Cited by 263Barrier Structure and Function StudiesInflammatory Bowel DiseaseGastrointestinal motility and disorders

The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.

TNF-α Modulation of Intestinal Epithelial Tight Junction Barrier Is Regulated by ERK1/2 Activation of Elk-1

Open access

Al-Sadi, Rana, Guo, Shuhong, Ye, Dongmei, Ma, Thomas Y.·2013·The American Journal of Pathology

DOI 10.1016/j.ajpath.2013.09.001PMC PMC5745548

Open this paper in CoChat — free account Open PDF

Abstract

Tumor necrosis factor (TNF-α) is a proinflammatory cytokine that plays a critical role in the pathogenesis of inflammatory bowel disease. TNF-α causes an increase in intestinal permeability; however, the signaling pathways and the molecular mechanisms involved remain unclear. The major purpose of this study was to investigate the role of MAP kinase pathways (ERK1/2 and p38 kinase) and the molecular processes involved. An in vitro intestinal epithelial model system consisting of Caco-2 monolayers and an in vivo mouse model system were used to delineate the cellular and molecular mechanisms involved in TNF-α effects on tight junction barrier. The TNF-α-induced increase in Caco-2 tight junction permeability was mediated by activation of the ERK1/2 signaling pathway, but not the p38 kinase pathway. Activation of the ERK1/2 pathway led to phosphorylation and activation of the ETS domain-containing transcription factor Elk-1. The activated Elk-1 translocated to the nucleus, where it bound to its binding motif on the myosin light chain kinase (MLCK) promoter region, leading to the activation of MLCK promoter activity and gene transcription. In addition, in vivo intestinal perfusion studies also indicated that the TNF-α-induced increase in mouse intestinal permeability requires ERK1/2-dependent activation of Elk-1. These studies provide novel insight into the cellular and molecular processes that regulate the TNF-α-induced increase in intestinal epithelial tight junction permeability.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.ajpath.2013.09.001

Cites

48 of 48 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Physiology of the Gastrointestinal Tract
Johnson, L. R. (2006) · Elsevier eBooks · doi:10.1016/b978-0-12-088394-3.x5000-4 · Cited by 4,616
Intestinal mucosal barrier function in health and disease
Turner, J. R. (2009) · Nature reviews. Immunology · doi:10.1038/nri2653 · Cited by 3,952
Integration of MAP Kinase Signal Transduction Pathways at the Serum Response Element
Whitmarsh, A. J., Shore, P., Sharrocks, A. D., & Davis, R. J. (1995) · Science · doi:10.1126/science.7618106 · Cited by 932
Enhand secretion of tumour necrosis factor-alpha, IL-6, and IL-1β by isolated lamina ropria monouclear cells from patients with ulcretive cilitis and Crohn's disease
REINECKER, H.-C., STEFFEN, M., Witthoeft, T., Pflüger, I., Schreiber, S., MacDermott, R. P., & Raedler, A. (1993) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.1993.tb05997.x · Cited by 855
TNF-α-induced increase in intestinal epithelial tight junction permeability requires NF-κB activation
Ma, T., Iwamoto, G. K., Hoa, N., Akotia, V., Pedram, A., Boivin, M., & Said, H. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00173.2003 · Cited by 811
Self-citation
Protein kinase cascades activated by stress and inflammatory cytokines
Kyriakis, J. M., & Avruch, J. (1996) · BioEssays · doi:10.1002/bies.950180708 · Cited by 709
ERK phosphorylation potentiates Elk‐1‐mediated ternary complex formation and transactivation.
Gille, H., Kortenjann, M., Thomae, O., Moomaw, C. R., Slaughter, C. A., Cobb, M. H., & Shaw, P. E. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07076.x · Cited by 665
IL-1β Causes an Increase in Intestinal Epithelial Tight Junction Permeability
Al-Sadi, R. M., & Ma, T. Y. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.7.4641 · Cited by 601
Self-citation
Tumor necrosis factor α-producing cells in the intestinal mucosa of children with inflammatory bowel disease
Breese, E. J., Michie, C. A., Nicholls, S. W., MURCH, S. H., Williams, C. B., Domizio, P., Walker-Smith, J. A., & MacDonald, T. T. (1994) · Gastroenterology · doi:10.1016/0016-5085(94)90398-0 · Cited by 566
Physiological regulation of epithelial tight junctions is associated with myosin light-chain phosphorylation
Turner, J. R., Rill, B. K., Carlson, S. L., Carnes, D., Kerner, R., Mrsny, R. J., & Madara, J. (1997) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1997.273.4.c1378 · Cited by 553

