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Volumn , Issue , 2009, Pages 201-220

Gap and tight junctions in liver: Composition, regulation, and function

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EID: 79960703006     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470747919.ch14     Document Type: Chapter
Times cited : (9)

References (96)
  • 1
    • 0002132395 scopus 로고
    • Gap junctions in liver: Composition, function and regulation
    • 3rd edn (eds I. Arias, J.L. Boyer, N. Jakoby, et al.), Raven Press, New York
    • Spray, D.C., Saez, J.C., Herzberg, E.L. et al. (1994) Gap junctions in liver: composition, function and regulation, in The Liver: Biology and Pathobiology, 3rd edn (eds I. Arias, J.L. Boyer, N. Jakoby, et al.), Raven Press, New York, pp. 951-67.
    • (1994) The Liver: Biology and Pathobiology , pp. 951-967
    • Spray, D.C.1    Saez, J.C.2    Herzberg, E.L.3
  • 2
    • 0001870791 scopus 로고    scopus 로고
    • Gap and tight junctions in liver: Composition, regulation and function
    • (eds I. Arias, et al.), Lippincott, Williams, & Wilkins, Philadelphia
    • Kojima, T., Sawada, N., Duffy, H.S. and Spra, D.C. (2001) Gap and tight junctions in liver: composition, regulation and function, in The Liver: Biology and Pathobiology (eds I. Arias, et al.), Lippincott, Williams, & Wilkins, Philadelphia, pp. 29-46.
    • (2001) The Liver: Biology and Pathobiology , pp. 29-46
    • Kojima, T.1    Sawada, N.2    Duffy, H.S.3    Spra, D.C.4
  • 3
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: Their regulation and functions
    • Saez, J.C., Berthoud, V.M., Branes, M.C. et al. (2003) Plasma membrane channels formed by connexins: their regulation and functions. Physiol Rev, 83, 1359-400.
    • (2003) Physiol Rev , vol.83 , pp. 1359-1400
    • Saez, J.C.1    Berthoud, V.M.2    Branes, M.C.3
  • 4
    • 40949111869 scopus 로고    scopus 로고
    • Biology and pathology of gap junctional channels in hepatocytes
    • Vinken, M., Henkens, T., De Rop, E. et al. (2008) Biology and pathology of gap junctional channels in hepatocytes. Hepatology, 47, 1077-88.
    • (2008) Hepatology , vol.47 , pp. 1077-1088
    • Vinken, M.1    Henkens, T.2    De Rop, E.3
  • 5
    • 0031850493 scopus 로고    scopus 로고
    • Innexins: A family of invertebrate gap-junction proteins
    • Phelan, P., Bacon, J.P., Davies, J.A. et al. (1998) Innexins: a family of invertebrate gap-junction proteins. Trends Genet, 14, 348-49.
    • (1998) Trends Genet , vol.14 , pp. 348-349
    • Phelan, P.1    Bacon, J.P.2    Davies, J.A.3
  • 6
    • 33646738415 scopus 로고    scopus 로고
    • Cell-cell communication beyond connexins: The pannexin channels [review]
    • Barbe, M.T., Monyer, H. and Bruzzone, R. (2006) Cell-cell communication beyond connexins: the pannexin channels [review]. Physiology (Bethesda), 21, 103-14.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 103-114
    • Barbe, M.T.1    Monyer, H.2    Bruzzone, R.3
  • 7
    • 18944394972 scopus 로고    scopus 로고
    • Evolution of gap junction proteins-the pannexin alternative [review]
    • Panchin, Y.V. (2005) Evolution of gap junction proteins-the pannexin alternative [review]. J Exp Biol, 208 (Pt 8), 1415-19.
    • (2005) J Exp Biol , vol.208 , pp. 1415-1419
    • Panchin, Y.V.1
  • 8
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • Pelegrin, P. and Surprenant, A. (2006) Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J, 25 (21), 5071-82.
    • (2006) EMBO J , vol.25 , Issue.21 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 9
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex
    • Locovei, S., Scemes, E., Qiu, F. et al. (2007) Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex. FEBS Lett, 581 (3), 483-88.
    • (2007) FEBS Lett , vol.581 , Issue.3 , pp. 483-488
    • Locovei, S.1    Scemes, E.2    Qiu, F.3
  • 10
    • 0036556336 scopus 로고    scopus 로고
    • Formation of the gap junction nexus: Binding partners for connexins
    • Duffy, H.S., Delmar, M. and Spray, D.C. (2002) Formation of the gap junction nexus: binding partners for connexins. J Physiol Paris, 96, 243-49.
    • (2002) J Physiol Paris , vol.96 , pp. 243-249
    • Duffy, H.S.1    Delmar, M.2    Spray, D.C.3
  • 11
    • 0342944791 scopus 로고    scopus 로고
    • Electrophysiological properties of gap junction channels in hepatocytes isolated from connexin32-deficient and wild-type mice
    • Valiunas, V., Niessen, H., Willecke, K. et al. (1999) Electrophysiological properties of gap junction channels in hepatocytes isolated from connexin32-deficient and wild-type mice. Pflugers Arch, 437, 846-56.
    • (1999) Pflugers Arch , vol.437 , pp. 846-856
    • Valiunas, V.1    Niessen, H.2    Willecke, K.3
  • 12
    • 0034712792 scopus 로고    scopus 로고
    • Liver cell-specific transcriptional regulation of connexin32
    • Piechocki, M.P., Toti, R.M., Fernstrom, M.J. et al. (2000) Liver cell-specific transcriptional regulation of connexin32. Biochim Biophys Acta, 1491, 107-22.
