Physiology and function of the tight junction
Open accessAbstract
Understanding of tight junctions has evolved from their historical perception as inert solute barriers to recognition of their physiological and biochemical complexity. Many proteins are specifically localized to tight junctions, including cytoplasmic actin-binding proteins and adhesive transmembrane proteins. Among the latter are claudins, which are critical barrier proteins. Current information suggests that the paracellular barrier is most usefully modeled as having two physiologic components: a system of charge-selective small pores, 4 A in radius, and a second pathway created by larger discontinuities in the barrier, lacking charge or size discrimination. The first pathway is influenced by claudin expression patterns and the second is likely controlled by different proteins and signals. Recent information on claudin function and disease-causing mutations have led to a more complete understanding of their role in barrier formation, but progress is impeded by lack of high resolution structural information.
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Tight junctions are the main functional components in sustaining the permeability barrier and controlling tissue homeostasis in the blood-brain barrier.
“In the BBB, tight junctions are the main functional components in sustaining the permeability barrier and controlling tissue homeostasis.88–91”
From The blood–brain barrier: Structure, regulation and drug delivery (2023) · cites this paper as [89]
The Abstract (page unavailable) describes tight junctions as barriers that separate tissue spaces and regulate solute movement. The Size section (page unavailable) reports that deleting claudin-5 increases tight-junction permeability in blood vessels. These passages support a permeability-barrier role, but do not establish that tight junctions are the main functional components of the blood-brain barrier or that they control its tissue homeostasis. (LLM, conf=0.84)
Experimental — accuracy not yet measuredSolutes and water cross tight junctions through 2 distinct pathways based on their size and charge selectivity: the pore pathway and the leak pathway.
“It was reported that solutes and water cross TJs through 2 distinct pathways based on their size and charge selectivity: the pore pathway48, 49, 50 and the leak pathway.48,51”
From Regulation of Intestinal Barrier Function by Microbial Metabolites (2021) · cites this paper as [50]
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Ionic channels of excitable membranes
(1985) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(85)90172-7 · Cited by 7,133 · see citing works
Ion Channels/Excitable Membranes
(2011) · Springer eBooks · doi:10.1007/springerreference_33998 · Cited by 4,066 · see citing works
JUNCTIONAL COMPLEXES IN VARIOUS EPITHELIA
Farquhar, M. G., & Palade, G. E. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.375 · Cited by 3,637 · see citing works
Occludin: a novel integral membrane protein localizing at tight junctions.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580 · see citing works
USSING, H. H., & ZERAHN, K. (1951) · Acta Physiologica Scandinavica · doi:10.1111/j.1748-1716.1951.tb00800.x · Cited by 2,406 · see citing works
Furuse, M., Fujita, K., Hiiragi, T., Fujimoto, K., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.7.1539 · Cited by 2,100 · see citing works
Size-selective loosening of the blood-brain barrier in claudin-5–deficient mice
Nitta, T., Hata, M., Gotoh, S., Seo, Y., Sasaki, H., Hashimoto, N., Furuse, M., & Tsukita, S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302070 · Cited by 1,917 · see citing works
Adherens and tight junctions: Structure, function and connections to the actin cytoskeleton
Hartsock, A., & Nelson, W. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.07.012 · Cited by 1,559 · see citing works
The tight junction: a multifunctional complex