Show all 48 references

Sorted by citations

Dietary metabolism, the gut microbiome, and heart failure
Tang, W. H. W., Li, D. Y., & Hazen, S. L. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-018-0108-7 · Cited by 789
Human Intestinal Barrier Function in Health and Disease
König, J., Wells, J. M., Cani, P. D., García‐Ródenas, C. L., MacDonald, T. T., Mercenier, A., Whyte, J., Troost, F. J., & Brummer, R. J. (2016) · Clinical and Translational Gastroenterology · doi:10.1038/ctg.2016.54 · Cited by 811
Intestinal epithelial barrier function and tight junction proteins with heat and exercise
Dokładny, K., Zuhl, M., & Moseley, P. L. (2015) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00536.2015 · Cited by 328
Histamine and T helper cytokine–driven epithelial barrier dysfunction in allergic rhinitis
Steelant, B., Seys, S., Gerven, L. V., Woensel, M. V., Farré, R., Wawrzyniak, P., Krohn, I. K., Bullens, D. M. A., Talavera, K., Raap, U., et al. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2017.08.039 · Cited by 244
Tumour Necrosis Factor Alpha in Intestinal Homeostasis and Gut Related Diseases
Ruder, B., Atreya, R., & Becker, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081887 · Cited by 228
TNF-α Modulation of Intestinal Tight Junction Permeability Is Mediated by NIK/IKK-α Axis Activation of the Canonical NF-κB Pathway
Al–Sadi, R., Guo, S., Ye, D., Rawat, M., & Ma, T. Y. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.12.016 · Cited by 224
Self-citation
Regulation of intestinal permeability: The role of proteases
Spaendonk, H. V., Ceuleers, H., Witters, L., Patteet, E., Joossens, J., Augustyns, K., Lambeir, A., Meester, I. D., Man, J. G. D., & Winter, B. Y. D. (2017) · World Journal of Gastroenterology · doi:10.3748/wjg.v23.i12.2106 · Cited by 191
The gut microbiota and its interactions with cardiovascular disease
Xu, H., Wang, X., Feng, W., Liu, Q., Zhou, S., Liu, Q., & Cai, L. (2020) · Microbial Biotechnology · doi:10.1111/1751-7915.13524 · Cited by 196
A Novel Role of SLC26A3 in the Maintenance of Intestinal Epithelial Barrier Integrity
Kumar, A., Priyamvada, S., Ge, Y., Jayawardena, D., Singhal, M., Anbazhagan, A. N., Chatterjee, I., Dayal, A., Patel, M., Zadeh, K., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.11.008 · Cited by 158
1,25-Dihydroxyvitamin D Protects Intestinal Epithelial Barrier by Regulating the Myosin Light Chain Kinase Signaling Pathway
Du, J., Chen, Y., Shi, Y., Liu, T., Cao, Y., Tang, Y., Ge, X., Nie, H., Zheng, C.-Q., & Li, Y. C. (2015) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000526 · Cited by 157
Modulation of gut microbiota contributes to curcumin-mediated attenuation of hepatic steatosis in rats
Feng, W., Wang, H., Zhang, P., Gao, C., Tao, J., Ge, Z., Zhu, D., & Bi, Y. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.03.017 · Cited by 158
(-)-Epicatechin protects the intestinal barrier from high fat diet-induced permeabilization: Implications for steatosis and insulin resistance
Cremonini, E., Wang, Z., Bettaieb, A., Adamo, A. M., Daveri, E., Mills, D. A., Kalanetra, K. M., Haj, F. G., Karakas, S. E., & Oteiza, P. I. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.002 · Cited by 154
Tight junctions: from molecules to gastrointestinal diseases
Moonwiriyakit, A., Pathomthongtaweechai, N., Steinhagen, P. R., Chantawichitwong, P., Satianrapapong, W., & Pongkorpsakol, P. (2022) · Tissue Barriers · doi:10.1080/21688370.2022.2077620 · Cited by 151
Contributions of Myosin Light Chain Kinase to Regulation of Epithelial Paracellular Permeability and Mucosal Homeostasis
He, W., Wang, J., Sheng, J.-Y., Zha, J., Graham, W. V., & Turner, J. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030993 · Cited by 140
Exopolysaccharides from Lactobacillus plantarum NCU116 Regulate Intestinal Barrier Function via STAT3 Signaling Pathway
Zhou, X., Qi, W., Hong, T., Xiong, T., Gong, D., Xie, M., & Nie, S. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03340 · Cited by 137
Periodontitis and cardiometabolic disorders: The role of lipopolysaccharide and endotoxemia
Pussinen, P. J., Kopra, E., Pietiäinen, M., Lehto, M. J., Zarić, S., Paju, S., & Salminen, A. (2022) · Periodontology 2000 · doi:10.1111/prd.12433 · Cited by 142
Piezo1 regulates intestinal epithelial function by affecting the tight junction protein claudin-1 via the ROCK pathway
Jiang, Y., Song, J., Xu, Y., Liu, C., Qian, W., Bai, T., & Hou, X. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119254 · Cited by 127