    • (2000) Biochim Biophys Acta , vol.1491 , pp. 107-122
    • Piechocki, M.P.1    Toti, R.M.2    Fernstrom, M.J.3
  • 13
    • 0030768747 scopus 로고    scopus 로고
    • Upstream genomic sequence of the human connexin26 gene
    • Kiang, D.T., Tu, Z.J. and Lin, H.H. (1997) Upstream genomic sequence of the human connexin26 gene. Gene, 199, 165-71.
    • (1997) Gene , vol.199 , pp. 165-171
    • Kiang, D.T.1    Tu, Z.J.2    Lin, H.H.3
  • 14
    • 0006323604 scopus 로고    scopus 로고
    • Mapping and characterization of the basal promoter of human connexin 26 gene
    • Tu, Z.J. and Kiang, D.T. (1998) Mapping and characterization of the basal promoter of human connexin 26 gene. Biochim Biophys Acta, 1443, 169-81.
    • (1998) Biochim Biophys Acta , vol.1443 , pp. 169-181
    • Tu, Z.J.1    Kiang, D.T.2
  • 15
    • 0033510237 scopus 로고    scopus 로고
    • TPA induced expression and function of human connexin 26 by post-translational mechanisms in stably transfected neuroblastoma cells
    • Kojima, T., Srinivas, M., Fort, A. et al. (1999) TPA induced expression and function of human connexin 26 by post-translational mechanisms in stably transfected neuroblastoma cells. Cell Struct Funct, 24, 435-41.
    • (1999) Cell Struct Funct , vol.24 , pp. 435-441
    • Kojima, T.1    Srinivas, M.2    Fort, A.3
  • 16
    • 0027715358 scopus 로고
    • Breaking through the tight junction barrier
    • Gumbiner, B.M. (1993) Breaking through the tight junction barrier. J Cell Biol, 123, 1631-33.
    • (1993) J Cell Biol , vol.123 , pp. 1631-1633
    • Gumbiner, B.M.1
  • 17
    • 0031918158 scopus 로고    scopus 로고
    • Role of tight junctions in establishing and maintaining cell polarity
    • Cereijido, M., Valdés, J., Shoshani, L. et al. (1998) Role of tight junctions in establishing and maintaining cell polarity. Annu Rev Physiol, 60, 161-77.
    • (1998) Annu Rev Physiol , vol.60 , pp. 161-177
    • Cereijido, M.1    Valdés, J.2    Shoshani, L.3
  • 18
    • 0037336565 scopus 로고    scopus 로고
    • Signalling to and from tight junctions
    • Matter, K. and Balda, M.S. (2003) Signalling to and from tight junctions. Nat Rev Mol Cell Biol, 4, 225-36.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 225-236
    • Matter, K.1    Balda, M.S.2
  • 19
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita, K., Furuse, M., Fujimoto, K. et al. (1999) Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci U S A, 96, 511-16.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3
  • 20
    • 2642614521 scopus 로고    scopus 로고
    • Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration
    • Martin-Padura, I., Lostaglio, S. et al. (1998) Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration. J Cell Biol, 142, 117-27.
    • (1998) J Cell Biol , vol.142 , pp. 117-127
    • Martin-Padura, I.1    Lostaglio, S.2
  • 21
    • 0031052263 scopus 로고    scopus 로고
    • Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5
    • Bergelson, J.M., Cunningham, J.A. and Droguett, G. (1997) Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science, 275, 1320-23.
    • (1997) Science , vol.275 , pp. 1320-1323
    • Bergelson, J.M.1    Cunningham, J.A.2    Droguett, G.3
  • 22
    • 0037013246 scopus 로고    scopus 로고
    • A transmembrane tight junction protein selectively expressed on endothelial cells and platelets
    • Nasdala, I., Wolburg-Buchholz, K., Wolburg, H. et al. (2002) A transmembrane tight junction protein selectively expressed on endothelial cells and platelets. J Biol Chem, G277, 16294-303.
    • (2002) J Biol Chem , vol.G277 , pp. 16294-16303
    • Nasdala, I.1    Wolburg-Buchholz, K.2    Wolburg, H.3
  • 23
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • Ikenouchi, J., Furuse, M., Furuse, K. et al. (2005) Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J Cell Biol, 171, 939-45.
    • (2005) J Cell Biol , vol.171 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3
  • 24
    • 2442619064 scopus 로고    scopus 로고
    • The tight junction: A multifunctional complex
    • Schneeberger, E.E. and Lynch, R.D. (2004) The tight junction: a multifunctional complex. Am J Physiol Cell Physio, 286, C1213-28.
    • (2004) Am J Physiol Cell Physio , vol.286 , pp. C1213-C1228
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 25
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie, C.M. and Anderson, J.M. (2006) Claudins and epithelial paracellular transport. Annu Rev Physiol, 68, 403-30.
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-430
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 26
    • 34147219730 scopus 로고    scopus 로고
    • Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry
    • Evans, M.J., von Hahn, T., Tscherne, D.M. et al. (2007) Claudin-1 is a hepatitis C virus co-receptor required for a late step in entry. Nature, 446, 801-5.
    • (2007) Nature , vol.446 , pp. 801-805
    • Evans, M.J.1    von Hahn, T.2    Tscherne, D.M.3
  • 28
    • 34948890139 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A is critical for the formation of pseudocanaliculi and modulates E-cadherin expression in hepatic cells
    • Konopka, G., Tekiela, J., Iverson, M. et al. (2007) Junctional adhesion molecule-A is critical for the formation of pseudocanaliculi and modulates E-cadherin expression in hepatic cells. J Biol Chem, 282, 28137-48.
