دورية أكاديمية
Characterization of human oxidoreductases involved in aldehyde odorant metabolism
| العنوان: | Characterization of human oxidoreductases involved in aldehyde odorant metabolism |
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| المؤلفون: | Boichot, Valentin, Menetrier, Franck, Saliou, Jean-Michel, Lirussi, Frederic, Canon, Francis, Folia, Mireille, Heydel, Jean-marie, Hummel, Thomas, Menzel, Susanne, Steinke, Maria, Hackenberg, Stephan, Schwartz, Mathieu, Neiers, F. |
| المساهمون: | Centre des Sciences du Goût et de l'Alimentation Dijon (CSGA), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Université Bourgogne Franche-Comté COMUE (UBFC), Plateformes Lilloises en Biologie et Santé - UAR 2014 - US 41 (PLBS), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire CHU Lille (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Lipides - Nutrition - Cancer Dijon - U1231 (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, CHU Dijon, Centre Hospitalier Universitaire de Dijon - Hôpital François Mitterrand (CHU Dijon), Technische Universität Dresden = Dresden University of Technology (TU Dresden), University Hospital Wuerzburg / Universitätsklinikum Würzburg, Fraunhofer Institute for Silicate Research (Fraunhofer ISC), Fraunhofer (Fraunhofer-Gesellschaft), Universitätsklinikum RWTH Aachen - University Hospital Aachen Aachen, Germany (UKA), Rheinisch-Westfälische Technische Hochschule Aachen University (RWTH), Agence Nationale de la Recherche., ANR-18-CE92-0018,NAOMI,Métabolites olfactifs des molécules odorantes : caractérisation et fonction dans la perception olfactive(2018), ANR-20-CE21-0002,MACARON,Pellicule mucosal, flaveur, interaction & perception(2020), ANR-22-CE21-0001,FLAMME,Métabolisme de la flaveur en bouche et modulation de la perception par les enzymes du microbiote oral(2022) |
| المصدر: | ISSN: 2045-2322. |
| بيانات النشر: | HAL CCSD Nature Publishing Group |
| سنة النشر: | 2023 |
| المجموعة: | LillOA (HAL Lille Open Archive, Université de Lille) |
| مصطلحات موضوعية: | Humans, Oxidoreductases/metabolism, Odorants/analysis, Xenobiotics/metabolism, Smell/physiology, Respiratory System/metabolism, Alcohol Oxidoreductases/metabolism, Receptors, Odorant/genetics/metabolism, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology |
| الوصف: | International audience ; Oxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal termination as well as in the generation of metabolites that change the activation pattern of chemosensory receptors. Oxidoreductases, especially aldehyde dehydrogenases and aldo-keto reductases, are the first barrier against aldehyde compounds, which include numerous odorants. Using a mass spectrometry approach, we characterized the most highly expressed members of these families in the human nasal mucus sampled in the olfactory vicinity. Their expression was also demonstrated using immunohistochemistry in human epitheliums sampled in the olfactory vicinity. Recombinant enzymes corresponding to three highly expressed human oxidoreductases (ALDH1A1, ALDH3A1, AKR1B10) were used to demonstrate the high enzymatic activity of these enzymes toward aldehyde odorants. The structure-function relationship set based on the enzymatic parameters characterization of a series of aldehyde odorant compounds was supported by the X-ray structure resolution of human ALDH3A1 in complex with octanal. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| العلاقة: | info:eu-repo/semantics/altIdentifier/pmid/36966166; hal-04080823; https://hal.inrae.fr/hal-04080823Test; https://hal.inrae.fr/hal-04080823/documentTest; https://hal.inrae.fr/hal-04080823/file/boichot_2023_vol13_4876_sci_rep.pdfTest; PUBMED: 36966166; PUBMEDCENTRAL: PMC10039900; WOS: 001017313600036 |
| DOI: | 10.1038/s41598-023-31769-4 |
| الإتاحة: | https://doi.org/10.1038/s41598-023-31769-4Test https://hal.inrae.fr/hal-04080823Test https://hal.inrae.fr/hal-04080823/documentTest https://hal.inrae.fr/hal-04080823/file/boichot_2023_vol13_4876_sci_rep.pdfTest |
| حقوق: | http://creativecommons.org/licenses/byTest/ ; info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.8902C1C0 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1038/s41598-023-31769-4 |
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