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2. Protein O ‐GlcNAcylation levels are regulated independently of dietary intake in a tissue and time‐specific manner during rat postnatal development

Author

Dupas, Thomas, Denis, Manon, Dontaine, Justine, Persello, Antoine, Bultot, Laurent, Erraud, Angélique, Vertommen, Didier, Bouchard, Bertrand, Tessier, Arnaud, Rivière, Matthieu, Lebreton, Jacques, Bigot‐Corbel, Edith, Montnach, Jérôme, De Waard, Michel, Gauthier, Chantal, Burelle, Yan, Olson, Aaron K., Rozec, Bertrand, Des Rosiers, Christine, Bertrand, Luc, Issad, Tarik, Lauzier, Benjamin, unité de recherche de l'institut du thorax UMR1087 UMR6291 (ITX), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN), Université Catholique de Louvain (UCL), de Duve Institute and Université catholique de Louvain, Université Catholique de Louvain (UCL)-de Duve Institute, Centre d’Ecologie Fonctionnelle et Evolutive (CEFE), Institut de Recherche pour le Développement (IRD [France-Sud])-Centre National de la Recherche Scientifique (CNRS)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), 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)-Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université Paul-Valéry - Montpellier 3 (UPVM), Chimie Et Interdisciplinarité : Synthèse, Analyse, Modélisation (CEISAM), Université de Nantes - Faculté des Sciences et des Techniques, Université de Nantes (UN)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS), UCL - SSS/IREC/CARD - Pôle de recherche cardiovasculaire, Université de Nantes - UFR de Médecine et des Techniques Médicales (UFR MEDECINE), Université de Nantes (UN)-Université de Nantes (UN)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Catholique de Louvain = Catholic University of Louvain (UCL), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Université Paul-Valéry - Montpellier 3 (UPVM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), 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)-Institut de Recherche pour le Développement (IRD [France-Sud]), Université de Nantes - UFR des Sciences et des Techniques (UN UFR ST), Université de Nantes (UN)-Université de Nantes (UN)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Unité de recherche de l'institut du thorax (ITX-lab), Université Paul-Valéry - Montpellier 3 (UPVM)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche pour le Développement (IRD [France-Sud])-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro - Montpellier SupAgro, 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 de Nantes (UN)-Université de Nantes (UN)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)

Subjects
O-GlcNAcylomic, [SDV]Life Sciences [q-bio], O‐GlcNAcylation, Metabolism and Nutritional Physiology, Mass Spectrometry, Acetylglucosamine, Rats, Eating, O-GlcNAcylation, Regular Paper, Animals, [CHIM]Chemical Sciences, hexosamine biosynthesis pathway, O‐GlcNAcylomic, Protein Processing, Post-Translational, development, metabolism, ComputingMilieux_MISCELLANEOUS, mass spectrometry
Abstract

International audience; AimMetabolic sources switch from carbohydrates in utero, to fatty acids after birth and then a mix once adults. O‐GlcNAcylation (O‐GlcNAc) is a post‐translational modification considered as a nutrient sensor. The purpose of this work was to assess changes in protein O‐GlcNAc levels, regulatory enzymes and metabolites during the first periods of life and decipher the impact of O‐GlcNAcylation on cardiac proteins.MethodsHeart, brain and liver were harvested from rats before and after birth (D‐1 and D0), in suckling animals (D12), after weaning with a standard (D28) or a low‐carbohydrate diet (D28F), and adults (D84). O‐GlcNAc levels and regulatory enzymes were evaluated by western blots. Mass spectrometry (MS) approaches were performed to quantify levels of metabolites regulating O‐GlcNAc and identify putative cardiac O‐GlcNAcylated proteins.ResultsProtein O‐GlcNAc levels decrease drastically and progressively from D‐1 to D84 (13‐fold, P < .05) in the heart, whereas the changes were opposite in liver and brain. O‐GlcNAc levels were unaffected by weaning diet in any tissues. Changes in expression of enzymes and levels of metabolites regulating O‐GlcNAc were tissue‐dependent. MS analyses identified changes in putative cardiac O‐GlcNAcylated proteins, namely those involved in the stress response and energy metabolism, such as ACAT1, which is only O‐GlcNAcylated at D0.ConclusionOur results demonstrate that protein O‐GlcNAc levels are not linked to dietary intake and regulated in a time and tissue‐specific manner during postnatal development. We have identified by untargeted MS putative proteins with a particular O‐GlcNAc signature across the development process suggesting specific role of these proteins.

Published
2020
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3. Protein O‐GlcNAcylation levels are regulated independently of dietary intake in a tissue and time‐specific manner during rat postnatal development.

Author

Dupas, Thomas, Denis, Manon, Dontaine, Justine, Persello, Antoine, Bultot, Laurent, Erraud, Angélique, Vertommen, Didier, Bouchard, Bertrand, Tessier, Arnaud, Rivière, Matthieu, Lebreton, Jacques, Bigot‐Corbel, Edith, Montnach, Jérôme, De Waard, Michel, Gauthier, Chantal, Burelle, Yan, Olson, Aaron K., Rozec, Bertrand, Des Rosiers, Christine, and Bertrand, Luc

Subjects
*LOW-carbohydrate diet, *SUCKLING in animals, *POST-translational modification, *PROTEINS, *MASS spectrometry
Abstract

Aim: Metabolic sources switch from carbohydrates in utero, to fatty acids after birth and then a mix once adults. O‐GlcNAcylation (O‐GlcNAc) is a post‐translational modification considered as a nutrient sensor. The purpose of this work was to assess changes in protein O‐GlcNAc levels, regulatory enzymes and metabolites during the first periods of life and decipher the impact of O‐GlcNAcylation on cardiac proteins. Methods: Heart, brain and liver were harvested from rats before and after birth (D‐1 and D0), in suckling animals (D12), after weaning with a standard (D28) or a low‐carbohydrate diet (D28F), and adults (D84). O‐GlcNAc levels and regulatory enzymes were evaluated by western blots. Mass spectrometry (MS) approaches were performed to quantify levels of metabolites regulating O‐GlcNAc and identify putative cardiac O‐GlcNAcylated proteins. Results: Protein O‐GlcNAc levels decrease drastically and progressively from D‐1 to D84 (13‐fold, P <.05) in the heart, whereas the changes were opposite in liver and brain. O‐GlcNAc levels were unaffected by weaning diet in any tissues. Changes in expression of enzymes and levels of metabolites regulating O‐GlcNAc were tissue‐dependent. MS analyses identified changes in putative cardiac O‐GlcNAcylated proteins, namely those involved in the stress response and energy metabolism, such as ACAT1, which is only O‐GlcNAcylated at D0. Conclusion: Our results demonstrate that protein O‐GlcNAc levels are not linked to dietary intake and regulated in a time and tissue‐specific manner during postnatal development. We have identified by untargeted MS putative proteins with a particular O‐GlcNAc signature across the development process suggesting specific role of these proteins. [ABSTRACT FROM AUTHOR]

Published
2021
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