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Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity 5.0
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Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity 5.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 30 June 2024 | Viewed by 2214

Special Issue Editors

Dr. Arthur Roberts

E-Mail Website
Guest Editor
Department of Pharmaceutical Biomedical Sciences, The University of Georgia, Athens, GA 30602, USA
Interests: cytochrome P450
Special Issues, Collections and Topics in MDPI journals
Dr. Patrick M. Dansette

E-Mail Website
Guest Editor
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, UMR 8601 CNRS, Université Paris Descartes, Sorbonne Paris Cité, 45 Rue des Saints-Pères, CEDEX 06, 75270 Paris, France
Interests: drug metabolism; cytochrome P450 structure and mechanism; biological reactive intermediates; thiophene-S-oxides; arene oxides; sulfenic acid; mechanism based inhibitors; ferrocifen; drug induced immunotoxicity.
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue is a continuation of the previous four Special Issues in the “Cytochromes P450: Drug Metabolism and Bioactivation and Biodiversity” series 1–4 (https://www.mdpi.com/journal/ijms/special_issues/p450).

Nearly seventy year ago, R.T. Williams and B.B. Brodie developed the concept of drug metabolism and explored the types of reactions and the mechanisms that must occur in order for the body to facilitate the excretion of a drug. Ten years later, Klingenberg and Garfinkel independently discovered the P450 protein, which was, five years later, demonstrated to be a cytochrome P450 by Omura and Sato. Later on, the prominent function of this enzyme and its role in drug metabolism and endobiotics biosynthesis were established. This resulted in a new chapter, and now more than 90,000 papers make reference to cytochrome P450. We are now well aware of this enzyme’s importance in clearance and potential toxicity, and, therefore, compounds are frequently tested for it. Moreover, this enzyme family is widely distributed in the bacterial, animal, plant, alga and viral kingdoms.

Volumes 1–4 of “Cytochromes P450: Drug Metabolism and Bioactivation and Biodiversity” were considerably successful, with each publishing more than 10 papers. Thus, we have decided to launch a new Special Issue with an expanded range of allowed topics. This fifth Special Issue focuses on cytochrome P450’s drug metabolism, bioactivation and biodiversity and will include papers on (1) its structures, (2) types and mechanisms of reactions, (3) pharmacogenomics, (4) bioactivation reactions and biological markers, (5) mechanism-based inactivation, (6) species differences and (7) biodiversity.

We warmly welcome submissions, including original papers and reviews, on these widely-discussed topics.

Dr. Arthur Roberts
Dr. Patrick M. Dansette
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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.

 

Keywords

  • cytochrome P450
  • drug metabolism
  • bioactivation
  • pharmacogenomics
  • reactive intermediates
  • drug induced toxicity
  • reaction mechanisms

Published Papers (2 papers)

