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Volumn 271, Issue 5 40-5, 1996, Pages

Expression of the catalytic domain of myosin light chain kinase increases paracellular permeability

Author keywords

cytoskeleton; epithelia; phosphorylation; tight junctions

Indexed keywords

BETA GALACTOSIDASE; MYOSIN LIGHT CHAIN KINASE;

EID: 0010617662     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1996.271.5.c1678     Document Type: Article
Times cited : (115)

References (32)
  • 2
    • 0021021559 scopus 로고
    • Phosphorylation controls brush border motility by regulating myosin structure and associating with the cytoskeleton
    • Broschat, K. O., R. P. Stidwell, and D. R. Burgess. Phosphorylation controls brush border motility by regulating myosin structure and associating with the cytoskeleton. Cell 35: 561-571, 1983.
    • (1983) Cell , vol.35 , pp. 561-571
    • Broschat, K.O.1    Stidwell, R.P.2    Burgess, D.R.3
  • 3
    • 0017891781 scopus 로고
    • Polarized monolayers formed by epithelial cells on a permeable and translucent support
    • Cereijido, M., E. S. Robbins, W. J. Dolan, C. A. Rotunno, and D. D. Sabitini. Polarized monolayers formed by epithelial cells on a permeable and translucent support. J. Cell Biol. 77: 853-876, 1978.
    • (1978) J. Cell Biol. , vol.77 , pp. 853-876
    • Cereijido, M.1    Robbins, E.S.2    Dolan, W.J.3    Rotunno, C.A.4    Sabitini, D.D.5
  • 4
    • 0026505270 scopus 로고
    • Protein kinase inhibitors prevent junction dissociation induced by low extracellular calcium in MDCK epithelial cells
    • Citi, S. Protein kinase inhibitors prevent junction dissociation induced by low extracellular calcium in MDCK epithelial cells. J. Cell Biol. 117: 169-178, 1992.
    • (1992) J. Cell Biol. , vol.117 , pp. 169-178
    • Citi, S.1
  • 5
    • 0020678721 scopus 로고
    • Light-chain phosphorylation controls the conformation of vertebrate nonmuscle and smooth muscle myosin molecules
    • Craig, R., R. Smith, and J. Kendrick-Jones. Light-chain phosphorylation controls the conformation of vertebrate nonmuscle and smooth muscle myosin molecules. Nature Lond. 302: 436-439, 1983.
    • (1983) Nature Lond. , vol.302 , pp. 436-439
    • Craig, R.1    Smith, R.2    Kendrick-Jones, J.3
  • 6
    • 0026456586 scopus 로고
    • Purification and characterization of platelet myosin
    • Daniel, J. L., and J. R. Sellers, Purification and characterization of platelet myosin. Methods Enzymol. 215: 78-88, 1992.
    • (1992) Methods Enzymol. , vol.215 , pp. 78-88
    • Daniel, J.L.1    Sellers, J.R.2
  • 7
    • 0017758863 scopus 로고
    • Na and Cl transport across the isolated turtle colon: Parallel pathways for transmural ion movement
    • Dawson, D. C. Na and Cl transport across the isolated turtle colon: parallel pathways for transmural ion movement. J. Membr. Biol. 37: 213-233, 1977.
    • (1977) J. Membr. Biol. , vol.37 , pp. 213-233
    • Dawson, D.C.1
  • 8
    • 0019838042 scopus 로고
    • Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells
    • De Lanerolle, P., R. S. Adelstein, J. R. Feramisco, and K. Burridge. Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells. Proc. Natl. Acad. Sci. USA 78: 4738-4742, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4738-4742
    • De Lanerolle, P.1    Adelstein, R.S.2    Feramisco, J.R.3    Burridge, K.4
  • 9
    • 0027292227 scopus 로고
    • Myosin light chain phosphorylation does not increase during yeast phagocytosis by macrophages
    • De Lanerolle, P., G. Gorgas, X. Li., and K. Schluns. Myosin light chain phosphorylation does not increase during yeast phagocytosis by macrophages. J. Biol. Chem. 268: 16883-16886, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16883-16886
    • De Lanerolle, P.1    Gorgas, G.2    Li, X.3    Schluns, K.4
  • 10
    • 0023894112 scopus 로고
    • Regulation of embryonic smooth muscle myosin by protein kinase C
    • De Lanerolle, P., and M. Nishikawa. Regulation of embryonic smooth muscle myosin by protein kinase C. J. Biol. Chem. 263: 9071-9074, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9071-9074
    • De Lanerolle, P.1    Nishikawa, M.2
  • 11
    • 0026058812 scopus 로고
    • Myosin phosphorylation/ dephosphorylation and regulation of airway smooth muscle contractility
    • Lung Cell. Mol. Physiol. 5
    • De Lanerolle, P., and R. J. Paul. Myosin phosphorylation/ dephosphorylation and regulation of airway smooth muscle contractility. Am. J. Physiol. 261 (Lung Cell. Mol. Physiol. 5): L1-L14, 1992.
