. http://www.theses.fr/1998PA114805.

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Book chapters on the topic "Cytochrome P450 3A"

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Guengerich, F. P., E. M. J. Gillam, M. V. Martin, T. Baba, B. R. Kim, T. Shimada, K. D. Raney, and C. H. Yun. "The Importance of Cytochrome P450 3A Enzymes in Drug Metabolism." In Assessment of the Use of Single Cytochrome P450 Enzymes in Drug Research, 161–86. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-662-03019-6_9.

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Wang, Jing, and Eugene Chen. "Assessing Cytochrome P450 3A (CYP3A) Induction and Suppression Using Primary Human Hepatocyte Spheroids." In Methods in Pharmacology and Toxicology, 217–27. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1542-3_13.

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Ghose, Romi, Pankajini Mallick, Guncha Taneja, Chun Chu, and Bhagavatula Moorthy. "In Vitro Approaches to Study Regulation of Hepatic Cytochrome P450 (CYP) 3A Expression by Paclitaxel and Rifampicin." In Methods in Molecular Biology, 55–68. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3347-1_4.

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