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15 pages, 4047 KiB  
Article
Dissecting CYP1A2 Activation by Arylalkanoic Acid Prodrugs toward the Development of Anti-Inflammatory Agents
by Maria Antonietta Occhiuzzi, Giuseppina Ioele, Michele De Luca, Bruno Rizzuti, Domenica Scordamaglia, Rosamaria Lappano, Marcello Maggiolini, Antonio Garofalo and Fedora Grande
Int. J. Mol. Sci. 2024, 25(1), 435; https://doi.org/10.3390/ijms25010435 - 28 Dec 2023
Viewed by 677
Abstract
Arylalkane-derived prodrugs of arylacetic acids are a small group of substances that have long been known for their anti-inflammatory action. Despite their ease of synthesis and good potential for the development of new potent and safe anti-inflammatory agents, this group of substances has [...] Read more.
Arylalkane-derived prodrugs of arylacetic acids are a small group of substances that have long been known for their anti-inflammatory action. Despite their ease of synthesis and good potential for the development of new potent and safe anti-inflammatory agents, this group of substances has not received much attention from researchers so far. Therefore, representative arylalkane derivatives were investigated through molecular docking techniques to verify the possible hepatic activation mode toward active metabolites by CYP1A2. In this regard, arylalkanoic acid prodrugs were docked with a crystallographic structure of human CYP1A2, in which the enzyme is co-crystallized with the selective competitive inhibitor α-naphthoflavone BHF. Of note, all the examined compounds proved capable of interacting with the enzyme active site in a manner similar to Nabumetone, thus confirming that a productive metabolic transformation is feasible. On the basis of these findings, it is possible to argue that subtle differences in the way CYP1A2 accommodates the ligands depend on the fine details of their molecular structures. Overall, these data suggest that compounds simply formed by an aromatic moiety bearing an appropriate alkane-derived chain could lead to innovative anti-inflammatory agents. Full article
(This article belongs to the Special Issue Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity 5.0)
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34 pages, 7100 KiB  
Article
AhR and CYP1B1 Control Oxygen Effects on Bone Marrow Progenitor Cells: The Enrichment of Multiple Olfactory Receptors as Potential Microbiome Sensors
by Michele C. Larsen, Catherine M. Rondelli, Ahmed Almeldin, Yong-Seok Song, Alhaji N’Jai, David L. Alexander, E. Camilla Forsberg, Nader Sheibani and Colin R. Jefcoate
Int. J. Mol. Sci. 2023, 24(23), 16884; https://doi.org/10.3390/ijms242316884 - 28 Nov 2023
Viewed by 1085
Abstract
Polycyclic aromatic hydrocarbon (PAH) pollutants and microbiome products converge on the aryl hydrocarbon receptor (AhR) to redirect selective rapid adherence of isolated bone marrow (BM) cells. In young adult mice, Cyp1b1-deficiency and AhR activation by PAH, particularly when prolonged by Cyp1a1 deletion, produce [...] Read more.
Polycyclic aromatic hydrocarbon (PAH) pollutants and microbiome products converge on the aryl hydrocarbon receptor (AhR) to redirect selective rapid adherence of isolated bone marrow (BM) cells. In young adult mice, Cyp1b1-deficiency and AhR activation by PAH, particularly when prolonged by Cyp1a1 deletion, produce matching gene stimulations in these BM cells. Vascular expression of Cyp1b1 lowers reactive oxygen species (ROS), suppressing NF-κB/RelA signaling. PAH and allelic selectivity support a non-canonical AhR participation, possibly through RelA. Genes stimulated by Cyp1b1 deficiency were further resolved according to the effects of Cyp1b1 and Cyp1a1 dual deletions (DKO). The adherent BM cells show a cluster of novel stimulations, including select developmental markers; multiple re-purposed olfactory receptors (OLFR); and α-Defensin, a microbial disruptor. Each one connects to an enhanced specific expression of the catalytic RNA Pol2 A subunit, among 12 different subunits. Mesenchymal progenitor BMS2 cells retain these features. Cyp1b1-deficiency removes lymphocytes from adherent assemblies as BM-derived mesenchymal stromal cells (BM-MSC) expand. Cyp1b1 effects were cell-type specific. In vivo, BM-MSC Cyp1b1 expression mediated PAH suppression of lymphocyte progenitors. In vitro, OP9-MSC sustained these progenitors, while Csf1 induced monocyte progenitor expansion to macrophages. Targeted Cyp1b1 deletion (Cdh5-Cre; Cyp1b1fl/fl) established endothelium control of ROS that directs AhR-mediated suppression of B cell progenitors. Monocyte Cyp1b1 deletion (Lyz2-Cre; Cyp1b1fl/fl) selectively attenuated M1 polarization of expanded macrophages, but did not enhance effects on basal M2 polarization. Thus, specific sources of Cyp1b1 link to AhR and to an OLFR network to provide BM inflammatory modulation via diverse microbiome products. Full article
(This article belongs to the Special Issue Cytochromes P450: Drug Metabolism, Bioactivation and Biodiversity 5.0)
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