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Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract
Asclepias subulata plant extract has previously demonstrated antiproliferative activity and antimutagenicity against heterocyclic aromatic amines (HAAs) commonly found in cooked meat. The objective of this work was to evaluate the in vitro ability of an ethanolic extract from the medicinal plant Asc...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10305697/ https://www.ncbi.nlm.nih.gov/pubmed/37375979 http://dx.doi.org/10.3390/plants12122354 |
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author | Gutiérrez-Pacheco, Samaria Lisdeth Peña-Ramos, Etna Aida Santes-Palacios, Rebeca Valenzuela-Melendres, Martin Hernández-Mendoza, Adrián Burgos-Hernández, Armando Robles-Zepeda, Ramón Enrique Espinosa-Aguirre, Jesús Javier |
author_facet | Gutiérrez-Pacheco, Samaria Lisdeth Peña-Ramos, Etna Aida Santes-Palacios, Rebeca Valenzuela-Melendres, Martin Hernández-Mendoza, Adrián Burgos-Hernández, Armando Robles-Zepeda, Ramón Enrique Espinosa-Aguirre, Jesús Javier |
author_sort | Gutiérrez-Pacheco, Samaria Lisdeth |
collection | PubMed |
description | Asclepias subulata plant extract has previously demonstrated antiproliferative activity and antimutagenicity against heterocyclic aromatic amines (HAAs) commonly found in cooked meat. The objective of this work was to evaluate the in vitro ability of an ethanolic extract from the medicinal plant Asclepias subulata extract (ASE), non-heated and heated (180 °C), to inhibit the activity of CYP1A1 and CYP1A2, which are largely responsible for HAAs bioactivation. Ethoxyresorufin and methoxyresorufin O-dealkylation assays were performed in rat liver microsomes exposed to ASE (0.002–960 µg/mL). ASE exerted an inhibitory effect in a dose-dependent manner. The half inhibitory concentration (IC(50)) for unheated ASE was 353.6 µg/mL and 75.9 µg/mL for heated ASE in EROD assay. An IC(40) value of 288.4 ± 5.8 µg/mL was calculated for non-heated ASE in MROD assay. However, after heat treatment, the IC(50) value was 232.1 ± 7.4 µg/mL. Molecular docking of corotoxigenin-3-O-glucopyranoside, one of the main components of ASE, with CYP1A1/2 structure, was performed. Results show that the interaction of corotoxigenin-3-O-glucopyranoside with CYP1A1/2s’ α-helices, which are related with the active site and the heme cofactor, may explain the plant extract’s inhibitory properties. Results showed that ASE inhibits CYP1A enzymatic subfamily and may potentially act as a chemopreventive agent by inhibiting bioactivation of promutagenic dietary HAAs. |
format | Online Article Text |
id | pubmed-10305697 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-103056972023-06-29 Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract Gutiérrez-Pacheco, Samaria Lisdeth Peña-Ramos, Etna Aida Santes-Palacios, Rebeca Valenzuela-Melendres, Martin Hernández-Mendoza, Adrián Burgos-Hernández, Armando Robles-Zepeda, Ramón Enrique Espinosa-Aguirre, Jesús Javier Plants (Basel) Article Asclepias subulata plant extract has previously demonstrated antiproliferative activity and antimutagenicity against heterocyclic aromatic amines (HAAs) commonly found in cooked meat. The objective of this work was to evaluate the in vitro ability of an ethanolic extract from the medicinal plant Asclepias subulata extract (ASE), non-heated and heated (180 °C), to inhibit the activity of CYP1A1 and CYP1A2, which are largely responsible for HAAs bioactivation. Ethoxyresorufin and methoxyresorufin O-dealkylation assays were performed in rat liver microsomes exposed to ASE (0.002–960 µg/mL). ASE exerted an inhibitory effect in a dose-dependent manner. The half inhibitory concentration (IC(50)) for unheated ASE was 353.6 µg/mL and 75.9 µg/mL for heated ASE in EROD assay. An IC(40) value of 288.4 ± 5.8 µg/mL was calculated for non-heated ASE in MROD assay. However, after heat treatment, the IC(50) value was 232.1 ± 7.4 µg/mL. Molecular docking of corotoxigenin-3-O-glucopyranoside, one of the main components of ASE, with CYP1A1/2 structure, was performed. Results show that the interaction of corotoxigenin-3-O-glucopyranoside with CYP1A1/2s’ α-helices, which are related with the active site and the heme cofactor, may explain the plant extract’s inhibitory properties. Results showed that ASE inhibits CYP1A enzymatic subfamily and may potentially act as a chemopreventive agent by inhibiting bioactivation of promutagenic dietary HAAs. MDPI 2023-06-17 /pmc/articles/PMC10305697/ /pubmed/37375979 http://dx.doi.org/10.3390/plants12122354 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Gutiérrez-Pacheco, Samaria Lisdeth Peña-Ramos, Etna Aida Santes-Palacios, Rebeca Valenzuela-Melendres, Martin Hernández-Mendoza, Adrián Burgos-Hernández, Armando Robles-Zepeda, Ramón Enrique Espinosa-Aguirre, Jesús Javier Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract |
title | Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract |
title_full | Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract |
title_fullStr | Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract |
title_full_unstemmed | Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract |
title_short | Inhibition of the CYP Enzymatic System Responsible of Heterocyclic Amines Bioactivation by an Asclepias subulata Extract |
title_sort | inhibition of the cyp enzymatic system responsible of heterocyclic amines bioactivation by an asclepias subulata extract |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10305697/ https://www.ncbi.nlm.nih.gov/pubmed/37375979 http://dx.doi.org/10.3390/plants12122354 |
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