Schneeberger, E. E., & Lynch, R. D. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00558.2003 · Cited by 1,401 · see citing works
Complex Phenotype of Mice Lacking Occludin, a Component of Tight Junction Strands
Saitou, M., Furuse, M., Sasaki, H., Schulzke, J.-D., Fromm, M., Takano, H., Noda, T., & Tsukita, S. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4131 · Cited by 1,195 · see citing works
The Nature of the Frog Skin Potential
KOEFOED‐JOHNSEN, V., & Ussing, H. H. (1958) · Acta Physiologica Scandinavica · doi:10.1111/j.1748-1716.1958.tb01563.x · Cited by 1,169 · see citing works
González‐Mariscal, L., Betanzos, A., Nava, P., & Jaramillo-Loranca, B. E. (2002) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(02)00037-8 · Cited by 1,164 · see citing works
Itoh, M., Furuse, M., Morita, K., Kubota, K., Saitou, M., & Tsukita, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.6.1351 · Cited by 1,151 · see citing works
Paracellin-1, a Renal Tight Junction Protein Required for Paracellular Mg 2+ Resorption
Simon, D. B., Lu, Y., Choate, K. A., Velázquez, H., Al-Sabban, E. A., Praga, M., Casari, G., Bettinelli, A., Colussi, G., Rodríguez‐Soriano, J., et al. (1999) · Science · doi:10.1126/science.285.5424.103 · Cited by 1,136 · see citing works
CLAUDINS AND EPITHELIAL PARACELLULAR TRANSPORT
Itallie, C. M. V., & Anderson, J. M. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.68.040104.131404 · Cited by 1,123 · see citing works
Self-citationStructure and function of claudins
Krause, G., Winkler, L., Mueller, S., Haseloff, R. F., Piontek, J., & Blasig, I. E. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.10.018 · Cited by 824 · see citing works
Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
Amasheh, S., Meiri, N., Gitter, A. H., Schöneberg, T., Mankertz, J., Schulzke, J. D., & Fromm, M. (2002) · Journal of Cell Science · doi:10.1242/jcs.00165 · Cited by 812 · see citing works
Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
Ikenouchi, J., Furuse, M., Furuse, K., Sasaki, H., Tsukita, S., & Tsukita, S. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200510043 · Cited by 787 · see citing works
Crosstalk of tight junction components with signaling pathways
González-Mariscal, L., Tapia, R., & Chamorro, D. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.08.018 · Cited by 759 · see citing works
Manner of Interaction of Heterogeneous Claudin Species within and between Tight Junction Strands
Furuse, M., Sasaki, H., & Tsukita, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.4.891 · Cited by 746 · see citing works
Medical physiology : a cellular and molecular approach
Boron, W. F., & Boulpaep, E. L. (2012) · Cited by 733 · see citing works
High-Throughput Mapping of a Dynamic Signaling Network in Mammalian Cells
Barrios‐Rodiles, M., Brown, K. R., Ozdamar, B., Bose, R., Liu, Z., Donovan, R. S., Shinjo, F., Liu, Y., Dembowy, J., Taylor, I. W., et al. (2005) · Science · doi:10.1126/science.1105776 · Cited by 726 · see citing works
Furuse, M., Furuse, K., Sasaki, H., & Tsukita, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.2.263 · Cited by 719 · see citing works
Powell, D. W. (1981) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1981.241.4.g275 · Cited by 624 · see citing works
Schmitz*, H., Barmeyer, C., Fromm, M., Runkel§, N., Foss, H., Bentzel, C. J., Riecken, E., & Schulzke, J.-D. (1999) · Gastroenterology · doi:10.1016/s0016-5085(99)70126-5 · Cited by 607 · see citing works
Itallie, C. M. V., Rahner, C., & Anderson, J. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12464 · Cited by 601 · see citing works
Self-citationClaude, P. (1978) · The Journal of Membrane Biology · doi:10.1007/bf01870332 · Cited by 569 · see citing works
Claudins create charge-selective channels in the paracellular pathway between epithelial cells
Colegio, O. R., Itallie, C. M. V., McCrea, H. J., Rahner, C., & Anderson, J. M. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00038.2002 · Cited by 545 · see citing works
