Food-Derived hemorphins cross intestinal ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Food-Derived hemorphins cross intestinal and Blood-Brain Barriers In Vitro
Auteur(s) :
Domenger, Dorothee [Auteur]
Institut Charles Viollette (ICV) - ULR 7394 [ICV]
Cudennec, Benoit [Auteur]
Institut Charles Viollette (ICV) - EA 7394 [ICV]
Institut Charles Viollette (ICV) - ULR 7394
BioEcoAgro - UMR-T 1158
Kouach, Mostafa [Auteur]
Groupe de Recherche sur les formes Injectables et les Technologies Associées (GRITA) - ULR 7365
Touche, Veronique [Auteur]
Institut Pasteur de Lille
Landry, Christophe [Auteur]
Laboratoire de la Barrière Hémato-Encéphalique [LBHE]
Lesage, Jean [Auteur]
Environnement Périnatal et Santé - EA 4489
Environnement périnatal et croissance - EA 4489 [EPS]
Gosselet, Fabien [Auteur]
Laboratoire de la Barrière Hémato-Encéphalique [LBHE]
Lestavel, Sophie [Auteur]
Récepteurs nucléaires, Maladies Cardiovasculaires et Diabète (RNMCD) - U1011
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Goossens, Jean-Francois [Auteur]
Groupe de Recherche sur les formes Injectables et les Technologies Associées - ULR 7365 [GRITA]
Dhulster, Pascal [Auteur]
Institut Charles Viollette (ICV) - EA 7394 [ICV]
Institut Charles Viollette (ICV) - ULR 7394
Ravallec, Rozenn [Auteur]
Institut Charles Viollette (ICV) - ULR 7394
Institut Charles Viollette (ICV) - EA 7394 [ICV]
BioEcoAgro - UMR-T 1158
Institut Charles Viollette (ICV) - ULR 7394 [ICV]
Cudennec, Benoit [Auteur]
Institut Charles Viollette (ICV) - EA 7394 [ICV]
Institut Charles Viollette (ICV) - ULR 7394
BioEcoAgro - UMR-T 1158
Kouach, Mostafa [Auteur]
Groupe de Recherche sur les formes Injectables et les Technologies Associées (GRITA) - ULR 7365
Touche, Veronique [Auteur]
Institut Pasteur de Lille
Landry, Christophe [Auteur]
Laboratoire de la Barrière Hémato-Encéphalique [LBHE]
Lesage, Jean [Auteur]
Environnement Périnatal et Santé - EA 4489
Environnement périnatal et croissance - EA 4489 [EPS]
Gosselet, Fabien [Auteur]
Laboratoire de la Barrière Hémato-Encéphalique [LBHE]
Lestavel, Sophie [Auteur]
Récepteurs nucléaires, Maladies Cardiovasculaires et Diabète (RNMCD) - U1011
Récepteurs nucléaires, maladies cardiovasculaires et diabète - U 1011 [RNMCD]
Goossens, Jean-Francois [Auteur]
Groupe de Recherche sur les formes Injectables et les Technologies Associées - ULR 7365 [GRITA]
Dhulster, Pascal [Auteur]
Institut Charles Viollette (ICV) - EA 7394 [ICV]
Institut Charles Viollette (ICV) - ULR 7394
Ravallec, Rozenn [Auteur]
Institut Charles Viollette (ICV) - ULR 7394
Institut Charles Viollette (ICV) - EA 7394 [ICV]
BioEcoAgro - UMR-T 1158
Titre de la revue :
Frontiers in Endocrinology
Nom court de la revue :
Front. Endocrinol.
Numéro :
9
Date de publication :
2018
ISSN :
1664-2392
Discipline(s) HAL :
Sciences du Vivant [q-bio]
Résumé en anglais : [en]
A qualitative study is presented, where the main question was whether food-derived hemorphins, i.e., originating from digested alimentary hemoglobin, could pass the intestinal barrier and/or the blood–brain barrier (BBB). ...