Role of Bifidobacterium in Modulating the Intestinal Epithelial Tight Junction Barrier: Current Knowledge and Perspectives
Abdulqadir, R. F., Engers, J., & Al–Sadi, R. (2023) · Current Developments in Nutrition · doi:10.1016/j.cdnut.2023.102026 · Cited by 136
Self-citation
Cytokines and intestinal epithelial permeability: A systematic review
Meyer, F., Wendling, D., Demougeot, C., Prati, C., & Verhoeven, F. (2023) · Autoimmunity Reviews · doi:10.1016/j.autrev.2023.103331 · Cited by 125
Reduced gut microbiome protects from alcohol-induced neuroinflammation and alters intestinal and brain inflammasome expression
Lowe, P., Gyöngyösi, B., Satishchandran, A., Iracheta‐Vellve, A., Cho, Y., Ambade, A., & Szabó, G. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1328-9 · Cited by 126
Is There an Exercise-Intensity Threshold Capable of Avoiding the Leaky Gut?
Ribeiro, F. M., Petriz, B. A., Marques, G., Kamilla, L. H., & Franco, O. L. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.627289 · Cited by 119
Polyphenol-Rich Propolis Extracts Strengthen Intestinal Barrier Function by Activating AMPK and ERK Signaling
Wang, K., Jin, X., Chen, Y., Song, Z., Jiang, X., Hu, F., Conlon, M. A., & Topping, D. L. (2016) · Nutrients · doi:10.3390/nu8050272 · Cited by 109
Lipopolysaccharide-Induced Increase in Intestinal Permeability Is Mediated by TAK-1 Activation of IKK and MLCK/MYLK Gene
Nighot, M., Rawat, M., Al–Sadi, R., Castillo, E. F., Nighot, P. K., & Ma, T. Y. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2018.12.016 · Cited by 111
Self-citation
Replication of CMV in the gut of HIV-infected individuals and epithelial barrier dysfunction
Maidji, E., Somsouk, M., Rivera, J. M., Hunt, P. W., & Stoddart, C. A. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006202 · Cited by 102
Health-Promoting Properties of Proanthocyanidins for Intestinal Dysfunction
González-Quilen, C., Rodríguez‐Gallego, E., Beltrán‐Debón, R., Pinent, M., Ardèvol, A., Blay, M., & Terra, X. (2020) · Nutrients · doi:10.3390/nu12010130 · Cited by 103
Citrus nobiletin ameliorates experimental colitis by reducing inflammation and restoring impaired intestinal barrier function.
Xiong, Y., Chen, D.-P., Yu, C.-C., Lv, B.-C., Peng, J.-Y., Wang, J.-Y., & Lin, Y. (2015) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400614 · Cited by 85
Cryptosporidium parvum disrupts intestinal epithelial barrier function via altering expression of key tight junction and adherens junction proteins
Kumar, A., Chatterjee, I., Anbazhagan, A. N., Jayawardena, D., Priyamvada, S., Alrefai, W. A., Sun, J., Borthakur, A., & Dudeja, P. K. (2018) · Cellular Microbiology · doi:10.1111/cmi.12830 · Cited by 90
Alcohol, microbiome, and their effect on psychiatric disorders
Hillemacher, T., Bachmann, O. P., Kahl, K. G., & Frieling, H. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2018.04.015 · Cited by 90
The Implication of the Gut Microbiome in Heart Failure
Lupu, V. V., Răileanu, A. A., Mihai, C. M., Morariu, I. D., Lupu, A., Stârcea, I. M., Frăsinariu, O. E., Mocanu, A., Dragan, F., & Fotea, S. (2023) · Cells · doi:10.3390/cells12081158 · Cited by 89
Viral Interactions with PDZ Domain-Containing Proteins—An Oncogenic Trait?
James, C. D., & Roberts, S. (2016) · Pathogens · doi:10.3390/pathogens5010008 · Cited by 78
Arginine metabolism and its protective effects on intestinal health and functions in weaned piglets under oxidative stress induced by diquat
Zheng, P., Yu, B., He, J., Yu, J., Mao, X., Luo, Y., Luo, J., Huang, Z., Tian, G., Zeng, Q., et al. (2017) · British Journal Of Nutrition · doi:10.1017/s0007114517001519 · Cited by 80
Is inflammageing influenced by the microbiota in the aged gut? A systematic review
Shintouo, C. M., Mets, T. F., Beckwée, D., Bautmans, I., Ghogomu, S. M., Souopgui, J., Leemans, L., Meriki, H. D., & Njemini, R. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.111079 · Cited by 80
1,25-Dihydroxyvitamin D3 preserves intestinal epithelial barrier function from TNF-α induced injury via suppression of NF-kB p65 mediated MLCK-P-MLC signaling pathway
Chen, S., Zhu, J., Chen, G., Zuo, S., Zhang, J., Chen, Z., Wang, X., Li, J., Liu, Y., & Wang, P. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.03.125 · Cited by 77
Collagen peptides ameliorate intestinal epithelial barrier dysfunction in immunostimulatory Caco-2 cell monolayers via enhancing tight junctions
Chen, Q., Chen, O., Martins, I. M., Hou, H., Zhao, X., Blumberg, J. B., & Li, B. (2017) · Food & Function · doi:10.1039/c6fo01347c · Cited by 77
