References
- E. Proksch, J. M. Brandner, and J. M. Jensen, The skin: an indispensable barrier, Exp. Dermatol., 17(12), 1063 (2008). https://doi.org/10.1111/j.1600-0625.2008.00786.x
- J. M. Brandner, Importance of tight junctions in relation to skin barrier function, Curr. Probl. Dermatol., 49, 27 (2016). https://doi.org/10.1159/000441541
- C. M. Van Itallie and J. M. Anderson, The molecular physiology of tight junction pores, Physiology (Bethesda), 19, 331 (2004). https://doi.org/10.1152/physiol.00027.2004
- J. M. Brandner, S. Kief, E. Wladykowski, P. Houdek, and I. Moll, Tight junction proteins in the skin, Skin Pharmacol. Physiol., 19(2):71 (2006). https://doi.org/10.1159/000091973
- J. Chen and M. Zhang, The Par3/Par6/aPKC complex and epithelial cell polarity, Exp. Cell Res., 319(10), 1357 (2013). https://doi.org/10.1016/j.yexcr.2013.03.021
- J. S. Kim and H. S. Jang, The expression pattern of the tight junction protein occludin in the epidermal context when comparing various physical samples, Korean Journal of Clinical Laboratory Science, 47(4), 267 (2015). https://doi.org/10.15324/kjcls.2015.47.4.267
- H. A. Ed ens, B. P. Levi, D. L. Jaye, S. Walsh, T. A. Reaves, J. R. Turner, A. Nusrat, and C. A. Parkos, Neutrophil transepithelial migration: evidence for sequential, contact-dependent signaling events and enhanced paracellular permeability independent of transjunctional migration, J. Immun., 169(1), 476 (2002). https://doi.org/10.4049/jimmunol.169.1.476
- D. Gunzel and A. S. Yu, Claudins and the modulation of tight junction permeability, Physiol. Rev., 93(2), 525 (2013). https://doi.org/10.1152/physrev.00019.2012
- J. M. Anderson, and C. M. Van Itallie, Physiology and function of the tight junction, Cold Spring Harb. Perspect. Biol., 1(2), a002584 (2009). https://doi.org/10.1101/cshperspect.a002584
- M. Lal-Nag and P. J. Morin, The claudins, Genome Biol., 10(8), 1 (2009).
- M. S. Balda, and K. Matter, Tight junctions and the regulation of gene expression, Biochim. Biophys. Acta -Biomembr., 1788(4), 761 (2009). https://doi.org/10.1016/j.bbamem.2008.11.024
- J. A. Palatinus, M. P. O'Quinn, R. J. Barker, B. S. Harris, J. Jourdan, and R. G. Gourdie, ZO-1 determines adherens and gap junction localization at intercalated disks, Am. J. Physiol. - Heart Circ. Physiol., 300(2), H583 (2011). https://doi.org/10.1152/ajpheart.00999.2010
- J. M. Brandner, Tight junctions and tight junction proteins in mammalian epidermis, Eur. J. Pharm. Biopharm., 72(2), 289 (2009). https://doi.org/10.1016/j.ejpb.2008.08.007
- A. Veshnyakova, J. Protze, J. Rossa, I. E. Blasig, G. Krause, and J. Piontek, On the interaction of Clostridium perfringens enterotoxin with claudins, Toxins (Basel)., 2(6), 1336 (2010). https://doi.org/10.3390/toxins2061336
- J. A. Guttman, and B. B. Finlay, Tight junctions as targets of infectious agent, Biochim. Biophys. Acta., 1788(4), 832 (2009). https://doi.org/10.1016/j.bbamem.2008.10.028
- I. Benedicto, F. Molina-Jimenez, B. Bartosch, F. L. Cosset, D. Lavillette, J. Prieto, R. Moreno-Otero, A. ValenzuelaFernandez, R. Aldabe, M. Lopez-Cabrera, and P. L. Majano, The tight junction-associated protein occludin is required for a postbinding step in hepatitis C virus entry and infection, J. Virol., 83(16), 8012 (2009). https://doi.org/10.1128/JVI.00038-09
- E. S. Barton, J. C. Forrest, J. L. Connolly, J. D. Chappell, Y. Liu, F. J. Schnell, A. Nusrat, C. A. Parkos, and T. S. Dermody, Junction adhesion molecule is a receptor for reovirus, Cell, 104(3), 441 (2001). https://doi.org/10.1016/S0092-8674(01)00231-8
- M. Reithofer and B. Jahn-Schmid, Allergens with protease activity from house dust mites, Int. J. Mol. Sci., 18(7), 1368 (2017). https://doi.org/10.3390/ijms18071368
- M. Furuse, M. Hata, K. Furuse, Y. Yoshida, A. Haratake, Y. Sugitani, T. Noda, A. Kubo, and S. Tsukita, Claudinbased tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice, J. Cell Biol., 156(6), 1099 (2002). https://doi.org/10.1083/jcb.200110122
- J. Shi, M. Barakat, D. Chen, and L. Chen, Bicellular tight junctions and wound healing, Int. J. Mol. Sci., 19(12), 3862 (2018). https://doi.org/10.3390/ijms19123862
- J. M. Brandner, S. Kief, C. Grund, M. Rendl, P. Houdek, C. Kuhn, E. Tschachler, W. W. Franke, and I. Moll, Organization and formation of the tight junction system in human epidermis and cultured keratinocytes, Eur. J. Cell Biol., 81(5), 253 (2002). https://doi.org/10.1078/0171-9335-00244
- I. Helfrich, A. Schmitz, P. Zigrino, C. Michels, I. Haase, A. le Bivic, M. Leitges, and C. M. Niessen, Role of aPKC isoforms and their binding partners Par3 and Par6 in epidermal barrier formation, J. Invest. Dermatol., 127(4), 782 (2007). https://doi.org/10.1038/sj.jid.5700621
- A. E. Mertens, T. P. Rygiel, C. Olivo, R. van der Kammen, and J. G. Collard, The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex, J. Cell Biol., 170(7), 1029 (2005). https://doi.org/10.1083/jcb.200502129
- T. Yuki, A. Haratake, H. Koishikawa, K. Morita, Y. Miyachi, and S. Inoue, Tight junction proteins in keratinocytes: localization and contribution to barrier function, Exp. Dermatol., 16(4), 324 (2007). https://doi.org/10.1111/j.1600-0625.2006.00539.x
- M. Furuse, M. Hata, K. Furuse, Y. Yoshida, A. Haratake, Y. Sugitani, T. Noda, A. Kubo, and S. Tsukita, Claudinbased tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice, J. Cell Biol., 156(6), 1099 (2002). https://doi.org/10.1083/jcb.200110122
- C. Leyvraz, R. P. Charles, I. Rubera, M. Guitard, S. Rotman, B. Breiden, K. Sandhoff, and E. Hummler, The epidermal barrier function is dependent on the serine protease CAP1/Prss8, J. Cell Biol., 170(3), 487 (2005). https://doi.org/10.1083/jcb.200501038
- T. C. Troy, A. Arabzadeh, N. M. Lariviere, A. Enikanolaiye, and K. Turksen, Dermatitis and agingrelated barrier dysfunction in transgenic mice overexpressing an epidermal-targeted claudin 6 tail deletion mutant, PLoS One, 4(11), e7814 (2009). https://doi.org/10.1371/journal.pone.0007814
- J. M. Brandner, Pores in the epidermis: aquaporins and tight junctions, Int. J. Cosmet. Sci., 29(6), 413 (2007). https://doi.org/10.1111/j.1468-2494.2007.00402.x
- R. Gruber, C. Bornchen, K. Rose, A. Daubmann, T. Volksd orf, E. Wlad ykowski, S. Vid al-Y-Sy, E. M. Peters, M. Danso, J. A. Bouwstra, H. C. Hennies, I. Moll, M. Schmuth, and J. M. Brandner, Diverse regulation of claudin-1 and claudin-4 in atopic dermatitis, Am. J. Clin. Pathol., 185(10), 2777 (2015). https://doi.org/10.1016/j.ajpath.2015.06.021
- A. Arabzadeh, T. C. Troy, and K. Turksen, Changes in the distribution pattern of Claudin tight junction proteins during the progression of mouse skin tumorigenesis, BMC cancer, 7, 196 (2007). https://doi.org/10.1186/1471-2407-7-196
- U. Ohnemus, K. Kohrmeyer, P. Houdek, H. Rohde, E. Wladykowski, S. Vidal, M. A. Horstkotte, M. Aepfelbacher, N. Kirschner, M. J. Behne, I. Moll, and J. M. Brandner, Regulation of epidermal tight-junctions (TJ) during infection with exfoliative toxin-negative Staphylococcus strains, J. Invest. Dermatol., 128(4), 906 (2008). https://doi.org/10.1038/sj.jid.5701070
- Y. Hashimoto, K. Tachibana, S. M. Krug, J. Kunisawa, M. Fromm, and M. Kondoh, Potential for tight junction protein-directed drug development using claudin binders and angubindin-1, Int. J. Mol. Sci., 20(16), 4016 (2019). https://doi.org/10.3390/ijms20164016
- J. Brunner, S. Ragupathy, and G. Borchard, Target specific tight junction modulators, Adv. Drug Deliv. Rev., 171, 266 (2021). https://doi.org/10.1016/j.addr.2021.02.008
- C. Gorzelanny, C. Mess, S. W. Schneid er, V. Huck, and J. M. Brandner, Skin barriers in dermal drug delivery: which barriers have to be overcome and how can we measure them?, Pharmaceutics, 12(7), 684 (2020). https://doi.org/10.3390/pharmaceutics12070684
- M. Kopecna, M. Machacek, A. Novackova, G. Paraskevopoulos, J. Roh, and K. Vavrova, Esters of terpene alcohols as highly potent, reversible, and low toxic skin penetration enhancers, Sci. Rep., 9(1), 14617 (2019). https://doi.org/10.1038/s41598-019-51226-5
- M. Kondoh, T. Yoshida, H. Kakutani, and K. Yagi, Targeting tight junction proteins-significance for drug development, Drug Discov., 13(3-4), 180 (2008).
- S. Maher, T. W. Leonard, J. Jacobsen, and D. J. Brayden, Safety and efficacy of sodium caprate in promoting oral drug absorption: from in vitro to the clinic, Adv. Drug Deliv. Rev., 61(15), 1427 (2009). https://doi.org/10.1016/j.addr.2009.09.006
- 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., 10(6), 857 (1993). https://doi.org/10.1023/A:1018909210879
- K. Nagasawa, H. Chiba, H. Fujita, T. Kojima, T. Saito, T. Endo, and N. Sawada, Possible involvement of gap junctions in the barrier function of tight junctions of brain and lung endothelial cells, J. Cell. Physiol, 208(1), 123 (2006). https://doi.org/10.1002/jcp.20647
- A. Fukui, Y. Naito, O. Handa, M. Kugai, T. Tsuji, H. Yoriki, Y. Qin, S. Adachi, Y. Higashimura, K. Mizushima, K. Kamad a, K. Katad a, K. Uchiyama, T. Ishikawa, T. Takagi, N. Yagi, S. Kokura, and T. Yoshikawa, Acetyl salicylic acid induces damage to intestinal epithelial cells by oxidation-related modifications of ZO-1, Am. J. Physiol. - Gastrointest. Liver Physiol., 303(8), G927 (2012). https://doi.org/10.1152/ajpgi.00236.2012
- M. A. Deli, Potential use of tight junction modulators to reversibly open membranous barriers and improve drug delivery, Biochim. Biophys. Acta, 1788(4), 892 (2009). https://doi.org/10.1016/j.bbamem.2008.09.016
- H. Lan, K. Hosomi, and J. Kunisawa, Clostridium perfringens enterotoxin-based protein engineering for the vaccine design and delivery system, Vaccine, 37(42), 6232 (2019). https://doi.org/10.1016/j.vaccine.2019.08.032
- N. N. Salama, N. D. Eddington, and A. Fasano, Tight junction modulation and its relationship to drug delivery, Adv. Drug Deliv. Rev., 58(1), 15 (2006). https://doi.org/10.1016/j.addr.2006.01.003
- T. Otani and M. Furuse, Tight junction structure and function revisited, Trends Cell Biol., 30(10), 805 (2020). https://doi.org/10.1016/j.tcb.2020.08.004
- C. M. Niessen, Tight junctions/adherens junctions: basic structure and function, J. Invest. Dermatol., 127(11), 2525 (2007). https://doi.org/10.1038/sj.jid.5700865
- K. Basler, S. Bergmann, M. Heisig, A. Naegel, M. Zorn-Kruppa, and J. M. Brandner, The role of tight junctions in skin barrier function and dermal absorption, J. Control Release, 242, 105 (2016). https://doi.org/10.1016/j.jconrel.2016.08.007
- J. M. Brandner, M. Zorn-Kruppa, T. Yoshida, I. Moll, L. A. Beck, and A. De Benedetto, Epidermal tight junctions in health and disease. Tissue barriers, 3(1-2), e974451 (2015). https://doi.org/10.4161/21688370.2014.974451