Lire la suite >A qualitative study is presented, where the main question was whether food-derived hemorphins, i.e., originating from digested alimentary hemoglobin, could pass the intestinal barrier and/or the blood–brain barrier (BBB). Once absorbed, hemorphins are opioid receptor (OR) ligands that may interact with peripheral and central OR and have effects on food intake and energy balance regulation. LLVV-YPWT (LLVV-H4), LVV-H4, VV-H4, VV-YPWTQRF (VV-H7), and VV-H7 hemorphins that were previously identified in the 120 min digest resulting from the simulated gastrointestinal digestion of hemoglobin have been synthesized to be tested in in vitro models of passage of IB and BBB. LC-MS/MS analyses yielded that all hemorphins, except the LLVV-H4 sequence, were able to cross intact the human intestinal epithelium model with Caco-2 cells within 5–60 min when applied at 5 mM. Moreover, all hemorphins crossed intact the human BBB model with brain-like endothelial cells (BLEC) within 30 min when applied at 100 µM. Fragments of these hemorphins were also detected, especially the YPWT common tetrapeptide that retains OR-binding capacity. A cAMP assay performed in Caco-2 cells indicates that tested hemorphins behave as OR agonists in these cells by reducing cAMP production. We further provide preliminary results regarding the effects of hemorphins on tight junction proteins, specifically here the claudin-4 that is involved in paracellular permeability. All hemorphins at 100 µM, except the LLVV-H4 peptide, significantly decreased claudin-4 mRNA levels in the Caco-2 intestinal model. This in vitro study is a first step toward demonstrating food-derived hemorphins bioavailability which is in line with the growing body of evidence supporting physiological functions for food-derived peptides.Lire moins >
Lire la suite >A qualitative study is presented, where the main question was whether food-derived hemorphins, i.e., originating from digested alimentary hemoglobin, could pass the intestinal barrier and/or the blood–brain barrier (BBB). Once absorbed, hemorphins are opioid receptor (OR) ligands that may interact with peripheral and central OR and have effects on food intake and energy balance regulation. LLVV-YPWT (LLVV-H4), LVV-H4, VV-H4, VV-YPWTQRF (VV-H7), and VV-H7 hemorphins that were previously identified in the 120 min digest resulting from the simulated gastrointestinal digestion of hemoglobin have been synthesized to be tested in in vitro models of passage of IB and BBB. LC-MS/MS analyses yielded that all hemorphins, except the LLVV-H4 sequence, were able to cross intact the human intestinal epithelium model with Caco-2 cells within 5–60 min when applied at 5 mM. Moreover, all hemorphins crossed intact the human BBB model with brain-like endothelial cells (BLEC) within 30 min when applied at 100 µM. Fragments of these hemorphins were also detected, especially the YPWT common tetrapeptide that retains OR-binding capacity. A cAMP assay performed in Caco-2 cells indicates that tested hemorphins behave as OR agonists in these cells by reducing cAMP production. We further provide preliminary results regarding the effects of hemorphins on tight junction proteins, specifically here the claudin-4 that is involved in paracellular permeability. All hemorphins at 100 µM, except the LLVV-H4 peptide, significantly decreased claudin-4 mRNA levels in the Caco-2 intestinal model. This in vitro study is a first step toward demonstrating food-derived hemorphins bioavailability which is in line with the growing body of evidence supporting physiological functions for food-derived peptides.Lire moins >
Langue :
Anglais
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CHU Lille
Inserm
INRA
ISA
Univ. Artois
Univ. Littoral Côte d’Opale
Institut Pasteur de Lille
CHU Lille
Inserm
INRA
ISA
Univ. Artois
Univ. Littoral Côte d’Opale
Institut Pasteur de Lille
Collections :
Équipe(s) de recherche :
Modélisation biopharmaceutique et pharmacocinétique
Date de dépôt :
2019-02-26T17:11:37Z
2022-01-12T11:00:55Z
2022-01-12T11:00:55Z