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Anderson J.M. Molecular structure of tight junctions and their role in epithelial transport. News Physiol Sci. 16:2001;126-130. This is a good review of our current understanding of the structure and barrier functions of tight junctions.
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Anderson, J.M.1
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Multifunctional strands in tight junctions
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This is a comprehensive review of the morphology, molecular biology and physiological functions of tight junctions.
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Tsukita S.h, Furuse M., Itoh M. Multifunctional strands in tight junctions. Nat Rev Mol Cell Biol. 2:2001;285-293. This is a comprehensive review of the morphology, molecular biology and physiological functions of tight junctions.
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Tsukita, S.H.1
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Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
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Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S.h. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol. 141:1998;1539-1550.
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Balda M.S., Matter K. Transmembrane proteins of tight junctions. Semin Cell Dev Biol. 11:2000;281-289.
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7
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Claudin-based tight junctions are crucial for the mammalian epidermal barrier: A lesson from claudin-1-deficient mice
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This paper reports the targeted inactivation of the mouse claudin-1 gene. These mice died within one day of birth, and showed severe defects in the permeability barrier of the epidermis, indicating that tight junctions are directly involved in the epidermal barrier. This study provides a completely new insight into the barrier mechanism of stratified epithelia, especially the skin.
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Furuse M., Hata M., Furuse K., Yoshida Y., Haratake A., Sugitani Y., Noda T., Kubo A., Tsukita S.h. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J Cell Biol. 156:2002;1099-1111. This paper reports the targeted inactivation of the mouse claudin-1 gene. These mice died within one day of birth, and showed severe defects in the permeability barrier of the epidermis, indicating that tight junctions are directly involved in the epidermal barrier. This study provides a completely new insight into the barrier mechanism of stratified epithelia, especially the skin.
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J Cell Biol
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Furuse, M.1
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Tsukita S.h, Furuse M., Itoh M. Structural and signalling molecules come together at tight junctions. Curr Opin Cell Biol. 11:1999;628-633.
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Morita K., Furuse M., Fujimoto K., Tsukita S.h. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA. 96:1999;511-516.
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Tsukita S.h, Furuse M. Occludin and claudins in tight-junction strands: leading or supporting players? Trends Cell Biol. 9:1999;268-273.
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Tsukita, S.H.1
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11
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A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
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Furuse M., Sasaki H., Fujimoto K., Tsukita S.h. A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol. 143:1998;391-401.
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12
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0033598188
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Manner of interaction of heterogeneous claudin species within and between tight junction strands
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Furuse M., Sasaki H., Tsukita S.h. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J Cell Biol. 147:1999;891-903.
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Furuse, M.1
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14
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0033523773
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Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: Evidence for direct involvement of claudins in tight junction barrier
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Sonoda N., Furuse M., Sasaki H., Yonemura S., Katahira J., Horiguchi Y., Tsukita S.h. Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: evidence for direct involvement of claudins in tight junction barrier. J Cell Biol. 147:1999;195-204.
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Sonoda, N.1
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15
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Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29
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This paper identifies claudin-14 as the gene responsible for human nonsyndromic hereditary deafness DEFB29. In the cochlea, claudin-14 was exclusively expressed in the sensory epithelium of the organ of Corti. These findings suggest that mutations in claudin-14 cause an increase in the tight junction permeability of the Corti organ, affecting compartmentalisation in the cochlea.
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Wilcox E.R., Burton Q.L., Naz S., Riazuddin S., Smith T.N., Ploplis B., Belyantseva I., Ben-Yosef T., Liburd N.A., Morell R.J., et al. Mutations in the gene encoding tight junction claudin-14 cause autosomal recessive deafness DFNB29. Cell. 104:2001;165-172. This paper identifies claudin-14 as the gene responsible for human nonsyndromic hereditary deafness DEFB29. In the cochlea, claudin-14 was exclusively expressed in the sensory epithelium of the organ of Corti. These findings suggest that mutations in claudin-14 cause an increase in the tight junction permeability of the Corti organ, affecting compartmentalisation in the cochlea.
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Cell
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Wilcox, E.R.1
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Morell, R.J.10
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16
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0035321325
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Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria
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This paper proposes a new mechanism for bacterial uptake in the mucosal tissues mediated by dendritic cells: dendritic cells open the tight junctions between epithelial cells, send dendrites outside the epithelium and directly sample bacteria. To prevent leakage of solutes through the paracellular pathway during this process, dendritic cells express tight-junction proteins such as occludin, claudin-1 and ZO-1 and form tight junctions with adjacent epithelial cells.
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Rescigno M., Urbano M., Valzasina B., Francolini M., Rotta G., Bonasio R., Granucci F., Kraehenbuhl J.P., Ricciardi-Castagnoli P. Dendritic cells express tight junction proteins and penetrate gut epithelial monolayers to sample bacteria. Nat Immunol. 2:2001;361-367. This paper proposes a new mechanism for bacterial uptake in the mucosal tissues mediated by dendritic cells: dendritic cells open the tight junctions between epithelial cells, send dendrites outside the epithelium and directly sample bacteria. To prevent leakage of solutes through the paracellular pathway during this process, dendritic cells express tight-junction proteins such as occludin, claudin-1 and ZO-1 and form tight junctions with adjacent epithelial cells.
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Nat Immunol
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17
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Pores in the wall: Claudins constitute tight junction strands containing aqueous pores
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Tsukita S.h, Furuse M. Pores in the wall: claudins constitute tight junction strands containing aqueous pores. J Cell Biol. 149:2000;13-16.
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J Cell Biol
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18
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0035897412
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This is the first report that claudins not only increase but also decrease the tightness of tight junction (TJ) strands depending on their combination within paired TJ strands. MDCK I and II cells, which are, respectively, tight and leaky in terms of their TJ barrier, express claudin-1/-4 and claudin-1/-2/-4, respectively. When claudin-2 was introduced into MDCK I cells to mimic the claudin combination pattern in MDCK II cells, these transfectants became as leaky as MDCK II cells without any change in the morphology of TJ strand networks.
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Furuse M., Furuse K., Sasaki H., Tsukita S.h. Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J Cell Biol. 153:2001;263-272. This is the first report that claudins not only increase but also decrease the tightness of tight junction (TJ) strands depending on their combination within paired TJ strands. MDCK I and II cells, which are, respectively, tight and leaky in terms of their TJ barrier, express claudin-1/-4 and claudin-1/-2/-4, respectively. When claudin-2 was introduced into MDCK I cells to mimic the claudin combination pattern in MDCK II cells, these transfectants became as leaky as MDCK II cells without any change in the morphology of TJ strand networks.
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J Cell Biol
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Furuse, M.1
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Tsukita, S.H.4
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19
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0035013499
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Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability
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Van Itallie, C.1
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