Myosin Light Chain Kinase: A Potential Target for Treatment of Inflammatory Diseases
Xiong, Y., Wang, C., Shi, L., Wang, L., Zhou, Z., Chen, D., Wang, J., & Guo, H. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00292 · Cited by 77
(−)-Epicatechin in the prevention of tumor necrosis alpha-induced loss of Caco-2 cell barrier integrity
Contreras, T. C., Ricciardi, E., Cremonini, E., & Oteiza, P. I. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.01.024 · Cited by 76
The Gastrointestinal Exertional Heat Stroke Paradigm: Pathophysiology, Assessment, Severity, Aetiology and Nutritional Countermeasures
Ogden, H. B., Child, R. B., Fallowfield, J. L., Delves, S. K., Westwood, C. S., & Layden, J. D. (2020) · Nutrients · doi:10.3390/nu12020537 · Cited by 78
Extracellular vesicles regulate immune responses and cellular function in intestinal inflammation and repair
Bui, T. M., Mascarenhas, L., & Sumagin, R. (2018) · Tissue Barriers · doi:10.1080/21688370.2018.1431038 · Cited by 75
Cell-to-Cell Communication by Host-Released Extracellular Vesicles in the Gut: Implications in Health and Disease
Díaz‐Garrido, N., Cordero, C., Olivo-Martínez, Y., Badı́a, J., & Baldomà, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042213 · Cited by 74
COVID-19 disrupts the blood–testis barrier through the induction of inflammatory cytokines and disruption of junctional proteins
Peirouvi, T., Aliaghaei, A., Farsani, B. E., Ziaeipour, S., Ebrahimi, V., Forozesh, M., Ghadipasha, M., Mahmoudiasl, G., Aryan, A., Moghimi, N., et al. (2021) · Inflammation Research · doi:10.1007/s00011-021-01497-4 · Cited by 73
Zinc and Selenium in Inflammatory Bowel Disease: Trace Elements with Key Roles?
Vaghari‐Tabari, M., Jafari-Gharabaghlou, D., Sadeghsoltani, F., Hassanpour, P., Qujeq, D., Rashtchizadeh, N., & Ghorbanihaghjo, A. (2020) · Biological Trace Element Research · doi:10.1007/s12011-020-02444-w · Cited by 71
Lactobacillus acidophilus inhibits the TNF-α-induced increase in intestinal epithelial tight junction permeability via a TLR-2 and PI3K-dependent inhibition of NF-κB activation
Haque, M., Kaminsky, L., Abdulqadir, R. F., Engers, J., Kovtunov, E., Rawat, M., Al-Sadi, R., & Ma, T. Y. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1348010 · Cited by 71
Self-citation
Mesalamine and azathioprine modulate junctional complexes and restore epithelial barrier function in intestinal inflammation
Khare, V., Krnjic, A., Frick, A., Gmainer, C., Asboth, M., Jimenez, K., Lang, M., Baumgartner, M., Evstatiev, R., & Gasche, C. (2019) · Scientific Reports · doi:10.1038/s41598-019-39401-0 · Cited by 70
Epithelial Barrier Function in Gut-Bone Signaling
Rios‐Arce, N. D., Collins, F. L., Schepper, J. D., Steury, M. D., Raehtz, S., Mallin, H., Schoenherr, D. T., Parameswaran, N., & McCabe, L. R. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-66653-2_8 · Cited by 72
Live probiotic bacteria administered in a pathomimetic Leaky Gut Chip ameliorate impaired epithelial barrier and mucosal inflammation
Min, S., Than, N., Shin, Y. C., Hu, G., Shin, W., Ambrosini, Y. M., & Kim, H. J. (2022) · Scientific Reports · doi:10.1038/s41598-022-27300-w · Cited by 64
The role of epithelial tight junctions involved in pathogen infections
Lu, R., Yang, W., & Hu, Y.-J. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3543-5 · Cited by 65
Curcumin protects against the intestinal ischemia-reperfusion injury: involvement of the tight junction protein ZO-1 and TNF-α related mechanism
Tian, S., Guo, R., Wei, S., Kong, Y., Wei, X., Wang, W., Shi, X., & Jiang, H. (2016) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2016.20.2.147 · Cited by 65
MMP-9-induced increase in intestinal epithelial tight permeability is mediated by p38 kinase signaling pathway activation of MLCK gene
Al–Sadi, R., Youssef, M., Rawat, M., Guo, S., Dokładny, K., Haque, M., Watterson, D. M., & Ma, T. Y. (2018) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00126.2018 · Cited by 66
Self-citation
Escherichia coli Nissle 1917 Protects Intestinal Barrier Function by Inhibiting NF-κ B-Mediated Activation of the MLCK-P-MLC Signaling Pathway
Guo, S., Chen, S., Ma, J., Ma, Y., Zhu, J., Ma, Y., Liu, Y., Wang, P., & Pan, Y. (2019) · Mediators of Inflammation · doi:10.1155/2019/5796491 · Cited by 64
Self-citation
(–)-Epicatechin in the control of glucose homeostasis: Involvement of redox-regulated mechanisms
Cremonini, E., Fraga, C. G., & Oteiza, P. I. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.11.010 · Cited by 65