Self-citationMolecular Basis of Epithelial Barrier Regulation
Turner, J. R. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060681 · Cited by 542 · see citing works
Konrad, M., Schaller, A., Seelow, D., Pandey, A. V., Waldegger, S., Lesslauer, A., Vitzthum, H., Suzuki, Y., Luk, J. M., Becker, C., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/508617 · Cited by 525 · see citing works
Human junction adhesion molecule regulates tight junction resealing in epithelia
Liu, Y., Nusrat, A., Schnell, F. J., Reaves, T. A., Walsh, S. V., Pochet, M., & Parkos, C. A. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.13.2363 · Cited by 525 · see citing works
JAM-A regulates permeability and inflammation in the intestine in vivo
Laukoetter, M. G., Nava, P., Lee, W. Y., Severson, E. A., Capaldo, C., Babbin, B. A., Williams, I. R., Koval, M. H., Peatman, E., Campbell, J. A., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20071416 · Cited by 512 · see citing works
IV. Regulation of tight junctions by extracellular stimuli: nutrients, cytokines, and immune cells
Nusrat, A., Turner, J. R., & Madara, J. (2000) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.2000.279.5.g851 · Cited by 499 · see citing works
Ma, T. Y., Boivin, M. A., Ye, D., Pedram, A., & Said, H. M. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00412.2004 · Cited by 452 · see citing works
Hadj-Rabia, S., Baala, L., Vabres, P., Hamel‐Teillac, D., Jacquemin, E., Fabrè, M., Lyonnet, S., Prost, Y. D., Münnich, A., Hadchouel, M., et al. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.07.022 · Cited by 426 · see citing works
Molecular Basis of the Core Structure of Tight JunctionsPreprint
Furuse, M. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002907 · Cited by 410 · see citing works
Itallie, C. M. V., Holmes, J. C., Bridges, A. S., Gookin, J. L., Coccaro, M. R., Proctor, W. R., Colegio, O. R., & Anderson, J. M. (2008) · Journal of Cell Science · doi:10.1242/jcs.021485 · Cited by 410 · see citing works
Self-citationFormation of tight junction: determinants of homophilic interaction between classic claudins
Piorntek, J., Winkler, L., Wolburg, H., Müller, S. L., Zuleger, N., Piehl, C., Wiesner, B., Krause, G., & Blasig, I. E. (2007) · The FASEB Journal · doi:10.1096/fj.07-8319com · Cited by 399 · see citing works
Colegio, O. R., Itallie, C. V., Rahner, C., & Anderson, J. M. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00547.2002 · Cited by 387 · see citing works
Self-citationItallie, C. M. V., Fanning, A. S., & Anderson, J. M. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00116.2003 · Cited by 372 · see citing works
Self-citationTight junction-based epithelial microenvironment and cell proliferation
Tsukita, S., Yamazaki, Y., Katsuno, T., Tamura, A., & Tsukita, S. (2008) · Oncogene · doi:10.1038/onc.2008.344 · Cited by 370 · see citing works
Hamazaki, Y., Itoh, M., Sasaki, H., Furuse, M., & Tsukita, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109005200 · Cited by 366 · see citing works
Nusrat, A., von Eichel-Streiber, C., Turner, J. R., Verkade, P., Madara, J., & Parkos, C. A. (2001) · Infection and Immunity · doi:10.1128/iai.69.3.1329-1336.2001 · Cited by 352 · see citing works
NATURE OF SHUNT PATH AND ACTIVE SODIUM TRANSPORT PATH THROUGH FROG SKIN EPITHELIUM.
Hh, U., & Windhager, E. E. (1964) · PubMed · Cited by 349 · see citing works
Angelow, S., Ahlstrom, R., & Yu, A. S. L. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90264.2008 · Cited by 344 · see citing works
Ben‐Yosef, T. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg210 · Cited by 339 · see citing works
Claudin-16 and claudin-19 interact and form a cation-selective tight junction complex
Hou, J., Renigunta, A., Konrad, M., Gomes, A. S., Schneeberger, E. E., Paul, D. L., Waldegger, S., & Goodenough, D. A. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33970 · Cited by 338 · see citing works
Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT
Carlton, V. E. H., Harris, B. Z., Puffenberger, E. G., Batta, A. K., Knisely, A. S., Robinson, D. L., Strauss, K. A., Shneider, B. L., Lim, W. A., Salen, G., et al. (2003) · Nature Genetics · doi:10.1038/ng1147 · Cited by 327 · see citing works
The JAM family of junctional adhesion molecules
Bazzoni, G. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00104-2 · Cited by 327 · see citing works
Epithelial transport and barrier function in occludin-deficient mice
Schulzke, J., Gitter, A. H., Mankertz, J., Spiegel, S., Seidler, U. E., Amasheh, S., Saitou, M., Tsukita, S., & Fromm, M. (2005) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2005.01.008 · Cited by 320 · see citing works
Artursson, P., Ungell, A.-L. B., & Löfroth, J. (1993) · Pharmaceutical Research · doi:10.1023/a:1018903931777 · Cited by 310 · see citing works
Yu, A. S. L., Cheng, M. H., Angelow, S., Günzel, D., Kanzawa, S. A., Schneeberger, E. E., Fromm, M., & Coalson, R. D. (2008) · The Journal of General Physiology · doi:10.1085/jgp.200810154 · Cited by 310 · see citing works
Knockdown of occludin expression leads to diverse phenotypic alterations in epithelial cells
Yu, A. S. L., McCarthy, K. M., Francis, S. A., McCormack, J. M., Lai, J., Rogers, R. A., Lynch, R. D., & Schneeberger, E. E. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00581.2004 · Cited by 307 · see citing works
Holmes, J. L., Itallie, C. V. V., Rasmussen, J. E., & Anderson, J. (2006) · Gene Expression Patterns · doi:10.1016/j.modgep.2005.12.001 · Cited by 297 · see citing works
Self-citationClaudin-1 contributes to the epithelial barrier function in MDCK cells
Inai, T., Kobayashi, J., & Shibata, Y. (1999) · European Journal of Cell Biology · doi:10.1016/s0171-9335(99)80086-7 · Cited by 285 · see citing works
Tricellulin is a tight-junction protein necessary for hearing
Riazuddin, S., Ahmed, Z. M., Fanning, A. S., Lagziel, A., Kitajiri, S.-I., Ramzan, K., Khan, S. N., Chattaraj, P., Friedman, P. L., Anderson, J. M., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/510022 · Cited by 283 · see citing works
Self-citationItallie, C. M. V., Rogan, S., Yu, A. S. L., et al. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00138.2006 · Cited by 279 · see citing works
Yu, A. S. L., Enck, A. H., Lencer, W. I., & Schneeberger, E. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213286200 · Cited by 273 · see citing works
Genetic control of single lumen formation in the zebrafish gut
Bagnat, M., Cheung, I. D., Mostov, K. E., & Stainier, D. Y. R. (2007) · Nature Cell Biology · doi:10.1038/ncb1621 · Cited by 262 · see citing works
ROLE OF TIGHT JUNCTIONS IN ESTABLISHING AND MAINTAINING CELL POLARITY
Cereijido, M., Valdés, J., Shoshani, L., & Contreras, R. G. (1998) · Annual Review of Physiology · doi:10.1146/annurev.physiol.60.1.161 · Cited by 257 · see citing works
Vetrano, S., Rescigno, M., Cera, M. R., Correale, C., Rumio, C., Doni, A., Fantini, M. C., Sturm, A., Borroni, E. M., Repici, A., et al. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.04.002 · Cited by 254 · see citing works
Twenty-first Bowditch lecture. The epithelial junction: bridge, gate, and fence.
Jm, D. (1977) · PubMed · Cited by 252 · see citing works
Watson, C. J. E., Rowland, M., & Warhurst, G. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.2.c388 · Cited by 251 · see citing works
CAR: A virus receptor within the tight junction
Coyne, C. B., & Bergelson, J. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.01.007 · Cited by 234 · see citing works
Dynamic Interaction of Stargazin-like TARPs with Cycling AMPA Receptors at Synapses
Tomita, S., Fukata, M., Nicoll, R. A., & Bredt, D. S. (2004) · Science · doi:10.1126/science.1090262 · Cited by 234 · see citing works
Ivanov, A. I., Hunt, D. A., Utech, M., Nusrat, A., & Parkos, C. A. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0043 · Cited by 232 · see citing works
