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Volumn 274, Issue 5 18-5, 1998, Pages

Carbachol-induced actin reorganization involves G(i) activation of Rho in human airway smooth muscle cells

Author keywords

Fluoroscein isothiocyanate labeled phalloidin; G(i) proteins; M2 muscarinic receptor; Rho proteins; Stress fiber formation; Texas Red labeled deoxyribonuclease

Indexed keywords

ACTIN; CARBACHOL; DEOXYRIBONUCLEASE; G ACTIN; MITOGENIC AGENT; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C;

EID: 0031807422     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1998.274.5.l803     Document Type: Article
Times cited : (88)

References (43)
  • 1
    • 0028964295 scopus 로고
    • ADP-ribosylation of rho enhances adhesion of U937 cells to fibronectin via the α5β1 integrin receptor
    • Aepfelbacher, M. ADP-ribosylation of rho enhances adhesion of U937 cells to fibronectin via the α5β1 integrin receptor. FEBS Lett. 363: 78-80, 1995.
    • (1995) FEBS Lett. , vol.363 , pp. 78-80
    • Aepfelbacher, M.1
  • 2
    • 0028139085 scopus 로고
    • Clostridial ADP-ribosylating toxins: Effects on ATP and GTP-binding proteins
    • Aktories, K. Clostridial ADP-ribosylating toxins: effects on ATP and GTP-binding proteins. Mol. Cell. Biochem. 138: 167-176, 1994.
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 167-176
    • Aktories, K.1
  • 3
    • 0030005715 scopus 로고    scopus 로고
    • Cell shape determination: A pivotal role for Rho
    • Bussey, H. Cell shape determination: a pivotal role for Rho. Science 272: 224-225, 1996.
    • (1996) Science , vol.272 , pp. 224-225
    • Bussey, H.1
  • 4
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P., P. Boquet, P. Madaule, M. R. Popoff, E. J. Rubin, and D. M. Gill. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8: 1087-1092, 1989.
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 5
    • 0031110583 scopus 로고    scopus 로고
    • Effects of protein tyrosine kinase inhibitors on contractility of isolated bronchioles of the rat
    • Chopra, L. C., D. Hucks, C. H. C. Twort, and J. P. T. Ward. Effects of protein tyrosine kinase inhibitors on contractility of isolated bronchioles of the rat. Am. J. Respir. Cell Mol. Biol. 16: 372-378, 1997.
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.16 , pp. 372-378
    • Chopra, L.C.1    Hucks, D.2    Twort, C.H.C.3    Ward, J.P.T.4
  • 6
    • 0030919582 scopus 로고    scopus 로고
    • Protein tyrosine phosphorylation in smooth muscle: A potential coupling mechanism between receptor activation and intracellular calcium
    • Di Salvo, J., S. R. Nelson, and N. Kaplan. Protein tyrosine phosphorylation in smooth muscle: a potential coupling mechanism between receptor activation and intracellular calcium. Proc. Soc. Exp. Biol. Med. 214: 285-301, 1997.
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.214 , pp. 285-301
    • Di Salvo, J.1    Nelson, S.R.2    Kaplan, N.3
  • 11
    • 0029013930 scopus 로고
    • Muscarinic acetylcholine receptors: Signal transduction through multiple effectors
    • Felder, C. C. Muscarinic acetylcholine receptors: signal transduction through multiple effectors. FASEB J. 9: 619-625, 1995.
    • (1995) FASEB J. , vol.9 , pp. 619-625
    • Felder, C.C.1
  • 12
    • 0026612959 scopus 로고
    • 2 muscarinic receptors inhibit isoproterenol-induced relaxation of canine airway smooth muscle
    • 2 muscarinic receptors inhibit isoproterenol-induced relaxation of canine airway smooth muscle. J. Pharmacol. Exp. Ther. 262: 119-126, 1992.
    • (1992) J. Pharmacol. Exp. Ther. , vol.262 , pp. 119-126
    • Fernandes, L.B.1    Fryer, A.D.2    Hirshman, C.A.3
  • 13
    • 0024994954 scopus 로고
    • Identification of three muscarinic receptor subtypes in rat lung using binding studies with selective antagonists
    • Fryer, A. D., and E. E. El-Fakahany. Identification of three muscarinic receptor subtypes in rat lung using binding studies with selective antagonists. Life Sci. 47: 611-618, 1990.
    • (1990) Life Sci. , vol.47 , pp. 611-618
