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Volumn 41, Issue 3, 2000, Pages 283-301

Modification of tight junction function by protein kinase C isoforms

Author keywords

Bryostatin 1; Epithelia; Phorbol esters; Protein kinase C; Tight junction permeability

Indexed keywords

BODY FLUIDS; CELLS; ENZYMES; ESTERS; MECHANICAL PERMEABILITY;

EID: 0034734030     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-409X(00)00047-8     Document Type: Article
Times cited : (85)

References (160)
  • 1
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar M.G., Palade G.E. Junctional complexes in various epithelia. J. Cell Biol. 17:1963;376-412.
    • (1963) J. Cell Biol. , vol.17 , pp. 376-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 2
    • 0015499192 scopus 로고
    • Passive intercellular pathway in amphibian epithelia
    • Di Bona D.R. Passive intercellular pathway in amphibian epithelia. Nat. New Biol. 238:1972;179-181.
    • (1972) Nat. New Biol. , vol.238 , pp. 179-181
    • Di Bona, D.R.1
  • 3
    • 0025083621 scopus 로고
    • Generation and maintenance of epithelial cell polarity
    • Gumbiner B. Generation and maintenance of epithelial cell polarity. Curr. Opin. Cell Biol. 2:1990;881-887.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 881-887
    • Gumbiner, B.1
  • 4
    • 0015851773 scopus 로고
    • Pathways for movement of ions and water across toad urinary bladder. I. Anatomic site of transepithelial shunt pathways
    • Di Bona D.R., Civan M.M. Pathways for movement of ions and water across toad urinary bladder. I. Anatomic site of transepithelial shunt pathways. J. Membr. Biol. 12:1973;101-128.
    • (1973) J. Membr. Biol. , vol.12 , pp. 101-128
    • Di Bona, D.R.1    Civan, M.M.2
  • 5
    • 0020973004 scopus 로고
    • Functional properties of the paracellular pathway in some leaky epithelia
    • Kottra G., Fromter E. Functional properties of the paracellular pathway in some leaky epithelia. J. Exp. Biol. 106:1983;217-229.
    • (1983) J. Exp. Biol. , vol.106 , pp. 217-229
    • Kottra, G.1    Fromter, E.2
  • 6
    • 0019391755 scopus 로고
    • Tumor promoter-induced changes in the permeability of epithelial cell tight junctions
    • Ojakian G.K. Tumor promoter-induced changes in the permeability of epithelial cell tight junctions. Cell. 23:1981;95-103.
    • (1981) Cell , vol.23 , pp. 95-103
    • Ojakian, G.K.1
  • 7
    • 0022970053 scopus 로고
    • 1 renal epithelial tight junctions and transepithelial fluxes
    • 1 renal epithelial tight junctions and transepithelial fluxes. Am. J. Physiol. 251:1986;C597-C602.
    • (1986) Am. J. Physiol. , vol.251
    • Mullin, J.M.1    O'Brien, T.G.2
  • 8
    • 0028258243 scopus 로고
    • Reversible disassembly of an intestinal epithelial monolayer by prolonged exposure to phorbol ester
    • Hecht G., Robinson B., Koutsouris A. Reversible disassembly of an intestinal epithelial monolayer by prolonged exposure to phorbol ester. Am. J. Physiol. 266:1994;G214-G221.
    • (1994) Am. J. Physiol. , vol.266
    • Hecht, G.1    Robinson, B.2    Koutsouris, A.3
  • 9
    • 0027133307 scopus 로고
    • Regulation of paracellular permeability in Caco-2 cell monolayers by protein kinase C
    • Stenson W.F., Easom R.A., Riehl T.E., Turk J. Regulation of paracellular permeability in Caco-2 cell monolayers by protein kinase C. Am. J. Physiol. 265:1993;G955-G962.
    • (1993) Am. J. Physiol. , vol.265
    • Stenson, W.F.1    Easom, R.A.2    Riehl, T.E.3    Turk, J.4
  • 10
    • 0032005048 scopus 로고    scopus 로고
    • Tumor necrosis factor a increases sodium and chloride conductance across the tight junction of CaCo-2 BBE, a human intestinal cell line
    • Marano C.W., Lewis S.A., Garulacan L.A., Peralta Soler A., Mullin J.M. Tumor necrosis factor a increases sodium and chloride conductance across the tight junction of CaCo-2 BBE, a human intestinal cell line. J. Membr. Biol. 161:1998;263-274.
    • (1998) J. Membr. Biol. , vol.161 , pp. 263-274
    • Marano, C.W.1    Lewis, S.A.2    Garulacan, L.A.3    Peralta Soler, A.4    Mullin, J.M.5
  • 11
    • 0025218790 scopus 로고
    • The effect of tumor necrosis factor on epithelial tight junctions and transepithelial permeability
    • Mullin J.M., Snock K.V. The effect of tumor necrosis factor on epithelial tight junctions and transepithelial permeability. Cancer Res. 50:1990;2172-2176.
    • (1990) Cancer Res. , vol.50 , pp. 2172-2176
    • Mullin, J.M.1    Snock, K.V.2
  • 12
    • 0024553788 scopus 로고
    • Interferon-gamma directly affects barrier function of cultured intestinal epithelial monolayers
    • Madara J.L., Stafford J. Interferon-gamma directly affects barrier function of cultured intestinal epithelial monolayers. J. Clin. Invest. 83:1989;724-727.
    • (1989) J. Clin. Invest. , vol.83 , pp. 724-727
    • Madara, J.L.1    Stafford, J.2
  • 13
    • 0017891781 scopus 로고
    • Polarized monolayers formed by epithelial cells on a permeable and translucent support
    • Cereijido M., Robbins E.S., Dolan W.J., Rotunno C.A., Sabatini D.D. Polarized monolayers formed by epithelial cells on a permeable and translucent support. J. Cell Biol. 77:1978;853-880.
    • (1978) J. Cell Biol. , vol.77 , pp. 853-880
    • Cereijido, M.1    Robbins, E.S.2    Dolan, W.J.3    Rotunno, C.A.4    Sabatini, D.D.5
  • 14
    • 0019275289 scopus 로고
    • Experimental modulation of occluding junctions in a cultured transporting epithelium
    • Martinez-Palomo A., Meza I., Beaty G., Cereijido M. Experimental modulation of occluding junctions in a cultured transporting epithelium. J. Cell Biol. 87:1980;736-745.
    • (1980) J. Cell Biol. , vol.87 , pp. 736-745
    • Martinez-Palomo, A.1    Meza, I.2    Beaty, G.3    Cereijido, M.4
  • 16
    • 0026346859 scopus 로고
    • Effect of reversible ATP depletion on tight junction integrity in LLC-PK1 cells
    • Canfield P.E., Geerdes A.M., Molitoris B.A. Effect of reversible ATP depletion on tight junction integrity in LLC-PK1 cells. Am. J. Physiol. 261:1991;F1038-F1045.
    • (1991) Am. J. Physiol. , vol.261
    • Canfield, P.E.1    Geerdes, A.M.2    Molitoris, B.A.3
  • 18
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • Staehlin L.A. Structure and function of intercellular junctions. Int. Rev. Cytol. 39:1974;191-283.
    • (1974) Int. Rev. Cytol. , vol.39 , pp. 191-283
    • Staehlin, L.A.1
  • 19
    • 0015994540 scopus 로고
    • The structure of the zonula occludens. A single fibril model based on freeze-fracture
    • Wade J.B., Karnovsky X. The structure of the zonula occludens. A single fibril model based on freeze-fracture. J. Cell Biol. 60:1974;168-180.
    • (1974) J. Cell Biol. , vol.60 , pp. 168-180
    • Wade, J.B.1    Karnovsky, X.2
  • 20
    • 0029087066 scopus 로고
    • Molecular environment of ZO-1 in epithelial and non-epithelial cells
    • Howarth A.G., Stevenson B.R. Molecular environment of ZO-1 in epithelial and non-epithelial cells. Cell Motil. Cytoskeleton. 31:1995;323-332.
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 323-332
    • Howarth, A.G.1    Stevenson, B.R.2
  • 21
    • 0007677693 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes
    • Fujimoto K. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes. J. Cell Biol. 123:1995;1777-1788.
    • (1995) J. Cell Biol. , vol.123 , pp. 1777-1788
    • Fujimoto, K.1
  • 22
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction-associated integral protein, induces the formation of multilamellar bodies bearing tight junction-like structures
    • Furuse M., Fujimoto K., Sato N., Hirase T., Tsukita S., Tsukita S. Overexpression of occludin, a tight junction-associated integral protein, induces the formation of multilamellar bodies bearing tight junction-like structures. J. Cell Sci. 109:1996;429-435.
    • (1996) J. Cell Sci. , vol.109 , pp. 429-435
    • Furuse, M.1    Fujimoto, K.2    Sato, N.3    Hirase, T.4    Tsukita, S.5    Tsukita, S.6
  • 24
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S. 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.
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 26
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson B.R., Siliciano J.D., Mooseker M.S., Goodenough D.A. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol. 103:1986;755-766.
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 27
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junctional protein ZO-1
    • Gumbiner B., Lowenkopf T., Apatira D. Identification of a 160-kDa polypeptide that binds to the tight junctional protein ZO-1. Proc. Natl. Acad. Sci. USA. 88:1991;3460-3464.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 28
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2 a tight junction protein homologous to ZO-1 and the Drosophila Discs-large tumor suppressor protein
    • Jesaitis L.A., Goodenough D.A. Molecular characterization and tissue distribution of ZO-2 a tight junction protein homologous to ZO-1 and the Drosophila Discs-large tumor suppressor protein. J. Cell Biol. 124:1994;949-961.
    • (1994) J. Cell Biol. , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 29
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • Haskins J., Gu L., Wittchen E.S., Hibbard J., Stevenson B. ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J. Cell Biol. 141:1998;199-208.
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.5
  • 31
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2
    • Zhong Y., Saitoh T., Minase N., Sawanda N., Enomoto K., Mori M. Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2. J. Cell Biol. 120:1993;477-483.
    • (1993) J. Cell Biol. , vol.120 , pp. 477-483
    • Zhong, Y.1    Saitoh, T.2    Minase, N.3    Sawanda, N.4    Enomoto, K.5    Mori, M.6
  • 34
    • 0023176321 scopus 로고
    • Intestinal absorptive cell tight junctions are linked to the cytoskeleton
    • Madara J.L. Intestinal absorptive cell tight junctions are linked to the cytoskeleton. Am. J. Physiol. 253:1987;C171-C175.
    • (1987) Am. J. Physiol. , vol.253
    • Madara, J.L.1
  • 35
    • 0023949917 scopus 로고
    • Functional coupling of tight junctions and microfilaments in T84 monolayers
    • Madara J.L., Stafford J., Barenberg D., Carlson S. Functional coupling of tight junctions and microfilaments in T84 monolayers. Am. J. Physiol. 254:1988;G416-G423.
    • (1988) Am. J. Physiol. , vol.254
    • Madara, J.L.1    Stafford, J.2    Barenberg, D.3    Carlson, S.4
  • 36
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning A.S., Jameson B.J., Jesaitis L.A., Anderson J.M. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J. Biol. Chem. 273:1998;29745-29753.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 37
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson J.M., Van Itallie C.M. Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269:1995;G467-G475.
    • (1995) Am. J. Physiol. , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 38
    • 0026752739 scopus 로고
    • Structure, function, and regulation of cellular tight junctions
    • Schneeberger E.E., Lynch R.D. Structure, function, and regulation of cellular tight junctions. Am. J. Physiol. 262:1992;L647-L661.
    • (1992) Am. J. Physiol. , vol.262
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 39
    • 0031695576 scopus 로고    scopus 로고
    • Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion
    • Gopalakrishnan S., Raman N., Atkinson S., Marrs J.A. Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion. Am. J. Physiol. 275:1998;C798-C809.
    • (1998) Am. J. Physiol. , vol.275
    • Gopalakrishnan, S.1    Raman, N.2    Atkinson, S.3    Marrs, J.A.4
  • 41
    • 0026338562 scopus 로고
    • The role of phosphorylation in development of tight junctions in cultured renal epithelia (MDCK) cells
    • Nigam S.K., Denisenko N., Rodriguez-Boulan E., Citi S. The role of phosphorylation in development of tight junctions in cultured renal epithelia (MDCK) cells. Biochem. Biophys. Res. Commun. 181:1991;548-553.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 548-553
    • Nigam, S.K.1    Denisenko, N.2    Rodriguez-Boulan, E.3    Citi, S.4
  • 42
    • 0029883798 scopus 로고    scopus 로고
    • Identification of isoforms of G proteins that colocalize with tight junctions
    • Dodane V., Kachar B. Identification of isoforms of G proteins that colocalize with tight junctions. J. Membr. Biol. 149:1996;199-209.
    • (1996) J. Membr. Biol. , vol.149 , pp. 199-209
    • Dodane, V.1    Kachar, B.2
  • 43
    • 0028831331 scopus 로고
    • Ionomycin and PDBU increase MDCK monolayer permeability independently of myosin light chain phosphorylation
    • Shasby D.M., Kamath J.M., Moy A.B., Shasby S.S. Ionomycin and PDBU increase MDCK monolayer permeability independently of myosin light chain phosphorylation. Am. J. Physiol. 269:1995;L144-L150.
    • (1995) Am. J. Physiol. , vol.269
    • Shasby, D.M.1    Kamath, J.M.2    Moy, A.B.3    Shasby, S.S.4
  • 44
    • 85058253651 scopus 로고    scopus 로고
    • Interaction of PKC and NOS in signal transduction of microvascular hyperpermeability
    • Huang Q.B., Yuan Y. Interaction of PKC and NOS in signal transduction of microvascular hyperpermeability. Am. J. Physiol. 275:1997;C798-C809.
    • (1997) Am. J. Physiol. , vol.275
    • Huang, Q.B.1    Yuan, Y.2
  • 45
    • 0032555295 scopus 로고    scopus 로고
    • Involvement of Gαi2 in the maintenance and biogenesis of epithelial cell tight junctions
    • Saha C., Nigam S.K., Denker B.M. Involvement of Gαi2 in the maintenance and biogenesis of epithelial cell tight junctions. J. Biol. Chem. 273:1998;21629-21633.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21629-21633
    • Saha, C.1    Nigam, S.K.2    Denker, B.M.3
  • 46
    • 33750841811 scopus 로고    scopus 로고
    • Protein kinase C modulates microvascular permeability through nitric oxide synthase
    • Ramirez M.M., Kim D.D., Duran W.N. Protein kinase C modulates microvascular permeability through nitric oxide synthase. Am. J. Physiol. 271:1996;H1702-H1705.
    • (1996) Am. J. Physiol. , vol.271
    • Ramirez, M.M.1    Kim, D.D.2    Duran, W.N.3
  • 48
    • 0031087537 scopus 로고    scopus 로고
    • Dual role for AlF4-sensitive G proteins in the function of T84 epithelial cells: Transport and barrier effects
    • Ries J., Stein J., Traynor-Kaplan A.E., Barrett K.E. Dual role for AlF4-sensitive G proteins in the function of T84 epithelial cells: transport and barrier effects. Am. J. Physiol. 272:1997;C794-C803.
    • (1997) Am. J. Physiol. , vol.272
    • Ries, J.1    Stein, J.2    Traynor-Kaplan, A.E.3    Barrett, K.E.4
  • 50
    • 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., Hammer E., Martinucci G., Meggio F., Citi S. Xenopus laevis occludin-identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin. Eur. J. Biochem. 264:1999;374-384.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 374-384
    • Cordenonsi, M.1    Turco, F.2    D'Atri, F.3    Hammer, E.4    Martinucci, G.5    Meggio, F.6    Citi, S.7
  • 56
    • 0028322134 scopus 로고
    • Relationship of serine/threonine phosphorylation/dephosphorylation signaling to glucocorticoid regulation of tight junction permeability and ZO-1 distribution in nontransformed mammary epithelial cells
    • Singer K.L., Stevenson B.R., Woo P.L., Firestone G.L. Relationship of serine/threonine phosphorylation/dephosphorylation signaling to glucocorticoid regulation of tight junction permeability and ZO-1 distribution in nontransformed mammary epithelial cells. J. Biol. Chem. 269:1994;16108-16115.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16108-16115
    • Singer, K.L.1    Stevenson, B.R.2    Woo, P.L.3    Firestone, G.L.4
  • 57
    • 0029664468 scopus 로고    scopus 로고
    • 2+-independent regulation of the thyroid epithelial junction complex by protein kinases
    • 2+-independent regulation of the thyroid epithelial junction complex by protein kinases. Exp. Cell Res. 225:1996;1-11.
    • (1996) Exp. Cell Res. , vol.225 , pp. 1-11
    • Nilsson, M.1    Fagman, H.2    Ericson, L.E.3
  • 58
    • 0002895666 scopus 로고
    • The relationship between structure and function of tight junctions
    • M. Cereijido. Boca Raton, FL: CRC Press
    • Gonzalez-Mariscal L. The relationship between structure and function of tight junctions. Cereijido M. Tight Junctions. 1991;67-76 CRC Press, Boca Raton, FL.
    • (1991) Tight Junctions , pp. 67-76
    • Gonzalez-Mariscal, L.1
  • 59
    • 0030946064 scopus 로고    scopus 로고
    • Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly
    • Tsukamoto T., Nigam S.K. Tight junction proteins form large complexes and associate with the cytoskeleton in an ATP depletion model for reversible junction assembly. J. Biol. Chem. 272:1997;16133-16139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16133-16139
    • Tsukamoto, T.1    Nigam, S.K.2
  • 60
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara A., Furuse M., Saitou M., Ando-Akatsuka Y., Tsukita S. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137:1997;1393-1401.
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 61
    • 0031809132 scopus 로고    scopus 로고
    • Increased tyrosine phosphorylation causes redistribution of adherens junction and tight junction proteins and perturbs paracellular barrier function in MDCK epithelia
    • Collares-Buzato C.B., Jepson M.A., Simmons N.L., Hirst B.H. Increased tyrosine phosphorylation causes redistribution of adherens junction and tight junction proteins and perturbs paracellular barrier function in MDCK epithelia. Eur. J. Cell Biol. 76:1998;85-92.
    • (1998) Eur. J. Cell Biol. , vol.76 , pp. 85-92
    • Collares-Buzato, C.B.1    Jepson, M.A.2    Simmons, N.L.3    Hirst, B.H.4
  • 62
    • 0030994411 scopus 로고    scopus 로고
    • Different size limitations for increased transepithelial paracellular solute flux across phorbol ester and tumor necrosis factor-treated epithelial cell sheets
    • Mullin J.M., Marano C.W., Laughlin K.V., Nuciglio M., Stevenson B.R., Peralta Soler A. Different size limitations for increased transepithelial paracellular solute flux across phorbol ester and tumor necrosis factor-treated epithelial cell sheets. J. Cell Physiol. 171:1997;226-233.
    • (1997) J. Cell Physiol. , vol.171 , pp. 226-233
    • Mullin, J.M.1    Marano, C.W.2    Laughlin, K.V.3    Nuciglio, M.4    Stevenson, B.R.5    Peralta Soler, A.6
  • 63
    • 0032102036 scopus 로고    scopus 로고
    • Molecular analyses of tight junctional physiology: Insights and paradoxes
    • Yap A.S., Mullin J.M., Stevenson B.R. Molecular analyses of tight junctional physiology: insights and paradoxes. J. Membr. Biol. 163:1998;159-167.
    • (1998) J. Membr. Biol. , vol.163 , pp. 159-167
    • Yap, A.S.1    Mullin, J.M.2    Stevenson, B.R.3
  • 64
    • 0027528474 scopus 로고
    • VIP, serotonin, and epinephrine modulate the ion selectivity of tight junctions of goldfish intestine
    • Bakker R., Dekker K., DeJong H.R., Groot J.A. VIP, serotonin, and epinephrine modulate the ion selectivity of tight junctions of goldfish intestine. Am. J. Physiol. 264:1993;R362-R368.
    • (1993) Am. J. Physiol. , vol.264
    • Bakker, R.1    Dekker, K.2    Dejong, H.R.3    Groot, J.A.4
  • 65
    • 0027757028 scopus 로고
    • 2+. I. Microscopic and general electrophysiological observations
    • 2+. I. Microscopic and general electrophysiological observations. Pflug. Arch. 425:1993;528-534.
    • (1993) Pflug. Arch. , vol.425 , pp. 528-534
    • Kottra, G.1    Hasse, W.2    Frömter, E.3
  • 66
    • 0031944543 scopus 로고    scopus 로고
    • Routes and mechanism of fluid transport by epithelia
    • Spring K.R. Routes and mechanism of fluid transport by epithelia. Annu. Rev. Physiol. 60:1998;105-119.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 105-119
    • Spring, K.R.1
  • 67
    • 0023748364 scopus 로고
    • Voltage- And time dependence of apical membrane conductance during current clamp in Necturus gallbladder epithelium
    • Stoddard J.S., Reuss L. Voltage- and time dependence of apical membrane conductance during current clamp in Necturus gallbladder epithelium. J. Membr. Biol. 103:1988;191-204.
    • (1988) J. Membr. Biol. , vol.103 , pp. 191-204
    • Stoddard, J.S.1    Reuss, L.2
  • 69
    • 0027380638 scopus 로고
    • Submembranous junctional plaque proteins include potential tumor suppressor molecules
    • Tsukida S., Itoh M., Nagafuchi A., Yonemure S., Tsukita S. Submembranous junctional plaque proteins include potential tumor suppressor molecules. J. Cell Biol. 123:1993;1049-1053.
    • (1993) J. Cell Biol. , vol.123 , pp. 1049-1053
    • Tsukida, S.1    Itoh, M.2    Nagafuchi, A.3    Yonemure, S.4    Tsukita, S.5
  • 70
    • 0028008838 scopus 로고
    • A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells
    • Zahraoui A., Joberty G., Arpin M., Fontaine J., Hellio R., Tavitian A., Louvard D. A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells. J. Cell Biol. 124:1994;101-115.
    • (1994) J. Cell Biol. , vol.124 , pp. 101-115
    • Zahraoui, A.1    Joberty, G.2    Arpin, M.3    Fontaine, J.4    Hellio, R.5    Tavitian, A.6    Louvard, D.7
  • 73
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • Takaishi K., Sasaki T., Kotani H., Nishioka H., Takai Y. Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J. Cell Biol. 139:1997;1047-1059.
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 74
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature. 334:1988;661-665.
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 75
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9:1995;484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 76
    • 0025885413 scopus 로고
    • Differential recovery of protein kinase C-α And -ε isozymes after long-term phorbol ester treatment in rat mesangial cells
    • Huwiler A., Fabbro D., Pfeilschifter J. Differential recovery of protein kinase C-α and -ε isozymes after long-term phorbol ester treatment in rat mesangial cells. Biochem. Biophys. Res. Commun. 180:1991;1422-1428.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1422-1428
    • Huwiler, A.1    Fabbro, D.2    Pfeilschifter, J.3
  • 77
    • 0027070452 scopus 로고
    • Effect of tumor promoting phorbal ester thrombin and vasopressin on translocation of three distinct protein kinase C isoforms in human platelets and regulation by calcium
    • Crabos M., Fabbro D., Stabel S., Erne P. Effect of tumor promoting phorbal ester thrombin and vasopressin on translocation of three distinct protein kinase C isoforms in human platelets and regulation by calcium. Biochem. J. 288:1992;891-896.
    • (1992) Biochem. J. , vol.288 , pp. 891-896
    • Crabos, M.1    Fabbro, D.2    Stabel, S.3    Erne, P.4
  • 78
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science. 258:1992;607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 79
    • 0027297104 scopus 로고
    • Characterization of ligand and substrate specificity for the calcium-dependent and calcium-independent protein kinase C isozymes
    • Kazanietz M.G., Areces L.B., Bahador A., Mischak H., Goodnight J., Mushinski J.F., Blumberg P. Characterization of ligand and substrate specificity for the calcium-dependent and calcium-independent protein kinase C isozymes. Mol. Pharmacol. 44:1993;298-307.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 298-307
    • Kazanietz, M.G.1    Areces, L.B.2    Bahador, A.3    Mischak, H.4    Goodnight, J.5    Mushinski, J.F.6    Blumberg, P.7
  • 81
    • 0019285495 scopus 로고
    • Tumor promoters and the mechanism of tumor promotion
    • Diamond L., O'Brien T.G., Baird W.M. Tumor promoters and the mechanism of tumor promotion. Adv. Cancer Res. 32:1980;1-74.
    • (1980) Adv. Cancer Res. , vol.32 , pp. 1-74
    • Diamond, L.1    O'Brien, T.G.2    Baird, W.M.3
  • 82
    • 77954577665 scopus 로고
    • The function and mechanism of promoters of carcinogenesis
    • Boutwell R.K. The function and mechanism of promoters of carcinogenesis. CRC Crit. Rev. Toxicol. 2:1974;419-443.
    • (1974) CRC Crit. Rev. Toxicol. , vol.2 , pp. 419-443
    • Boutwell, R.K.1
  • 83
    • 0021137833 scopus 로고
    • Turnover of inositol phospholipids and signal transduction
    • Nishizuka Y. Turnover of inositol phospholipids and signal transduction. Science. 225:1984;1365-1370.
    • (1984) Science , vol.225 , pp. 1365-1370
    • Nishizuka, Y.1
  • 84
    • 0028958758 scopus 로고
    • The protein kinase C inhibitor, bisindolylmaleimide inhibits the TPA-induced but not the TNF-induced increase in LLC-PK1 transepithelial permeability
    • Marano C.W., Laughlin K.V., Russo L.M., Mullin J.M. The protein kinase C inhibitor, bisindolylmaleimide inhibits the TPA-induced but not the TNF-induced increase in LLC-PK1 transepithelial permeability. Biochem. Biophys. Res. Commun. 209:1995;669-676.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 669-676
    • Marano, C.W.1    Laughlin, K.V.2    Russo, L.M.3    Mullin, J.M.4
  • 85
    • 0025164934 scopus 로고
    • The effect of the teleocidin and aplysiatoxin tumor promoters on epithelial tight junctions and transepithelial permeability
    • Mullin J.M., McGinn M.T., Snock K.V., Imaizumi S. The effect of the teleocidin and aplysiatoxin tumor promoters on epithelial tight junctions and transepithelial permeability. Carcinogenesis. 11:1990;377-385.
    • (1990) Carcinogenesis , vol.11 , pp. 377-385
    • Mullin, J.M.1    McGinn, M.T.2    Snock, K.V.3    Imaizumi, S.4
  • 86
    • 0023945559 scopus 로고
    • Effects of diacylglycerols on LLC-PK1 renal epithelia: Similarity to phorbol ester tumor promoters
    • Mullin J.M., McGinn M.T. Effects of diacylglycerols on LLC-PK1 renal epithelia: similarity to phorbol ester tumor promoters. J. Cell Physiol. 134:1988;357-366.
    • (1988) J. Cell Physiol. , vol.134 , pp. 357-366
    • Mullin, J.M.1    McGinn, M.T.2
  • 90
    • 0026759470 scopus 로고
    • Cellular variability in the development of tight junctions after activation of protein kinase C
    • Ellis B., Schneeberger E.E., Rabito C.A. Cellular variability in the development of tight junctions after activation of protein kinase C. Am. J. Physiol. 263:1992;F293-F300.
    • (1992) Am. J. Physiol. , vol.263
    • Ellis, B.1    Schneeberger, E.E.2    Rabito, C.A.3
  • 91
    • 0030053505 scopus 로고    scopus 로고
    • Protein kinase C β1 overexpression augments phorbol ester-induced increase in endothelial permeability
    • Nagpala P.G., Malik A.B. Protein kinase C β1 overexpression augments phorbol ester-induced increase in endothelial permeability. J. Cell. Physiol. 166:1996;249-255.
    • (1996) J. Cell. Physiol. , vol.166 , pp. 249-255
    • Nagpala, P.G.1    Malik, A.B.2
  • 92
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y., Hirose T., Tamai Y., Hirai S., Nagashima Y., Fujimoto T., Tabuse Y., Kemphues K.J., Ohno S. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143:1998;95-106.
    • (1998) J. Cell Biol. , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5    Fujimoto, T.6    Tabuse, Y.7    Kemphues, K.J.8    Ohno, S.9
  • 93
    • 0028142091 scopus 로고
    • Activation of protein kinase C isoenzymes is associated with post-mitotic events in intestinal epithelial cells in situ
    • Saxon M.L., Zhao X., Black J.D. Activation of protein kinase C isoenzymes is associated with post-mitotic events in intestinal epithelial cells in situ. J. Cell Biol. 126:1994;747-763.
    • (1994) J. Cell Biol. , vol.126 , pp. 747-763
    • Saxon, M.L.1    Zhao, X.2    Black, J.D.3
  • 94
    • 0023880172 scopus 로고
    • Protein kinase C as the receptor for the phorbol ester tumor promoters: Sixth Rhoads memorial award lecture
    • Blumberg P.M. Protein kinase C as the receptor for the phorbol ester tumor promoters: sixth Rhoads memorial award lecture. Cancer Res. 48:1988;1-8.
    • (1988) Cancer Res. , vol.48 , pp. 1-8
    • Blumberg, P.M.1
  • 95
    • 0022375243 scopus 로고
    • Bryostatins: Potent, new mitogens that mimic phorbol ester tumor promoters
    • Smith J.B., Smith L., Pettit G.R. Bryostatins: potent, new mitogens that mimic phorbol ester tumor promoters. Biochem. Biophys. Res. Commun. 132:1985;939-945.
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , pp. 939-945
    • Smith, J.B.1    Smith, L.2    Pettit, G.R.3
  • 96
    • 0010543768 scopus 로고
    • Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester induced differentiation of human promyelocytic leukemia cells HL-60
    • Kraft A.S., Smith J.B., Berkow R.L. Bryostatin, an activator of the calcium phospholipid-dependent protein kinase, blocks phorbol ester induced differentiation of human promyelocytic leukemia cells HL-60. Proc. Natl. Acad. Sci. USA. 83:1986;1334-1338.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1334-1338
    • Kraft, A.S.1    Smith, J.B.2    Berkow, R.L.3
  • 97
    • 0030807576 scopus 로고    scopus 로고
    • Bryostatin 1: Differentiating agent from the depths
    • Stone R. Bryostatin 1: differentiating agent from the depths. Leuk. Res. 21:1997;399-401.
    • (1997) Leuk. Res. , vol.21 , pp. 399-401
    • Stone, R.1
  • 98
    • 0030856559 scopus 로고    scopus 로고
    • Bryostatin 1 induces biphasic activation of protein kinase D in intact cells
    • Matthews S., Pettit G.R., Rozengurt E. Bryostatin 1 induces biphasic activation of protein kinase D in intact cells. J. Biol. Chem. 272:1997;20245-20250.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20245-20250
    • Matthews, S.1    Pettit, G.R.2    Rozengurt, E.3
  • 99
    • 0028055160 scopus 로고
    • Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts
    • Szallasi Z., Smith C.B., Pettit G.R., Blumberg P.M. Differential regulation of protein kinase C isozymes by bryostatin 1 and phorbol 12-myristate 13-acetate in NIH 3T3 fibroblasts. J. Biol. Chem. 269:1994;2118-2154.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2118-2154
    • Szallasi, Z.1    Smith, C.B.2    Pettit, G.R.3    Blumberg, P.M.4
  • 100
    • 33745334429 scopus 로고    scopus 로고
    • Dephosphorylation of protein kinase C contributes to downregulation by bryostatin
    • Lee H., Smith L., Pettit G.R., Smith J. Dephosphorylation of protein kinase C contributes to downregulation by bryostatin. Am. J. Physiol. 271:1996;C304-C311.
    • (1996) Am. J. Physiol. , vol.271
    • Lee, H.1    Smith, L.2    Pettit, G.R.3    Smith, J.4
  • 101
    • 0023603491 scopus 로고
    • Inhibition of bryostatin 1 of the phorbol ester-induced blockage of differentiation in hexamethylene bisacetamide-treated Friend erythroleukemia cells
    • Dell'Aquila M.L., Nguyen H.T., Herald C.L., Pettit G.R., Blumberg P.M. Inhibition of bryostatin 1 of the phorbol ester-induced blockage of differentiation in hexamethylene bisacetamide-treated Friend erythroleukemia cells. Cancer Res. 47:1987;6006-6009.
    • (1987) Cancer Res. , vol.47 , pp. 6006-6009
    • Dell'Aquila, M.L.1    Nguyen, H.T.2    Herald, C.L.3    Pettit, G.R.4    Blumberg, P.M.5
  • 102
    • 0023629814 scopus 로고
    • Partial parallelism and partial blockade by bryostatin 1 of effects of phorbol ester tumor promoters on primary mouse epidermal cells
    • Sako T., Yuspa S.H., Herald C.L., Pettit G.R., Blumberg P.M. Partial parallelism and partial blockade by bryostatin 1 of effects of phorbol ester tumor promoters on primary mouse epidermal cells. Cancer Res. 47:1987;5445-5450.
    • (1987) Cancer Res. , vol.47 , pp. 5445-5450
    • Sako, T.1    Yuspa, S.H.2    Herald, C.L.3    Pettit, G.R.4    Blumberg, P.M.5
  • 103
    • 0002488134 scopus 로고
    • Molecular and catalytic properties of protein kinase C
    • J.F. Kuo. New York: Oxford University Press
    • Mahoney C.W., Huang K.P. Molecular and catalytic properties of protein kinase C. Kuo J.F. Protein Kinase C. 1994;16-63 Oxford University Press, New York.
    • (1994) Protein Kinase C , pp. 16-63
    • Mahoney, C.W.1    Huang, K.P.2
  • 104
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton A.C. Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270:1995;28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 105
    • 0023655187 scopus 로고
    • Down-regulation of protein kinase C is due to an increased rate of degradation
    • Young S., Parker P.J., Ullrich A., Stabel S. Down-regulation of protein kinase C is due to an increased rate of degradation. Biochem. J. 244:1987;775-779.
    • (1987) Biochem. J. , vol.244 , pp. 775-779
    • Young, S.1    Parker, P.J.2    Ullrich, A.3    Stabel, S.4
  • 106
    • 0026180277 scopus 로고
    • Overexpression of the alpha-type protein kinase (PK) in LLC-PK1 cells does not lead to a proportional increase in the induction of two 12-O-tetradecanoylphorbol-13 acetate-inducible genes
    • Wartmann M., Jans D.A., Parker P.J., Nagamine Y., Hemmings B.A., Jaken S., Eppenberger U., Fabbro D. Overexpression of the alpha-type protein kinase (PK) in LLC-PK1 cells does not lead to a proportional increase in the induction of two 12-O-tetradecanoylphorbol-13 acetate-inducible genes. Cell Regul. 2:1991;491-502.
    • (1991) Cell Regul. , vol.2 , pp. 491-502
    • Wartmann, M.1    Jans, D.A.2    Parker, P.J.3    Nagamine, Y.4    Hemmings, B.A.5    Jaken, S.6    Eppenberger, U.7    Fabbro, D.8
  • 107
    • 0031419675 scopus 로고    scopus 로고
    • Transepithelial paracellular leakiness induced by chronic phorbol ester exposure correlates with polyp-like foci and redistribution of protein kinase C-α
    • Mullin J.M., Kampherstein J.A., Laughlin K.V., Saladik D.T., Peralta Soler A. Transepithelial paracellular leakiness induced by chronic phorbol ester exposure correlates with polyp-like foci and redistribution of protein kinase C-α Carcinogenesis. 18:1997;2339-2345.
    • (1997) Carcinogenesis , vol.18 , pp. 2339-2345
    • Mullin, J.M.1    Kampherstein, J.A.2    Laughlin, K.V.3    Saladik, D.T.4    Peralta Soler, A.5
  • 108
    • 0030601332 scopus 로고    scopus 로고
    • Chronic exposure of LLC-PK1 epithelia to the phorbol ester TPA produces polyp-like foci with leaky tight junctions and altered protein kinase C-α expression and localization
    • Mullin J.M., Peralta Soler A., Laughlin K.V., Kampherstein J.A., Russo L.M., Saladik D.T., George K., Shurina R.D., O'Brien T.G. Chronic exposure of LLC-PK1 epithelia to the phorbol ester TPA produces polyp-like foci with leaky tight junctions and altered protein kinase C-α expression and localization. Exp. Cell Res. 227:1996;12-22.
    • (1996) Exp. Cell Res. , vol.227 , pp. 12-22
    • Mullin, J.M.1    Peralta Soler, A.2    Laughlin, K.V.3    Kampherstein, J.A.4    Russo, L.M.5    Saladik, D.T.6    George, K.7    Shurina, R.D.8    O'Brien, T.G.9
  • 109
    • 85058253286 scopus 로고    scopus 로고
    • The phorbol ester TPA, and bryostatin 1 exert different effects on PKC-α downregulation and tight junctional permeability
    • Clarke H., Ginanni N., Laughlin K.V., Smith J.B., Pettit G.R., Mullin J.M. The phorbol ester TPA, and bryostatin 1 exert different effects on PKC-α downregulation and tight junctional permeability. Mol. Biol. Cell. 10:(Suppl.):1999;409a.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.SUPPL.
    • Clarke, H.1    Ginanni, N.2    Laughlin, K.V.3    Smith, J.B.4    Pettit, G.R.5    Mullin, J.M.6
  • 110
    • 0031856770 scopus 로고    scopus 로고
    • Effects of bryostatin 1, a novel anticancer agent on intestinal transport and barrier function: Role of protein kinase C
    • Farokhzad O.C., Mun E.C., Sicklick J.K., Smith J.A., Matthews J.B. Effects of bryostatin 1, a novel anticancer agent on intestinal transport and barrier function: role of protein kinase C. Surgery. 124:1998;380-386.
    • (1998) Surgery , vol.124 , pp. 380-386
    • Farokhzad, O.C.1    Mun, E.C.2    Sicklick, J.K.3    Smith, J.A.4    Matthews, J.B.5
  • 111
    • 0030940852 scopus 로고    scopus 로고
    • Protein kinase C activity modulates transepithelial permeability and cell junctions in the LLC-PK1 epithelial cell line
    • Rosson D., O'Brien T., Kampherstein J.A., Szallasi Z., Bogi K., Blumberg P.M., Mullin J.M. Protein kinase C activity modulates transepithelial permeability and cell junctions in the LLC-PK1 epithelial cell line. J. Biol. Chem. 272:1997;14950-14953.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14950-14953
    • Rosson, D.1    O'Brien, T.2    Kampherstein, J.A.3    Szallasi, Z.4    Bogi, K.5    Blumberg, P.M.6    Mullin, J.M.7
  • 113
    • 0023227708 scopus 로고
    • The phorbol ester, TPA, increases transepithelial epidermal growth factor flux
    • Mullin J.M., McGinn M.T. The phorbol ester, TPA, increases transepithelial epidermal growth factor flux. FEBS Lett. 221:1987;359-364.
    • (1987) FEBS Lett. , vol.221 , pp. 359-364
    • Mullin, J.M.1    McGinn, M.T.2
  • 114
    • 0032522796 scopus 로고    scopus 로고
    • Protein kinase C activation increases transepithelial transport of biologically active insulin
    • Mullin J.M., Ginanni N., Laughlin K.V. Protein kinase C activation increases transepithelial transport of biologically active insulin. Cancer Res. 58:1998;1641-1645.
    • (1998) Cancer Res. , vol.58 , pp. 1641-1645
    • Mullin, J.M.1    Ginanni, N.2    Laughlin, K.V.3
  • 115
    • 0028954548 scopus 로고
    • Epidermal growth factor related peptides and their reliance to gastrointestinal pathophysiology
    • Barnard J.A., Beauchamp R.D., Russell W.E., DuBois R.N., Coffey R.J. Epidermal growth factor related peptides and their reliance to gastrointestinal pathophysiology. Gastroenterology. 108:1995;564-580.
    • (1995) Gastroenterology , vol.108 , pp. 564-580
    • Barnard, J.A.1    Beauchamp, R.D.2    Russell, W.E.3    Dubois, R.N.4    Coffey, R.J.5
  • 116
    • 0026446487 scopus 로고
    • Human epidermal growth factor - On molecular forms present in urine and blood
    • Nexo E., Jorgensen P.E., Hansen M.R. Human epidermal growth factor - on molecular forms present in urine and blood. Regul. Pept. 42:1992;75-84.
    • (1992) Regul. Pept. , vol.42 , pp. 75-84
    • Nexo, E.1    Jorgensen, P.E.2    Hansen, M.R.3
  • 118
    • 0343218200 scopus 로고
    • Mitosis in domes of renal epithelial (LLC-PK1) cell cultures
    • Mullin J.M., Fluk L., Tchao R. Mitosis in domes of renal epithelial (LLC-PK1) cell cultures. Mol. Physiol. 8:1985;317-328.
    • (1985) Mol. Physiol. , vol.8 , pp. 317-328
    • Mullin, J.M.1    Fluk, L.2    Tchao, R.3
  • 120
    • 0027499799 scopus 로고
    • Epithelial cells retain junctions during mitosis
    • Baker J., Garrod D. Epithelial cells retain junctions during mitosis. J. Cell Sci. 104:1993;415-425.
    • (1993) J. Cell Sci. , vol.104 , pp. 415-425
    • Baker, J.1    Garrod, D.2
  • 121
    • 0026561134 scopus 로고
    • Electron microscopic observations on the maintenance of the tight junction during cell division in the epithelium of the mouse small intestine
    • Jinguji Y., Ishikawa H. Electron microscopic observations on the maintenance of the tight junction during cell division in the epithelium of the mouse small intestine. Cell Struct. Funct. 17:1992;27-37.
    • (1992) Cell Struct. Funct. , vol.17 , pp. 27-37
    • Jinguji, Y.1    Ishikawa, H.2
  • 122
    • 0022974086 scopus 로고
    • Effects of phorbol esters on sodium and chloride transport in rat colon
    • Donowitz M., Cheng H.Y., Sharp G.W.G. Effects of phorbol esters on sodium and chloride transport in rat colon. Am. J. Physiol. 251:1986;G509-G517.
    • (1986) Am. J. Physiol. , vol.251
    • Donowitz, M.1    Cheng, H.Y.2    Sharp, G.W.G.3
  • 123
    • 0022065641 scopus 로고
    • Effects of tumor promoters on sodium ion transport across frog skin
    • Civan M.M., Rubenstein D., Mauro T., O'Brien T.G. Effects of tumor promoters on sodium ion transport across frog skin. Am. J. Physiol. 248:1985;C457-465.
    • (1985) Am. J. Physiol. , vol.248 , pp. 457-465
    • Civan, M.M.1    Rubenstein, D.2    Mauro, T.3    O'Brien, T.G.4
  • 124
    • 0025763935 scopus 로고
    • Effects of pH on phosphate transport by flounder renal tubule primary cultures
    • Gupta A., Renfro J.L. Effects of pH on phosphate transport by flounder renal tubule primary cultures. Am. J. Physiol. 260:1991;R704-R711.
    • (1991) Am. J. Physiol. , vol.260
    • Gupta, A.1    Renfro, J.L.2
  • 125
    • 0025938210 scopus 로고
    • Effects of cyclic AMP and phorbol ester on transepithelial electrical resistance of Sertoli cell monolayers in two-compartment culture
    • Janecki A., Jakubowiak A., Steinberger A. Effects of cyclic AMP and phorbol ester on transepithelial electrical resistance of Sertoli cell monolayers in two-compartment culture. Mol. Cell. Endocrinol. 82:1991;61-69.
    • (1991) Mol. Cell. Endocrinol. , vol.82 , pp. 61-69
    • Janecki, A.1    Jakubowiak, A.2    Steinberger, A.3
  • 126
    • 0028824763 scopus 로고
    • Phorbol myristate acetate ex vivo model of enhanced colonic epithelial permeability - Reactive oxygen metabolite and protease independence
    • Berin M.C., Buell M.G. Phorbol myristate acetate ex vivo model of enhanced colonic epithelial permeability - Reactive oxygen metabolite and protease independence. Dig. Dis. Sci. 40:1995;2268-2279.
    • (1995) Dig. Dis. Sci. , vol.40 , pp. 2268-2279
    • Berin, M.C.1    Buell, M.G.2
  • 127
    • 0030738020 scopus 로고    scopus 로고
    • Modulation of intestinal paracellular permeability by intracellular mediators and cytoskeleton
    • Perez M., Barber A., Ponz F. Modulation of intestinal paracellular permeability by intracellular mediators and cytoskeleton. Can. J. Physiol. Pharmacol. 75:1997;287-292.
    • (1997) Can. J. Physiol. Pharmacol. , vol.75 , pp. 287-292
    • Perez, M.1    Barber, A.2    Ponz, F.3
  • 128
    • 0031959370 scopus 로고    scopus 로고
    • Pentobarbital affects transepithelial electrophysiological parameters regulated by protein kinase C in rat distal colon
    • Simons R.M., Laughlin K.V., Kampherstein J.A., Desai D.C., Shurina R.D., Mullin J.M. Pentobarbital affects transepithelial electrophysiological parameters regulated by protein kinase C in rat distal colon. Dig. Dis. Sci. 43:1998;632-640.
    • (1998) Dig. Dis. Sci. , vol.43 , pp. 632-640
    • Simons, R.M.1    Laughlin, K.V.2    Kampherstein, J.A.3    Desai, D.C.4    Shurina, R.D.5    Mullin, J.M.6
  • 130
    • 0021267486 scopus 로고
    • Ultrastructural changes on the junctional complexes in the human urinary bladder carcinoma by thin sectioning and freeze fracture
    • Saito T. Ultrastructural changes on the junctional complexes in the human urinary bladder carcinoma by thin sectioning and freeze fracture. J. Clin. Electron Miscrosc. 17:1984;201-209.
    • (1984) J. Clin. Electron Miscrosc. , vol.17 , pp. 201-209
    • Saito, T.1
  • 131
    • 0014810406 scopus 로고
    • Ultrastructural modifications of intercellular junctions between tumor cells
    • Martinez-Palomo A. Ultrastructural modifications of intercellular junctions between tumor cells. In Vitro. 6:1970;15-20.
    • (1970) In Vitro , vol.6 , pp. 15-20
    • Martinez-Palomo, A.1
  • 132
    • 0029122307 scopus 로고
    • Phosphorylation of the tight junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells
    • Citi S., Denisenko N. Phosphorylation of the tight junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells. J. Cell Sci. 108:1995;2917-2926.
    • (1995) J. Cell Sci. , vol.108 , pp. 2917-2926
    • Citi, S.1    Denisenko, N.2
  • 133
    • 0028109285 scopus 로고
    • Localization of the 7H6 antigen at tight junctions correlates with the paracellular barrier function of MDCK cells
    • Zhong Y., Enomoto K., Isomura H., Sawada N., Minase T., Oyamada M., Konishi Y., Mori M. Localization of the 7H6 antigen at tight junctions correlates with the paracellular barrier function of MDCK cells. Exp. Cell Res. 214:1994;614-620.
    • (1994) Exp. Cell Res. , vol.214 , pp. 614-620
    • Zhong, Y.1    Enomoto, K.2    Isomura, H.3    Sawada, N.4    Minase, T.5    Oyamada, M.6    Konishi, Y.7    Mori, M.8
  • 134
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophilia disc-large tumor suppressor protein of septate junctions
    • Willott E., Balda M.S., Fanning A.S., Jamenson B., Van Itallie C., Anderson J.M. The tight junction protein ZO-1 is homologous to the Drosophilia disc-large tumor suppressor protein of septate junctions. Proc. Natl. Acad. Sci. USA. 90:1993;399-409.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 399-409
    • Willott, E.1    Balda, M.S.2    Fanning, A.S.3    Jamenson, B.4    Van Itallie, C.5    Anderson, J.M.6
  • 135
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse M., Itoh M., Hirase T., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127:1994;1617-1626.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 136
    • 0027300689 scopus 로고
    • The 220 kDa 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 S., Yonemurea S., Kitani-Yasuda T., Tsukits Sa., Tsukita Sh. The 220 kDa 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. 121:1993;491-502.
    • (1993) J. Cell Biol. , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, S.2    Yonemurea, S.3    Kitani-Yasuda, T.4    Tsukits, Sa.5    Tsukita, Sh.6
  • 137
    • 0030293766 scopus 로고    scopus 로고
    • Protein-protein interactions: PDZ domain networks
    • Fanning A.S., Anderson J.M. Protein-protein interactions: PDZ domain networks. Curr. Biol. 6:1996;1385-1388.
    • (1996) Curr. Biol. , vol.6 , pp. 1385-1388
    • Fanning, A.S.1    Anderson, J.M.2
  • 138
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by the expression of a mutant tight junction membrane protein
    • Balda M.S., Whitney J.A., Flores C., Gonzalez-Mariscal L., Cereijido M., Matter K. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by the expression of a mutant tight junction membrane protein. J. Cell Biol. 134:1996;1031-1049.
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez-Mariscal, L.4    Cereijido, M.5    Matter, K.6
  • 139
    • 0028931103 scopus 로고
    • Evidence that tyrosine phosphorylation may increase tight junction permeability
    • Staddon J.M., Herrenknecht K., Smales C., Rubin L.L. Evidence that tyrosine phosphorylation may increase tight junction permeability. J. Cell Sci. 108:1995;609-619.
    • (1995) J. Cell Sci. , vol.108 , pp. 609-619
    • Staddon, J.M.1    Herrenknecht, K.2    Smales, C.3    Rubin, L.L.4
  • 140
    • 0028819708 scopus 로고
    • Effects of tyrosine phosphorylation on tight junctions in temperature-sensitive v-src-transfected MDCK cells
    • Takeda H., Tsukita S. Effects of tyrosine phosphorylation on tight junctions in temperature-sensitive v-src-transfected MDCK cells. Cell Struct. Funct. 20:1995;387-393.
    • (1995) Cell Struct. Funct. , vol.20 , pp. 387-393
    • Takeda, H.1    Tsukita, S.2
  • 141
    • 0024456733 scopus 로고
    • Phosphorylation of the tight junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance
    • Stevenson B.R., Anderson J.M., Braun I.D., Mooseker M.S. Phosphorylation of the tight junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Biochem. J. 263:1989;597-599.
    • (1989) Biochem. J. , vol.263 , pp. 597-599
    • Stevenson, B.R.1    Anderson, J.M.2    Braun, I.D.3    Mooseker, M.S.4
  • 142
    • 0029122307 scopus 로고
    • Phosphorylation of the tight junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells
    • Citi S., Denisenko N. Phosphorylation of the tight junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells. J. Cell Sci. 108:1995;2917-2926.
    • (1995) J. Cell Sci. , vol.108 , pp. 2917-2926
    • Citi, S.1    Denisenko, N.2
  • 143
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara A., Furuse M., Saitou M., Ando-Akatsuka Y., Tsukita S. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137:1997;1393-1401.
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 144
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four transmembrane domain protein components of tight junction strands
    • Morita K., Furuse M., Fujimoto K., Tsukita S. Claudin multigene family encoding four transmembrane domain protein components of tight junction strands. Proc. Natl. Acad. Sci. USA. 96:1999;511-516.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, S.4
  • 145
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong V., Gumbiner B.M. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136:1997;399-409.
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 147
    • 0030748172 scopus 로고    scopus 로고
    • COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos
    • Chen Y., Merzdorf C., Paul D.L., Goodenough D.A. COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos. J. Cell Biol. 138:1997;891-899.
    • (1997) J. Cell Biol. , vol.138 , pp. 891-899
    • Chen, Y.1    Merzdorf, C.2    Paul, D.L.3    Goodenough, D.A.4
  • 149
    • 0029041046 scopus 로고
    • Regulated assembly of tight junctions by protein kinase C
    • Stuart R.O., Nigam S.K. Regulated assembly of tight junctions by protein kinase C. Proc. Natl. Acad. Sci. USA. 92:1995;6072-6076.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6072-6076
    • Stuart, R.O.1    Nigam, S.K.2
  • 150
    • 0033004247 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins
    • Tsukamoto T., Nigam S. Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins. Am. J. Physiol. 276:1999;F737-F750.
    • (1999) Am. J. Physiol. , vol.276
    • Tsukamoto, T.1    Nigam, S.2
  • 152
    • 2142793340 scopus 로고    scopus 로고
    • Protein Kinase C activation by the phorbol ester, TPA leads to increased tight junction permeability and altered phosphorylation of occludin
    • Clarke H., Peralta Soler A., Mullin J.M. Protein Kinase C activation by the phorbol ester, TPA leads to increased tight junction permeability and altered phosphorylation of occludin. Mol. Biol. Cell. 10:(Suppl.):1999;410a.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.SUPPL.
    • Clarke, H.1    Peralta Soler, A.2    Mullin, J.M.3
  • 153
    • 0031032318 scopus 로고    scopus 로고
    • The toxin of diarrheic shellfish poisoning, okadaic acid, increases intestinal epithelial paracellular permeability
    • Tripuraneni J., Koutsouris A., Pestic L., De Lanerolle P., Hecht G. The toxin of diarrheic shellfish poisoning, okadaic acid, increases intestinal epithelial paracellular permeability. Gastroenterology. 112:1997;100-108.
    • (1997) Gastroenterology , vol.112 , pp. 100-108
    • Tripuraneni, J.1    Koutsouris, A.2    Pestic, L.3    De Lanerolle, P.4    Hecht, G.5
  • 154
    • 0032792058 scopus 로고    scopus 로고
    • Redistribution and phosphorylation of occludin during opening and resealing of tight junction junctions in cultured epithelial cells
    • Farshori P., Kachar B. Redistribution and phosphorylation of occludin during opening and resealing of tight junction junctions in cultured epithelial cells. J. Membr. Biol. 170:1999;147-156.
    • (1999) J. Membr. Biol. , vol.170 , pp. 147-156
    • Farshori, P.1    Kachar, B.2
  • 155
    • 0031438083 scopus 로고    scopus 로고
    • Dephosphorylation of cadherin-associated p100/p120 proteins in response to activation of protein kinase C in epithelial cells
    • Ratcliffe M.J., Rubin L.L., Staddon J.M. Dephosphorylation of cadherin-associated p100/p120 proteins in response to activation of protein kinase C in epithelial cells. J. Biol. Chem. 272:1997;31894-31901.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31894-31901
    • Ratcliffe, M.J.1    Rubin, L.L.2    Staddon, J.M.3
  • 156
    • 0033104860 scopus 로고    scopus 로고
    • Dephosphorylation of the catenins p120 and p100 in endothelial cells in response to inflammatory stimuli
    • Ratcliffe M.J., Smales C., Staddon J.M. Dephosphorylation of the catenins p120 and p100 in endothelial cells in response to inflammatory stimuli. Biochem. J. 338:1999;471-478.
    • (1999) Biochem. J. , vol.338 , pp. 471-478
    • Ratcliffe, M.J.1    Smales, C.2    Staddon, J.M.3
  • 158
    • 15444343889 scopus 로고    scopus 로고
    • Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes
    • Moroi S., Saitou M., Fujimoto K., Sakakibara A., Furuse M., Yoshida O., Tsukita S. Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes. Am. J. Physiol. 274:1998;C1708-C1717.
    • (1998) Am. J. Physiol. , vol.274
    • Moroi, S.1    Saitou, M.2    Fujimoto, K.3    Sakakibara, A.4    Furuse, M.5    Yoshida, O.6    Tsukita, S.7
  • 159
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou M., Fujimoto K., Doi Y., Itoh M., Fujimoto T., Furuse M., Takano H., Noda T., Tsukita S. Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J. Cell Biol. 141:1998;397-408.
    • (1998) J. Cell Biol. , vol.141 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3    Itoh, M.4    Fujimoto, T.5    Furuse, M.6    Takano, H.7    Noda, T.8    Tsukita, S.9


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