Human immunodeficiency virus-associated disruption of mucosal barriers and its role in HIV transmission and pathogenesis of HIV/AIDS disease
Tugizov, S. M. (2016) · Tissue Barriers · doi:10.1080/21688370.2016.1159276 · Cited by 62
Rheumatoid arthritis is associated with increased gut permeability and bacterial translocation that are reversed by inflammation control
Audo, R., Sanchez, P., Rivière, B., Mielle, J., Tan, J., Lukas, C., Macia, L., Morel, J., & Daïen, C. (2022) · Lara D. Veeken · doi:10.1093/rheumatology/keac454 · Cited by 59
Exploiting the Zonulin Mouse Model to Establish the Role of Primary Impaired Gut Barrier Function on Microbiota Composition and Immune Profiles
Miranda-Ribera, A., Ennamorati, M., Serena, G., Çetinbaş, M., Lan, J., Sadreyev, R. I., Jain, N., Fasano, A., & Fiorentino, M. R. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02233 · Cited by 56
(-)-Epicatechin and NADPH oxidase inhibitors prevent bile acid-induced Caco-2 monolayer permeabilization through ERK1/2 modulation
Wang, Z., Litterio, M. C., Müller, M. M., Vauzour, D., & Oteiza, P. I. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101360 · Cited by 57
Catechin and Procyanidin B2 Modulate the Expression of Tight Junction Proteins but Do Not Protect from Inflammation-Induced Changes in Permeability in Human Intestinal Cell Monolayers
Bianchi, M. G., Chiu, M., Taurino, G., Brighenti, F., Rio, D. D., Mena, P. R., & Bussolati, O. (2019) · Nutrients · doi:10.3390/nu11102271 · Cited by 54
The role of polymorphonuclear neutrophils during HIV-1 infection
Yaseen, M. M., Abuharfeil, N. M., Yaseen, M. M., & Shabsoug, B. M. (2017) · Archives of Virology · doi:10.1007/s00705-017-3569-9 · Cited by 55
Accessory Toxins of Vibrio Pathogens and Their Role in Epithelial Disruption During Infection
Pérez-Reytor, D., Jaña, V., Pavéz, L., Navarrete, P., & GARCÍA, K. P. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02248 · Cited by 52
Ellagic acid protects Caco-2 cell monolayers against inflammation-induced permeabilization
Iglesias, D. E., Cremonini, E., Fraga, C. G., & Oteiza, P. I. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.01.022 · Cited by 52
New Insights into the Mechanisms of Chinese Herbal Products on Diabetes: A Focus on the “Bacteria-Mucosal Immunity-Inflammation-Diabetes” Axis
Gao, Z., Li, Q., Wu, X., Zhao, X., Zhao, L., & Tong, X. (2017) · Journal of Immunology Research · doi:10.1155/2017/1813086 · Cited by 50
Modulations of genes related to gut integrity, apoptosis, and immunity underlie the beneficial effects of Bacillus amyloliquefaciens CECT 5940 in broilers fed diets with different protein levels in a necrotic enteritis challenge model
Gharib-Naseri, K., Dorigam, J. C. D. P., Doranalli, K., Kheravii, S. K., Swick, R. A., Choct, M., & Wu, S. (2020) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-020-00508-4 · Cited by 48
Claudin-3 is required for modulation of paracellular permeability by TNF-α through ERK1/2/slug signaling axis in submandibular gland
Mei, M., Xiang, R., Cong, X., Zhang, Y., Li, J., Yi, X., Park, K., Han, J., Wu, L., & Yu, G. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.07.002 · Cited by 46
Biomaterial–tight junction interaction and potential impacts
Han, X., Zhang, E., Shi, Y., Song, B., Du, H., & Cao, Z. (2019) · Journal of Materials Chemistry B · doi:10.1039/c9tb01081e · Cited by 46
M2-like tumor-associated macrophage-secreted CCL2 facilitates gallbladder cancer stemness and metastasis
Chen, W., Chen, M., Hong, L., Abudukeremu, X., Huang, M., Tang, N., Yang, X., She, F., & Chen, Y. (2024) · Experimental Hematology and Oncology · doi:10.1186/s40164-024-00550-2 · Cited by 49
Perspective: Prospects for Nutraceutical Support of Intestinal Barrier Function
McCarty, M. F., & Lerner, A. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa139 · Cited by 44
The Possible Role of Probiotic Supplementation in Inflammation: A Narrative Review
Colletti, A., Pellizzato, M., & Cicero, A. F. G. (2023) · Microorganisms · doi:10.3390/microorganisms11092160 · Cited by 46
Salvianolic Acid B Restored Impaired Barrier Function via Downregulation of MLCK by microRNA-1 in Rat Colitis Model
Xiong, Y., Wang, J.-Y., Chu, H., Chen, D.-P., & Guo, H.-S. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00134 · Cited by 43
Tight Junctions and the Intestinal Barrier
Ma, T. Y., Nighot, P. K., & Al–Sadi, R. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00025-6 · Cited by 42
Self-citation
