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Recent Advances in Cytochrome P450 (CYP)

A special issue of Current Issues in Molecular Biology (ISSN 1467-3045). This special issue belongs to the section "Biochemistry, Molecular and Cellular Biology".

Deadline for manuscript submissions: closed (30 September 2022) | Viewed by 1332

Special Issue Editors


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Guest Editor
Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030, USA
Interests: cytochrome P450; Ah receptor; hyperoxic lung injury; ARDS; bronchopulmonary dysplasia; polycyclic aromatic hydrocarbons; carcinogenesis; oxidative stress
Special Issues, Collections and Topics in MDPI journals
1. Department of Pharmacological and Pharmaceutical Sciences, College of Pharmacy, University of Houston (G.T., R.G.), Houston, TX, USA
2. Department of Pediatrics, Baylor College of Medicine (C.C., P.M., B.M.), Houston, TX, USA
Interests: regulation of drug metabolizing enzymes during inflammation; obesity and diseases; gastrointestinal toxicity of chemotherapy drugs; pharmacokinetic/pharmacodynamic studies
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are in the midst of establishing a Special Issue on the hot topic “Cytochrome P450” for the journal CIMB. Cytochrome P450 (CYP) is a superfamily of enzymes that function as monooxygenases and contain heme as a cofactor. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds as well as for hormone synthesis and breakdown. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones.

CYP enzymes have been identified in all kingdoms of life: animals, plants, fungi, protists, bacteria, archaea, and even in viruses. More than 50,000 distinct CYP proteins are known. CYPs are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems. There are 57 CYP isoforms in humans, and their role in human drug metabolism, including chemotherapeutic drugs, is well known. However, their role in the metabolism of endogenous substrates is not completely understood. Hence, there is a need for further research to elucidate the mechanisms of CYP regulation and the molecular role of CYP in the metabolism of drugs, nutrients, xenobiotics, and endogenous compounds.

Original manuscripts and reviews dealing with the regulation and role of CYP enzymes in metabolism of xenobiotics or endobiotics are invited for consideration, for publication in CIMB.

Prof. Dr. Bhagavatula Moorthy
Dr. Romi Ghose
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Current Issues in Molecular Biology is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (1 paper)

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Research

17 pages, 3112 KiB  
Article
Mutual Modulation of the Activities of Human CYP2D6 and Four UGTs during the Metabolism of Propranolol
by Fan Yang, Sangeeta Shrestha Sharma, Matthias Bureik and Maria Kristina Parr
Curr. Issues Mol. Biol. 2023, 45(9), 7130-7146; https://0-doi-org.brum.beds.ac.uk/10.3390/cimb45090451 - 26 Aug 2023
Cited by 1 | Viewed by 1091
Abstract
Cytochromes P450 (CYP) and UDP-glucuronosyltransferases (UGT) are two enzyme families that play an important role in drug metabolism, catalyzing either the functionalization or glucuronidation of xenobiotics. However, their mutual interactions are poorly understood. In this study, the functional interactions of human CYP2D6 with [...] Read more.
Cytochromes P450 (CYP) and UDP-glucuronosyltransferases (UGT) are two enzyme families that play an important role in drug metabolism, catalyzing either the functionalization or glucuronidation of xenobiotics. However, their mutual interactions are poorly understood. In this study, the functional interactions of human CYP2D6 with four human UGTs (UGT1A7, UGT1A8, UGT1A9, and UGT2A1) were investigated using our previously established co-expression model system in the fission yeast Schizosaccharomyces pombe. The substrate employed was propranolol because it is well metabolized by CYP2D6. Moreover, the CYP2D6 metabolite 4-hydroxypropranolol is a known substrate for the four UGTs included in this study. Co-expression of either UGT1A7, UGT1A8, or UGT1A9 was found to increase the activity of CYP2D6 by a factor of 3.3, 2.1 or 2.8, respectively, for the conversion of propranolol to 4-hydroxypropranolol. In contrast, UGT2A1 co-expression did not change CYP2D6 activity. On the other hand, the activities of all four UGTs were completely suppressed by co-expression of CYP2D6. This data corroborates our previous report that CYP2D6 is involved in functional CYP-UGT interactions and suggest that such interactions can contribute to both adverse drug reactions and changes in drug efficacy. Full article
(This article belongs to the Special Issue Recent Advances in Cytochrome P450 (CYP))
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