Academic Journal
Sialic acids cleavage induced by elastin-derived peptides impairs the interaction between insulin and its receptor in adipocytes 3T3-L1
| العنوان: | Sialic acids cleavage induced by elastin-derived peptides impairs the interaction between insulin and its receptor in adipocytes 3T3-L1 |
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| المؤلفون: | Guillot, Alexandre, Toussaint, Kevin, Ebersold, Lucrece, Elbtaouri, Hassan, Thiebault, Emilie, Issad, T., Peretti, Franck, Maurice, Pascal, Sartelet, Hervé, Bennasroune, Amar, Martiny, Laurent, Dauchez, Manuel, Duca, Laurent, Durlach, Vincent, Romier, Béatrice, Baud, Stéphanie, Blaise, Sébastien |
| المساهمون: | Matrice Extracellulaire et Dynamique Cellulaire - UMR CNRS 7369 (MEDyC), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), 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 Paris Cité (UPCité), Centre recherche en CardioVasculaire et Nutrition = Center for CardioVascular and Nutrition research (C2VN), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Protéomique et Peptides Modifiés - PLBS (P3M), PAGés-PSM - Glycomique & protéomique - PLBS (PAGés-PSM), Plateformes Lilloises en Biologie et Santé - UAR 2014 - US 41 (PLBS), Institut Pasteur de Lille, Pasteur Network (Réseau International des Instituts Pasteur)-Pasteur Network (Réseau International des Instituts Pasteur)-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)-Institut Pasteur de Lille, Pasteur Network (Réseau International des Instituts Pasteur)-Pasteur Network (Réseau International des Instituts Pasteur)-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)-Plateformes Lilloises en Biologie et Santé - UAR 2014 - US 41 (PLBS), Pasteur Network (Réseau International des Instituts Pasteur)-Pasteur Network (Réseau International des Instituts Pasteur)-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), Hôpital universitaire Robert Debré Reims (CHU Reims) |
| المصدر: | ISSN: 1138-7548 ; Journal of Physiology and Biochemistry ; https://hal.science/hal-04737347 ; Journal of Physiology and Biochemistry, 2024, 80 (2), pp.363-379. ⟨10.1007/s13105-024-01010-5⟩. |
| بيانات النشر: | CCSD Springer Verlag (Germany) |
| سنة النشر: | 2024 |
| المجموعة: | LillOA (HAL Lille Open Archive, Université de Lille) |
| مصطلحات موضوعية: | N-glycan, Insulin receptor, Elastin-derived-peptides, insulin resistance, ligandreceptor affinity, [SDV]Life Sciences [q-bio] |
| الوصف: | International audience ; The insulin receptor (IR) plays an important role in insulin signal transduction, the defect of which is believed to be the root cause of type 2 diabetes. In 3T3-L1 adipocytes as in other cell types, the mature IR is a heterotetrameric cell surface glycoprotein composed of two α subunits and two β subunits. Our objective in our study, is to understand how the desialylation of N-glycan chains, induced by elastin-derived peptides, plays a major role in the function of the IR. Using the 3T3-L1 adipocyte line, we show that removal of the sialic acid from N-glycan chains (N893 and N908), induced by the elastin receptor complex (ERC) and elastin derived-peptides (EDPs), leads to a decrease in the autophosphorylation activity of the insulin receptor. We demonstrate by molecular dynamics approaches that the absence of sialic acids on one of these two sites is sufficient to generate local and general modifications of the structure of the IR. Biochemical approaches highlight a decrease in the interaction between insulin and its receptor when ERC sialidase activity is induced by EDPs. Therefore, desialylation by EDPs is synonymous with a decrease of IR sensitivity in adipocytes and could thus be a potential source of insulin resistance associated with diabetic conditions. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/38393636; PUBMED: 38393636 |
| DOI: | 10.1007/s13105-024-01010-5 |
| الاتاحة: | https://hal.science/hal-04737347 https://hal.science/hal-04737347v1/document https://hal.science/hal-04737347v1/file/Guillot_et_al_2024.pdf https://doi.org/10.1007/s13105-024-01010-5 |
| Rights: | info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.C9776A8A |
| قاعدة البيانات: | BASE |
| DOI: | 10.1007/s13105-024-01010-5 |
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