Ginger and 6-shogaol protect intestinal tight junction and enteric dopaminergic neurons against 1-methyl-4-phenyl 1,2,3,6-tetrahydropyridine in mice
Huh, E., Choi, J. G., Noh, D., Yoo, H., Ryu, J., Kim, N., Kim, H., & Oh, M. S. (2018) · Nutritional Neuroscience · doi:10.1080/1028415x.2018.1520477 · Cited by 42
Anthocyanin actions at the gastrointestinal tract: Relevance to their health benefits
Oteiza, P. I., Cremonini, E., & Fraga, C. G. (2022) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2022.101156 · Cited by 42
(−)-Epicatechin and the comorbidities of obesity
Cremonini, E., Iglesias, D. E., Kang, J., Lombardo, G. E., Mostofinejad, Z., Wang, Z., Zhu, W., & Oteiza, P. I. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108505 · Cited by 42
Arsenite-induced downregulation of occludin in mouse lungs and BEAS-2B cells via the ROS/ERK/ELK1/MLCK and ROS/p38 MAPK signaling pathways
Liu, Y., Tang, J., Yuan, J., Yao, C., Hosoi, K., Han, Y. K., Yu, S., Wei, H., & Chen, G. (2020) · Toxicology Letters · doi:10.1016/j.toxlet.2020.07.010 · Cited by 40
Regulation of TWIK-related potassium channel-1 (Trek1) restitutes intestinal epithelial barrier function
Huang, H., Liu, J., Yu, Y., Mo, L., Ge, R.-T., Zhang, H., Liu, Z., Zheng, P., & Yang, P. (2015) · Cellular and Molecular Immunology · doi:10.1038/cmi.2014.137 · Cited by 40
Anti-inflammatory mechanisms of neovestitol from Brazilian red propolis in LPS-activated macrophages
Bueno‐Silva, B., Rosalen, P. L., de Alencar, S. M., & Mayer, M. P. A. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.07.029 · Cited by 40
Protective Effect of Pure Sour Cherry Anthocyanin Extract on Cytokine-Induced Inflammatory Caco-2 Monolayers
Nguyen, T. L. P., Fenyvesi, F., Remenyik, J., Homoki, J. R., Gogolák, P., Bácskay, I., Fehér, P. S., Ujhelyi, Z., Vasvári, G., Vecsernyés, M., et al. (2018) · Nutrients · doi:10.3390/nu10070861 · Cited by 40
Lysophosphatidic Acid Receptor 1 Is Important for Intestinal Epithelial Barrier Function and Susceptibility to Colitis
Lin, S., Han, Y., Jenkin, K. A., Lee, S., Sasaki, M., Klapproth, J. A., He, P., & Yun, C. C. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.10.006 · Cited by 38
'Dietary Arginine Supplementation Affects Intestinal Function by Enhancing Antioxidant Capacity of a Nitric Oxide–Independent Pathway in Low-Birth-Weight Piglets
Zheng, P., Song, Y., Tian, Y., Zhang, H., Yu, B., He, J., Mao, X., Yu, J., Luo, Y., Luo, J., et al. (2018) · Journal of Nutrition · doi:10.1093/jn/nxy198 · Cited by 38
Anti-inflammatory and Intestinal Barrier–protective Activities of Commensal Lactobacilli and Bifidobacteria in Thoroughbreds: Role of Probiotics in Diarrhea Prevention in Neonatal Thoroughbreds
Tanabe, S., Suzuki, T., WASANO, Y., Nakajima, F., KAWASAKI, H., TSUDA, T., Nagamine, N., TSURUMACHI, T., SUGAYA, K., AKITA, H., et al. (2014) · Journal of Equine Science · doi:10.1294/jes.25.37 · Cited by 35
Somatostatin regulates NHE8 protein expression via the ERK1/2 MAPK pathway in DSS-induced colitis mice
Li, X., Cai, L., Xu, H. J., Geng, C., Lu, J., Tao, L., Sun, D., Ghishan, F. K., & Wang, C. (2016) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00239.2016 · Cited by 36
Interactions between Food Hazards and Intestinal Barrier: Impact on Foodborne Diseases
Li, X., Tan, C. P., Liu, Y., & Xu, Y. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c07378 · Cited by 37
Systems biology in inflammatory bowel diseases
Polytarchou, C., Κούκος, Γ., & Iliopoulos, D. (2014) · Current Opinion in Gastroenterology · doi:10.1097/mog.0000000000000081 · Cited by 35
The Role of TNF-α in Neuropathic Pain: An Immunotherapeutic Perspective
García‐Domínguez, M. (2025) · Life · doi:10.3390/life15050785 · Cited by 40
Alpha-Melanocyte Stimulating Hormone Protects against Cytokine-Induced Barrier Damage in Caco-2 Intestinal Epithelial Monolayers
Váradi, J., Harazin, A., Fenyvesi, F., Réti-Nagy, K. S., Gogolák, P., Vámosi, G., Bácskay, I., Fehér, P. S., Ujhelyi, Z., Vasvári, G., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170537 · Cited by 34
Damage to intestinal barrier integrity in piglets caused by porcine reproductive and respiratory syndrome virus infection
Zhao, J., Wan, S., Sun, N., Sun, P., Sun, Y., Khan, A., Guo, J., Zheng, X., Fan, K., Yin, W., et al. (2021) · Veterinary Research · doi:10.1186/s13567-021-00965-3 · Cited by 38
They Must Hold Tight: Junction Proteins, Microbiota And Immunity In Intestinal Mucosa
Castoldi, Â., de Aguiar, C. F., Moraes‐Vieira, P. M., & Câmara, N. O. S. (2015) · Current Protein and Peptide Science · doi:10.2174/1389203716666150630133141 · Cited by 33