    • (2007) J Biol Chem , vol.282 , pp. 28137-28148
    • Konopka, G.1    Tekiela, J.2    Iverson, M.3
  • 29
    • 39149136881 scopus 로고    scopus 로고
    • JAM-A is both essential and inhibitory to development of hepatic polarity in WIF-B cells
    • Braiterman, L.T., Heffernan, S., Nyasae, L. et al. (2008) JAM-A is both essential and inhibitory to development of hepatic polarity in WIF-B cells. Am J Physiol Gastrointest Liver Physiol, 294, G576-88.
    • (2008) Am J Physiol Gastrointest Liver Physiol , vol.294 , pp. G576-G588
    • Braiterman, L.T.1    Heffernan, S.2    Nyasae, L.3
  • 30
    • 33747155076 scopus 로고    scopus 로고
    • ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation
    • Umeda, K., Ikenouchi, J., Katahira-Tayama, S. et al. (2006) ZO-1 and ZO-2 independently determine where claudins are polymerized in tight-junction strand formation. Cell, 126, 741-54.
    • (2006) Cell , vol.126 , pp. 741-754
    • Umeda, K.1    Ikenouchi, J.2    Katahira-Tayama, S.3
  • 31
    • 0027300689 scopus 로고
    • The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: CDNA cloning and immunoelectron microscopy
    • Itoh, M., Nagafuchi, A., Yonemura, S. et al. (1993) The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy. J Cell Biol, 121, 491-502.
    • (1993) J Cell Biol , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3
  • 32
    • 0035864383 scopus 로고    scopus 로고
    • Cx32 but not Cx26 is associated with tight junctions in primary cultures of rat hepatocytes
    • Kojima, T., Kokai, Y., Chiba, H. et al. (2001) Cx32 but not Cx26 is associated with tight junctions in primary cultures of rat hepatocytes. Exp Cell Res, 263, 193-201.
    • (2001) Exp Cell Res , vol.263 , pp. 193-201
    • Kojima, T.1    Kokai, Y.2    Chiba, H.3
  • 33
    • 0036343899 scopus 로고    scopus 로고
    • Cx32 formation and/or Cx32 mediated intercellular communication induce expression and function of tight junctions in hepatocytic cell line
    • Kojima, T., Spray, D.C., Kokai, Y. et al. (2002) Cx32 formation and/or Cx32 mediated intercellular communication induce expression and function of tight junctions in hepatocytic cell line. Exp Cell Res, 276, 40-51.
    • (2002) Exp Cell Res , vol.276 , pp. 40-51
    • Kojima, T.1    Spray, D.C.2    Kokai, Y.3
  • 34
    • 12944319328 scopus 로고    scopus 로고
    • Tight junction protein MAGI-1 is up-regulated by transfection with connexin 32 in an immortalized mouse hepatic cell line: CDNA microarray analysis
    • Murata, M., Kojima, T., Yamamoto, T. et al. (2005) Tight junction protein MAGI-1 is up-regulated by transfection with connexin 32 in an immortalized mouse hepatic cell line: cDNA microarray analysis. Cell Tissue Res, 319, 341-47.
    • (2005) Cell Tissue Res , vol.319 , pp. 341-347
    • Murata, M.1    Kojima, T.2    Yamamoto, T.3
  • 35
    • 34248224743 scopus 로고    scopus 로고
    • The gap junction protein connexin32 interacts with the Src homology 3/hook domain of discs large homolog 1
    • Duffy, H.S., Iacobas, I., Hotchkiss, K. et al. (2007) The gap junction protein connexin32 interacts with the Src homology 3/hook domain of discs large homolog 1. J Biol Chem, 282, 9789-96.
    • (2007) J Biol Chem , vol.282 , pp. 9789-9796
    • Duffy, H.S.1    Iacobas, I.2    Hotchkiss, K.3
  • 36
    • 0022545495 scopus 로고
    • Physiological properties of dissociated rat hepatocytes
    • Spray, D.C., Ginzberg, R.D., Morales, E.A. et al. (1986) Physiological properties of dissociated rat hepatocytes. J Cell Biol, 103, 135-44.
    • (1986) J Cell Biol , vol.103 , pp. 135-144
    • Spray, D.C.1    Ginzberg, R.D.2    Morales, E.A.3
  • 37
    • 0343058567 scopus 로고
    • Hepatocytes gap junctions are permeable to the second messengers inositol 1, 4, 5-trisphosphate and calcium ions
    • Sáez, J.C., Connor, J.A., Spray, D.C. et al. (1989) Hepatocytes gap junctions are permeable to the second messengers inositol 1, 4, 5-trisphosphate and calcium ions. Proc Natl Acad Sci U S A, 86, 2708-12.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 2708-2712
    • Sáez, J.C.1    Connor, J.A.2    Spray, D.C.3
  • 38
    • 77956692741 scopus 로고    scopus 로고
    • Intercellular calcium wave communication via gap junction-dependent and independent mechanisms
    • (ed. C. Peracchia), Academic Press, San Diego
    • Scemes, E., Suadicani, S.O. and Spray, D.C. (2000) Intercellular calcium wave communication via gap junction-dependent and independent mechanisms, in Current Topics in Membranes, Vol. 49 (ed. C. Peracchia), Academic Press, San Diego, pp. 145-73.