Paracellin-1 and the modulation of ion selectivity of tight junctions
Hou, J., Paul, D. L., & Goodenough, D. A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02631 · Cited by 232 · see citing works
Study of Claudin Function by RNA Interference
Hou, J., Gomes, A. S., Paul, D. L., & Goodenough, D. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608853200 · Cited by 231 · see citing works
Matsuda, M., Kubo, A., Furuse, M., & Tsukita, S. (2004) · Journal of Cell Science · doi:10.1242/jcs.00972 · Cited by 225 · see citing works
Behr, M., Riedel, D., & Schuh, R. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00275-2 · Cited by 224 · see citing works
Bruewer, M., Hopkins, A. M., Hobert, M. E., Nusrat, A., & Madara, J. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00087.2004 · Cited by 223 · see citing works
Megaintestine in Claudin-15–Deficient Mice
Tamura, A., Kitano, Y., Hata, M., Katsuno, T., Moriwaki, K., Sasaki, H., Hayashi, H., Suzuki, Y., Noda, T., Furuse, M., et al. (2007) · Gastroenterology · doi:10.1053/j.gastro.2007.11.040 · Cited by 219 · see citing works
Knipp, G. T., Ho, N. F. H., Barsuhn, C. L., & Borchardt, R. T. (1997) · Journal of Pharmaceutical Sciences · doi:10.1021/js9700309 · Cited by 208 · see citing works
Wen, H., Watry, D. D., Marcondes, M. C. G., & Fox, H. S. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8408-8417.2004 · Cited by 208 · see citing works
Alexandre, M. D., Lu, Q., & Chen, Y. (2005) · Journal of Cell Science · doi:10.1242/jcs.02406 · Cited by 203 · see citing works
Wu, V., Schulte, J., Hirschi, A., Tepaß, U., & Beitel, G. J. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200309134 · Cited by 201 · see citing works
Kubota, K., Furuse, M., Sasaki, H., Sonoda, N., Fujita, K., Nagafuchi, A., & Tsukita, S. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80452-7 · Cited by 201 · see citing works
Kausalya, P. J. (2006) · Journal of Clinical Investigation · doi:10.1172/jci26323 · Cited by 201 · see citing works
McCarthy, K. M., Francis, S. A., McCormack, J. M., Lai, J., Rogers, R. A., Skare, I. B., Lynch, R. D., & Schneeberger, E. E. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.19.3387 · Cited by 199 · see citing works
Contribution of claudin-5 to barrier properties in tight junctions of epithelial cells
Amasheh, S., Schmidt, T. P., Mahn, M., Florian, P., Mankertz, J., Tavalali, S., Gitter, A. H., Schulzke, J., & Fromm, M. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-1101-0 · Cited by 194 · see citing works
Yeaman, C. A., Grindstaff, K. K., & Nelson, W. J. (2004) · Journal of Cell Science · doi:10.1242/jcs.00893 · Cited by 188 · see citing works
Tiwari-Woodruff, S. K., Buznikov, A. G., Vu, T., Micevych, P. E., Chen, K., Kornblum, H. I., & Bronstein, J. M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.2.295 · Cited by 183 · see citing works
Roh, M. H., Liu, C., Laurinec, S., & Margolis, B. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201177200 · Cited by 181 · see citing works
Watson, C. J. E., Hoare, C. J., Garrod, D. R., Carlson, G., & Warhurst, G. (2005) · Journal of Cell Science · doi:10.1242/jcs.02630 · Cited by 171 · see citing works
Wright, E. M., & Diamond, J. M. (1968) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(68)90033-3 · Cited by 170 · see citing works
Epithelial cell adhesion and the regulation of gene expression
Balda, M. S. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(03)00105-3 · Cited by 165 · see citing works
The cell–cell adhesion molecule EpCAM interacts directly with the tight junction protein claudin-7
Ladwein, M., Pape, U., SCHMIDT, D., et al. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.06.013 · Cited by 164 · see citing works
Regulation of Heterotypic Claudin Compatibility
Daugherty, B. L., Ward, C., Smith, T., Ritzenthaler, J. D., & Koval, M. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703547200 · Cited by 158 · see citing works
Electrical resistance of a capillary endothelium.