Batf2 differentially regulates tissue immunopathology in Type 1 and Type 2 diseases
Guler, R., Mpotje, T., Ozturk, M., Nono, J. K., Parihar, S. P., Chia, J. E., Aziz, N. A., Hlaka, L., Kumar, S., Roy, S., et al. (2018) · Mucosal Immunology · doi:10.1038/s41385-018-0108-2 · Cited by 33
Very early-life exposure to microbiota-induced TNF drives the maturation of neonatal pre-cDC1
Köhler, A., Delbauve, S., Smout, J., Torres, D., & Flamand, V. (2020) · Gut · doi:10.1136/gutjnl-2019-319700 · Cited by 33
Intestinal congestion and reperfusion injury: damage caused to the intestinal tract and distal organs
Chen, Y., Pu, W., Maswikiti, E. P., Tao, P., Li, X., Wang, D., Gu, B., Yu, Y., Gao, L., Zhao, C., et al. (2021) · Bioscience Reports · doi:10.1042/bsr20211560 · Cited by 34
Ginsenoside Rc attenuates DSS-induced ulcerative colitis, intestinal inflammatory, and barrier function by activating the farnesoid X receptor
Tang, K., Kong, D., Peng, Y., Guo, J., Zhong, Y., Yu, H., Mai, Z., Chen, Y., Chen, Y., Cui, T., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1000444 · Cited by 33
Changes of cytokine levels in a mouse model of post-infectious irritable bowel syndrome
Yang, B. K., Zhou, X., & Cheng, L. (2015) · BMC Gastroenterology · doi:10.1186/s12876-015-0272-8 · Cited by 33
Momordica charantia (bitter melon) modulates adipose tissue inflammasome gene expression and adipose-gut inflammatory cross talk in high-fat diet (HFD)-fed mice
Nerurkar, P. V., Orias, D., Soares, N., Kumar, M., & Nerurkar, V. R. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.03.003 · Cited by 32
Intestinal microbiota changes induced by TNF-inhibitors in IBD-related spondyloarthritis
Ditto, M. C., Parisi, S., Landolfi, G., Borrelli, R., Realmuto, C., Finucci, A., Caviglia, G. P., Ribaldone, D. G., Astegiano, M., Zanetti, A., et al. (2021) · RMD Open · doi:10.1136/rmdopen-2021-001755 · Cited by 31
Protective effect of probiotic bacteria and estrogen in preventing HIV-1-mediated impairment of epithelial barrier integrity in female genital tract
Dizzell, S., Nazli, A., Reid, G., & Kaushic, C. (2019) · Cells · doi:10.3390/cells8101120 · Cited by 30
S-1-propenylcysteine improves TNF-α-induced vascular endothelial barrier dysfunction by suppressing the GEF-H1/RhoA/Rac pathway
Kunimura, K., Miki, S., Takashima, M., & Suzuki, J. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-020-00692-w · Cited by 30
Epoxy Triglyceride Enhances Intestinal Permeability via Caspase-1/NLRP3/GSDMD and cGAS-STING Pathways in Dextran Sulfate Sodium-Induced Colitis Mice
Li, X., Liu, Y., Wang, Y., Liu, Y., & Xu, Y. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c08134 · Cited by 30
Identification and Structure–Activity Relationship of Intestinal Epithelial Barrier Function Protective Collagen Peptides from Alaska Pollock Skin
Song, W., Chen, Q., Wang, Y., Han, Y., Zhang, H., Li, B., & Yu, G. (2019) · Marine Drugs · doi:10.3390/md17080450 · Cited by 31
All-Trans Retinoic Acid Inhibits Human Colorectal Cancer Cells RKO Migration via Downregulating Myosin Light Chain Kinase Expression through MAPK Signaling Pathway
Zuo, L., Yang, X., Lu, M., Hu, R., Zhu, H., Zhang, S., Zhou, Q., Chen, F., Gui, S., & Wang, Y. (2016) · Nutrition and Cancer · doi:10.1080/01635581.2016.1216138 · Cited by 29
Total Flavonoid Extract from Hawthorn (Crataegus pinnatifida) Improves Inflammatory Cytokines-Evoked Epithelial Barrier Deficit
Liu, F., Zhang, X., & Ji, Y. (2020) · Medical Science Monitor · doi:10.12659/msm.920170 · Cited by 29
Transforming Growth Factor β1/SMAD Signaling Pathway Activation Protects the Intestinal Epithelium from Clostridium difficile Toxin A-Induced Damage
Veras, C. M. T., Santos, A. A. Q. A., Stipursky, J., Meloni, M., Araújo, A. P. B., Foschetti, D. A., López‐Ureña, D., Quesada-Gómez, C., Leitão, R. F. D. C., Gomes, F. C. A., et al. (2017) · Infection and Immunity · doi:10.1128/iai.00430-17 · Cited by 29
Repurposing metformin as adjuvant therapy in patients with ulcerative colitis treated with mesalamine: A randomized controlled double-blinded study
El-Haggar, S. M., Hegazy, S. K., Maher, M., Bahgat, M. M., & Bahaa, M. M. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112541 · Cited by 28
Modulation of Inflammatory Pathways and Adipogenesis by the Action of Gentisic Acid in RAW 264.7 and 3T3-L1 Cell Lines
Kang, M., Choi, W., Yoo, S. H., Nam, S., Shin, P.-G., Kim, K. K., & Kim, G. (2021) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2105.05004 · Cited by 27

