P. .. Conclusion,

. .. Appendices,

. .. Acknowledgements,

S. D. Conner and S. L. Schmid, Regulated portals of entry into the cell, Nature, vol.422, pp.37-44, 2003.

P. J. Sansonetti, War and peace at mucosal surfaces, Nature Reviews Immunology, vol.4, pp.953-64, 2004.

T. Kökten, F. Hansmannel, H. Melhem, and L. Peyrin-biroulet, Physiopathologie des maladies inflammatoires chroniques de l'intestin (MICI). HEGEL -HEpato-GastroEntérologie Libérale, 2016.

R. Moriez, C. Salvador-cartier, V. Theodorou, J. Fioramonti, H. Eutamene et al., Myosin light chain kinase is involved in lipopolysaccharide-induced disruption of colonic epithelial barrier and bacterial translocation in rats, Am J Pathol, vol.167, pp.1071-1080, 2005.

S. Y. Salim and J. D. Söderholm, Importance of disrupted intestinal barrier in inflammatory bowel diseases, Inflammatory Bowel Diseases, vol.17, pp.362-81, 2011.

S. J. Fletcher and J. Z. Rappoport, The role of vesicle trafficking in epithelial cell motility, Biochem Soc Trans, vol.37, pp.1072-1078, 2009.

H. Bauer, W. Stelzhammer, R. Fuchs, T. M. Weiger, C. Danninger et al., Astrocytes and neurons express the tight junction-specific protein occludin in vitro, Exp Cell Res, vol.250, pp.434-442, 1999.

K. Turksen and T. Troy, Barriers built on claudins. J Cell Sci, vol.117, pp.2435-2482, 2004.

K. Ebnet, A. Suzuki, S. Ohno, and D. Vestweber, Junctional adhesion molecules (JAMs): more molecules with dual functions?, J Cell Sci, vol.117, pp.19-29, 2004.

G. Bazzoni, The JAM family of junctional adhesion molecules, Curr Opin Cell Biol, vol.15, pp.525-555, 2003.

M. Furuse, M. Itoh, T. Hirase, A. Nagafuchi, S. Yonemura et al., Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions, J Cell Biol, vol.127, pp.1617-1643, 1994.

K. Morita, M. Furuse, K. Fujimoto, and S. Tsukita, Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands, Proc Natl Acad Sci, vol.96, pp.511-517, 1999.

K. Ebnet, Organization of multiprotein complexes at cell-cell junctions, Histochem Cell Biol, vol.130, pp.1-20, 2008.

Y. S. Kim and S. B. Ho, Intestinal Goblet Cells and Mucins in Health and Disease: Recent Insights and Progress, Current Gastroenterology Reports, vol.12, pp.319-349, 2010.

G. C. Hansson, Role of mucus layers in gut infection and inflammation, Current Opinion in Microbiology, vol.15, pp.57-62, 2012.

M. Elderman, B. Sovran, F. Hugenholtz, K. Graversen, M. Huijskes et al., The effect of age on the intestinal mucus thickness, microbiota composition and immunity in relation to sex in mice, PLOS ONE, vol.12, p.184274, 2017.

J. S. Cornes, Number, size, and distribution of Peyer's patches in the human small intestine: Part I The development of Peyer's patches, Gut, vol.6, pp.225-234, 1965.

R. H. Stead, M. F. Dixon, N. H. Bramwell, R. H. Riddell, and J. Bienenstock, Mast cells are closely apposed to nerves in the human gastrointestinal mucosa, Gastroenterology, vol.97, pp.575-85, 1989.

S. Ichikawa, N. Eda, and S. Uchino, Close association of peptidergic nerves with lymphocytes in canine and monkey ileal villi, Okajimas Folia Anat Jpn, vol.69, pp.199-207, 1992.

L. Vulchanova, M. Casey, G. Crabb, W. Kennedy, and D. Brown, Anatomical evidence for enteric neuroimmune interactions in Peyer's patches, Journal of Neuroimmunology, vol.185, pp.64-74, 2007.

T. C. Savidge, P. Newman, C. Pothoulakis, A. Ruhl, M. Neunlist et al., Enteric Glia Regulate Intestinal Barrier Function and Inflammation Via Release of S-Nitrosoglutathione, Gastroenterology, vol.132, pp.1344-58, 2007.

M. Lal-nag and P. J. Morin, The claudins, Genome Biology, vol.10, p.235, 2009.

F. Krämer, K. White, M. Kubbies, K. Swisshelm, and B. H. Weber, Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer, Hum Genet, vol.107, pp.249-56, 2000.

S. L. Kominsky, P. Argani, D. Korz, E. Evron, V. Raman et al., Loss of the tight junction protein claudin-7 correlates with histological grade in both ductal carcinoma in situ and invasive ductal carcinoma of the breast, Oncogene, vol.22, pp.2021-2054, 2003.

S. L. Kominsky, M. Vali, D. Korz, T. G. Gabig, S. A. Weitzman et al., Clostridium perfringens enterotoxin elicits rapid and specific cytolysis of breast carcinoma cells mediated through tight junction proteins claudin 3 and 4, Am J Pathol, vol.164, issue.10, pp.63721-63723, 2004.

K. Umeda, J. Ikenouchi, S. Katahira-tayama, K. Furuse, H. Sasaki et al., ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation, Cell, vol.126, pp.741-54, 2006.

J. Nomme, A. Antanasijevic, M. Caffrey, C. M. Van-itallie, J. M. Anderson et al., Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins, Journal of Biological Chemistry, vol.290, pp.16595-606, 2015.

S. M. Krug, D. Günzel, M. P. Conrad, I. Lee, S. Amasheh et al., Chargeselective claudin channels: Charge-selective claudin channels, Annals of the New York Academy of Sciences, vol.1257, pp.20-28, 2012.

O. R. Colegio, C. M. Van-itallie, H. J. Mccrea, C. Rahner, and J. M. Anderson, Claudins create charge-selective channels in the paracellular pathway between epithelial cells

, Am J Physiol, vol.283, pp.142-147, 2002.

J. Piontek, L. Winkler, H. Wolburg, S. L. Müller, N. Zuleger et al., Formation of tight junction: determinants of homophilic interaction between classic claudins, The FASEB Journal, vol.22, pp.146-58, 2008.

C. M. Van-itallie, T. M. Gambling, J. L. Carson, and J. M. Anderson, Palmitoylation of claudins is required for efficient tight-junction localization, J Cell Sci, vol.118, pp.1427-1463, 2005.

C. M. Van-itallie, A. J. Tietgens, K. Logrande, A. Aponte, M. Gucek et al., Phosphorylation of claudin-2 on serine 208 promotes membrane retention and

M. Hayashi and M. Tomita, Mechanistic Analysis for Drug Permeation Through Intestinal Membrane, Drug Metabolism and Pharmacokinetics, vol.22, pp.67-77, 2007.

H. Bergmann, D. Rogoll, W. Scheppach, R. Melcher, and E. Richling, The Ussing type chamber model to study the intestinal transport and modulation of specific tightjunction genes using a colonic cell line, Molecular Nutrition & Food Research, vol.53, pp.1211-1236, 2009.

S. M. Krug, M. Amasheh, I. Dittmann, I. Christoffel, M. Fromm et al., Sodium caprate as an enhancer of macromolecule permeation across tricellular tight junctions of intestinal cells, Biomaterials, vol.34, pp.275-82, 2013.

D. J. Brayden, S. Maher, B. Bahar, and E. Walsh, Sodium caprate-induced increases in intestinal permeability and epithelial damage are prevented by misoprostol, European Journal of Pharmaceutics and Biopharmaceutics, vol.94, pp.194-206, 2015.

L. K. Chico, L. J. Van-eldik, and D. M. Watterson, Targeting protein kinases in central nervous system disorders, Nature Reviews Drug Discovery, vol.8, pp.892-909, 2009.

Y. Fujita and T. Yamashita, Axon growth inhibition by RhoA/ROCK in the central nervous system, Frontiers in Neuroscience, vol.8, 2014.

Y. Feng, P. V. Lograsso, O. Defert, and R. Li, Rho Kinase (ROCK) Inhibitors and Their Therapeutic Potential, Journal of Medicinal Chemistry, vol.59, pp.2269-300, 2016.

Y. Huang, S. Xiao, and Q. Jiang, Role of Rho kinase signal pathway in inflammatory bowel disease, Int J Clin Exp Med, vol.8, pp.3089-97, 2015.

E. Elamin, A. Masclee, J. Dekker, and D. Jonkers, Ethanol disrupts intestinal epithelial tight junction integrity through intracellular calcium-mediated Rho/ROCK activation, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.306, pp.677-85, 2014.

N. Petersen, T. M. Frimurer, T. Pedersen, M. Egerod, K. L. Wewer-albrechtsen et al., Inhibiting RHOA Signaling in Mice Increases Glucose Tolerance and Numbers of Enteroendocrine and Other Secretory Cells in the Intestine, Gastroenterology, vol.155, pp.1164-1176, 2018.

Y. Wang, X. Wang, W. Yang, X. Zhao, and R. Zhang, Effect of Simvastatin on the Intestinal Rho/ROCK Signaling Pathway in Rats With Sepsis, Journal of Surgical Research, vol.232, pp.531-539, 2018.

Z. Li, M. Gao, B. Yang, H. Zhang, K. Wang et al., Naringin attenuates MLC phosphorylation and NF-?B activation to protect sepsis-induced intestinal injury via RhoA/ROCK pathway, Biomedicine & Pharmacotherapy, vol.103, pp.50-58, 2018.

Y. Zolotarevsky, G. Hecht, A. Koutsouris, D. E. Gonzalez, C. Quan et al., A membrane-permeant peptide that inhibits MLC kinase restores barrier function in in vitro models of intestinal disease, Gastroenterology, vol.123, pp.163-72, 2002.

F. Wang, W. V. Graham, Y. Wang, E. D. Witkowski, B. T. Schwarz et al., Interferongamma and tumor necrosis factor-alpha synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression, Am J Pathol, vol.166, pp.409-428, 2005.

R. Al-sadi, S. Guo, D. Ye, M. Rawat, and T. Y. Ma, TNF-? Modulation of Intestinal Tight Junction Permeability Is Mediated by NIK/IKK-? Axis Activation of the Canonical NF-?B Pathway, The American Journal of Pathology, vol.186, pp.1151-65, 2016.

B. T. Schwarz, F. Wang, L. Shen, D. R. Clayburgh, L. Su et al., LIGHT Signals Directly to Intestinal Epithelia to Cause Barrier Dysfunction via Cytoskeletal and Endocytic Mechanisms, Gastroenterology, vol.132, pp.2383-94, 2007.

L. Wu, W. Peng, W. Kuo, C. Huang, Y. Ni et al., Commensal bacterial endocytosis in epithelial cells is dependent on myosin light chain kinaseactivated brush border fanning by interferon-?, Am J Pathol, vol.184, pp.2260-74, 2014.

M. Bruewer, M. Utech, A. I. Ivanov, A. M. Hopkins, C. A. Parkos et al., Interferongamma induces internalization of epithelial tight junction proteins via a macropinocytosis-like process, FASEB J, vol.19, pp.923-956, 2005.

C. A. Dinarello, The interleukin-1 family: 10 years of discovery, FASEB J, vol.8, pp.1314-1339, 1994.

K. Kusugami, A. Fukatsu, M. Tanimoto, M. Shinoda, J. Haruta et al., Elevation of interleukin-6 in inflammatory bowel disease is macrophage-and epithelial cell-dependent, Dig Dis Sci, vol.40, pp.949-59, 1995.

T. Suzuki, N. Yoshinaga, and S. Tanabe, Interleukin-6 (IL-6) Regulates Claudin-2 Expression and Tight Junction Permeability in Intestinal Epithelium, Journal of Biological Chemistry, vol.286, pp.31263-71, 2011.

Y. Xiao, Y. Cao, Y. Yan, J. Cai, and W. , Neutralization of IL-6 and TNF-? ameliorates intestinal permeability in DSS-induced colitis, Cytokine, vol.83, pp.189-92, 2016.

Y. Wang, J. B. Mumm, R. Herbst, R. Kolbeck, and Y. Wang, IL-22 Increases Permeability of Intestinal Epithelial Tight Junctions by Enhancing Claudin-2 Expression, The Journal of Immunology, vol.199, pp.3316-3341, 2017.

F. Furfaro, D. Gilardi, M. Allocca, C. Cicerone, C. Correale et al., IL-23 Blockade for Crohn s disease: next generation of anti-cytokine therapy, Expert Review of Clinical Immunology, vol.13, pp.457-67, 2017.

M. F. Neurath, IL-23 in inflammatory bowel diseases and colon cancer, Cytokine & Growth Factor Reviews, vol.45, pp.1-8, 2019.

C. C?tan?, B. Neagoe, I. Cozma, V. Magda?, C. T?b?ran et al., Contribution of the IL-17/IL-23 axis to the pathogenesis of inflammatory bowel disease, World J Gastroenterol, vol.21, pp.5823-5853, 2015.

M. Saraiva, O. Garra, and A. , The regulation of IL-10 production by immune cells, Nature Reviews Immunology, vol.10, pp.170-81, 2010.

T. Ochi, Y. Feng, S. Kitamoto, H. Nagao-kitamoto, P. Kuffa et al., Dietdependent, microbiota-independent regulation of IL-10-producing lamina propria macrophages in the small intestine, Scientific Reports, vol.6, 2016.

C. Gu, L. Wu, and X. Li, IL-17 family: cytokines, receptors and signaling, Cytokine, vol.64, pp.477-85, 2013.

W. Jin and C. Dong, IL-17 cytokines in immunity and inflammation, Emerging Microbes & Infections, vol.2, pp.1-5, 2013.

T. L. Denning, Y. Wang, S. R. Patel, I. R. Williams, and B. Pulendran, Lamina propria macrophages and dendritic cells differentially induce regulatory and interleukin 17-producing T cell responses, Nature Immunology, vol.8, pp.1086-94, 2007.

W. Hueber, B. E. Sands, S. Lewitzky, M. Vandemeulebroecke, W. Reinisch et al., Secukinumab, a human anti-IL-17A monoclonal antibody, for moderate to severe Crohn's disease: unexpected results of a randomised, doubleblind placebo-controlled trial, Gut, vol.61, pp.1693-700, 2012.

L. W. Collison, C. J. Workman, T. T. Kuo, K. Boyd, Y. Wang et al., The inhibitory cytokine IL-35 contributes to regulatory T-cell function, Nature, vol.450, pp.566-575, 2007.

P. Shen, T. Roch, V. Lampropoulou, R. A. O'connor, U. Stervbo et al., IL-35-producing B cells are critical regulators of immunity during autoimmune and infectious diseases, Nature, vol.507, pp.366-70, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02639864

Y. Wang, Y. Mao, J. Zhang, G. Shi, L. Cheng et al., IL-35 recombinant protein reverses inflammatory bowel disease and psoriasis through regulation of inflammatory cytokines and immune cells, J Cell Mol Med, vol.22, pp.1014-1039, 2018.

L. Zhou, J. E. Lopes, M. Chong, I. I. Ivanov, R. Min et al., TGF-?induced Foxp3 inhibits TH17 cell differentiation by antagonizing ROR?t function, Nature, vol.453, pp.236-276, 2008.

K. L. Howe, R. J. Lorentz, A. Assa, L. J. Pinnell, K. C. Johnson-henry et al., Transforming Growth Factor-?1 Protects Against Intestinal Epithelial Barrier Dysfunction Caused By Hypoxia-Reoxygenation, Shock, vol.43, pp.483-492, 2015.

D. Bauché and J. C. Marie, Transforming growth factor ?: a master regulator of the gut microbiota and immune cell interactions, Clinical & Translational Immunology, vol.6, p.136, 2017.

N. Barker, Adult intestinal stem cells: critical drivers of epithelial homeostasis and regeneration, Nat Rev Mol Cell Biol, vol.15, pp.19-33, 2014.

M. R. Neutra, L. J. O'malley, and R. D. Specian, Regulation of intestinal goblet cell secretion. II. A survey of potential secretagogues, Am J Physiol, vol.242, pp.380-387, 1982.

J. K. Gustafsson, A. Ermund, M. Johansson, A. Schütte, G. C. Hansson et al., An ex vivo method for studying mucus formation, properties, and thickness in human colonic biopsies and mouse small and large intestinal explants, Am J Physiol Gastrointest Liver Physiol, vol.302, pp.430-438, 2012.

D. R. Halm and S. T. Halm, Secretagogue response of goblet cells and columnar cells in human colonic crypts, Am J Physiol, vol.278, pp.212-233, 2000.

L. Vereecke, S. Vieira-silva, T. Billiet, J. H. Van-es, M. Guire et al., A20 controls intestinal homeostasis through cell-specific activities, Nature Communications, vol.5, 2014.

M. Van-der-sluis, D. Koning, B. , D. Bruijn, A. Velcich et al., Muc2-Deficient Mice Spontaneously Develop Colitis, Indicating That MUC2 Is Critical for Colonic Protection, Gastroenterology, vol.131, pp.117-146, 2006.

P. Lu, N. Burger-van-paassen, M. Van-der-sluis, J. Witte-bouma, J. Kerckaert et al., Colonic gene expression patterns of mucin muc2 knockout mice reveal various phases in colitis development1, Inflammatory Bowel Diseases, vol.17, pp.2047-57, 2011.

S. Z. Hasnain, S. Tauro, I. Das, H. Tong, A. Chen et al., IL-10 Promotes Production of Intestinal Mucus by Suppressing Protein Misfolding and Endoplasmic Reticulum Stress in Goblet Cells, Gastroenterology, vol.144, pp.357-368, 2013.

M. Van-der-sluis, J. Bouma, A. Vincent, A. Velcich, K. L. Carraway et al., Combined defects in epithelial and immunoregulatory factors exacerbate the pathogenesis of inflammation: mucin 2-interleukin 10-deficient mice, Lab Invest, vol.88, pp.634-676, 2008.

P. Plaisancié, A. Barcelo, F. Moro, J. Claustre, J. A. Chayvialle et al., Effects of neurotransmitters, gut hormones, and inflammatory mediators on mucus discharge in rat colon, Am J Physiol, vol.275, pp.1073-1084, 1998.

K. Dabbagh, K. Takeyama, H. M. Lee, I. F. Ueki, J. A. Lausier et al., IL-4 induces mucin gene expression and goblet cell metaplasia in vitro and in vivo, J Immunol, vol.162, pp.6233-6240, 1999.

R. L. Coffman, B. W. Seymour, S. Hudak, J. Jackson, and D. Rennick, Antibody to interleukin-5 inhibits helminth-induced eosinophilia in mice, Science, vol.245, pp.308-318, 1989.

M. L. Enss, M. Cornberg, S. Wagner, A. Gebert, M. Henrichs et al., Proinflammatory cytokines trigger MUC gene expression and mucin release in the intestinal cancer cell line LS180, Inflamm Res, vol.49, pp.162-171, 2000.

G. Birchenough, M. E. Johansson, J. K. Gustafsson, J. H. Bergström, and G. C. Hansson, New developments in goblet cell mucus secretion and function, Mucosal Immunology, vol.8, pp.712-721, 2015.

V. Liévin-le-moal and A. L. Servin, The front line of enteric host defense against unwelcome intrusion of harmful microorganisms: mucins, antimicrobial peptides, and microbiota, Clin Microbiol Rev, vol.19, pp.315-352, 2006.

P. Van-den-abbeele, C. Belzer, M. Goossens, M. Kleerebezem, D. Vos et al., Butyrate-producing Clostridium cluster XIVa species specifically colonize mucins in an in vitro gut model, The ISME Journal, vol.7, pp.949-61, 2013.

L. V. Hooper and A. J. Macpherson, Immune adaptations that maintain homeostasis with the intestinal microbiota, Nature Reviews Immunology, vol.10, pp.159-69, 2010.

L. Arike and G. C. Hansson, The Densely O-Glycosylated MUC2 Mucin Protects the Intestine and Provides Food for the Commensal Bacteria, J Mol Biol, vol.428, pp.3221-3230, 2016.

H. Li, J. P. Limenitakis, T. Fuhrer, M. B. Geuking, M. A. Lawson et al., The outer mucus layer hosts a distinct intestinal microbial niche, Nature Communications, vol.6, 2015.

E. Rogier, A. Frantz, M. Bruno, and C. Kaetzel, Secretory IgA is Concentrated in the Outer Layer of Colonic Mucus along with Gut Bacteria, Pathogens, vol.3, pp.390-403, 2014.

K. Suzuki, B. Meek, Y. Doi, M. Muramatsu, T. Chiba et al., Aberrant expansion of segmented filamentous bacteria in IgA-deficient gut, Proceedings of the National Academy of Sciences, vol.101, pp.1981-1987, 2004.

M. Wlodarska, C. A. Thaiss, R. Nowarski, J. Henao-mejia, J. Zhang et al., NLRP6 Inflammasome Orchestrates the Colonic Host-Microbial Interface by Regulating Goblet Cell Mucus Secretion, Cell, vol.156, pp.1045-59, 2014.

L. K. Vigsnaes, P. Van-den-abbeele, K. Sulek, H. L. Frandsen, C. Steenholdt et al., Microbiotas from UC patients display altered metabolism and reduced ability of LAB to colonize mucus, Sci Rep, vol.3, p.1110, 2013.

M. Johansson and G. C. Hansson, Immunological aspects of intestinal mucus and mucins, Nature Reviews Immunology, vol.16, pp.639-688, 2016.

E. Cario, Toll-like receptors in inflammatory bowel diseases: a decade later, Inflamm Bowel Dis, vol.16, pp.1583-97, 2010.

A. L. Frantz, E. W. Rogier, C. R. Weber, L. Shen, D. A. Cohen et al., Targeted deletion of MyD88 in intestinal epithelial cells results in compromised antibacterial immunity associated with downregulation of polymeric immunoglobulin receptor, mucin-2 and antibacterial peptides, Mucosal Immunology, vol.5, pp.501-513, 2012.

S. Rakoff-nahoum, J. Paglino, F. Eslami-varzaneh, S. Edberg, and R. Medzhitov, Recognition of Commensal Microflora by Toll-Like Receptors Is Required for Intestinal Homeostasis, Cell, vol.118, pp.229-270, 2004.

O. Shibolet and D. K. Podolsky, TLRs in the Gut.IV. Negative regulation of Toll-like receptors and intestinal homeostasis: addition by subtraction, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.292, pp.1469-73, 2007.

J. M. Lehmann, L. B. Moore, T. A. Smith-oliver, W. O. Wilkison, T. M. Willson et al., An antidiabetic thiazolidinedione is a high affinity ligand for peroxisome proliferator-activated receptor gamma (PPAR gamma), J Biol Chem, vol.270, pp.12953-12959, 1995.

K. L. Schaefer, S. Denevich, C. Ma, S. R. Cooley, A. Nakajima et al., Intestinal Antiinflammatory Effects of Thiazolidenedione Peroxisome Proliferator-Activated Receptor-? Ligands on T Helper Type 1 Chemokine Regulation Include Nontranscriptional Control Mechanisms, Inflammatory Bowel Diseases, vol.11, pp.244-52, 2005.

E. Saez, P. Tontonoz, M. C. Nelson, J. G. Alvarez, U. T. Ming et al., Activators of the nuclear receptor PPARgamma enhance colon polyp formation, Nat Med, vol.4, pp.1058-61, 1998.

C. G. Su, X. Wen, S. T. Bailey, W. Jiang, S. M. Rangwala et al., A novel therapy for colitis utilizing PPAR-gamma ligands to inhibit the epithelial inflammatory response, J Clin Invest, vol.104, pp.383-392, 1999.

P. Desreumaux, L. Dubuquoy, S. Nutten, M. Peuchmaur, W. Englaro et al., Attenuation of colon inflammation through activators of the retinoid X receptor (RXR)/peroxisome proliferator-activated receptor gamma (PPARgamma) heterodimer. A basis for new therapeutic strategies, J Exp Med, vol.193, pp.827-865, 2001.

M. X. Byndloss, E. E. Olsan, F. Rivera-chávez, C. R. Tiffany, S. A. Cevallos et al., Microbiota-activated PPAR-? signaling inhibits dysbiotic Enterobacteriaceae expansion, Science, vol.357, pp.570-575, 2017.

M. Nepelska, T. De-wouters, E. Jacouton, F. Béguet-crespel, N. Lapaque et al., Commensal gut bacteria modulate phosphorylation-dependent PPAR? transcriptional activity in human intestinal epithelial cells, Scientific Reports, vol.7, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02628360

D. R. Donohoe, N. Garge, X. Zhang, W. Sun, T. M. O'connell et al., The microbiome and butyrate regulate energy metabolism and autophagy in the mammalian colon, Cell Metab, vol.13, pp.517-543, 2011.

P. Lu, C. P. Sodhi, Y. Yamaguchi, H. Jia, T. Prindle et al., Intestinal epithelial Toll-like receptor 4 prevents metabolic syndrome by regulating interactions between microbes and intestinal epithelial cells in mice, Mucosal Immunology, vol.11, pp.727-767, 2018.

D. L. Boone, E. E. Turer, E. G. Lee, R. Ahmad, M. T. Wheeler et al., The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses, Nature Immunology, vol.5, pp.1052-60, 2004.

T. Kawai, S. Akira, and . Tlr, Seminars in Immunology, vol.19, pp.24-32, 2007.

A. S. Chitre, M. G. Kattah, Y. Y. Rosli, M. Pao, M. Deswal et al., A20 upregulation during treated HIV disease is associated with intestinal epithelial cell recovery and function, PLOS Pathogens, vol.14, p.1006806, 2018.

B. Malcomson, H. Wilson, E. Veglia, G. Thillaiyampalam, R. Barsden et al., Connectivity mapping (ssCMap) to predict A20-inducing drugs and their antiinflammatory action in cystic fibrosis, Proceedings of the National Academy of Sciences, vol.113, pp.3725-3759, 2016.

Y. Ogura, D. K. Bonen, N. Inohara, D. L. Nicolae, F. F. Chen et al., A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease, Nature, vol.411, pp.603-609, 2001.

S. Buhner, Genetic basis for increased intestinal permeability in families with Crohn's disease: role of CARD15 3020insC mutation?, Gut, vol.55, pp.342-349, 2006.

A. Nabhani, Z. Dietrich, G. Hugot, J. Barreau, and F. , Nod2: The intestinal gate keeper, PLOS Pathogens, vol.13, p.1006177, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01602910

F. Barreau, U. Meinzer, F. Chareyre, D. Berrebi, M. Niwa-kawakita et al., CARD15/NOD2 is required for Peyer's patches homeostasis in mice, PLoS ONE, vol.2, p.523, 2007.

A. Rehman, C. Sina, O. Gavrilova, R. Häsler, S. Ott et al., Nod2 is essential for temporal development of intestinal microbial communities, Gut, vol.60, pp.1354-62, 2011.

D. N. Frank, C. E. Robertson, C. M. Hamm, Z. Kpadeh, T. Zhang et al., Disease phenotype and genotype are associated with shifts in intestinalassociated microbiota in inflammatory bowel diseases, Inflamm Bowel Dis, vol.17, pp.179-84, 2011.

E. Li, C. M. Hamm, A. S. Gulati, R. B. Sartor, H. Chen et al., Inflammatory bowel diseases phenotype, C. difficile and NOD2 genotype are associated with shifts in human ileum associated microbial composition, PLoS ONE, vol.7, p.26284, 2012.

T. Cars, B. Wettermark, R. Löfberg, I. Eriksson, J. Sundström et al., Healthcare Utilisation and Drug Treatment in a Large Cohort of Patients with Inflammatory Bowel Disease, Journal of Crohn's and Colitis, vol.10, pp.556-65, 2016.

G. Kolios, V. Valatas, and S. G. Ward, Nitric oxide in inflammatory bowel disease: a universal messenger in an unsolved puzzle, Immunology, vol.113, pp.427-464, 2004.

M. J. Menconi, N. Unno, M. Smith, D. E. Aguirre, and M. P. Fink, Nitric oxide donor-induced hyperpermeability of cultured intestinal epithelial monolayers: role of superoxide radical, hydroxyl radical, and peroxynitrite, Biochim Biophys Acta, vol.1425, pp.189-203, 1998.

B. L. Tepperman and B. Whittel, Physiological and Pathophysiological Roles of Nitric Oxide in Gastrointestinal Function, Nitric Oxide, pp.725-756, 2000.

N. I. Kochar, A. V. Chandewal, R. L. Bakal, and P. N. Kochar, Nitric Oxide and the Gastrointestinal Tract, International Journal of Pharmacology, vol.7, pp.31-40, 2011.

J. B. Dattilo and R. G. Makhoul, The Role of Nitric Oxide in, Vascular Biology and Pathobiology. Annals of Vascular Surgery, vol.11, pp.307-321, 1997.

M. Parent, F. Dupuis, P. Maincent, C. Vigneron, P. Leroy et al., Quel avenir en thérapeutique cardiovasculaire pour le monoxyde d'azote et ses dérivés ?, Annales Pharmaceutiques Françaises, vol.71, pp.84-94, 2013.

G. A. Cheadle, T. W. Costantini, N. Lopez, V. Bansal, B. P. Eliceiri et al., Enteric Glia Cells Attenuate Cytomix-Induced Intestinal Epithelial Barrier Breakdown, PLoS ONE, vol.8, p.69042, 2013.

S. Kanwar, J. L. Wallace, D. Befus, and P. Kubes, Nitric oxide synthesis inhibition increases epithelial permeability via mast cells, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.266, pp.222-231, 1994.

W. K. Macnaughton, Nitric oxide-donating compounds stimulate electrolyte transport in the guinea pig intestine in vitro, Life Sci, vol.53, pp.585-93, 1993.

H. Tamai and T. S. Gaginella, Direct evidence for nitric oxide stimulation of electrolyte secretion in the rat colon, Free Radic Res Commun, vol.19, pp.229-268, 1993.

I. T. Lippe and P. Holzer, Participation of endothelium-derived nitric oxide but not prostacyclin in the gastric mucosal hyperaemia due to acid back-diffusion, Br J Pharmacol, vol.105, pp.708-722, 1992.

P. Kubes, M. Suzuki, and D. N. Granger, Nitric oxide: an endogenous modulator of leukocyte adhesion, Proc Natl Acad Sci, vol.88, pp.4651-4656, 1991.

P. Kubes, S. Kanwar, X. F. Niu, and J. P. Gaboury, Nitric oxide synthesis inhibition induces leukocyte adhesion via superoxide and mast cells, FASEB J, vol.7, pp.1293-1302, 1993.

Z. Li, X. Zhang, H. Zhou, W. Liu, and J. Li, Exogenous S-nitrosoglutathione attenuates inflammatory response and intestinal epithelial barrier injury in endotoxemic rats, Journal of Trauma and Acute Care Surgery, vol.80, pp.977-84, 2016.

I. Turan, S. Ozacmak, H. Ozacmak, V. H. Barut, F. Ozacmak et al., The effects of S-nitrosoglutathione on intestinal ischemia reperfusion injury and acute lung injury in rats: Roles of oxidative stress and NF-?B, Tissue and Cell, vol.52, pp.35-41, 2018.

M. Flamant, P. Aubert, M. Rolli-derkinderen, A. Bourreille, M. R. Neunlist et al., Enteric glia protect against Shigella flexneri invasion in intestinal epithelial cells: a role for S-nitrosoglutathione, Gut, vol.60, pp.473-84, 2011.

G. De-souza, P. Taladriz-blanco, L. Velloso, and M. De-oliveira, Nitric Oxide Released from Luminal S-Nitroso-N-Acetylcysteine Increases Gastric Mucosal Blood Flow, Molecules, vol.20, pp.4109-4132, 2015.

J. L. Wallace, S. N. Elliott, D. Soldato, P. Mcknight, W. Sannicolo et al., Gastrointestinal-sparing anti-inflammatory drugs: The development of nitric oxidereleasing NSAIDs, Drug Development Research, vol.42, pp.144-153, 1997.

M. N. Muscará and J. V. Wallace, Therapeutic potential of nitric oxide donors and inhibitors, American Journal of Physiology -Gastrointestinal and Liver Physiology, vol.276, pp.1313-1319, 1999.

N. Aoki, G. Johnson, and A. M. Lefer, Beneficial effects of two forms of NO administration in feline splanchnic artery occlusion shock, Am J Physiol, vol.258, pp.275-281, 1990.

N. Numata, K. Takahashi, N. Mizuno, N. Utoguchi, Y. Watanabe et al., Improvement of Intestinal Absorption of Macromolecules by Nitric Oxide Donor, Journal of Pharmaceutical Sciences, vol.89, pp.1296-304, 2000.

D. Xu, Q. Lu, and E. A. Deitch, Nitric oxide directly impairs intestinal barrier function, Shock, vol.17, pp.139-184, 2002.

T. W. Gauthier, K. L. Davenpeck, and A. M. Lefer, Nitric oxide attenuates leukocyteendothelial interaction via P-selectin in splanchnic ischemia-reperfusion, Am J Physiol, vol.267, pp.562-568, 1994.

C. S. Potten, G. Owen, and D. Booth, Intestinal stem cells protect their genome by selective segregation of template DNA strands, J. Cell. Sci, vol.115, pp.2381-2388, 2002.

J. R. Turner, Show me the pathway! Regulation of paracellular permeability by Na(+)-glucose cotransport, Adv. Drug Deliv. Rev, vol.41, pp.265-281, 2000.

Y. S. Kim and S. B. Ho, Intestinal Goblet Cells and Mucins in Health and Disease: Recent Insights and Progress, Current Gastroenterology Reports, vol.12, pp.319-330, 2010.

L. V. Hooper and A. J. Macpherson, Immune adaptations that maintain homeostasis with the intestinal microbiota, Nature Reviews Immunology, vol.10, pp.159-169, 2010.

D. Payros, T. Secher, M. Boury, C. Brehin, S. Ménard et al., Maternally acquired genotoxic Escherichia coli alters offspring's intestinal homeostasis, Gut Microbes, vol.5, pp.313-512, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02935531

L. L. Clarke, A guide to Ussing chamber studies of mouse intestine, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.296, pp.1151-1166, 2009.

B. Srinivasan, A. R. Kolli, M. B. Esch, H. E. Abaci, M. L. Shuler et al., TEER Measurement Techniques for In Vitro Barrier Model Systems, Journal of Laboratory Automation, vol.20, pp.107-126, 2015.

J. Bonetti, Y. Zhou, M. Parent, I. Clarot, H. Yu et al., Intestinal absorption of S-nitrosothiols: Permeability and transport mechanisms, Biochemical Pharmacology, vol.155, pp.21-31, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01824879

M. Gabello, M. C. Valenzano, E. P. Zurbach, and J. M. Mullin, Omeprazole induces gastric transmucosal permeability to the peptide bradykinin, World J. Gastroenterol, vol.16, pp.1097-1103, 2010.

M. Hayashi and M. Tomita, Mechanistic Analysis for Drug Permeation Through Intestinal Membrane, Drug Metabolism and Pharmacokinetics, vol.22, pp.67-77, 2007.

D. J. Brayden, S. Maher, B. Bahar, and E. Walsh, Sodium caprate-induced increases in intestinal permeability and epithelial damage are prevented by misoprostol, European Journal of Pharmaceutics and Biopharmaceutics, vol.94, pp.194-206, 2015.

B. Van-der-loo, R. Labugger, J. N. Skepper, M. Bachschmid, J. Kilo et al., Enhanced Peroxynitrite Formation Is Associated with Vascular Aging, J Exp Med, vol.192, pp.1731-1744, 2000.

C. Gaucher, A. Boudier, F. Dahboul, M. Parent, and P. Leroy, Snitrosation/Denitrosation in Cardiovascular Pathologies: Facts and Concepts for the Rational Design of S-nitrosothiols, Current Pharmaceutical Design, vol.19, pp.458-472, 2012.

G. L. Amidon, H. Lennernäs, V. P. Shah, and J. R. Crison, A theoretical basis for a biopharmaceutic drug classification: the correlation of in vitro drug product dissolution and in vivo bioavailability, Pharmaceutical Research, vol.12, pp.413-420, 1995.

J. Fallingborg, L. A. Christensen, M. Ingeman-nielsen, B. A. Jacobsen, K. Abildgaard et al., pH-profile and regional transit times of the normal gut measured by a radiotelemetry device, Aliment. Pharmacol. Ther, vol.3, pp.605-613, 1989.

C. Atuma, V. Strugala, A. Allen, and L. Holm, The adherent gastrointestinal mucus gel layer: thickness and physical state in vivo, Am. J. Physiol. Gastrointest. Liver Physiol, vol.280, pp.922-929, 2001.

W. Shen and T. Matsui, Intestinal absorption of small peptides: a review, Int J Food Sci Technol, vol.54, pp.1942-1948, 2019.

P. Billat, E. Roger, S. Faure, and F. Lagarce, Models for drug absorption from the small intestine: where are we and where are we going?, Drug Discovery Today, vol.22, pp.761-775, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02615955

H. Yu, P. Chaimbault, I. Clarot, Z. Chen, and P. Leroy, Labeling nitrogen species with the stable isotope 15N for their measurement by separative methods coupled with mass spectrometry: A review, Talanta, vol.191, pp.491-503, 2019.
URL : https://hal.archives-ouvertes.fr/hal-01874147

N. V. Marozkina and B. Gaston, S-Nitrosylation signaling regulates cellular protein interactions, Biochimica et Biophysica Acta (BBA) -General Subjects, vol.1820, pp.722-729, 2012.

W. Wu, C. Gaucher, I. Fries, X. Hu, P. Maincent et al., Polymer nanocomposite particles of S -nitrosoglutathione: A suitable formulation for protection and sustained oral delivery, International Journal of Pharmaceutics, vol.495, pp.354-361, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01281137

J. Bonetti, Y. Zhou, M. Parent, I. Clarot, H. Yu et al., Intestinal absorption of S-nitrosothiols: Permeability and transport mechanisms, Biochemical Pharmacology, vol.155, pp.21-31, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01824879

M. H. Hanigan and H. F. Frierson, Immunohistochemical detection of gammaglutamyl transpeptidase in normal human tissue, Journal of Histochemistry & Cytochemistry, vol.44, pp.1101-1108, 1996.

F. Q. Schafer and G. R. Buettner, Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple, Free Radical Biology and Medicine, vol.30, pp.480-484, 2001.

D. P. Jones, Redox potential of GSH/GSSG couple: Assay and biological significance, Methods in Enzymology, issue.11, pp.93-112, 2002.

S. Wickham, M. B. West, P. F. Cook, and M. H. Hanigan, Gamma-glutamyl compounds: Substrate specificity of gamma-glutamyl transpeptidase enzymes, Analytical Biochemistry, vol.414, pp.208-214, 2011.

J. F. Riordan, The role of metals in enzyme activity, Ann. Clin. Lab. Sci, vol.7, pp.119-129, 1977.

E. Bramanti, V. Angeli, A. Paolicchi, and A. Pompella, The determination of Snitrosothiols in biological samples-Procedures, problems and precautions, Life Sciences, vol.88, pp.126-129, 2011.

H. H. Al-sa'doni, I. Y. Khan, L. Poston, I. Fisher, and A. Ferro, A Novel Family of S-Nitrosothiols: Chemical Synthesis and Biological Actions, Nitric Oxide, vol.4, pp.550-560, 2000.

K. A. Broniowska, A. R. Diers, N. Hogg, and S. -nitrosoglutathione, Biochimica et Biophysica Acta (BBA) -General Subjects, vol.1830, pp.3173-3181, 2013.

V. Angeli, A. Tacito, A. Paolicchi, R. Barsacchi, M. Franzini et al., A kinetic study of gammaglutamyltransferase (GGT)-mediated S-nitrosoglutathione catabolism, Archives of Biochemistry and Biophysics, vol.481, pp.191-196, 2009.

F. Dahboul, P. Leroy, K. Gate, A. Boudier, C. Gaucher et al., Endothelial ?-Glutamyltransferase Contributes to the Vasorelaxant Effect of S-Nitrosoglutathione in Rat Aorta, PLoS ONE, vol.7, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01491876

S. Park, G. Zhen, C. Verhaeghe, Y. Nakagami, L. T. Nguyenvu et al., The protein disulfide isomerase AGR2 is essential for production of intestinal mucus, Proc. Natl. Acad. Sci. U.S.A, vol.106, pp.6950-6955, 2009.

S. Tate and A. Meister, Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase, Proc. Natl. Acad. Sci. U.S.A, vol.75, pp.4806-4809, 1978.

N. S. Bryan and M. B. Grisham, Methods to detect nitric oxide and its metabolites in biological samples, Free Radical Biology and Medicine, vol.43, pp.645-657, 2007.

N. Benjamin, F. O'driscoll, H. Dougall, C. Duncan, L. Smith et al., Stomach NO synthesis, Nature, vol.368, pp.502-502, 1994.

L. C. Pinheiro, J. H. Amaral, G. C. Ferreira, R. L. Portella, C. S. Ceron et al., Gastric S-nitrosothiol formation drives the antihypertensive effects of oral sodium nitrite and nitrate in a rat model of renovascular hypertension, Free Radical Biology and Medicine, vol.87, pp.252-262, 2015.

M. Khan, H. Sakakima, T. S. Dhammu, A. Shunmugavel, Y. Im et al., S-nitrosoglutathione reduces oxidative injury and promotes mechanisms of neurorepair following traumatic brain injury in rats, J Neuroinflammation, vol.8, 2011.

M. Parent, A. Boudier, J. Perrin, C. Vigneron, P. Maincent et al.,

I. Bisson, F. Lartaud, and . Dupuis, Situ Microparticles Loaded with S-Nitrosoglutathione Protect from Stroke, vol.10, p.144659, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01279697

W. Wu, C. Perrin-sarrado, H. Ming, I. Lartaud, P. Maincent et al., Polymer nanocomposites enhance Snitrosoglutathione intestinal absorption and promote the formation of releasable nitric oxide stores in rat aorta, Nanomedicine: Nanotechnology, Biology and Medicine, vol.12, pp.1795-1803, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01493332

M. Parent, F. Dahboul, R. Schneider, I. Clarot, P. Maincent et al., A Complete Physicochemical Identity Card of S-nitrosoglutathione, Current Pharmaceutical Analysis, vol.9, pp.31-42, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00807801

F. Schiele, Y. Artur, D. Bagrel, C. Petitclerc, and G. Siest, Measurement of plasma gamma-glutamyltransferase in clinical chemistry: kinetic basis and standardisation propositions, Clinica Chimica Acta, vol.112, pp.90377-90383, 1981.

C. Damacena-angelis, G. H. Oliveira-paula, L. C. Pinheiro, E. J. Crevelin, R. L. Portella et al., Nitrate decreases xanthine oxidoreductase-mediated nitrite reductase activity and attenuates vascular and blood pressure responses to nitrite, Redox Biology, vol.12, pp.291-299, 2017.

S. Shin and H. Fung, Evaluation of an LC-MS/MS assay for 15N-nitrite for cellular studies of L-arginine action, J Pharm Biomed Anal, vol.56, pp.1127-1131, 2011.

B. Srinivasan, A. R. Kolli, M. B. Esch, H. E. Abaci, M. L. Shuler et al., TEER Measurement Techniques for In Vitro Barrier Model Systems, Journal of Laboratory Automation, vol.20, pp.107-126, 2015.

H. Yu, R. Schmitt, A. Sapin, P. Chaimbault, and P. Leroy, Comparison between two derivatization methods of nitrite ion labeled with 15 N applied to liquid chromatography-tandem mass spectrometry, Anal. Methods, vol.10, pp.3830-3836, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01874145

H. Yu, J. Bonetti, C. Gaucher, I. Fries, L. Vernex-loset et al., Higher-energy collision-induced dissociation for the quantification by liquid chromatography/tandem ion trap mass spectrometry of nitric oxide metabolites coming from S-nitroso-glutathione in an in vitro model of the intestinal barrier, Rapid Commun. Mass Spectrom, vol.33, pp.1-11, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02044975

L. H. Lash, W. Qian, D. A. Putt, K. Jacobs, A. A. Elfarra et al., Glutathione conjugation of trichloroethylene in rats and mice: sex-, species-, and tissue-dependent differences, Drug Metab. Dispos, vol.26, pp.12-19, 1998.

B. Z. Carter, A. L. Wiseman, R. Orkiszewski, K. D. Ballard, C. Ou et al., Metabolism of Leukotriene C 4 in ?-Glutamyl Transpeptidasedeficient Mice, J. Biol. Chem, vol.272, pp.12305-12310, 1997.

T. Liu, Q. Yan, L. Feng, X. Ma, X. Tian et al., Isolation of ?-Glutamyl-Transferase Rich-Bacteria from Mouse Gut by a Near-Infrared Fluorescent Probe with Large Stokes Shift, Anal. Chem, vol.90, pp.9921-9928, 2018.

M. Hayashi and M. Tomita, Mechanistic Analysis for Drug Permeation Through Intestinal Membrane, Drug Metabolism and Pharmacokinetics, vol.22, pp.67-77, 2007.

O. Parodi, R. De-maria, and E. Roubina, Redox state, oxidative stress and endothelial dysfunction in heart failure: the puzzle of nitrate-thiol interaction, Journal of Cardiovascular Medicine, vol.8, pp.765-774, 2007.

G. A. Cheadle, T. W. Costantini, N. Lopez, V. Bansal, B. P. Eliceiri et al., Enteric glia cells attenuate cytomix-induced intestinal epithelial barrier breakdown, PloS one, vol.8, p.69042, 2013.

L. L. Clarke, A guide to Ussing chamber studies of mouse intestine, Am J Physiol Gastrointest Liver Physiol, vol.296, pp.1151-66, 2009.

N. Clère, S. Faure, and M. Guerriaud, Bases fondamentales en pharmacologie: Sciences du médicament, 2014.

J. B. Dattilo and R. G. Makhoul, The role of nitric oxide in vascular biology and pathobiology, Annals of vascular surgery, vol.11, pp.307-314, 1997.

R. Forsgård, R. Korpela, L. Stenman, P. Österlund, and R. Holma, Deoxycholic acid induced changes in electrophysiological parameters and macromolecular permeability in murine small intestine with and without functional enteric nervous system plexuses, Neurogastroenterology & Motility, vol.26, pp.1179-1187, 2014.

A. Fortuna, G. Alves, A. Falcao, and P. Soares-da-silva, Evaluation of the permeability and P-glycoprotein efflux of carbamazepine and several derivatives across mouse small intestine by the Ussing chamber technique, Epilepsia, vol.53, pp.529-567, 2012.

L. V. Hooper and A. J. Macpherson, Immune adaptations that maintain homeostasis with the intestinal microbiota, Nature reviews. Immunology, vol.10, p.159, 2010.

Y. S. Kim and S. B. Ho, Intestinal goblet cells and mucins in health and disease: recent insights and progress, Current gastroenterology reports, vol.12, pp.319-330, 2010.

N. I. Kochar, A. V. Chandewal, R. L. Bakal, and P. N. Kochar, Nitric oxide and the gastrointestinal tract, Int. J. Pharmacol, vol.7, pp.31-39, 2011.

G. Kolios, V. Valatas, and S. G. Ward, Nitric oxide in inflammatory bowel disease: a universal messenger in an unsolved puzzle, Immunology, vol.113, pp.427-437, 2004.

Z. Li, X. Zhang, H. Zhou, W. Liu, and J. Li, Exogenous S-nitrosoglutathione attenuates inflammatory response and intestinal epithelial barrier injury in endotoxemic rats, Journal of Trauma and Acute Care Surgery, vol.80, pp.977-984, 2016.

N. Marin, P. Zamorano, R. Carrasco, P. Mujica, F. G. Gonzalez et al., S-Nitrosation of beta-catenin and p120 catenin: a novel regulatory mechanism in endothelial hyperpermeability, Circ Res, vol.111, pp.553-63, 2012.

M. Parent, F. Dahboul, R. Schneider, I. Clarot, P. Maincent et al., A complete physicochemical identity card of S-nitrosoglutathione, Current Pharmaceutical Analysis, vol.9, pp.31-42, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00807801

M. Parent, F. Dupuis, P. Maincent, C. Vigneron, P. Leroy et al., Year. Quel avenir en thérapeutique cardiovasculaire pour le monoxyde d'azote et ses dérivés?, Annales Pharmaceutiques Françaises, pp.84-94
URL : https://hal.archives-ouvertes.fr/in2p3-00482639

D. Payros, T. Secher, M. Boury, C. Brehin, S. Ménard et al., Maternally acquired genotoxic Escherichia coli alters offspring's intestinal homeostasis, Gut Microbes, vol.5, pp.313-512, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02935531

C. S. Potten, G. Owen, and D. Booth, Intestinal stem cells protect their genome by selective segregation of template DNA strands, J Cell Sci, vol.115, pp.2381-2388, 2002.

T. C. Savidge, P. Newman, C. Pothoulakis, A. Ruhl, M. Neunlist et al., Enteric glia regulate intestinal barrier function and inflammation via release of S-nitrosoglutathione, Gastroenterology, vol.132, pp.1344-1358, 2007.

B. Srinivasan, A. R. Kolli, M. B. Esch, H. E. Abaci, M. L. Shuler et al., TEER measurement techniques for in vitro barrier model systems, Journal of laboratory automation, vol.20, pp.107-126, 2015.

R. H. Stephens, J. Tanianis-hughes, N. B. Higgs, M. Humphrey, and G. Warhurst, Region-dependent modulation of intestinal permeability by drug efflux transporters: in vitro studies in mdr1a(-/-) mouse intestine, J Pharmacol Exp Ther, vol.303, pp.1095-101, 2002.

Z. Références-aktary, M. Alaee, and M. Pasdar, Beyond cell-cell adhesion: Plakoglobin and the regulation of tumorigenesis and metastasis, Oncotarget, vol.8, pp.32270-32291, 2017.

H. H. Al-sa'doni, I. Y. Khan, L. Poston, I. Fisher, and A. Ferro, A Novel Family of S-Nitrosothiols: Chemical Synthesis and Biological Actions, Nitric Oxide, vol.4, pp.550-560, 2000.

G. L. Amidon, H. Lennernäs, V. P. Shah, and J. R. Crison, A theoretical basis for a biopharmaceutic drug classification: the correlation of in vitro drug product dissolution and in vivo bioavailability, Pharmaceutical Research, vol.12, pp.413-420, 1995.

A. Amiot, D. Cazals-hatem, O. Corcos, X. Treton, C. Stefanescu et al., Maladies de la motricité de l'intestin grêle, Hépato-Gastro & Oncologie Digestive, vol.19, pp.536-582, 2012.

E. K. Anderberg, T. Lindmark, and P. Artursson, Sodium caprate elicits dilatations in human intestinal tight junctions and enhances drug absorption by the paracellular route, Pharm. Res, vol.10, pp.857-864, 1993.

G. J. Anderson and D. M. Frazer, Current understanding of iron homeostasis, Am. J. Clin. Nutr, vol.106, pp.1559-1566, 2017.

V. Angeli, A. Tacito, A. Paolicchi, R. Barsacchi, M. Franzini et al., A kinetic study of gamma-glutamyltransferase (GGT)-mediated S-nitrosoglutathione catabolism, Archives of Biochemistry and Biophysics, vol.481, pp.191-196, 2009.

Y. Arnold, J. Thorens, S. Bernard, and Y. Kalia, Drug Transport across Porcine Intestine Using an Ussing Chamber System: Regional Differences and the Effect of P-Glycoprotein and CYP3A4 Activity on Drug Absorption, Pharmaceutics, vol.11, p.139, 2019.

K. Asanuma, X. Huo, A. Agoston, X. Zhang, C. Yu et al., In oesophageal squamous cells, nitric oxide causes S-nitrosylation of Akt and blocks SOX2 (sex determining region Y-box 2) expression, Gut, vol.65, pp.1416-1426, 2016.

C. Atuma, V. Strugala, A. Allen, and L. Holm, The adherent gastrointestinal mucus gel layer: thickness and physical state in vivo, Am. J. Physiol. Gastrointest. Liver Physiol, vol.280, pp.922-929, 2001.

N. Avdagi?, A. Za?iragi?, N. Babi?, M. Huki?, M. ?eremet et al., Nitric oxide as a potential biomarker in inflammatory bowel disease, Bosn J of Basic Med Sci, vol.13, 2013.

C. B?l?e?, B. I. Coculescu, G. Manole, M. B?l?e?, and G. V. Dinc?, Gammaglutamyltransferase, possible novel biomarker in colon diverticulosis: a case-control study, Journal of Enzyme Inhibition and Medicinal Chemistry, vol.33, pp.428-432, 2018.

S. Balzan, C. De-almeida-quadros, R. De-cleva, B. Zilberstein, and I. Cecconello, Bacterial translocation: Overview of mechanisms and clinical impact, Journal of Gastroenterology and Hepatology, vol.22, pp.464-471, 2007.

S. D. Barnett and I. L. Buxton, The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy, Crit. Rev. Biochem. Mol. Biol, vol.52, pp.340-354, 2017.

R. L. Bateman, D. Rauh, B. Tavshanjian, and K. M. Shokat, Human Carbonyl Reductase 1 Is an S -Nitrosoglutathione Reductase, J. Biol. Chem, vol.283, pp.35756-35762, 2008.

H. Bauer, W. Stelzhammer, R. Fuchs, T. M. Weiger, C. Danninger et al., Astrocytes and neurons express the tight junction-specific protein occludin in vitro, Exp. Cell Res, vol.250, pp.434-438, 1999.

G. Bazzoni, The JAM family of junctional adhesion molecules, Curr. Opin. Cell Biol, vol.15, pp.525-530, 2003.

F. Bedioui, A. Ismail, and S. Griveau, Electrochemical detection of nitric oxide and Snitrosothiols in biological systems: Past, present & future, Current Opinion in Electrochemistry, vol.12, pp.42-50, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02159765

E. Belcastro, W. Wu, I. Fries-raeth, A. Corti, A. Pompella et al., Oxidative stress enhances and modulates protein S -nitrosation in smooth muscle cells exposed to S -nitrosoglutathione, Nitric Oxide, vol.69, pp.10-21, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01593873

N. Benjamin, F. O'driscoll, H. Dougall, C. Duncan, L. Smith et al., Stomach NO synthesis, Nature, vol.368, pp.502-502, 1994.

K. Berginc, A. Kristl, and J. Trontelj, Physiological barriers to the oral delivery of curcumin 518-524, 2012.

J. J. Berglund, M. Riegler, Y. Zolotarevsky, E. Wenzl, and J. R. Turner, Regulation of human jejunal transmucosal resistance and MLC phosphorylation by Na(+)-glucose cotransport, Am. J. Physiol. Gastrointest. Liver Physiol, vol.281, pp.1487-1493, 2001.

H. Bergmann, D. Rogoll, W. Scheppach, R. Melcher, and E. Richling, The Ussing type chamber model to study the intestinal transport and modulation of specific tightjunction genes using a colonic cell line, Molecular Nutrition & Food Research, vol.53, pp.1211-1225, 2009.

P. Billat, E. Roger, S. Faure, and F. Lagarce, Models for drug absorption from the small intestine: where are we and where are we going?, Drug Discovery Today, vol.22, pp.761-775, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02615955

J. Bonetti, Y. Zhou, M. Parent, I. Clarot, H. Yu et al., Intestinal absorption of S-nitrosothiols: Permeability and transport mechanisms, Biochemical Pharmacology, vol.155, pp.21-31, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01824879

M. Boucher, P. Laprise, and N. Rivard, Cyclic AMP-dependent protein kinase A negatively modulates adherens junction integrity and differentiation of intestinal epithelial cells, Journal of Cellular Physiology, vol.202, pp.178-190, 2005.

E. Bramanti, V. Angeli, A. Paolicchi, and A. Pompella, The determination of Snitrosothiols in biological samples-Procedures, problems and precautions, Life Sciences, vol.88, pp.126-129, 2011.

D. J. Brayden, V. A. Bzik, A. L. Lewis, and L. Illum, CriticalSorb TM Promotes Permeation of Flux Markers Across Isolated Rat Intestinal Mucosae and Caco-2 Monolayers, Pharmaceutical Research, vol.29, pp.2543-2554, 2012.

D. J. Brayden, S. Maher, B. Bahar, and E. Walsh, Sodium caprate-induced increases in intestinal permeability and epithelial damage are prevented by misoprostol, European Journal of Pharmaceutics and Biopharmaceutics, vol.94, pp.194-206, 2015.

E. Breen, G. Steele, and A. M. Mercurio, Role of the E-cadherin/alpha-catenin complex in modulating cell-cell and cell-matrix adhesive properties of invasive colon carcinoma cells, Ann. Surg. Oncol, vol.2, pp.378-385, 1995.

J. M. Brenchley and D. C. Douek, Microbial Translocation Across the GI Tract, Annual Review of Immunology, vol.30, pp.149-173, 2012.

K. A. Broniowska, A. R. Diers, N. ;. Hogg, and . S-nitrosoglutathione, Biochimica et Biophysica Acta, pp.3173-3181, 2013.

N. S. Bryan and M. B. Grisham, Methods to detect nitric oxide and its metabolites in biological samples, Free Radical Biology and Medicine, vol.43, pp.645-657, 2007.

D. L. Carbone, J. A. Doorn, Z. Kiebler, and D. R. Petersen, Cysteine Modification by Lipid Peroxidation Products Inhibits Protein Disulfide Isomerase, Chemical Research in Toxicology, vol.18, pp.1324-1331, 2005.

B. Z. Carter, A. L. Wiseman, R. Orkiszewski, K. D. Ballard, C. Ou et al., Metabolism of Leukotriene C 4 in ?-Glutamyl Transpeptidase-deficient Mice, J. Biol. Chem, vol.272, pp.12305-12310, 1997.

I. Castellano and A. Merlino, Gamma-glutamyl transpeptidases: structure and function, SpringerBriefs in biochemistry and molecular biology, 2013.

M. R. Cera, A. Del-prete, A. Vecchi, M. Corada, I. Martin-padura et al., Increased DC trafficking to lymph nodes and contact hypersensitivity in junctional adhesion molecule-A-deficient mice, J. Clin. Invest, vol.114, pp.729-738, 2004.

G. A. Cheadle, T. W. Costantini, N. Lopez, V. Bansal, B. P. Eliceiri et al., Enteric Glia Cells Attenuate Cytomix-Induced Intestinal Epithelial Barrier Breakdown, PLoS ONE, vol.8, 2013.

H. Chiba, M. Osanai, M. Murata, T. Kojima, and N. Sawada, Transmembrane proteins of tight junctions, Biochimica et Biophysica Acta (BBA) -Biomembranes, vol.1778, pp.588-600, 2008.

Y. Cho, L. Yu, M. A. Abdelmegeed, S. Yoo, and B. Song, Apoptosis of enterocytes and nitration of junctional complex proteins promote alcohol-induced gut leakiness and liver injury, Journal of Hepatology, vol.69, pp.142-153, 2018.

M. S. Choi, Pathophysiological Role of S-Nitrosylation and Transnitrosylation Depending on S-Nitrosoglutathione Levels Regulated by S-Nitrosoglutathione Reductase, Biomol Ther (Seoul), vol.26, pp.533-538, 2018.

L. L. Clarke, A guide to Ussing chamber studies of mouse intestine, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.296, pp.1151-1166, 2009.

H. Clevers, Wnt/beta-catenin signaling in development and disease, Cell, vol.127, pp.469-480, 2006.

J. T. Collins and M. Badireddy, Anatomy, Abdomen and Pelvis, Small Intestine, 2019.

S. D. Conner and S. L. Schmid, Regulated portals of entry into the cell, Nature, vol.422, pp.37-44, 2003.

M. Costa, Anatomy and physiology of the enteric nervous system, Gut, vol.47, pp.15-1519, 2000.

P. M. Cummins, Occludin: One Protein, Many Forms, Molecular and Cellular Biology, vol.32, pp.242-250, 2012.

D. Silva, L. C. Da-silva, T. L. Antunes, A. H. Rezende, and K. R. , A Sensitive Medium-Throughput Method to Predict Intestinal Absorption in Humans Using Rat Intestinal Tissue Segments, Journal of Pharmaceutical Sciences, vol.104, pp.2807-2812, 2015.

F. Dahboul, P. Leroy, K. Maguin-gate, A. Boudier, C. Gaucher et al., Endothelial ?-Glutamyltransferase Contributes to the Vasorelaxant Effect of S-Nitrosoglutathione in Rat Aorta, PLoS ONE, vol.7, 2012.
URL : https://hal.archives-ouvertes.fr/hal-01491876

F. Dahboul, C. Perrin-sarrado, A. Boudier, I. Lartaud, R. Schneider et al., S,S?-dinitrosobucillamine, a new nitric oxide donor, induces a better vasorelaxation than other S-nitrosothiols, European Journal of Pharmacology, vol.730, pp.171-179, 2014.
URL : https://hal.archives-ouvertes.fr/hal-00967357

. Damacena-angelis, . Célio, G. H. Oliveira-paula, L. C. Pinheiro, E. J. Crevelin et al., Nitrate decreases xanthine oxidoreductasemediated nitrite reductase activity and attenuates vascular and blood pressure responses to nitrite, Redox Biology, vol.12, pp.291-299, 2017.

. Damacena-angelis, . Celio, G. H. Oliveira-paula, L. C. Pinheiro, E. J. Crevelin et al., Nitrate decreases xanthine oxidoreductasemediated nitrite reductase activity and attenuates vascular and blood pressure responses to nitrite, Redox Biol, vol.12, pp.291-299, 2017.

J. B. Dattilo and R. G. Makhoul, The Role of Nitric Oxide in Vascular Biology and Pathobiology, Annals of Vascular Surgery, vol.11, pp.307-314, 1997.

M. A. Davis and A. B. Reynolds, Blocked acinar development, E-cadherin reduction, and intraepithelial neoplasia upon ablation of p120-catenin in the mouse salivary gland, Dev. Cell, vol.10, pp.21-31, 2006.

D. De-la-pomélie, V. Santé-lhoutellier, and P. Gatellier, Mechanisms and kinetics of heme iron nitrosylation in an in vitro gastro-intestinal model, Food Chemistry, vol.239, pp.86-93, 2018.

D. De-la-pomélie, V. Santé-lhoutellier, T. Sayd, and P. Gatellier, Oxidation and nitrosation of meat proteins under gastro-intestinal conditions: Consequences in terms of nutritional and health values of meat, Food Chemistry, vol.243, pp.295-304, 2018.

G. Dijkstra, H. Moshage, and P. L. Jansen, Blockade of NF-? B Activation and Donation of Nitric Oxide: New Treatment Options in Inflammatory Bowel Disease?, Scandinavian Journal of Gastroenterology, vol.37, pp.37-41, 2002.

K. Ebnet, Organization of multiprotein complexes at cell-cell junctions, Histochem. Cell Biol, vol.130, pp.1-20, 2008.

K. Ebnet, A. Suzuki, S. Ohno, and D. Vestweber, Junctional adhesion molecules (JAMs): more molecules with dual functions?, J. Cell. Sci, vol.117, pp.19-29, 2004.

J. D. Eichman and J. R. Robinson, Mechanistic studies on effervescent-induced permeability enhancement, Pharm. Res, vol.15, pp.925-930, 1998.

N. Elginaid-osman, B. Weström, Q. Wang, L. Persson, and B. Karlsson, Spermine affects intestinal in vitro permeability to different-sized molecules in rats, Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, vol.120, pp.211-216, 1998.

L. Ellgaard and L. W. Ruddock, The human protein disulphide isomerase family: substrate interactions and functional properties, EMBO Rep, vol.6, pp.28-32, 2005.

J. Fallingborg, L. A. Christensen, M. Ingeman-nielsen, B. A. Jacobsen, K. Abildgaard et al., pH-profile and regional transit times of the normal gut measured by a radiotelemetry device, Aliment. Pharmacol. Ther, vol.3, pp.605-613, 1989.

S. Faure, N. Clère, M. Guerriaud, and M. Plotkine, Bases fondamentales en pharmacologie sciences du médicament, 2014.

T. Fevr, S. Robine, D. Louvard, and J. Huelsken, Wnt/ -Catenin Is Essential for Intestinal Homeostasis and Maintenance of Intestinal Stem Cells, Molecular and Cellular Biology, vol.27, pp.7551-7559, 2007.

B. M. Fihn, A. Sjöqvist, and M. Jodal, Permeability of the rat small intestinal epithelium along the villus-crypt axis: effects of glucose transport, Gastroenterology, vol.119, pp.1029-1036, 2000.

S. J. Fletcher and J. Z. Rappoport, The role of vesicle trafficking in epithelial cell motility, Biochem. Soc. Trans, vol.37, pp.1072-1076, 2009.

R. A. Forsgård, R. Korpela, L. K. Stenman, P. Österlund, and R. Holma, Deoxycholic acid induced changes in electrophysiological parameters and macromolecular permeability in murine small intestine with and without functional enteric nervous system plexuses, Neurogastroenterology & Motility, vol.26, pp.1179-1187, 2014.

J. B. Furness, B. P. Callaghan, L. R. Rivera, and H. Cho, The enteric nervous system and gastrointestinal innervation: integrated local and central control, Adv. Exp. Med. Biol, vol.817, pp.39-71, 2014.

M. Furuse, M. Hata, K. Furuse, Y. Yoshida, A. Haratake et al., Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice, J. Cell Biol, vol.156, pp.1099-1111, 2002.

M. Furuse, M. Itoh, T. Hirase, A. Nagafuchi, S. Yonemura et al., Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions, J. Cell Biol, vol.127, pp.1617-1626, 1994.

J. J. Galligan and D. R. Petersen, The human protein disulfide isomerase gene family, Human Genomics, vol.6, 2012.

C. Gaucher, A. Boudier, F. Dahboul, M. Parent, and P. Leroy, Snitrosation/Denitrosation in Cardiovascular Pathologies: Facts and Concepts for the Rational Design of S-nitrosothiols, Current Pharmaceutical Design, vol.19, pp.458-472, 2012.

S. Getsios, A. C. Huen, and K. J. Green, Working out the strength and flexibility of desmosomes, Nat. Rev. Mol. Cell Biol, vol.5, pp.271-281, 2004.

A. Gomes, E. Fernandes, and J. L. Lima, Use of fluorescence probes for detection of reactive nitrogen species: a review, J Fluoresc, vol.16, pp.119-139, 2006.

J. L. Gookin, L. L. Duckett, M. U. Armstrong, S. H. Stauffer, C. P. Finnegan et al., Nitric oxide synthase stimulates prostaglandin synthesis and barrier function in C. parvum -infected porcine ileum, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.287, pp.571-581, 2004.

J. L. Gookin, J. M. Rhoads, and R. A. Argenzio, Inducible nitric oxide synthase mediates early epithelial repair of porcine ileum, American Journal of Physiology-Gastrointestinal and Liver Physiology, vol.283, pp.157-168, 2002.

L. S. Green, L. E. Chun, A. K. Patton, X. Sun, G. J. Rosenthal et al., Mechanism of Inhibition for N6022, a First-in-Class Drug Targeting S -Nitrosoglutathione Reductase, Biochemistry, vol.51, pp.2157-2168, 2012.

J. Greenspon, R. Li, L. Xiao, J. N. Rao, R. Sun et al., Sphingosine-1-Phosphate Regulates the Expression of Adherens Junction Protein E-Cadherin and Enhances Intestinal Epithelial Cell Barrier Function, Digestive Diseases and Sciences, vol.56, pp.1342-1353, 2011.

K. R. Groschwitz and S. P. Hogan, Intestinal barrier function: Molecular regulation and disease pathogenesis, Journal of Allergy and Clinical Immunology, vol.124, pp.3-20, 2009.

A. Gross, L. A. Pack, G. M. Schacht, S. Kant, H. Ungewiss et al., Desmoglein 2, but not desmocollin 2, protects intestinal epithelia from injury, Mucosal Immunology, vol.11, pp.1630-1639, 2018.

X. Guo, J. N. Rao, L. Liu, T. Zou, D. J. Turner et al., Regulation of adherens junctions and epithelial paracellular permeability: a novel function for polyamines, American Journal of Physiology-Cell Physiology, vol.285, pp.1174-1187, 2003.

Y. Haiyan, S. Romain, S. Anne, C. Patrick, and L. Pierre, Comparison between two derivatization methods of nitrite ion labeled with 15N applied to liquid chromatography-tandem mass spectrometry, Anal. Methods, vol.10, pp.3830-3836, 2018.

T. Han, Y. Tang, . Li, . Jing, B. Xue et al., Nitric oxide donor protects against acetic acid-induced gastric ulcer in rats via S-nitrosylation of TRPV1 on vagus nerve, Scientific Reports, vol.7, 2017.

M. H. Hanigan and H. F. Frierson, Immunohistochemical detection of gamma-glutamyl transpeptidase in normal human tissue, Journal of Histochemistry & Cytochemistry, vol.44, pp.1101-1108, 1996.

A. Hara, S. Endo, T. Matsunaga, O. El-kabbani, T. Miura et al., Human carbonyl reductase 1 participating in intestinal first-pass drug metabolism is inhibited by fatty acids and acyl-CoAs, Biochemical Pharmacology, vol.138, pp.185-192, 2017.

O. J. Harrison, J. Brasch, G. Lasso, P. S. Katsamba, G. Ahlsen et al., Structural basis of adhesive binding by desmocollins and desmogleins, Proc. Natl. Acad. Sci. U.S.A, vol.113, pp.7160-7165, 2016.

Ø. Hauso, T. C. Martinsen, and H. Waldum, 5-Aminosalicylic acid, a specific drug for ulcerative colitis, Scandinavian Journal of Gastroenterology, vol.50, pp.933-941, 2015.

D. Häussinger, T. Ahrens, H. Sass, O. Pertz, J. Engel et al., Calciumdependent homoassociation of E-cadherin by NMR spectroscopy: changes in mobility, conformation and mapping of contact regions, J. Mol. Biol, vol.324, pp.823-839, 2002.

M. Hayashi and M. Tomita, Mechanistic Analysis for Drug Permeation Through Intestinal Membrane, Drug Metabolism and Pharmacokinetics, vol.22, pp.67-77, 2007.

T. A. Heinrich, R. S. Da-silva, K. M. Miranda, C. H. Switzer, D. A. Wink et al., Biological nitric oxide signalling: chemistry and terminology: NO chemical biology and terminology, British Journal of Pharmacology, vol.169, pp.1417-1429, 2013.

H. F. Helander and L. Fändriks, Surface area of the digestive tract -revisited, Scand. J. Gastroenterol, vol.49, pp.681-689, 2014.

M. Heyman and J. F. Desjeux, Cytokine-Induced Alteration of the Epithelial Barrier to Food Antigens in Disease, Annals of the New York Academy of Sciences, vol.915, pp.304-311, 2006.

L. V. Hooper and A. J. Macpherson, Immune adaptations that maintain homeostasis with the intestinal microbiota, Nature Reviews Immunology, vol.10, pp.159-169, 2010.

A. H. Huber and W. I. Weis, The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin, Cell, vol.105, pp.391-402, 2001.

R. A. Hunter, B. J. Privett, W. H. Henley, E. R. Breed, Z. Liang et al., Microfluidic amperometric sensor for analysis of nitric oxide in whole blood, Anal. Chem, vol.85, pp.6066-6072, 2013.

L. J. Ignarro, Nitric oxide biology and pathobiology, 2000.

K. I. Iida, O. Miyaishi, Y. Iwata, K. I. Kozaki, M. Matsuyama et al., Distinct distribution of protein disulfide isomerase family proteins in rat tissues, J. Histochem. Cytochem, vol.44, pp.751-759, 1996.

M. Itoh, M. Furuse, K. Morita, K. Kubota, M. Saitou et al., Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins, J. Cell Biol, vol.147, pp.1351-1363, 1999.

A. I. Ivanov and N. G. Naydenov, Dynamics and Regulation of Epithelial Adherens Junctions, International Review of Cell and Molecular Biology, pp.27-99, 2013.

G. C. Jensen, Z. Zheng, and M. E. Meyerhoff, Amperometric nitric oxide sensors with enhanced selectivity over carbon monoxide via platinum oxide formation under alkaline conditions, Anal. Chem, vol.85, pp.10057-10061, 2013.

L. H. Jimison, S. A. Tria, D. Khodagholy, M. Gurfinkel, E. Lanzarini et al., Measurement of Barrier Tissue Integrity with an Organic Electrochemical Transistor, Adv. Mater, vol.24, pp.5919-5923, 2012.
URL : https://hal.archives-ouvertes.fr/emse-00853414

W. S. Jobgen, S. C. Jobgen, H. Li, C. J. Meininger, and G. Wu, Analysis of nitrite and nitrate in biological samples using high-performance liquid chromatography, Journal of Chromatography B, vol.851, pp.71-82, 2007.

D. P. Jones, Redox potential of GSH/GSSG couple: Assay and biological significance, pp.93-112, 2002.

N. Kaji, K. Horiguchi, S. Iino, S. Nakayama, T. Ohwada et al., Nitric oxide-induced oxidative stress impairs pacemaker function of murine interstitial cells of Cajal during inflammation, Pharmacological Research, vol.111, pp.838-848, 2016.

A. L. Kauffman, A. V. Gyurdieva, J. R. Mabus, C. Ferguson, Z. Yan et al., Alternative functional in vitro models of human intestinal epithelia, Frontiers in Pharmacology, vol.4, 2013.

M. Khan, H. Sakakima, T. S. Dhammu, A. Shunmugavel, Y. Im et al., S-nitrosoglutathione reduces oxidative injury and promotes mechanisms of neurorepair following traumatic brain injury in rats, J Neuroinflammation, vol.8, 2011.

Y. S. Kim and S. B. Ho, Intestinal Goblet Cells and Mucins in Health and Disease: Recent Insights and Progress, Current Gastroenterology Reports, vol.12, pp.319-330, 2010.

L. J. Klunder, K. N. Faber, G. Dijkstra, and S. C. Van-ijzendoorn, Mechanisms of Cell Polarity-Controlled Epithelial Homeostasis and Immunity in the Intestine, Cold Spring Harb Perspect Biol, vol.9, 2017.

A. W. Koch, S. Pokutta, A. Lustig, and J. Engel, Calcium binding and homoassociation of E-cadherin domains, Biochemistry, vol.36, pp.7697-7705, 1997.

N. I. Kochar, A. V. Chandewal, R. L. Bakal, and P. N. Kochar, Nitric Oxide and the Gastrointestinal Tract, International Journal of Pharmacology, vol.7, pp.31-39, 2011.

H. Kojima, N. Nakatsubo, K. Kikuchi, S. Kawahara, Y. Kirino et al., Detection and Imaging of Nitric Oxide with Novel Fluorescent Indicators: Diaminofluoresceins, Anal. Chem, vol.70, pp.2446-2453, 1998.

G. Kolios, V. Valatas, and S. G. Ward, Nitric oxide in inflammatory bowel disease: a universal messenger in an unsolved puzzle, Immunology, vol.113, pp.427-437, 2004.

Y. Konishi and M. Shimizu, Transepithelial Transport of Ferulic Acid by Monocarboxylic Acid Transporter in Caco-2 Cell Monolayers, Biotechnology, and Biochemistry, vol.67, pp.856-862, 2003.

M. D. Kottke, E. Delva, and A. P. Kowalczyk, The desmosome: cell science lessons from human diseases, J. Cell. Sci, vol.119, pp.797-806, 2006.

A. Kourtidis, S. P. Ngok, and P. Z. Anastasiadis, Progress in Molecular Biology and Translational Science, pp.409-432, 2013.

A. P. Kowalczyk and K. J. Green, Structure, Function, and Regulation of Desmosomes, Progress in Molecular Biology and Translational Science, pp.95-118, 2013.

J. Kratz, N. Schneider, T. Caon, R. Teixeira, M. Mascarello et al., Evaluation of In Vitro Intestinal and Cutaneous Permeability of Pentyl Gallate, Lat Am J Pharm, vol.30, pp.1508-1515, 2013.

M. Lal-nag and P. J. Morin, The claudins, Genome Biology, vol.10, 2009.

L. H. Lash, W. Qian, D. A. Putt, K. Jacobs, A. A. Elfarra et al., Glutathione conjugation of trichloroethylene in rats and mice: sex-, species-, and tissue-dependent differences, Drug Metab. Dispos, vol.26, pp.12-19, 1998.

M. G. Laukoetter, P. Nava, W. Y. Lee, E. A. Severson, C. T. Capaldo et al., JAM-A regulates permeability and inflammation in the intestine in vivo, J. Exp. Med, vol.204, pp.3067-3076, 2007.

L. Lee, C. Wu, C. Wang, J. Yu, Y. Liang et al., Expression of matrix metalloproteinases MMP-2 and MMP-9 in gastric cancer and their relation to claudin-4 expression, Histol. Histopathol, vol.23, pp.515-521, 2008.

I. Legen and A. Kristl, pH and energy dependent transport of ketoprofen across rat jejunum in vitro, European Journal of Pharmaceutics and Biopharmaceutics, vol.56, pp.87-94, 2003.

K. Leithner, V. Grabovac, K. Albrecht, J. Hombach, G. Klima et al., Permeation studies on freshly excised rat gastric mucosa: influence of pH, Drug Development and Industrial Pharmacy, vol.37, pp.518-525, 2011.

H. Lennernas, Animal data: The contributions of the Ussing Chamber and perfusion systems to predicting human oral drug delivery in vivo?, Advanced Drug Delivery Reviews, vol.59, pp.1103-1120, 2007.

H. Li, H. Jin, W. Shim, and C. Shim, An improved prediction of the human in vivo intestinal permeability and BCS class of drugs using the in vitro permeability ratio obtained for rat intestine using an Ussing chamber system, Drug Development and Industrial Pharmacy, vol.39, pp.1515-1522, 2013.

Z. Li, X. Zhang, H. Zhou, W. Liu, and J. Li, Exogenous S-nitrosoglutathione attenuates inflammatory response and intestinal epithelial barrier injury in endotoxemic rats, Journal of Trauma and Acute Care Surgery, vol.80, pp.977-984, 2016.

M. C. Linder, N. R. Zerounian, M. Moriya, and R. Malpe, Iron and copper homeostasis and intestinal absorption using the Caco2 cell model, Biometals, vol.16, pp.145-160, 2003.

T. Liu, Q. Yan, L. Feng, X. Ma, X. Tian et al., Isolation of ?-Glutamyl-Transferase Rich-Bacteria from Mouse Gut by a Near-Infrared Fluorescent Probe with Large Stokes Shift, Anal. Chem, vol.90, pp.9921-9928, 2018.

A. Macierzanka, A. R. Mackie, and L. Krupa, Permeability of the small intestinal mucus for physiologically relevant studies: Impact of mucus location and ex vivo treatment, Sci Rep, vol.9, 2019.

C. Manichanh, N. Borruel, F. Casellas, and F. Guarner, The gut microbiota in IBD, Nat Rev Gastroenterol Hepatol, vol.9, pp.599-608, 2012.

E. B. Manukhina, B. V. Smirin, I. Malyshev, . Yu, J. Stoclet et al., Biology Bulletin of the Russian Academy of Sciences, vol.29, pp.477-486, 2002.

N. Marín, P. Zamorano, R. Carrasco, P. Mujica, F. G. González et al., S-Nitrosation of ?-Catenin and p120 Catenin: A Novel Regulatory Mechanism in Endothelial Hyperpermeability, 2012.

, Circ Res, vol.111, pp.553-563

A. G. Markov, O. N. Vishnevskaya, L. S. Okorokova, A. A. Fedorova, N. M. Kruglova et al., Cholera toxin perturbs the paracellular barrier in the small intestinal epithelium of rats by affecting claudin-2 and tricellulin, Pflugers Arch -Eur J Physiol, vol.471, pp.1183-1189, 2019.

N. V. Marozkina and B. Gaston, S-Nitrosylation signaling regulates cellular protein interactions, Biochimica et Biophysica Acta, pp.722-729, 2012.

R. U. Meckenstock, S. B. Haderlein, T. C. Schmidt, L. Zwank, M. Elsner et al., Compound-specific stable isotope analysis of organic contaminants in natural environments: a critical review of the state of the art, prospects, and future challenges, Analytical and Bioanalytical Chemistry, vol.378, pp.283-300, 2004.

S. Mehta, A. Nijhuis, T. Kumagai, J. Lindsay, and A. Silver, Defects in the adherens junction complex (E-cadherin/ ?-catenin) in inflammatory bowel disease, Cell and Tissue Research, vol.360, pp.749-760, 2015.

A. Meister, S. S. Tate, and O. W. Griffith, Gamma-glutamyl transpeptidase, Meth. Enzymol, vol.77, pp.237-253, 1981.

M. Meng, N. J. Klingensmith, and C. M. Coopersmith, New insights into the gut as the driver of critical illness and organ failure, Curr Opin Crit Care, vol.23, pp.143-148, 2017.

R. M. Menon and W. H. Barr, Comparison of ceftibuten transport across Caco-2 cells and rat jejunum mounted on modified ussing chambers, Biopharmaceutics & Drug Disposition, vol.24, pp.299-308, 2003.

H. Mineo, M. Amano, H. Chiji, N. Shigematsu, F. Tomita et al., Indigestible disaccharides open tight junctions and enhance net calcium, magnesium, and zinc absorption in isolated rat small and large intestinal epithelium, Dig. Dis. Sci, vol.49, pp.122-132, 2004.

H. Mineo, H. Hara, N. Shigematsu, Y. Okuhara, and F. Tomita, Melibiose, difructose anhydride III and difructose anhydride IV enhance net calcium absorption in rat small and large intestinal epithelium by increasing the passage of tight junctions in vitro, J. Nutr, vol.132, pp.3394-3399, 2002.

R. Mittal and C. M. Coopersmith, Redefining the gut as the motor of critical illness, Trends Mol Med, vol.20, pp.214-223, 2014.

R. Moriez, C. Salvador-cartier, V. Theodorou, J. Fioramonti, H. Eutamene et al., Myosin light chain kinase is involved in lipopolysaccharide-induced disruption of colonic epithelial barrier and bacterial translocation in rats, Am. J. Pathol, vol.167, issue.10, pp.61196-61196, 2005.

K. Morita, M. Furuse, K. Fujimoto, and S. Tsukita, Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands, Proc. Natl. Acad. Sci. U.S.A, vol.96, pp.511-516, 1999.

A. Mutlib, W. Lam, J. Atherton, H. Chen, P. Galatsis et al., Application of stable isotope labeled glutathione and rapid scanning mass spectrometers in detecting and characterizing reactive metabolites, Rapid Commun. Mass Spectrom, vol.19, pp.3482-3492, 2005.

K. Natarajan and P. Abraham, Methotrexate administration induces differential and selective protein tyrosine nitration and cysteine nitrosylation in the subcellular organelles of the small intestinal mucosa of rats, Chemico-Biological Interactions, vol.251, pp.45-59, 2016.

P. Nava, M. G. Laukoetter, A. M. Hopkins, O. Laur, K. Gerner-smidt et al., Desmoglein-2: A Novel Regulator of Apoptosis in the Intestinal Epithelium, Molecular Biology of the Cell, vol.18, pp.4565-4578, 2007.

O. Nekrasova and K. J. Green, Desmosome assembly and dynamics, Trends Cell Biol, vol.23, pp.537-546, 2013.

F. H. Netter, . Philadelphia, S. C. Ng, H. Y. Shi, N. Hamidi et al., Worldwide incidence and prevalence of inflammatory bowel disease in the 21st century: a systematic review of population-based studies, The Lancet, vol.390, pp.2769-2778, 2017.

A. B. Noach, Y. Kurosaki, M. C. Blom-roosemalen, A. G. De-boer, and D. D. Breimer, Cell-polarity dependent effect of chelation on the paracellular permeability of confluent caco-2 cell monolayers, International Journal of Pharmaceutics, vol.90, pp.229-237, 1993.

R. Noth, J. Lange-grumfeld, E. Stüber, M. Kruse, M. Ellrichmann et al., Increased intestinal permeability and tight junction disruption by altered expression and localization of occludin in a murine graft versus host disease model, BMC Gastroenterol, vol.11, 2011.

V. Nunbhakdi-craig, T. Machleidt, E. Ogris, D. Bellotto, C. L. White et al., Protein phosphatase 2A associates with and regulates atypical PKC and the epithelial tight junction complex, J. Cell Biol, vol.158, pp.967-978, 2002.

G. H. Oliveira-paula and J. E. Tanus-santos, Nitrite-stimulated Gastric Formation of Snitrosothiols As An Antihypertensive Therapeutic Strategy, CDT, vol.20, pp.431-443, 2019.

M. Orlowski and A. Meister, Gamma-Glutamyl-Rho-Nitroanilide -a New Convenient Substrate for Determination and Study of L-and D-Gamma-Glutamyltranspeptidase Activities, Biochimica Et Biophysica Acta, vol.73, 1963.

K. Ozeki, M. Kato, Y. Sakurai, M. Ishigai, T. Kudo et al., Evaluation of the appropriate time range for estimating the apparent permeability coefficient (Papp) in a transcellular transport study, International Journal of Pharmaceutics, vol.495, pp.963-971, 2015.

P. Palumbo, U. Picchini, B. Beck, J. Van-gelder, N. Delbar et al., A general approach to the apparent permeability index, J Pharmacokinet Pharmacodyn, vol.35, pp.235-248, 2008.

M. Parent, A. Boudier, J. Perrin, C. Vigneron, P. Maincent et al., Situ Microparticles Loaded with S-Nitrosoglutathione Protect from Stroke, vol.10, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01279697

M. Parent, F. Dahboul, R. Schneider, I. Clarot, P. Maincent et al., A Complete Physicochemical Identity Card of S-nitrosoglutathione, Current Pharmaceutical Analysis, vol.9, pp.31-42, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00807801

M. Parent, F. Dupuis, P. Maincent, C. Vigneron, P. Leroy et al., Quel avenir en thérapeutique cardiovasculaire pour le monoxyde d'azote et ses dérivés ?, Annales Pharmaceutiques Françaises, vol.71, pp.84-94, 2013.

J. W. Park, C. Lee, J. S. Cheng, and E. T. Morgan, Posttranslational regulation of CYP2J2 by nitric oxide, Free Radical Biology and Medicine, vol.121, pp.149-156, 2018.

S. Park, G. Zhen, C. Verhaeghe, Y. Nakagami, L. T. Nguyenvu et al., The protein disulfide isomerase AGR2 is essential for production of intestinal mucus, Proc. Natl. Acad. Sci. U.S.A, vol.106, pp.6950-6955, 2009.

O. Parodi, R. De-maria, and E. Roubina, Redox state, oxidative stress and endothelial dysfunction in heart failure: the puzzle of nitrate-thiol interaction, Journal of Cardiovascular Medicine, vol.8, pp.765-774, 2007.

D. Payros, T. Secher, M. Boury, C. Brehin, S. Ménard et al., Maternally acquired genotoxic Escherichia coli alters offspring's intestinal homeostasis, Gut Microbes, vol.5, pp.313-512, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02935531

M. Perez-moreno, C. Jamora, and E. Fuchs, Sticky Business. Cell, vol.112, pp.535-548, 2003.

C. Perrin-sarrado, M. Pongas, F. Dahboul, P. Leroy, A. Pompella et al., Reduced Activity of the Aortic Gamma-Glutamyltransferase Does Not Decrease S-Nitrosoglutathione Induced Vasorelaxation of Rat Aortic Rings, Front Physiol, vol.7, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02150281

S. B. Petersen, G. Nolan, S. Maher, U. L. Rahbek, M. Guldbrandt et al., Evaluation of alkylmaltosides as intestinal permeation enhancers: Comparison between rat intestinal mucosal sheets and Caco-2 monolayers, European Journal of Pharmaceutical Sciences, vol.47, pp.701-712, 2012.

L. Peyrin-biroulet, Y. Bouhnik, X. Roblin, G. Bonnaud, H. Hagège et al., French national consensus clinical guidelines for the management of ulcerative colitis, Digestive and Liver Disease, vol.48, pp.726-733, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01662142

L. C. Pinheiro, J. H. Amaral, G. C. Ferreira, R. L. Portella, C. S. Ceron et al., Gastric S-nitrosothiol formation drives the antihypertensive effects of oral sodium nitrite and nitrate in a rat model of renovascular hypertension, Free Radical Biology and Medicine, vol.87, pp.252-262, 2015.

J. Piontek, L. Winkler, H. Wolburg, S. L. Müller, N. Zuleger et al., Formation of tight junction: determinants of homophilic interaction between classic claudins, The FASEB Journal, vol.22, pp.146-158, 2008.

B. I. Polentarutti, A. L. Peterson, A. K. Sjöberg, E. K. Anderberg, L. M. Utter et al., Evaluation of viability of excised rat intestinal segments in the Ussing chamber: investigation of morphology, electrical parameters, and permeability characteristics, Pharm. Res, vol.16, pp.446-454, 1999.

A. Pompella, A. Corti, A. Paolicchi, C. Giommarelli, and F. Zunino, Gammaglutamyltransferase, redox regulation and cancer drug resistance, Curr Opin Pharmacol, vol.7, pp.360-366, 2007.

C. S. Potten, G. Owen, and D. Booth, Intestinal stem cells protect their genome by selective segregation of template DNA strands, J. Cell. Sci, vol.115, pp.2381-2388, 2002.

N. A. Punchard, S. M. Greenfield, and R. P. Thompson, Mechanism of action of 5-arninosalicylic acid, Mediators of Inflammation, vol.1, pp.151-165, 1992.

J. F. Riordan, The role of metals in enzyme activity, Ann. Clin. Lab. Sci, vol.7, pp.119-129, 1977.

B. S. Rocha, M. G. Correia, R. C. Fernandes, J. S. Gonçalves, and J. Laranjinha, Dietary nitrite induces occludin nitration in the stomach, Free Radical Research, vol.50, pp.1257-1264, 2016.

S. F. Rodrigues and D. N. Granger, Blood cells and endothelial barrier function. Tissue Barriers 3, e978720, 2015.

J. Rodriguez, R. E. Maloney, T. Rassaf, N. S. Bryan, and M. Feelisch, Chemical nature of nitric oxide storage forms in rat vascular tissue, Proceedings of the National Academy of Sciences, vol.100, pp.336-341, 2003.

J. L. Rombeau and J. Takala, Gut Dysfunction in Critical Illness, Update in Intensive Care and Emergency Medicine, 1996.

B. Rubinfeld, B. Souza, I. Albert, S. Munemitsu, and P. Polakis, The APC protein and Ecadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin, J. Biol. Chem, vol.270, pp.5549-5555, 1995.

A. Ruhl, Y. Nasser, and K. A. Sharkey, Enteric glia, Neurogastroenterol Motil, vol.16, pp.44-49, 2004.

S. Y. Salim and J. D. Söderholm, Importance of disrupted intestinal barrier in inflammatory bowel diseases, Inflammatory Bowel Diseases, vol.17, pp.362-381, 2011.

F. A. Sánchez, I. P. Ehrenfeld, and W. N. Durán, S-nitrosation of proteins: An emergent regulatory mechanism in microvascular permeability and vascular function. Tissue Barriers 1, e23896, 2013.

P. J. Sansonetti, War and peace at mucosal surfaces, Nature Reviews Immunology, vol.4, pp.953-964, 2004.

T. C. Savidge, P. Newman, C. Pothoulakis, A. Ruhl, M. Neunlist et al., Enteric Glia Regulate Intestinal Barrier Function and Inflammation Via Release of S-Nitrosoglutathione, Gastroenterology, vol.132, pp.1344-1358, 2007.

N. Saxena, J. Won, S. Choi, A. K. Singh, and I. Singh, S-nitrosoglutathione reductase (GSNOR) inhibitor as an immune modulator in experimental autoimmune encephalomyelitis, Free Radical Biology and Medicine, vol.121, pp.57-68, 2018.

F. Q. Schafer and G. R. Buettner, Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radical Biology and Medicine, vol.30, pp.1191-1212, 2001.

F. Schiele, Y. Artur, D. Bagrel, C. Petitclerc, and G. Siest, Measurement of plasma gamma-glutamyltransferase in clinical chemistry: kinetic basis and standardisation propositions, Clinica Chimica Acta, vol.112, issue.81, pp.90377-90383, 1981.

M. R. Schneider, M. Dahlhoff, D. Horst, B. Hirschi, K. Trülzsch et al., A Key Role for E-cadherin in Intestinal Homeostasis and Paneth Cell Maturation, PLoS ONE, vol.5, 2010.

B. O. Schroeder, Fight them or feed them: how the intestinal mucus layer manages the gut microbiota, Gastroenterology Report, vol.7, pp.3-12, 2019.

J. D. Schulzke, A. H. Gitter, J. Mankertz, S. Spiegel, U. Seidler et al., Epithelial transport and barrier function in occludindeficient mice, Biochim. Biophys. Acta, vol.1669, pp.34-42, 2005.

C. M. Shah, S. E. Bell, I. C. Locke, H. S. Chowdrey, and M. P. Gordge, Interactions between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery, Nitric Oxide, vol.16, pp.135-142, 2007.

K. U. Shah, S. U. Shah, N. Dilawar, G. M. Khan, and S. Gibaud, Thiomers and their potential applications in drug delivery, Expert Opinion on Drug Delivery, vol.14, pp.601-610, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01377809

W. Shen and T. Matsui, Intestinal absorption of small peptides: a review, Int J Food Sci Technol, vol.54, pp.1942-1948, 2019.

Z. Shen, A. Mannion, M. T. Whary, S. Muthupalani, A. Sheh et al., Helicobacter saguini, a Novel Helicobacter Isolated from Cotton-Top Tamarins with Ulcerative Colitis, Has Proinflammatory Properties and Induces Typhlocolitis and Dysplasia in Gnotobiotic IL-10-/-Mice, Infect. Immun, vol.84, pp.2307-2316, 2016.

S. Shin and H. Fung, Evaluation of an LC-MS/MS assay for 15N-nitrite for cellular studies of L-arginine action, J Pharm Biomed Anal, vol.56, pp.1127-1131, 2011.

S. Shin and H. Fung, Evaluation of an LC-MS/MS assay for 15N-nitrite for cellular studies of l-arginine action, Journal of Pharmaceutical and Biomedical Analysis, vol.56, pp.1127-1131, 2011.

I. Sliskovic, A. Raturi, and B. Mutus, Characterization of the S-Denitrosation Activity of Protein Disulfide Isomerase, Journal of Biological Chemistry, vol.280, pp.8733-8741, 2005.

W. G. Smalley-freed, A. Efimov, P. E. Burnett, S. P. Short, M. A. Davis et al., p120-catenin is essential for maintenance of barrier function and intestinal homeostasis in mice, Journal of Clinical Investigation, vol.120, pp.1824-1835, 2010.

J. N. Smith and T. P. Dasgupta, Kinetics and mechanism of the decomposition of Snitrosoglutathione by l-ascorbic acid and copper ions in aqueous solution to produce nitric oxide, Nitric Oxide, vol.4, pp.57-66, 2000.

V. Spindler, M. Meir, B. Vigh, S. Flemming, K. Hütz et al., Loss of Desmoglein 2 Contributes to the Pathogenesis of Crohn?s Disease, Inflammatory Bowel Diseases, vol.1, 2015.

B. Srinivasan, A. R. Kolli, M. B. Esch, H. E. Abaci, M. L. Shuler et al., TEER Measurement Techniques for In Vitro Barrier Model Systems, Journal of Laboratory Automation, vol.20, pp.107-126, 2015.

C. A. Staab, T. Hartmanová, Y. El-hawari, B. Ebert, M. Kisiela et al., Studies on reduction of S-nitrosoglutathione by human carbonyl reductases 1 and 3, Chemico-Biological Interactions, vol.191, pp.95-103, 2011.

X. Sun, J. W. Wasley, J. Qiu, J. P. Blonder, A. M. Stout et al., Discovery of S -Nitrosoglutathione Reductase Inhibitors: Potential Agents for the Treatment of Asthma and Other Inflammatory Diseases, ACS Med. Chem. Lett, vol.2, pp.402-406, 2011.

H. Takanaga, I. Tamai, and A. Tsuji, pH-Dependent and Carrier-mediated Transport of Salicylic Acid Across Caco-2 Cells, Journal of Pharmacy and Pharmacology, vol.46, pp.567-570, 1994.

S. Tate and A. Meister, Serine-borate complex as a transition-state inhibitor of gammaglutamyl transpeptidase, Proc. Natl. Acad. Sci. U.S.A, vol.75, pp.4806-4809, 1978.

S. Thibeault, Y. Rautureau, M. Oubaha, D. Faubert, B. C. Wilkes et al., S-Nitrosylation of ?-Catenin by eNOS-Derived NO Promotes VEGF-Induced Endothelial Cell Permeability, Molecular Cell, vol.39, pp.468-476, 2010.

A. Thomson, K. Smart, M. S. Somerville, S. N. Lauder, G. Appanna et al., The Ussing chamber system for measuring intestinal permeability in health and disease, BMC Gastroenterol, vol.19, 2019.

M. A. Thoreson, P. Z. Anastasiadis, J. M. Daniel, R. C. Ireton, M. J. Wheelock et al., Selective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesion, J. Cell Biol, vol.148, pp.189-202, 2000.

H. H. Tønnesen and J. Karlsen, Alginate in Drug Delivery Systems, Drug Development and Industrial Pharmacy, vol.28, pp.621-630, 2002.

A. V. Treuer and D. R. Gonzalez, Nitric oxide synthases, S-nitrosylation and cardiovascular health: From molecular mechanisms to therapeutic opportunities (Review), Molecular Medicine Reports, vol.11, pp.1555-1565, 2015.

A. Tsuji, H. Takanaga, I. Tamai, and T. Terasaki, Pharmaceutical Research, vol.11, pp.30-37, 1994.

S. Tsukita, M. Furuse, and M. Itoh, Multifunctional strands in tight junctions, Nat. Rev. Mol. Cell Biol, vol.2, pp.285-293, 2001.

K. Turksen and T. Troy, Barriers built on claudins, J. Cell. Sci, vol.117, pp.2435-2447, 2004.

J. R. Turner, Intestinal mucosal barrier function in health and disease, Nature Reviews Immunology, vol.9, pp.799-809, 2009.

J. R. Turner, Show me the pathway! Regulation of paracellular permeability by Na(+)-glucose cotransport, Adv. Drug Deliv. Rev, vol.41, pp.265-281, 2000.

J. R. Turner, B. K. Rill, S. L. Carlson, D. Carnes, R. Kerner et al., Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation, Am. J. Physiol, vol.273, pp.1378-1385, 1997.

T. Uchiyama, T. Sugiyama, Y. S. Quan, A. Kotani, N. Okada et al., Enhanced permeability of insulin across the rat intestinal membrane by various absorption enhancers: their intestinal mucosal toxicity and absorption-enhancing mechanism of n-lauryl-beta-D-maltopyranoside, J. Pharm. Pharmacol, vol.51, pp.1241-1250, 1999.

D. Ulluwishewa, R. C. Anderson, W. C. Mcnabb, P. J. Moughan, J. M. Wells et al., Regulation of Tight Junction Permeability by Intestinal Bacteria and Dietary Components, The Journal of Nutrition, vol.141, pp.769-776, 2011.

A. L. Ungell, S. Nylander, S. Bergstrand, A. Sjöberg, and H. Lennernäs, Membrane transport of drugs in different regions of the intestinal tract of the rat, J Pharm Sci, vol.87, pp.360-366, 1998.

H. Ungewiß, F. Vielmuth, S. T. Suzuki, A. Maiser, H. Harz et al., Innovative Methods to Study Human Intestinal Drug Metabolism in Vitro: Precision-Cut Slices Compared with Ussing Chamber Preparations, Drug Metabolism and Disposition, vol.7, pp.1893-1902, 2006.

B. Van-der-loo, R. Labugger, J. N. Skepper, M. Bachschmid, J. Kilo et al., Enhanced Peroxynitrite Formation Is Associated with Vascular Aging, J Exp Med, vol.192, pp.1731-1744, 2000.

V. V. Verma, R. Gupta, and M. Goel, Phylogenetic and evolutionary analysis of functional divergence among Gamma glutamyl transpeptidase (GGT) subfamilies, Biol Direct, vol.10, 2015.

V. Volynets, A. Rings, G. Bárdos, M. J. Ostaff, J. Wehkamp et al., Intestinal barrier analysis by assessment of mucins, tight junctions, and ?-defensins in healthy C57BL/6J and BALB/cJ mice, 2016.

S. Wickham, M. B. West, P. F. Cook, and M. H. Hanigan, Gamma-glutamyl compounds: Substrate specificity of gamma-glutamyl transpeptidase enzymes, Analytical Biochemistry, vol.414, pp.208-214, 2011.

W. Wu, C. Gaucher, I. Fries, X. Hu, P. Maincent et al., Polymer nanocomposite particles of S -nitrosoglutathione: A suitable formulation for protection and sustained oral delivery, International Journal of Pharmaceutics, vol.495, pp.354-361, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01281137

W. Wu, C. Perrin-sarrado, H. Ming, I. Lartaud, P. Maincent et al., Polymer nanocomposites enhance S -nitrosoglutathione intestinal absorption and promote the formation of releasable nitric oxide stores in rat aorta, Nanomedicine: Nanotechnology, Biology and Medicine, vol.12, pp.1795-1803, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01493332

K. Yamauchi, T. Rai, K. Kobayashi, E. Sohara, T. Suzuki et al., Disease-causing mutant WNK4 increases paracellular chloride permeability and phosphorylates claudins, Proc. Natl. Acad. Sci. U.S.A, vol.101, pp.4690-4694, 2004.

B. B. Yoo and S. K. Mazmanian, The Enteric Network: Interactions between the Immune and Nervous Systems of the Gut, Immunity, vol.46, pp.910-926, 2017.

H. Yu, J. Bonetti, C. Gaucher, I. Fries, L. Vernex-loset et al., Higher-energy collision-induced dissociation for the quantification by liquid chromatography/tandem ion trap mass spectrometry of nitric oxide metabolites coming from S-nitroso-glutathione in an in vitro model of the intestinal barrier, Rapid Commun. Mass Spectrom, vol.33, pp.1-11, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02044975

H. Yu, P. Chaimbault, I. Clarot, Z. Chen, and P. Leroy, Labeling nitrogen species with the stable isotope 15N for their measurement by separative methods coupled with mass spectrometry: A review, Talanta, vol.191, pp.491-503, 2019.
URL : https://hal.archives-ouvertes.fr/hal-01874147

H. Yu, R. Schmitt, A. Sapin, P. Chaimbault, and P. Leroy, Comparison between two derivatization methods of nitrite ion labeled with 15 N applied to liquid chromatography-tandem mass spectrometry, Anal. Methods, vol.10, pp.3830-3836, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01874145

Q. Yu, Z. Wang, P. Li, and Q. Yang, The effect of various absorption enhancers on tight junction in the human intestinal Caco-2 cell line, Drug Dev Ind Pharm, vol.39, pp.587-592, 2013.

S. ?akelj, I. Legen, M. Veber, and A. Kristl, The influence of buffer composition on tissue integrity during permeability experiments "in vitro, International Journal of Pharmaceutics, vol.272, pp.173-180, 2004.

E. , Déshydratation et inclusion en paraffine du tissu 1-Après 24 h dans le liquide de Bouin

, Conserver à 4°C, et renouveler l'alcool 80% v/v toutes les > 2 h

F. , Coupe du tissu 1-Placer le bloc de paraffine

, Allumer le banc chauffant

, Déposer de l'albumine glycérinée 2% sur les lames préalablement annotées

, Préchauffer les lames sur le banc

, Couper le bloc de paraffine : les coupes doivent alors être récupérées délicatement avec une pince

, Une fois remplies, laisser sécher les lames, en position verticale

G. , Déparaffinage et réhydratation des coupes 1-Chauffer les lames dans une étuve à 56°C, pendant 15 min. 2-Mettre du xylène dans un bac de coloration

, Mettre de l'alcool 100% v/v dans un bac de coloration, effectuer 8 à 10 plongées

, Mettre de l'alcool 95% v/v dans un bac de coloration, et effectuer un bain de 3 min

, Mettre de l'alcool 80% v/v dans un bac de coloration, et effectuer un bain de 3 min

H. , Coloration et observation microscopique des coupes 1-Déposer 5 gouttes d'hématoxyline sur les coupes à l'aide d'une pipette

, Déposer 5 gouttes d'alcool chlorhydrique sur les coupes à l'aide d'une pipette, laisser à exposition pendant 5 secondes puis rincer à l'eau purifiée

, Déposer 5 gouttes de solution de Scott sur les coupes à l'aide d'une pipette, laisser à exposition pendant 30 secondes puis rincer à l'eau purifiée

, Déposer 5 gouttes d'éosine sur les coupes à l'aide d'une pipette, laisser à exposition pendant 2 min puis rincer à l'eau purifiée

, -Déshydrater les coupes par bains successifs d'alcool à 50%

-. Hotte, déposer du xylène afin de recouvrir les coupes, et retirer le xylène en disposant les lames verticalement

-. Hotte, Poly-Mount) afin de recouvrir les coupes, puis déposer la lamelle couvre-objet délicatement, déposer du milieu de montage

, Laisser sécher les lames ainsi préparées, sous hotte active, pendant au moins 12 à 24 h. 10-Procéder à l'observation microscopique. Cf. Mode Opératoire Normalisé (EA 3452 M2_P2_I01 2.1. Physiological media Conservation time: one week at 4°C after preparation

, Phosphate Buffer Saline (PBS) solution: weigh 8.00 g NaCl, 0.20 g KCl, vol.2, p.32

, Hank's Balanced Salt Solution (HBSS): use commercial HBSS (ref Gibco: 14185-045) made of 8.0 g/L NaCl

M. Hcl, Mw = 36.46 g/mol; commercial solution) in a of DAN (Mw = 158 g/mol; ref Sigma D-2757of HgCl2 (Mw = 271.5 g/mol

, Nitrite, nitrate ions and Snitrosothiols measurement using 2,3-diaminonaphthalene assay by spectrofluorometry References

M. Chao, Y. Shih, Y. Hsu, H. Liu, Y. Chang et al., Urinary nitrite/nitrate ratio measured by isotope-dilution LC-MS/MS as a tool to screen for urinary tract infections

, Biol. Med, vol.93, pp.77-83, 2016.

E. R. Axton, E. A. Hardardt, and J. F. Stevens, Stable isotope-assisted LC-MS/MS monitoring of glyceryl trinitrate bioactivation in a cell culture model of nitrate tolerance, J. Chromatogr. B, vol.1019, pp.156-163, 2016.

S. Shin and H. Fung, Evaluation of an LC-MS/MS assay for 15N-nitrite for cellular studies of l-arginine action, J. Pharm. Biomed. Anal, vol.56, pp.1127-1131, 2011.

, Reagents All solutions are prepared with fresh cold ultrapure water (> 18.2 M?.cm) and

, Physiological media Conservation time: one week at 4°C after preparation

, Phosphate Buffer Saline (PBS) solution: weigh 8.00 g NaCl, 0.20 g KCl, vol.2, p.32

, by using a pH meter) with 10 M NaOH solution. Sterilize and aliquot in 35 mL fractions

, Hank's Balanced Salt Solution (HBSS): use commercial HBSS (ref Gibco: 14185-045) made of 8.0 g/L NaCl

M. Hcl, Mw = 36.46 g/mol; commercial solution) in a 500 of DAN (Mw = 158 g/mol

, Nitrite, nitrate ions and Snitrosothiols measurement using 2,3-diaminonaphthalene assay by HPLC coupled with tandem mass spectrometry Intra-day Inter-day

S. Shin and H. Fung, Evaluation of an LC-MS/MS assay for 15N-nitrite for cellular studies of l-arginine action, J. Pharm. Biomed. Anal, vol.56, pp.1127-1131, 2011.

C. Damacena-angelis, G. H. Oliveira-paula, L. C. Pinheiro, E. J. Crevelin, R. L. Portella et al., Nitrate decreases xanthine oxidoreductase-mediated nitrite reductase activity and attenuates vascular and blood pressure responses to nitrite, Redox Biol, vol.12, pp.291-299, 2017.

, Reagents All solutions are prepared with fresh cold ultrapure water (> 18.2 M?.cm) and

, Physiological media Conservation time: one week at 4°C after preparation

, Phosphate Buffer Saline (PBS) solution: weigh 8.00 g NaCl, 0.20 g KCl, vol.2, p.32

, M Tris buffer (pH = 7.4): weigh 1.576 g of Trizma-HCl (Mw = 158 g/mol, ref

, Sigma T040) and dissolve in 100 mL of ultrapure water

, 2) is a membrane-bound protein that catalyzes the transfer of ?-glutamyl moieties to acceptor molecules such as amino acids or peptides. As GGT can catalyze the transfer of a -glutamyl group from the colorless substrate of L-?-glutamyl-3-carboxy-4-nitroanilide, to the acceptor of glycylglycine with production of the colored product of 3-carboxy-4-nitroanilide, the enzyme activity is related to the absorbance measured at 405 nm, with molar absorbance (?) equal to 9, 1963.

M. Orlowski and A. Meister, Gamma-Glutamyl-Rho-Nitroanilide -a New Convenient Substrate for Determination and Study of L-and D-Gamma-Glutamyltranspeptidase Activities, Biochim. Biophys. Acta, vol.73, p.679, 1963.

, Reagents All solutions are prepared with fresh cold ultrapure water (> 18.2 M?.cm) and

, Physiological media Conservation time: one week at 4°C after preparation

, M Tris buffer (pH = 7.4): weigh 1.576 g of Trizma-HCl (Mw = 158 g/mol, ref

, Sigma T040), dissolve with 100 mL of ultrapure water; and adjust the pH to 7.40 ± 0.05 with 10 M NaOH solution

, M Phosphate buffer (pH = 7.4): Weigh 1.36 g of KH2PO4 (Mw =

, ref Merck 646A148973) and 0of L-?-glutamyl-3-carboxy-4-nitroanilide (Mw = 328.3 g/mol, ref

, 31 g/mol, ref Sigma M9272) and 52.8 mg of glycylglycine (Mw = 132.1, ref Sigma G1002), dissolve with 20 mL of Tris buffer. Protect solution from light. The same solution is prepared without adding the substrate for the blank, Sigma AC98), 40.6 mg of MgCl2·6H2O (Mw = 203

, Weigh 1 mg of GGT (26 UI*/mL, bovine kidney), dissolve with 1 mL of phosphate buffer, divide the solution in aliquots of 100 µL (1.1 UI/mL) and store them at -20°C for maximum five months (determine the GGT concentration by the BCA Protein Assay kit (Pierce? BCA Protein Assay Kit, 23225.

, 100 mM Serine-borate complex (SBC) Weigh 0.503 g of sodium borate (Mw = 201.372 g/mol, ref Sigma S4500) and 0.2665 g of serine (Mw = 105.09, ref Sigma G100)

, Prepare 20 mM SBC by mixing 5 mL of 100 mM SBC and 20 mL of 100 mM Tris buffer. Weigh and dissolve 6.6 mg of L-?

, ref Sigma AC98) with 20 mL of 20 mM SBC solution

, Equilibrate the temperature of the incubator at 37°C, transfer 5 mL of solution with substrate to a 1.5 mL microtube, incubate at 37°C in the dark for 5 min. Next, dilute GGT (1.1 UI/mL) 1:10 in Tris buffer and add 25 µL of GGT

P. Billat, E. Roger, S. Faure, and F. Lagarce, Models for drug absorption from the small intestine: where are we and where are we going?, Drug Discovery Today, vol.22, pp.761-775, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02615955

,

E. Neirinckx, C. Vervaet, J. Michiels, S. Smet, and W. Van-den-broeck,

. Croubels, Feasibility of the Ussing chamber technique for the determination of in vitro jejunal permeability of passively absorbed compounds in different animal species, J. Vet. Pharmacol. Ther, vol.34, pp.290-297, 2011.

, Reagents All solutions are prepared with fresh cold ultrapure water (> 18.2 M?.cm) and

, Set the Ussing chamber at 37 o C with an O2/CO2 (95 %/5 %) mixture bubbling

, Remove the fat tissue along the mesenteric attachment and open the intestine longitudinally. Rinse segments from the distal portion of the ileum with pre-heated Krebs solution