Crone, C. G., & Christensen, O. (1981) · The Journal of General Physiology · doi:10.1085/jgp.77.4.349 · Cited by 157 · see citing works
On the self-association potential of transmembrane tight junction proteins
Blasig, I. E., Winkler, L., Lassowski, B., Mueller, S., Zuleger, N., Krause, E., Krause, G., Gast, K., Kolbe, M., & Piontek, J. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5472-x · Cited by 130 · see citing works
The peripheral myelin protein 22 and epithelial membrane protein family
Jetten, A. M., & Suteri, U. (2000) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(00)64003-5 · Cited by 125 · see citing works
Null Mutation of PCLN-1/Claudin-16 Results in Bovine Chronic Interstitial NephritisPreprint
Hirano, T., Kobayashi, N., Itoh, T., et al. (2000) · Genome Research · doi:10.1101/gr.10.5.659 · Cited by 111 · see citing works
Mitic, L. L., Unger, V. M., & Anderson, J. M. (2003) · Protein Science · doi:10.1110/ps.0233903 · Cited by 110 · see citing works
Self-citationPeripheral myelin protein 22 is a constituent of intercellular junctions in epithelia
Notterpek, L. M., Roux, K. J., Amici, S. A., Yazdanpour, A., Rahner, C., & Fletcher, B. S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251548398 · Cited by 101 · see citing works
A mutation in the connexin 50 (Cx50) gene is a candidate for the No2 mouse cataract
Steele, E. C., Lyon, M. F., Favor, J., et al. (1998) · Current Eye Research · doi:10.1076/ceyr.17.9.883.5144 · Cited by 100 · see citing works
The Role of Claudins in Determining Paracellular Charge Selectivity
Itallie, C. M. V., & Anderson, J. M. (2004) · Proceedings of the American Thoracic Society · doi:10.1513/pats.2306013 · Cited by 95 · see citing works
Self-citationClaudin‐8 modulates paracellular permeability to acidic and basic ions in MDCK II cells
Angelow, S., Kim, K., & Yu, A. S. L. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2005.099135 · Cited by 87 · see citing works
Claudins in Caenorhabditis elegans
Asano, A., Asano, K., Sasaki, H., Furuse, M., & Tsukita, S. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00395-6 · Cited by 87 · see citing works
Jeansonne, B. G., Lu, Q., Goodenough, D. A., & Chen, Y. H. (2003) · PubMed · Cited by 85 · see citing works
Ussing, H. H., & Zerahn, K. (1999) · PubMed · Cited by 83 · see citing works
Madara, J., Trier, J. S., & Neutra, M. R. (1980) · Gastroenterology · doi:10.1016/0016-5085(80)90778-7 · Cited by 79 · see citing works
The second loop of occludin is required for suppression of Raf1-induced tumor growth
Wang, Z., Mandell, K. J., Parkos, C. A., et al. (2005) · Oncogene · doi:10.1038/sj.onc.1208634 · Cited by 76 · see citing works
Channels in epithelial cell membranes and junctions.
Jm, D. (1978) · PubMed · Cited by 63 · see citing works
Brancolini, C., Edomi, P., Marzinotto, S., et al. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.9.2901 · Cited by 57 · see citing works
Function of tetraspan proteins in the myelin sheath
Bronstein, J. M. (2000) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(00)00125-2 · Cited by 52 · see citing works
Himmerkus, N., Shan, Q., Goerke, B., et al. (2008) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90388.2008 · Cited by 50 · see citing works
Price, M. G., Davis, C., Deng, F., & Burgess, D. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500623200 · Cited by 50 · see citing works
Roux, K. J., Amici, S. A., Fletcher, B. S., et al. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-07-0551 · Cited by 48 · see citing works
Human Nerve Pathology Caused by Different Mutational Mechanisms of the PMP22 Gene
Gabreëls‐Festen, A. A. W. M., & van de Wetering, R. A. C. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb08595.x · Cited by 47 · see citing works
Ikari, A., Ito, M., Okude, C., Sawada, H., Harada, H., Degawa, M., 酒井, 秀., Takahashi, T., Sugatani, J., & Miwa, M. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21178 · Cited by 42 · see citing works
Twenty-First Bowditch Lecture.
Diamond, J. M. (1977) · The Physiologist/The physiologist · Cited by 33 · see citing works
Optimized Proteomic Analysis on Gels of Cell−Cell Adhering Junctional Membrane Proteins
Yamazaki, Y., Okawa, K., Yano, T., et al. (2008) · Biochemistry · doi:10.1021/bi8002567 · Cited by 32 · see citing works
Naour, F. L. (2008) · Frontiers in bioscience · doi:10.2741/3121 · Cited by 29 · see citing works
Roux, K. J., Amici, S. A., & Notterpek, L. (2004) · Journal of Comparative Neurology · doi:10.1002/cne.20154 · Cited by 27 · see citing works
A novel four transmembrane spanning protein, CLP24
Kearsey, J., Petit, S., Oliveira, C. D., & Schweighoffer, F. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04186.x · Cited by 24 · see citing works
Introduction: Evolution of Ideas on the Tight Junction
(2001) · CRC Press eBooks · doi:10.1201/9781420038538-3 · Cited by 23 · see citing works
JAM-A regulates permeability and inflammation in the intestine in vivo
Laukoetter, M. G., Nava, P., Lee, W. Y., et al. (2007) · The Journal of Cell Biology · doi:10.1083/jcb1795oia14 · Cited by 20 · see citing works
Kaushansky, N., Hemo, R., Eisenstein, M., & Ben‐Nun, A. (2007) · European Journal of Immunology · doi:10.1002/eji.200636965 · Cited by 18 · see citing works
Purification and oligomeric state of the major lens fiber cell membrane proteins
Jarvis, L. J., & Louis, C. F. (1995) · Current Eye Research · doi:10.3109/02713689508995802 · Cited by 14 · see citing works
CNS myelin and Sertoli cell tight junction stands are absent in Osp/claudin 11-null mice
Gow, A., Southwood, C. M., Li, J. S., et al. (2000) · Cited by 6 · see citing works
Vetrano, S., Rescigno, M., Cera, M. R., et al. (2008) · Gastroenterology · doi:10.1016/s0016-5085(08)60672-1 · Cited by 5 · see citing works
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The blood–brain barrier: Structure, regulation and drug delivery
Wu, D., Chen, Q., Chen, X., Han, F., Chen, Z., & Wang, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01481-w · Cited by 1,906 · see citing works
Regulation of Intestinal Barrier Function by Microbial Metabolites
Ghosh, S., Whitley, C. S., Haribabu, B., & Jala, V. R. (2021) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2021.02.007 · Cited by 835 · see citing works
Accessing analytes in biofluids for peripheral biochemical monitoring
Heikenfeld, J., Jajack, A., Feldman, B., Granger, S. W., Gaitonde, S., Begtrup, G., & Katchman, B. A. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0040-3 · Cited by 758 · see citing works
Impact of Diet-Modulated Butyrate Production on Intestinal Barrier Function and Inflammation
Bach Knudsen, K. E., Lærke, H. N., Hedemann, M. S., Nielsen, T. S., Ingerslev, A. K., Gundelund Nielsen, D. S., Theil, P. K., Purup, S., Hald, S., Schioldan, A. G., et al. (2018) · Nutrients · doi:10.3390/nu10101499 · Cited by 572 · see citing works
Micro- and nanoplastic induced cellular toxicity in mammals: A review
Banerjee, A., & Shelver, W. L. (2021) · Science of The Total Environment · doi:10.1016/j.scitotenv.2020.142518 · Cited by 492 · see citing works
Groeger, S., & Meyle, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00208 · Cited by 473 · see citing works
Epidermal barrier dysfunction and cutaneous sensitization in atopic diseases
Kubo, A., Nagao, K., & Amagai, M. (2012) · Journal of Clinical Investigation · doi:10.1172/jci57416 · Cited by 378 · see citing works
Intestinal Permeability Defects: Is It Time to Treat?
Odenwald, M. A., & Turner, J. R. (2013) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2013.07.001 · Cited by 366 · see citing works
Probiotic bacteria induce maturation of intestinal claudin 3 expression and barrier function
Patel, R. M., Myers, L. S., Kurundkar, A. R., Maheshwari, A., Nusrat, A., & Lin, P. W. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2011.10.025 · Cited by 341 · see citing works
Stress induces endotoxemia and low-grade inflammation by increasing barrier permeability
de Punder, K., & Pruimboom, L. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00223 · Cited by 321 · see citing works
Blood-brain barrier permeability and physical exercise
Małkiewicz, M. A., Szarmach, A., Sabisz, A., Cubała, W. J., Szurowska, E., & Winklewski, P. J. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-019-1403-x · Cited by 276 · see citing works
Chichlowski, M., De Lartigue, G., German, J. B., Raybould, H. E., & Mills, D. A. (2012) · Journal of Pediatric Gastroenterology and Nutrition · doi:10.1097/mpg.0b013e31824fb899 · Cited by 276 · see citing works
The intestinal barrier in disorders of the central nervous system
Pellegrini, C., Fornai, M., D'Antongiovanni, V., Antonioli, L., Bernardini, N., & Derkinderen, P. (2023) · The Lancet Gastroenterology & Hepatology · doi:10.1016/s2468-1253(22)00241-2 · Cited by 239 · see citing works
Nutritional Keys for Intestinal Barrier Modulation
De Santis, S., Cavalcanti, E., Mastronardi, M., Jirillo, E., & Chieppa, M. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00612 · Cited by 232 · see citing works
Regulation of blood-retinal barrier cell-junctions in diabetic retinopathy
Rudraraju, M., Narayanan, S. P., & Somanath, P. R. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105115 · Cited by 217 · see citing works
Lipoprotein‐associated phospholipase A2: The story continues
Huang, F., Wang, K., & Shen, J. (2020) · Medicinal Research Reviews · doi:10.1002/med.21597 · Cited by 212 · see citing works
The role of molecular remodeling in differential regulation of tight junction permeability
Turner, J. R., Buschmann, M. M., Romero-Calvo, I., Sailer, A., & Shen, L. (2014) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2014.09.022 · Cited by 200 · see citing works
Buschmann, M. M., Shen, L., Rajapakse, H., Raleigh, D. R., Wang, Y., Wang, Y., Lingaraju, A., Zha, J., Abbott, E., McAuley, E. M., et al. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-09-0688 · Cited by 192 · see citing works
Tight junctions as targets and effectors of mucosal immune homeostasis
Zuo, L., Kuo, W.-T., & Turner, J. R. (2020) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2020.04.001 · Cited by 191 · see citing works
Patra, A. K., Amasheh, S., & Aschenbach, J. R. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1486284 · Cited by 130 · see citing works
Adams, E. D. M., Goss, G. G., & Leys, S. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015040 · Cited by 74 · see citing works
The Yin and Yang of bile acid action on tight junctions in a model colonic epithelium
Sarathy, J., Detloff, S. J., Ao, M., Khan, N., French, S., Sirajuddin, H., Nair, T., & Rao, M. C. (2017) · Physiological Reports · doi:10.14814/phy2.13294 · Cited by 72 · see citing works
TMIGD1 Is a Novel Adhesion Molecule That Protects Epithelial Cells from Oxidative Cell Injury
Arafa, E., Bondzie, P. A., Rezazadeh, K., Meyer, R. D., Hartsough, E., Henderson, J. M., Schwartz, J. H., Chitalia, V., & Rahimi, N. (2015) · The American Journal of Pathology · doi:10.1016/j.ajpath.2015.06.006 · Cited by 40 · see citing works
Enhancing glucose flux into sweat by increasing paracellular permeability of the sweat gland
Jajack, A., Brothers, M., Kasting, G., & Heikenfeld, J. (2018) · PLOS ONE · doi:10.1371/journal.pone.0200009 · Cited by 35 · see citing works
Parenteral Nutrition, Inflammatory Bowel Disease, and Gut Barrier: An Intricate Plot
Covello, C., Becherucci, G., Di Vincenzo, F., Del Gaudio, A., Pizzoferrato, M., Cammarota, G., Gasbarrini, A., Scaldaferri, F., & Mentella, M. C. (2024) · Nutrients · doi:10.3390/nu16142288 · Cited by 21 · see citing works
Claudin expression in the bone-lining cells of female rats exposed to long-standing acidemia
Wongdee, K., Riengrojpitak, S., Krishnamra, N., & Charoenphandhu, N. (2010) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2009.12.005 · Cited by 14 · see citing works
- Authors
- Anderson, J. M., & Van Itallie, C. M.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2009-08-01
- Volume
- 1
- Issue
- 2
- Pages
- a002584-a002584
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC2742087
- OpenAlex
- W4297977229
- Cited by
- 1,059
- References
- 121
- Citations by year
- 2026: 44 · 2025: 61 · 2024: 75 · 2023: 64 · 2022: 72 · 2021: 88 · 2020: 91 · 2019: 78 · 2018: 62 · 2017: 69 · 2016: 56 · 2015: 66 · 2014: 60 · 2013: 63 · 2012: 56
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Institutes of Health (DK034987, DK61397)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK45134, R01DK045134, DK61397, R56DK061397, R01DK061397, P30DK034987)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- tight junctions, paracellular barrier, claudins, tight junction proteins, barrier permeability, actin-binding proteins
- MeSH terms
- Amino Acid Sequence, Animals, Biological Transport, Cell Membrane, Cytoplasm, Electrophysiology, Humans, Models, Biological, Molecular Sequence Data, Sequence Homology, Amino Acid, Tight Junctions, Genetic Predisposition to Disease, Claudins
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.
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