    • (1992) Am. J. Physiol. , vol.261
    • De Lanerolle, P.1    Paul, R.J.2
  • 12
    • 0026345292 scopus 로고
    • Identification of a 160 kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner, B., T. Lowenkopf, and D. Apatira. Identification of a 160 kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci. USA 88: 3460-3464, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 13
    • 0025819344 scopus 로고
    • Definition of the inhibitory domain of smooth muscle myosin light chain kinase by site-directed mutagenesis
    • Ito, M., V. Guerriero, Jr., X. Chen, and D. J. Hartshorne. Definition of the inhibitory domain of smooth muscle myosin light chain kinase by site-directed mutagenesis. Biochemistry 30: 3498-3503, 1991.
    • (1991) Biochemistry , vol.30 , pp. 3498-3503
    • Ito, M.1    Guerriero Jr., V.2    Chen, X.3    Hartshorne, D.J.4
  • 14
    • 0020368721 scopus 로고
    • 2+-calmodulin dependent phosphorylation of myosin, and its role in brush border contraction in vitro
    • 2+-calmodulin dependent phosphorylation of myosin, and its role in brush border contraction in vitro. J. Cell Biol. 95: 943-959, 1982.
    • (1982) J. Cell Biol. , vol.95 , pp. 943-959
    • Keller, T.C.S.1    Mooseker, M.S.2
  • 15
    • 0026044692 scopus 로고
    • Extracellular ATP, intracellular calcium and canalicular contraction in rat hepatocyte doublets
    • Kitamura, T., B. Ulrike, Z. Gatmaitan, and I. M. Arias. Extracellular ATP, intracellular calcium and canalicular contraction in rat hepatocyte doublets. Hepatology 14: 640-647, 1991.
    • (1991) Hepatology , vol.14 , pp. 640-647
    • Kitamura, T.1    Ulrike, B.2    Gatmaitan, Z.3    Arias, I.M.4
  • 16
    • 0022451875 scopus 로고
    • Effects of cytochalasin D on occluding junctions of intestinal absorptive cells
    • Madara, J. L., D. Barenberg, and S. Carlson. Effects of cytochalasin D on occluding junctions of intestinal absorptive cells. J. Cell Biol. 102: 2125-2135, 1986.
    • (1986) J. Cell Biol. , vol.102 , pp. 2125-2135
    • Madara, J.L.1    Barenberg, D.2    Carlson, S.3
  • 17
    • 0002524056 scopus 로고
    • Tight (occluding) junctions in cultured (and native) epithelial cells
    • edited by K. S. Matlin and J. D. Valentich. New York: Liss
    • Madara, J. L., and G. Hecht. Tight (occluding) junctions in cultured (and native) epithelial cells. In: Functional Epithelial Cells in Culture, edited by K. S. Matlin and J. D. Valentich. New York: Liss, 1989, p. 131-163.
    • (1989) Functional Epithelial Cells in Culture , pp. 131-163
    • Madara, J.L.1    Hecht, G.2
  • 18
    • 0023510866 scopus 로고
    • The structural basis for physiological regulation of paracellular pathways in intestinal epithelia
    • Madara, J. L., and J. R. Pappenheimer. The structural basis for physiological regulation of paracellular pathways in intestinal epithelia. J. Membr. Biol. 100: 149-164, 1987.
    • (1987) J. Membr. Biol. , vol.100 , pp. 149-164
    • Madara, J.L.1    Pappenheimer, J.R.2
  • 19
    • 0019275289 scopus 로고
    • Experimental modulation of occluding junctions in a transporting epithelium
    • Martinez-Palomo, A., I. Meza, G. Beaty, and M. Cerejeido. Experimental modulation of occluding junctions in a transporting epithelium. J. Cell Biol. 87: 736-745, 1980.
    • (1980) J. Cell Biol. , vol.87 , pp. 736-745
    • Martinez-Palomo, A.1    Meza, I.2    Beaty, G.3    Cerejeido, M.4
  • 20
    • 0020370127 scopus 로고
    • Occluding junctions in MDCK cells: Modulation of transepithelial permeability by the cytoskeleton
    • Meza, I., A. Sabanero, E. Stefani, and M. Cereijido. Occluding junctions in MDCK cells: modulation of transepithelial permeability by the cytoskeleton. J. Cell Biochem. 18: 407-421, 1982.
    • (1982) J. Cell Biochem. , vol.18 , pp. 407-421
    • Meza, I.1    Sabanero, A.2    Stefani, E.3    Cereijido, M.4
  • 21
    • 0024460181 scopus 로고
    • Improved retroviral vectors for gene transfer and expression
    • Miller, A. D., and G. J. Rosman. Improved retroviral vectors for gene transfer and expression. Biotechniques 7: 980-990, 1989.
    • (1989) Biotechniques , vol.7 , pp. 980-990
    • Miller, A.D.1    Rosman, G.J.2
  • 22
    • 0029099125 scopus 로고
    • Fibroblast contractility without an increase in basal myosin light chain phosphorylation in wild type cells and cells expressing the catalytic domain of myosin light chain kinase
    • Obara, K., G. Nikcevic, L. Pestic, G. Nowak, D. D. Lorimer, V. Guerriero, Jr., E. E. Elson, R. J. Paul, and P. de Lanerolle. Fibroblast contractility without an increase in basal myosin light chain phosphorylation in wild type cells and cells expressing the catalytic domain of myosin light chain kinase. J. Biol. Chem. 270: 18734-18737, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18734-18737
    • Obara, K.1    Nikcevic, G.2    Pestic, L.3    Nowak, G.4    Lorimer, D.D.5    Guerriero Jr., V.6    Elson, E.E.7    Paul, R.J.8    De Lanerolle, P.9
  • 23
    • 0023520885 scopus 로고
    • Physiological regulation of transepithelial impedance in the intestinal mucosa of rats and hamsters
    • Pappenheimer, J. R. Physiological regulation of transepithelial impedance in the intestinal mucosa of rats and hamsters. J. Membr. Biol. 100: 136-148, 1987.
    • (1987) J. Membr. Biol. , vol.100 , pp. 136-148
    • Pappenheimer, J.R.1
  • 24
    • 0024436810 scopus 로고
    • Capping of surface receptors and concomitant cortical tension are generated by conventional myosin
    • Pasternak, C., J. A. Spudich, and E. L. Elson. Capping of surface receptors and concomitant cortical tension are generated by conventional myosin. Nature Lond. 341: 549-551, 1989.
    • (1989) Nature Lond. , vol.341 , pp. 549-551
    • Pasternak, C.1    Spudich, J.A.2    Elson, E.L.3
  • 25
    • 0022988979 scopus 로고
    • Use of a recombinant retrovirus to study post-implantation cell lineage in mouse embryos
    • Sanes, J. R., J. L. R. Rubenstein, and J. F. Nicolas. Use of a recombinant retrovirus to study post-implantation cell lineage in mouse embryos. EMBO J. 5: 3133-3142, 1986.
    • (1986) EMBO J. , vol.5 , pp. 3133-3142
    • Sanes, J.R.1    Rubenstein, J.L.R.2    Nicolas, J.F.3
  • 26
    • 0017198462 scopus 로고
    • Ionic permeability of epithelial tissues
    • Schultz, S. E., and R. A. Frizzell. Ionic permeability of epithelial tissues. Biochim. Biophys. Acta 443: 181-189, 1976.
    • (1976) Biochim. Biophys. Acta , vol.443 , pp. 181-189
    • Schultz, S.E.1    Frizzell, R.A.2
  • 27
    • 0024211161 scopus 로고
    • Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance
    • Stevenson, B. R., J. M. Anderson, D. A. Goodenough, and M. S. Mooseker. Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. J. Cell Biol. 107: 2401-2408, 1988.
    • (1988) J. Cell Biol. , vol.107 , pp. 2401-2408
    • Stevenson, B.R.1    Anderson, J.M.2    Goodenough, D.A.3    Mooseker, M.S.4
  • 28
    • 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., J. D. Siliciano, M. S. Mooseker, and D. A. Goodenough. 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: 755-766, 1986.
    • (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
  • 29
    • 0025913788 scopus 로고
    • Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated
    • Tsukita, S., K. Oishi, T. Akiyama, Y. Yamanashi, and T. Yamamoto. Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J. Cell Biol. 113: 867-879, 1991.
    • (1991) J. Cell Biol. , vol.113 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanashi, Y.4    Yamamoto, T.5
  • 30
    • 0025834881 scopus 로고
    • An increase or a decrease in myosin II phosphorylation inhibits macrophage motility
    • Wilson, A. K., G. Gorgas, W. D. Claypool, and P. de Lanerolle. An increase or a decrease in myosin II phosphorylation inhibits macrophage motility. J. Cell Biol. 114: 277-283, 1991.
    • (1991) J. Cell Biol. , vol.114 , pp. 277-283
    • Wilson, A.K.1    Gorgas, G.2    Claypool, W.D.3    De Lanerolle, P.4
  • 31
    • 0025186832 scopus 로고
    • Involvement of myosin light-chain kinase in endothelial cell retraction
    • Wysolmerski, R. B., and D. Lagunoff. Involvement of myosin light-chain kinase in endothelial cell retraction. Proc. Natl. Acad. Sci. USA 87: 16-20, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 16-20
    • Wysolmerski, R.B.1    Lagunoff, D.2
  • 32
    • 0026072414 scopus 로고
    • Vasopressin and A23187 stimulate phosphorylation of myosin light chain-1 in isolated rat hepatocytes
    • Gastrointest. Liver Physiol. 24
    • Yamaguchi, Y., E. Dalle-Molle, and W. G. M. Hardison. Vasopressin and A23187 stimulate phosphorylation of myosin light chain-1 in isolated rat hepatocytes. Am. J. Physiol. 261 (Gastrointest. Liver Physiol. 24): G312-G319, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Yamaguchi, Y.1    Dalle-Molle, E.2    Hardison, W.G.M.3


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