Authors: Al-Sadi, R., Guo, S., Ye, D., & Ma, T. Y.
Affiliations: University of New Mexico (US)
Corresponding author: Ma, Thomas Y.
ORCID: Ye, Dongmei
Ma, Thomas Y.
Venue: The American Journal of Pathology
Publisher: Elsevier BV
Published: 2013-12
Volume: 183
Issue: 6
Pages: 1871-1884
ISSN: 0002-9440 (ISSN-L)
DOI: 10.1016/j.ajpath.2013.09.001
PMC: PMC5745548
OpenAlex: W1964163204
Cited by: 262
References: 48
Citations by year: 2026: 18 · 2025: 21 · 2024: 23 · 2023: 22 · 2022: 29 · 2021: 36 · 2020: 24 · 2019: 20 · 2018: 22 · 2017: 17 · 2016: 14 · 2015: 10 · 2014: 5 · 2013: 1
FWCI: 5.60
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
Locations: American Journal Of Pathology (publishedVersion, cc-by-nc-nd)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs
National Institutes of Health (R01-DK081429, R01-DK064165)
Topics: Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Health Sciences › Medicine › Gastroenterology › Inflammatory Bowel Disease
Health Sciences › Medicine › Gastroenterology › Gastrointestinal motility and disorders
Keywords: TNF-α, tight junction barrier function, intestinal permeability, ERK signaling, Elk-1, p38 MAPK, myosin light chain kinase, Caco-2 cell monolayers, inflammatory bowel disease, MAPK signaling
MeSH terms: Animals, Cell Nucleus, Enzyme Activation, Humans, Intestinal Mucosa, Myosin-Light-Chain Kinase, Permeability, Promoter Regions, Genetic, Transcription, Genetic, Tumor Necrosis Factor-alpha, Caco-2 Cells, Tight Junctions, Mitogen-Activated Protein Kinase 1, MAP Kinase Signaling System, Active Transport, Cell Nucleus, Mitogen-Activated Protein Kinase 3, ets-Domain Protein Elk-1, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

TNF-α Modulation of Intestinal Epithelial Tight Junction Barrier Is Regulated by ERK1/2 Activation of Elk-1

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks