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Volumn 272, Issue 1 16-1, 1997, Pages

Glucosylation of small GTP-binding Rho proteins disrupts endothelial barrier function

Author keywords

albumin reflection coefficient; Clostridium difficile toxin B; cultured pulmonary endothelial cells; hydraulic conductivity

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0031035834     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1997.272.1.l38     Document Type: Article
Times cited : (64)

References (30)
  • 1
    • 0024341897 scopus 로고
    • Botulinum ADP-ribosyltransferase C3: A new tool to study low molecular weight GTP-binding proteins
    • Aktories, K., and A. Hall. Botulinum ADP-ribosyltransferase C3: a new tool to study low molecular weight GTP-binding proteins. Trends Pharmacol. Sci. 10: 415-418, 1989.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 415-418
    • Aktories, K.1    Hall, A.2
  • 2
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad, L., F. Markey, L. Carrlson, T. Persson, and U. Lindberg. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 15: 935-943, 1978.
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, L.1    Markey, F.2    Carrlson, L.3    Persson, T.4    Lindberg, U.5
  • 3
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., A. Traynor-Kaplan, G. M. Bokosch, and M. A. Schwartz. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79: 507-513, 1994.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokosch, G.M.3    Schwartz, M.A.4
  • 4
    • 0029055812 scopus 로고
    • The small GTP-binding proteins rac1 and cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso, O. A., M. Chiariello, J. C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and S. Gutkind. The small GTP-binding proteins rac1 and cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81: 1137-1146, 1995.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, S.8
  • 5
    • 0016698833 scopus 로고
    • Interaction of actin with phalloidin: Polymerization and stabilization of F-actin
    • Dancker, P., I. Löw, W. Hassclbach, and T. Wieland. Interaction of actin with phalloidin: polymerization and stabilization of F-actin. Biochim. Biophys. Acta 400: 407-414, 1975.
    • (1975) Biochim. Biophys. Acta , vol.400 , pp. 407-414
    • Dancker, P.1    Löw, I.2    Hassclbach, W.3    Wieland, T.4
  • 7
    • 0023175490 scopus 로고
    • Purification of two high molecular weight toxins of Clostridium difficile which are antigenetically related
    • Eichel-Streiber, C. von, U. Harperath, U. Bosse, and U. Hadding. Purification of two high molecular weight toxins of Clostridium difficile which are antigenetically related. Microb. Pathog. 2: 307-318, 1987.
    • (1987) Microb. Pathog. , vol.2 , pp. 307-318
    • Von Eichel-Streiber, C.1    Harperath, U.2    Bosse, U.3    Hadding, U.4
  • 8
    • 0029086528 scopus 로고
    • Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B
    • Eichel-Streiber, C. von, D. Meyer zu Heringdorf, E. Habermann, and S. Sartingen. Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B. Mol. Microbiol. 17: 313-321, 1995.
    • (1995) Mol. Microbiol. , vol.17 , pp. 313-321
    • Von Eichel-Streiber, C.1    Meyer Zu Heringdorf, D.2    Habermann, E.3    Sartingen, S.4
  • 9
    • 0022443783 scopus 로고
    • Lysosomal involvment in cellular intoxication with Clostridium difficile toxin B
    • Florin, I., and M. Thelestam. Lysosomal involvment in cellular intoxication with Clostridium difficile toxin B. Microb. Pathog. 1: 373-385, 1986.
    • (1986) Microb. Pathog. , vol.1 , pp. 373-385
    • Florin, I.1    Thelestam, M.2
  • 10
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphos-phate
    • Gilmore, P. G., and K. Burridge. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphos-phate. Nature Lond. 381: 531-533, 1996.
    • (1996) Nature Lond. , vol.381 , pp. 531-533
    • Gilmore, P.G.1    Burridge, K.2
  • 11
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10: 31-54, 1994.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 12
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., G. M. Bokoch, C. L. Carpenter, P. A. Janmey, L. A. Taylor, A. Toker, and T. P. Stossel. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82: 643-653, 1995.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 13
    • 0026577118 scopus 로고
    • Clostridium difficile toxin B disrupts the barrier function of T84 monolayers
    • Hecht, G., A. Koutsouris, C. Pothoulakis, J. T. LaMont, and J. L. Madara. Clostridium difficile toxin B disrupts the barrier function of T84 monolayers. Gastroenterology 102: 416-423, 1992.
    • (1992) Gastroenterology , vol.102 , pp. 416-423
    • Hecht, G.1    Koutsouris, A.2    Pothoulakis, C.3    Lamont, J.T.4    Madara, J.L.5
  • 14
    • 0029027683 scopus 로고
    • Sequencing and analysis of the gene encoding the α-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile
    • Hofmann, F., A. Herrmann, E. Habermann, and C. von Eichel-Streiber. Sequencing and analysis of the gene encoding the α-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile. Mol. Gen. Genet. 247: 670-679, 1995.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 670-679
    • Hofmann, F.1    Herrmann, A.2    Habermann, E.3    Von Eichel-Streiber, C.4
  • 18
    • 0023183341 scopus 로고
    • Biochemical studies of the effect of Clostridium difficile toxin B on actin in vivo and in vitro
    • Mitchell, M. J., B. E. Laughon, and S. Lin. Biochemical studies of the effect of Clostridium difficile toxin B on actin in vivo and in vitro. Infect. Immun. 55: 1610-1615, 1987.
    • (1987) Infect. Immun. , vol.55 , pp. 1610-1615
    • Mitchell, M.J.1    Laughon, B.E.2    Lin, S.3
  • 19
    • 0027178669 scopus 로고
    • The effect of histamine and cyclic adenosine monophospate on myosin light chain phosphorylation in human umbilical vein endothelial cells
    • Moy, A. B., S. S. Shasby, B. D. Scott, and D. M. Shasby. The effect of histamine and cyclic adenosine monophospate on myosin light chain phosphorylation in human umbilical vein endothelial cells. J. Clin. Invest. 92: 1198-1206, 1993.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1198-1206
    • Moy, A.B.1    Shasby, S.S.2    Scott, B.D.3    Shasby, D.M.4
  • 20
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81: 53-62, 1995.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 21
    • 0026650356 scopus 로고
    • Morphological and biochemical study of cytoskeletal changes in cultered cells after extracellular application of Clostridium novyi α-toxin
    • Oksche, A., R. Nakov, and E. Habermann. Morphological and biochemical study of cytoskeletal changes in cultered cells after extracellular application of Clostridium novyi α-toxin. Infect. Immun. 60: 3002-3006, 1992.
    • (1992) Infect. Immun. , vol.60 , pp. 3002-3006
    • Oksche, A.1    Nakov, R.2    Habermann, E.3
  • 22
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: Requirement for a tyrosine kinase
    • Ridley, J. A., and A. Hall. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J. 13: 2600-2610, 1994.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, J.A.1    Hall, A.2
  • 23
    • 0025642947 scopus 로고
    • Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium
    • Schnittler, H. J., A. Wilke, T. Gress, N. Suttorp, and D. Drenckhahn. Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium. J. Physiol. Lond. 431: 379-401, 1990.
    • (1990) J. Physiol. Lond. , vol.431 , pp. 379-401
    • Schnittler, H.J.1    Wilke, A.2    Gress, T.3    Suttorp, N.4    Drenckhahn, D.5
  • 24
    • 0023807110 scopus 로고
    • Bacterial exotoxins and endothelial permeability for water and albumin in vitro
    • Cell Physiol. 24
    • Suttorp, N., T. Hessz, W. Seeger, A. Wilke, R. Koob, F. Lutz, and D. Drenckhahn. Bacterial exotoxins and endothelial permeability for water and albumin in vitro. Am. J. Physiol. 255 (Cell Physiol. 24): C369-C376, 1988.
    • (1988) Am. J. Physiol. , vol.255
    • Suttorp, N.1    Hessz, T.2    Seeger, W.3    Wilke, A.4    Koob, R.5    Lutz, F.6    Drenckhahn, D.7
  • 25
    • 0029874897 scopus 로고    scopus 로고
    • Role of nitric oxide and phosphodiesterase isoenzyme II for reduction of endothelial hyperpermeability
    • Cell Physiol. 39
    • Suttorp, N., S. Hippenstiel, M. Fuhrmann, M. Krüll, and T. Podzuweit. Role of nitric oxide and phosphodiesterase isoenzyme II for reduction of endothelial hyperpermeability. Am. J. Physiol. 270 (Cell Physiol. 39): C778-C785, 1996.
    • (1996) Am. J. Physiol. , vol.270
    • Suttorp, N.1    Hippenstiel, S.2    Fuhrmann, M.3    Krüll, M.4    Podzuweit, T.5
  • 27
    • 0027195164 scopus 로고
    • Role of phosphodiesterases in the regulation of endothelial permeability in vitro
    • Suttorp, N., U. Weber, T. Welsch, and C. Schudt. Role of phosphodiesterases in the regulation of endothelial permeability in vitro. J. Clin. Invest. 91: 1421-1428, 1993.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1421-1428
    • Suttorp, N.1    Weber, U.2    Welsch, T.3    Schudt, C.4
  • 28
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., L. C. Cantley, and C. L. Carpenter. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270: 17656-17659, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 29
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • Vojtek, A. B., and J. A. Cooper. Rho family members: activators of MAP kinase cascades. Cell 82: 527-529, 1995.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 30
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond, S. H. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8: 66-73, 1996.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 66-73
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.