    • (2000) Current Topics in Membranes , vol.49 , pp. 145-173
    • Scemes, E.1    Suadicani, S.O.2    Spray, D.C.3
  • 39
    • 0347126459 scopus 로고    scopus 로고
    • Role of the p38 MAP-kinase signaling pathway for Cx32 and claudin-1 in the rat liver
    • Kojima, T., Yamamoto, T., Murata, M. et al. (2003) Role of the p38 MAP-kinase signaling pathway for Cx32 and claudin-1 in the rat liver. Cell Commun Adhes, 10, 1-7.
    • (2003) Cell Commun Adhes , vol.10 , pp. 1-7
    • Kojima, T.1    Yamamoto, T.2    Murata, M.3
  • 40
    • 0023433973 scopus 로고
    • Major loss of the 28 kDa protein of gap junction in proliferating hepatocytes
    • Dermietzel, R., Yancey, S.B., Traub, O. et al. (1987) Major loss of the 28 kDa protein of gap junction in proliferating hepatocytes. J Cell Biol, 105, 1928-34.
    • (1987) J Cell Biol , vol.105 , pp. 1928-1934
    • Dermietzel, R.1    Yancey, S.B.2    Traub, O.3
  • 41
    • 0022776965 scopus 로고
    • Reduced number of gap junctions in rat hepatocarcinomas detected by monoclonal antibody
    • Janssen-Timmen, U., Traub, O., Dermietzel, R. et al. (1986) Reduced number of gap junctions in rat hepatocarcinomas detected by monoclonal antibody. Carcinogenesis, 7, 1475-82.
    • (1986) Carcinogenesis , vol.7 , pp. 1475-1482
    • Janssen-Timmen, U.1    Traub, O.2    Dermietzel, R.3
  • 42
    • 0033002783 scopus 로고    scopus 로고
    • Genetic diseases and gene knockouts reveal diverse connexin functions
    • White, T.W. and Paul, D.L. (1999) Genetic diseases and gene knockouts reveal diverse connexin functions. Annu Rev Physiol, 61, 283-310.
    • (1999) Annu Rev Physiol , vol.61 , pp. 283-310
    • White, T.W.1    Paul, D.L.2
  • 43
    • 0343687249 scopus 로고    scopus 로고
    • Defective propagation of signals generated by sympathetic nerve stimulation in the liver of connexin32-deficient mice
    • Nelles, E., Butzler, C., Jung, D. et al. (1996) Defective propagation of signals generated by sympathetic nerve stimulation in the liver of connexin32-deficient mice. Proc Natl Acad Sci U S A, 93, 9565-70.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9565-9570
    • Nelles, E.1    Butzler, C.2    Jung, D.3
  • 44
    • 0031240077 scopus 로고    scopus 로고
    • High incidence of spontaneous and chemically induced liver tumors in mice deficient for connexin32
    • Temme, A., Buchmann, A., Gabriel, H.D. et al. (1997) High incidence of spontaneous and chemically induced liver tumors in mice deficient for connexin32. Curr Biol, 7, 713-16.
    • (1997) Curr Biol , vol.7 , pp. 713-716
    • Temme, A.1    Buchmann, A.2    Gabriel, H.D.3
  • 45
    • 0032773598 scopus 로고    scopus 로고
    • The effect of connexin32 null mutation on hepatocarcinogenesis in different mouse strains
    • Moennikes, O., Buchmann, A., Ott, T. et al. (1999) The effect of connexin32 null mutation on hepatocarcinogenesis in different mouse strains. Carcinogenesis, 20, 1379-82.
    • (1999) Carcinogenesis , vol.20 , pp. 1379-1382
    • Moennikes, O.1    Buchmann, A.2    Ott, T.3
  • 46
    • 0141590651 scopus 로고    scopus 로고
    • WY-14, 643-mediated promotion of hepatocarcinogenesis in connexin32-wild-type and connexin32-null mice
    • Moennikes, O., Stahl, S., Bannasch, P. et al. (2003) WY-14, 643-mediated promotion of hepatocarcinogenesis in connexin32-wild-type and connexin32-null mice. Carcinogenesis, 24, 1561-65.
    • (2003) Carcinogenesis , vol.24 , pp. 1561-1565
    • Moennikes, O.1    Stahl, S.2    Bannasch, P.3
  • 47
    • 0034796366 scopus 로고    scopus 로고
    • Gap junction expression and function in primary cultures of Cx32 deficient (KO) mouse hepatocytes
    • Kojima, T., Fort, A., Tao, M. et al. (2001) Gap junction expression and function in primary cultures of Cx32 deficient (KO) mouse hepatocytes. Am J Physiol, 281, G1004-13.
    • (2001) Am J Physiol , vol.281 , pp. G1004-G1013
    • Kojima, T.1    Fort, A.2    Tao, M.3
  • 48
    • 0034030450 scopus 로고    scopus 로고
    • The extent of synchronous initiation and termination of DNA synthesis in regenerating mouse liver is dependent on connexin32 expressing gap junctions
    • Temme, A., Ott, T., Dombrowski, F. et al. (2000) The extent of synchronous initiation and termination of DNA synthesis in regenerating mouse liver is dependent on connexin32 expressing gap junctions. J Hepatol, 32, 627-35.
    • (2000) J Hepatol , vol.32 , pp. 627-635
    • Temme, A.1    Ott, T.2    Dombrowski, F.3
  • 49
    • 3042849092 scopus 로고    scopus 로고
    • Delayed liver regeneration and increased susceptibility to chemical hepatocarcinogenesis in transgenic mice expressing a dominant-negative mutant of connexin32 only in the liver
    • Dagli, M.L., Yamasaki, H., Krutovskikh, V. et al. (2004) Delayed liver regeneration and increased susceptibility to chemical hepatocarcinogenesis in transgenic mice expressing a dominant-negative mutant of connexin32 only in the liver. Carcinogenesis, 25, 483-92.
    • (2004) Carcinogenesis , vol.25 , pp. 483-492
    • Dagli, M.L.1    Yamasaki, H.2    Krutovskikh, V.3
  • 50
    • 3042821628 scopus 로고    scopus 로고
    • Connexin32 dominant-negative mutant transgenic rats are resistant to hepatic damage by chemicals
    • Asamoto, M., Hokaiwado, N., Murasaki, T. et al. (2004) Connexin32 dominant-negative mutant transgenic rats are resistant to hepatic damage by chemicals. Hepatology, 40, 205-10.
    • (2004) Hepatology , vol.40 , pp. 205-210
    • Asamoto, M.1    Hokaiwado, N.2    Murasaki, T.3
  • 51
    • 0037036426 scopus 로고    scopus 로고
    • Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization
    • Sarma, J.D., Wang, F. and Koval, M. (2002) Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization. J Biol Chem, 277, 20911-18.
    • (2002) J Biol Chem , vol.277 , pp. 20911-20918
    • Sarma, J.D.1    Wang, F.2    Koval, M.3
  • 52
    • 20444387943 scopus 로고    scopus 로고
    • Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum
    • Maza, J., Das Sarma, J. and Koval, M. (2005) Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum. J Biol Chem, 280, 21115-21.
    • (2005) J Biol Chem , vol.280 , pp. 21115-21121
    • Maza, J.1    Das Sarma, J.2    Koval, M.3
  • 53
    • 0034234655 scopus 로고    scopus 로고
    • Targeting motifs and functional parameters governing the assembly of connexins into gap junctions
    • Martin, P.E., Steggles, J., Wilson, C. et al. (2000) Targeting motifs and functional parameters governing the assembly of connexins into gap junctions. Biochem J, 349, 281-87.
    • (2000) Biochem J , vol.349 , pp. 281-287
    • Martin, P.E.1    Steggles, J.2    Wilson, C.3
  • 54
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions
    • Shaw, R.M., Fay, A.J., Puthenveedu, M.A. et al. (2007) Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions. Cell, 128, 547-60.
    • (2007) Cell , vol.128 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3
  • 55
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf, U., Giepmans, B.N., Lopez, P. et al. (2002) Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc Natl Acad Sci U S A, 99, 10446-51.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3
  • 56
    • 0345865199 scopus 로고    scopus 로고
    • Tetracysteine genetic tags complexed with biarsenical ligands as a tool for investigating gap junction structure and dynamics
    • Sosinsky, G.E., Gaietta, G.M., Hand, G. et al. (2003) Tetracysteine genetic tags complexed with biarsenical ligands as a tool for investigating gap junction structure and dynamics. Cell Commun Adhes, 10, 181-86.
    • (2003) Cell Commun Adhes , vol.10 , pp. 181-186
    • Sosinsky, G.E.1    Gaietta, G.M.2    Hand, G.3
  • 57
    • 33846817049 scopus 로고    scopus 로고
    • Internalization of large double-membrane intercellular vesicles by a clathrin-dependent endocytic process
    • Piehl, M., Lehmann, C., Gumpert, A. et al. (2007) Internalization of large double-membrane intercellular vesicles by a clathrin-dependent endocytic process. Mol Biol Cell, 18, 337-47.
    • (2007) Mol Biol Cell , vol.18 , pp. 337-347
    • Piehl, M.1    Lehmann, C.2    Gumpert, A.3
  • 58
    • 14944353719 scopus 로고    scopus 로고
    • Trafficking pathways of Cx49-GFP in living mammalian cells
    • Breidert, S., Jacob, R., Ngezahayo, A. et al. (2005) Trafficking pathways of Cx49-GFP in living mammalian cells. Biol Chem, 386, 155-60.
    • (2005) Biol Chem , vol.386 , pp. 155-160
    • Breidert, S.1    Jacob, R.2    Ngezahayo, A.3
  • 59
    • 0032102036 scopus 로고    scopus 로고
    • Molecular analyses of tight junction physiology: Insight and paradoxes
    • Yap, A.S., Mullin, J.M. and Stevenson, B.R. (1998) Molecular analyses of tight junction physiology: insight and paradoxes. J Membr Biol, 163, 159-67.
    • (1998) J Membr Biol , vol.163 , pp. 159-167
    • Yap, A.S.1    Mullin, J.M.2    Stevenson, B.R.3
  • 60
    • 40949123971 scopus 로고    scopus 로고
    • Transforming growth factor-beta induces epithelial to mesenchymal transition by down-regulation of claudin-1 expression and the fence function in adult rat hepatocytes
    • Kojima, T., Takano, K., Yamamoto, T. et al. (2008) Transforming growth factor-beta induces epithelial to mesenchymal transition by down-regulation of claudin-1 expression and the fence function in adult rat hepatocytes. Liver Int, 28, 534-45.
    • (2008) Liver Int , vol.28 , pp. 534-545
    • Kojima, T.1    Takano, K.2    Yamamoto, T.3
  • 61
    • 4444335486 scopus 로고    scopus 로고
    • IL-1beta regulates expression of Cx32, occludin, and claudin-2 of rat hepatocytes via distinct signal transduction pathways
    • Yamamoto, T., Kojima, T., Murata, M. et al. (2004) IL-1beta regulates expression of Cx32, occludin, and claudin-2 of rat hepatocytes via distinct signal transduction pathways. Exp Cell Res, 299, 427-41.
    • (2004) Exp Cell Res , vol.299 , pp. 427-441
    • Yamamoto, T.1    Kojima, T.2    Murata, M.3
  • 62
    • 0038106228 scopus 로고    scopus 로고
    • Regulation of tight junctions during the epithelium-mesenchyme transition: Direct repression of the gene expression of claudins/occludin by Snail
    • Ikenouchi, J., Matsuda, M., Furuse, M. et al. (2003) Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins/occludin by Snail. J Cell Sci, 116, 1959-67.
    • (2003) J Cell Sci , vol.116 , pp. 1959-1967
    • Ikenouchi, J.1    Matsuda, M.2    Furuse, M.3
  • 63
    • 28344448267 scopus 로고    scopus 로고
    • Phosphorylation of ezrin enhances microvillus length via a p38 MAP-kinase pathway in an immortalized mouse hepatic cell line
    • Lan, M., Kojima, T., Murata, M. et al. (2006) Phosphorylation of ezrin enhances microvillus length via a p38 MAP-kinase pathway in an immortalized mouse hepatic cell line. Exp Cell Res, 312, 111-20.
    • (2006) Exp Cell Res , vol.312 , pp. 111-120
    • Lan, M.1    Kojima, T.2    Murata, M.3
  • 64
    • 0032752371 scopus 로고    scopus 로고
    • Requirement for ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells
    • Woo, P.L., Ching, D., Guan, Y. et al. (1999) Requirement for ras and phosphatidylinositol 3-kinase signaling uncouples the glucocorticoid-induced junctional organization and transepithelial electrical resistance in mammary tumor cells. J Biol Chem, 274, 32818-28.
    • (1999) J Biol Chem , vol.274 , pp. 32818-32828
    • Woo, P.L.1    Ching, D.2    Guan, Y.3
  • 65
    • 0034068866 scopus 로고    scopus 로고
    • Tight junctions are membrane microdomains
    • Nusrat, A., Parkos, C.A., Verkade, P. et al. (2000) Tight junctions are membrane microdomains. J Cell Sci, 113, 1771-81.
    • (2000) J Cell Sci , vol.113 , pp. 1771-1781
    • Nusrat, A.1    Parkos, C.A.2    Verkade, P.3
  • 66
    • 0036226069 scopus 로고    scopus 로고
    • Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells
    • Chen, Y.H., Lu, Q., Goodenough, D.A. and Jeansonne, B. (2002) Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells. Mol Biol Cell, 13, 1227-37.
    • (2002) Mol Biol Cell , vol.13 , pp. 1227-1237
    • Chen, Y.H.1    Lu, Q.2    Goodenough, D.A.3    Jeansonne, B.4
  • 67
    • 34249668828 scopus 로고    scopus 로고
    • Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer
    • Seth, A., Sheth, P., Elias, B.C. et al. (2007) Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer. J Biol Chem, 282, 11487-98.
    • (2007) J Biol Chem , vol.282 , pp. 11487-11498
    • Seth, A.1    Sheth, P.2    Elias, B.C.3
  • 68
    • 25844492029 scopus 로고    scopus 로고
    • Down-regulation of survival signaling through MAPK and Akt in occludin-deficient mouse hepatocytes in vitro
    • Murata, M., Kojima, T., Yamamoto, T. et al. (2005) Down-regulation of survival signaling through MAPK and Akt in occludin-deficient mouse hepatocytes in vitro. Exp Cell Res, 310, 140-51.
    • (2005) Exp Cell Res , vol.310 , pp. 140-151
    • Murata, M.1    Kojima, T.2    Yamamoto, T.3
  • 69
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Denker, B.M. and Nigam, S.K. (1998) Molecular structure and assembly of the tight junction. Am J Physiol, 274, F1-F9.
    • (1998) Am J Physiol , vol.274 , pp. F1-F9
    • Denker, B.M.1    Nigam, S.K.2
  • 71
    • 0032834070 scopus 로고    scopus 로고
    • PKC-dependent regulation of transepithelial resistance: Roles of MLC and MLC kinase
    • Turner, J.R., Angle, J.M., Black, E.D. et al. (1999) PKC-dependent regulation of transepithelial resistance: roles of MLC and MLC kinase. Am J Physiol, 277, C554-62.
    • (1999) Am J Physiol , vol.277 , pp. C554-C562
    • Turner, J.R.1    Angle, J.M.2    Black, E.D.3
  • 72
    • 0029161839 scopus 로고
    • Zonula occludens toxin (ZOT) modulates tight junctions through protein kinase C-dependent actin reorganization in vitro
    • Fasano, A., Fiorentini, C., Donelli, G. et al. (1995) Zonula occludens toxin (ZOT) modulates tight junctions through protein kinase C-dependent actin reorganization in vitro. J Clin Invest, 96, 710-20.
    • (1995) J Clin Invest , vol.96 , pp. 710-720
    • Fasano, A.1    Fiorentini, C.2    Donelli, G.3
  • 73
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA, and Rac1 small GTPases
    • Jou, T.-S., Schneeberger, E.E. and Nelson, W.J. (1998) Structural and functional regulation of tight junctions by RhoA, and Rac1 small GTPases. J Cell Biol, 142, 101-15.
    • (1998) J Cell Biol , vol.142 , pp. 101-115
    • Jou, T.-S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 74
    • 0032923590 scopus 로고    scopus 로고
    • Different lobular distributions of altered hepatocyte tight junctions in rat models of intrahepatic and extrahepatic cholestasis
    • Kawaguchi, T., Sakisaka, S., Sata, M. et al. (1999) Different lobular distributions of altered hepatocyte tight junctions in rat models of intrahepatic and extrahepatic cholestasis. Hepatology, 29, 205-16.
    • (1999) Hepatology , vol.29 , pp. 205-216
    • Kawaguchi, T.1    Sakisaka, S.2    Sata, M.3
  • 75
    • 18344370041 scopus 로고    scopus 로고
    • Dynamic changes in protein components of the tight junction during liver regeneration
    • Takaki, Y., Hirai, S., Manabe, N. et al. (2001) Dynamic changes in protein components of the tight junction during liver regeneration. Cell Tissue Res, 305, 399-409.
    • (2001) Cell Tissue Res , vol.305 , pp. 399-409
    • Takaki, Y.1    Hirai, S.2    Manabe, N.3
  • 76
    • 0037994064 scopus 로고    scopus 로고
    • Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT
    • Carlton, V.E., Harris, B.Z., Puffenberger, E.G. et al. (2003) Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet, 34, 91-96.
    • (2003) Nat Genet , vol.34 , pp. 91-96
    • Carlton, V.E.1    Harris, B.Z.2    Puffenberger, E.G.3
  • 77
    • 7644230747 scopus 로고    scopus 로고
    • Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: A tight junction disease
    • Hadj-Rabia, S., Baala, L., Vabres, P. et al. (2004) Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: a tight junction disease. Gastroenterology, 127, 1386-90.
    • (2004) Gastroenterology , vol.127 , pp. 1386-1390
    • Hadj-Rabia, S.1    Baala, L.2    Vabres, P.3
  • 78
    • 0033199904 scopus 로고    scopus 로고
    • Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin
    • Cordenonsi, M., Turco, F., D’atri, F. et al. (1999) Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin. Eur J Biochem, 264, 374-84.
    • (1999) Eur J Biochem , vol.264 , pp. 374-384
    • Cordenonsi, M.1    Turco, F.2    D’atri, F.3
  • 79
    • 0036435718 scopus 로고    scopus 로고
    • Gene expression of the tight junction protein occludin includes differential splicing and alternative promoter usage
    • Mankertz, J., Waller, J.S., Hillenbrand, B. et al. (2002) Gene expression of the tight junction protein occludin includes differential splicing and alternative promoter usage. Biochem Biophys Res Commun, 298, 657-66.
    • (2002) Biochem Biophys Res Commun , vol.298 , pp. 657-666
    • Mankertz, J.1    Waller, J.S.2    Hillenbrand, B.3
  • 80
    • 36049047582 scopus 로고    scopus 로고
    • Tight junction targeting and intracellular trafficking of occludin in polarized epithelial cells
    • Subramanian, V.S., Marchant, J.S., Ye, D. et al. (2007) Tight junction targeting and intracellular trafficking of occludin in polarized epithelial cells. Am J Physiol Cell Physiol, 293, C1717-26.
    • (2007) Am J Physiol Cell Physiol , vol.293 , pp. C1717-C1726
    • Subramanian, V.S.1    Marchant, J.S.2    Ye, D.3
  • 81
    • 4444253507 scopus 로고    scopus 로고
    • Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells
    • Yamada, A., Irie, K., Fukuhara, A. et al. (2004) Requirement of the actin cytoskeleton for the association of nectins with other cell adhesion molecules at adherens and tight junctions in MDCK cells. Genes Cells, 9, 843-55.
    • (2004) Genes Cells , vol.9 , pp. 843-855
    • Yamada, A.1    Irie, K.2    Fukuhara, A.3
  • 82
    • 0037155884 scopus 로고    scopus 로고
    • The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch
    • Traweger, A., Fang, D., Liu, Y.C. et al. (2002) The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch. J Biol Chem, 277, 10201-208.
    • (2002) J Biol Chem , vol.277 , pp. 10201-10208
    • Traweger, A.1    Fang, D.2    Liu, Y.C.3
  • 83
    • 24344457031 scopus 로고    scopus 로고
    • Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis
    • Shen, L. and Turner, J.R. (2005) Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. Mol Biol Cell, 16, 3919-36.
    • (2005) Mol Biol Cell , vol.16 , pp. 3919-3936
    • Shen, L.1    Turner, J.R.2
  • 84
    • 0347360336 scopus 로고    scopus 로고
    • Endocytosis of epithelial apical junctional proteins by a clathrin-mediated pathway into a unique storage compartment
    • Ivanov, A.I., Nusrat, A. and Parkos, C.A. (2004) Endocytosis of epithelial apical junctional proteins by a clathrin-mediated pathway into a unique storage compartment. Mol Biol Cell, 15, 176-88.
    • (2004) Mol Biol Cell , vol.15 , pp. 176-188
    • Ivanov, A.I.1    Nusrat, A.2    Parkos, C.A.3
  • 85
    • 19944433375 scopus 로고    scopus 로고
    • Rab13 mediates the continuous endocytic recycling of occludin to the cell surface
    • Morimoto, S., Nishimura, N., Terai, T. et al. (2005) Rab13 mediates the continuous endocytic recycling of occludin to the cell surface. J Biol Chem, 280, 2220-28.
    • (2005) J Biol Chem , vol.280 , pp. 2220-2228
    • Morimoto, S.1    Nishimura, N.2    Terai, T.3
  • 86
    • 33747817008 scopus 로고    scopus 로고
    • Requirement of nectin, but not cadherin, for formation of claudin-based tight junctions in annexin II-knockdown MDCK cells
    • Yamada, A., Fujita, N., Sato, T. et al. (2006) Requirement of nectin, but not cadherin, for formation of claudin-based tight junctions in annexin II-knockdown MDCK cells. Oncogene, 25, 5085-102.
    • (2006) Oncogene , vol.25 , pp. 5085-5102
    • Yamada, A.1    Fujita, N.2    Sato, T.3
  • 87
    • 1842426940 scopus 로고    scopus 로고
    • A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells
    • Matsuda, M., Kubo, A., Furuse, M. et al. (2004) A peculiar internalization of claudins, tight junction-specific adhesion molecules, during the intercellular movement of epithelial cells. J Cell Sci, 117, 1247-57.
    • (2004) J Cell Sci , vol.117 , pp. 1247-1257
    • Matsuda, M.1    Kubo, A.2    Furuse, M.3
  • 88
    • 7644230747 scopus 로고    scopus 로고
    • Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: A tight junction disease
    • Furuse, M., Hata, M., Furuse, K. et al. (2004) Claudin-1 gene mutations in neonatal sclerosing cholangitis associated with ichthyosis: a tight junction disease. Gastroenterology, 127, 1386-90.
    • (2004) Gastroenterology , vol.127 , pp. 1386-1390
    • Furuse, M.1    Hata, M.2    Furuse, K.3
  • 89
    • 38549086984 scopus 로고    scopus 로고
    • Hepatitis C virus entry into host cells
    • Helle, F. and Dubuisson, J. (2008) Hepatitis C virus entry into host cells. Cell Mol Life Sci, 65, 100-112.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 100-112
    • Helle, F.1    Dubuisson, J.2
  • 90
    • 41149117446 scopus 로고    scopus 로고
    • The tight junction proteins claudin-1, -6, and -9 are entry cofactors for hepatitis C virus
    • Meertens, L., Bertaux, C., Cukierman, L. et al. (2008) The tight junction proteins claudin-1, -6, and -9 are entry cofactors for hepatitis C virus. J Virol, 82, 3555-60.
    • (2008) J Virol , vol.82 , pp. 3555-3560
    • Meertens, L.1    Bertaux, C.2    Cukierman, L.3
  • 91
    • 0346220255 scopus 로고    scopus 로고
    • Structure-function analysis of reovirus binding to junctional adhesion molecule. 1. Implications for the mechanism of reovirus attachment
    • Forrest, J.C., Campbell, J.A., Schelling, P., Stehle, T. and Dermondy, T.S. (2003) Structure-function analysis of reovirus binding to junctional adhesion molecule. 1. Implications for the mechanism of reovirus attachment. J Biol Chem, 278, 48243-44.
    • (2003) J Biol Chem , vol.278 , pp. 48243-48244
    • Forrest, J.C.1    Campbell, J.A.2    Schelling, P.3    Stehle, T.4    Dermondy, T.S.5
  • 92
    • 0038185285 scopus 로고    scopus 로고
    • Crystal structure of human junctional adhesion molecule 1: Implications for reovirus binding
    • Prota, A.E., Campbell, J.A., Schelling, P. et al. (2003) Crystal structure of human junctional adhesion molecule 1: implications for reovirus binding. Proc Natl Acad Sci U S A, 100, 5366-71.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 5366-5371
    • Prota, A.E.1    Campbell, J.A.2    Schelling, P.3
  • 93
    • 16844382964 scopus 로고    scopus 로고
    • CAR: A virus receptor within the tight junction
    • Cyone, C.B. and Bergelson, J.M. (2005) CAR: a virus receptor within the tight junction. Adv Drug Del Rev, 57, 869-82.
    • (2005) Adv Drug Del Rev , vol.57 , pp. 869-882
    • Cyone, C.B.1    Bergelson, J.M.2
  • 94
    • 34547803161 scopus 로고    scopus 로고
    • Human hepatic stem cells from fetal and postnatal donors
    • Schmelzer, E., Zhang, L., Bruce, A. et al. (2007) Human hepatic stem cells from fetal and postnatal donors. J Exp Med, 204, 1973-87.
    • (2007) J Exp Med , vol.204 , pp. 1973-1987
    • Schmelzer, E.1    Zhang, L.2    Bruce, A.3
  • 95
    • 33749182067 scopus 로고    scopus 로고
    • The phenotypes of pluripotent human hepatic progenitors
    • Schmelzer, E., Wauthier, E. and Reid, L.M. (2006) The phenotypes of pluripotent human hepatic progenitors. Stem Cells, 24, 1852-58.
    • (2006) Stem Cells , vol.24 , pp. 1852-1858
    • Schmelzer, E.1    Wauthier, E.2    Reid, L.M.3
  • 96
    • 36349013698 scopus 로고    scopus 로고
    • Connexins induce and maintain tight junctions in epithelial cells
    • Kojima, T., Murata, M., Go, M. et al. (2007) Connexins induce and maintain tight junctions in epithelial cells. J Membr Biol, 217, 13-19.
    • (2007) J Membr Biol , vol.217 , pp. 13-19
    • Kojima, T.1    Murata, M.2    Go, M.3


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