Zonula occludens |
ZO1
|
Maintains and regulates epithelial barriers, participates in the regulation of cell material transport, and maintains epithelial polarity. |
Neunlist et al., 2003Neunlist, M.; Toumi, F.; Oreschkova, T.; Denis, M.; Leborgne, J.; Laboisse, C. L. and Jarry, A. 2003. Human ENS regulates the intestinal epithelial barrier permeability and a tight junction-associated protein ZO-1 via VIPergic pathways. American Journal of Physiology-Gastrointestinal and Liver Physiology 285:G1028-G1036. https://doi.org/10.1152/ajpgi.00066.2003 https://doi.org/10.1152/ajpgi.00066.2003...
|
ZO2
|
Occludin |
OCLN
|
Promotes the formation of selective ion channels in tight junctions and is associated with intercellular adhesion, migration, and permeability. |
Berkes et al., 2003Berkes, J.; Viswanathan, V. K.; Savkovic, S. D. and Hecht, G. 2003. Intestinal epithelial responses to enteric pathogens: effects on the tight junction barrier, ion transport, and inflammation. Gut 52:439-451. https://doi.org/10.1136/gut.52.3.439 https://doi.org/10.1136/gut.52.3.439...
|
|
CLDN1
|
|
|
Claudins |
CLDN4
|
Regulates the pore pathway, determines TER as well as paracellular charge selectivity. |
Colegio et al., 2003Colegio, O. R.; Itallie, C. V.; Rahner, C. and Anderson, J. M. 2003. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. American Journal of Physiology-Cell Physiology 284:C1346-C1354. https://doi.org/10.1152/ajpcell.00547.2002 https://doi.org/10.1152/ajpcell.00547.20...
|
|
CLDN5
|
|
|
Cingulin |
CGN
|
Regulates expression of TJ proteins through the RhoA signal pathway. |
Hamard et al., 2010Hamard, A.; Mazurais, D.; Boudry, G.; Le Huërou-Luron, I.; Sève, B. and Le Floc'h, N. 2010. A moderate threonine deficiency affects gene expression profile, paracellular permeability and glucose absorption capacity in the ileum of piglets. The Journal of Nutritional Biochemistry 21:914-921. https://doi.org/10.1016/j.jnutbio.2009.07.004 https://doi.org/10.1016/j.jnutbio.2009.0...
|
Glucagon-like peptide 2 |
GLP2
|
Induces the proliferation and reduces the internalization of enterobacteriaceae, regenerates the intestinal mucosa, and improves the intestinal barrier function. |
Cani et al., 2009Cani, P. D.; Possemiers, S.; Van de Wiele, T.; Guiot, Y.; Everard, A.; Rottier, O.; Geurts, L.; Naslain, D.; Neyrinck, A.; Lambert, D. M.; Muccioli, G. G. and Delzenne, N. M. 2009. Changes in gut microbiota control inflammation in obese mice through a mechanism involving GLP-2-driven improvement of gut permeability. Gut 58:1091-1103. https://doi.org/10.1136/gut.2008.165886 https://doi.org/10.1136/gut.2008.165886...
|
E-cadherin |
E-CDH
|
Tight attachment of adjacent epithelial cells is ensured by allelic interactions at their basolateral adhesive junctions. |
Uemura, 1998Uemura, T. 1998. The cadherin superfamily at the synapse: more members, more missions. Cell 93:1095-1098. https://doi.org/10.1016/S0092-8674(00)81452-X https://doi.org/10.1016/S0092-8674(00)81...
|
Integrin |
ITG
|
Establishes a physical connection between the extracellular matrix and the cytoskeleton that mediates the activation of cell adhesion signaling pathways. |
Stupack and Cheresh, 2002Stupack, D. G. and Cheresh, D. A. 2002. Get a ligand, get a life: integrins, signaling and cell survival. Journal of Cell Science 115:3729-3738. https://doi.org/10.1242/jcs.00071 https://doi.org/10.1242/jcs.00071...
|
Nectin1 |
NECTIN1
|
Participates in intercellular adhesion and recruits TJ components. |
Rikitake and Takai, 2008Rikitake, Y. and Takai, Y. 2008. Interactions of the cell adhesion molecule nectin with transmembrane and peripheral membrane proteins for pleiotropic functions. Cellular and Molecular Life Sciences 65:253-263. https://doi.org/10.1007/s00018-007-7290-9 https://doi.org/10.1007/s00018-007-7290-...
|
Aquaporin 3 |
AQP3
|
Changes the ability of the intestinal tract to move water, causes diarrhea or constipation. |
Li et al., 2008Li, X.; Lei, T.; Xia, T.; Chen, X.; Feng, S.; Chen, H.; Chen, Z.; Peng, Y. and Yang, Z. 2008. Molecular characterization, chromosomal and expression patterns of three aquaglyceroporins (AQP3, 7, 9) from pig. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 149:468-476. https://doi.org/10.1016/j.cbpb.2007.11.014 https://doi.org/10.1016/j.cbpb.2007.11.0...
|
Aquaporin 8 |
AQP8
|
Changes the intestinal mucosal water exchange capacity, disrupts the intestinal mucosal barrier, and causes chronic inflammation and ulcers. |
Gao et al., 2014Gao, Y.; Deng, Q.; Zhang, Y.; Zhang, S.; Zhu, Y. and Zhang, J. 2014. The expression of the multiple splice variants of AQP8 in porcine testes at different developmental stages. Journal of Applied Genetics 55:511-514. https://doi.org/10.1007/s13353-014-0219-8 https://doi.org/10.1007/s13353-014-0219-...
|
Neonatal Fc receptor |
FcRN
|
Specific receptor of IgG, which interacts with IgG to produce effects on the intestinal mucosa. |
Dong et al., 2016Dong, L.; Zhong, X.; He, J.; Zhang, L.; Bai, K.; Xu, W.; Wang, T. and Huang, X. 2016. Supplementation of tributyrin improves the growth and intestinal digestive and barrier functions in intrauterine growth-restricted piglets. Clinical Nutrition 35:399-407. https://doi.org/10.1016/j.clnu.2015.03.002 https://doi.org/10.1016/j.clnu.2015.03.0...
|
Mucins |
MUC1
|
Lubricates and protects the intestinal mucosa, provides adhesion sites for probiotics, regulates intestinal bacteria balance, enhances intestinal barrier function, assists the intestinal immune system, and inhibits the production of proinflammatory factors. |
Johansson et al., 2013Johansson, M. E.; Sjövall, H. and Hansson, G. C. 2013. The gastrointestinal mucus system in health and disease. Nature reviews Gastroenterology & Hepatology 10:352. https://doi.org/10.1038/nrgastro.2013.35 https://doi.org/10.1038/nrgastro.2013.35...
|
MUC2
|
MUC4
|
MUC5AC
|
Trefoil factor 1 |
TFF1
|
Interacts with mucins such as MUC2, and preserves mucosal integrity. |
Laukoetter et al., 2008Laukoetter, M. G.; Nava, P. and Nusrat, A. 2008. Role of the intestinal barrier in inflammatory bowel disease. World Journal of Gastroenterology 14:401-407.
|
β-defensin 1 |
PBD1
|
Has broad-spectrum antimicrobial activity, induces the production of inflammatory mediators, and regulates innate and immune adaptive immunity. |
Yang et al., 2004Yang, D.; Biragyn, A.; Hoover, D. M.; Lubkowski, J. and Oppenheim, J. J. 2004. Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense. Annual Review of Immunology 22:181-215. https://doi.org/10.1146/annurev.immunol.22.012703.104603 https://doi.org/10.1146/annurev.immunol....
|
β-defensin 2 |
PBD2
|
Prevents infection by bacteria and viruses, regulates immune factors, and participates in immune regulation. |
Veldhuizen et al., 2008Veldhuizen, E. J.; Rijnders, M.; Claassen, E. A.; van Dijk, A. and Haagsman, H. P. 2008. Porcine β-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria. Molecular Immunology 45:386-394. https://doi.org/10.1016/j.molimm.2007.06.001 https://doi.org/10.1016/j.molimm.2007.06...
|
Porcine myeloid antibacterial peptide 37 |
PMAP37
|
Inhibits gram-positive and -negative bacteria. |
Tossi et al., 1995Tossi, A.; Scocchi, M.; Zanetti, M.; Storici, P. and Gennaro, R. 1995. PMAP-37, a novel antibacterial peptide from pig myeloid cells: cDNA cloning, chemical synthesis and activity. European Journal of Biochemistry 228:941-946.
|
Discs large homolog 5 |
DLG5
|
Stabilizes the apical protein complex and is associated with the maintenance of the integrity and polarity of epithelial cells. |
Friedrichs and Stoll, 2006Friedrichs, F. and Stoll, M. 2006. Role of discs large homolog 5. World Journal of Gastroenterology 12:3651-3656.
|
Tumor necrosis factor- α
|
TNFA
|
Modulates the function of a tight junction between epithelial cells of the intestine, kidney, lung, and salivary glands. |
Baker et al., 2008Baker, O. J.; Camden, J. M.; Redman, R. S.; Jones, J. E.; Seye, C. I.; Erb, L. and Weisman, G. A. 2008. Proinflammatory cytokines tumor necrosis factor-α and interferon-γ alter tight junction structure and function in the rat parotid gland Par-C10 cell line. American Journal of Physiology-Cell Physiology 295:C1191-C1201. https://doi.org/10.1152/ajpcell.00144.2008 https://doi.org/10.1152/ajpcell.00144.20...
|
Interferon-γ |
IFNG
|
Modulates the function of a tight junction between epithelial cells of the intestine, kidney, lung, and salivary glands. |
Baker et al., 2008Baker, O. J.; Camden, J. M.; Redman, R. S.; Jones, J. E.; Seye, C. I.; Erb, L. and Weisman, G. A. 2008. Proinflammatory cytokines tumor necrosis factor-α and interferon-γ alter tight junction structure and function in the rat parotid gland Par-C10 cell line. American Journal of Physiology-Cell Physiology 295:C1191-C1201. https://doi.org/10.1152/ajpcell.00144.2008 https://doi.org/10.1152/ajpcell.00144.20...
|