    • Fryer, A.D.1    El-Fakahany, E.E.2
  • 15
    • 0027991902 scopus 로고
    • Lysophosphatidic acid activation of phosphatidylcholine-hydrolysing phospholipase D and actin polymerization by a pertussis toxin-sensitive mechanism
    • Ha, K.-S., E.-J. Yeo, and J. H. Exton. Lysophosphatidic acid activation of phosphatidylcholine-hydrolysing phospholipase D and actin polymerization by a pertussis toxin-sensitive mechanism. Biochem. J. 303: 55-59, 1994.
    • (1994) Biochem. J. , vol.303 , pp. 55-59
    • Ha, K.-S.1    Yeo, E.-J.2    Exton, J.H.3
  • 16
    • 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
  • 17
    • 0029015774 scopus 로고
    • The Rho family GTPases rhoA, rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill, C. S., J. Wynne, and R. Treisman. The Rho family GTPases rhoA, rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 81: 1159-1170, 1995.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 19
    • 0029855239 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton, integrins and cell growth by the Rho family of small GTPases
    • Hotchin, N. A., and A. Hall. Regulation of the actin cytoskeleton, integrins and cell growth by the Rho family of small GTPases. Cancer Surv. 27: 311-322, 1996.
    • (1996) Cancer Surv. , vol.27 , pp. 311-322
    • Hotchin, N.A.1    Hall, A.2
  • 20
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink, K., E. J. Van Corven, T. Hengeveld, N. Morii, S. Narumiya, and W. H. Moolenaar. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J. Cell Biol. 126: 801-810, 1994.
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 21
    • 0028274104 scopus 로고
    • Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly
    • Janmey, P. A. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu. Rev. Physiol. 56: 169-191, 1994.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 169-191
    • Janmey, P.A.1
  • 22
    • 0026774583 scopus 로고
    • Simultaneous localization and quantification of relative G and F actin content: Optimization of fluorescence labeling methods
    • Knowles, G. C., and C. A. G. McCulloch. Simultaneous localization and quantification of relative G and F actin content: optimization of fluorescence labeling methods. J. Histochem. Cytochem. 40: 1605-1612, 1992.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1605-1612
    • Knowles, G.C.1    McCulloch, C.A.G.2
  • 24
    • 0025160266 scopus 로고
    • Tyrphostins - Potential antiproliferative agents and novel molecular tools
    • Levitzki, A. Tyrphostins - potential antiproliferative agents and novel molecular tools. Biochem. Pharmacol. 40: 913-918, 1990.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 913-918
    • Levitzki, A.1
  • 25
    • 0029166671 scopus 로고
    • Rho, rac and cdc42 GTPases: Regulators of actin structures, cell adhesion and motility
    • Nobes, C. D., and A. Hall. Rho, rac and cdc42 GTPases: regulators of actin structures, cell adhesion and motility. Biochem. Soc. Trans. 23: 456-459, 1995.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 456-459
    • Nobes, C.D.1    Hall, A.2
  • 26
    • 0031050809 scopus 로고    scopus 로고
    • Involvement of tyrosine phosphorylation in endothelin-1-induced calcium-sensitization in rat small mesenteric arteries
    • Ohanian, J., V. Ohanian, L. Shaw, C. Bruce, and A. M. Heagerty. Involvement of tyrosine phosphorylation in endothelin-1-induced calcium-sensitization in rat small mesenteric arteries. Br. J. Pharmacol. 120: 653-661, 1997.
    • (1997) Br. J. Pharmacol. , vol.120 , pp. 653-661
    • Ohanian, J.1    Ohanian, V.2    Shaw, L.3    Bruce, C.4    Heagerty, A.M.5
  • 27
    • 0029831696 scopus 로고    scopus 로고
    • Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscle
    • Otto, B., A. Steusloff, I. Just, K. Aktories, and G. Pfitzer. Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscle. J. Physiol. (Lond.) 496: 317-329, 1996.
    • (1996) J. Physiol. (Lond.) , vol.496 , pp. 317-329
    • Otto, B.1    Steusloff, A.2    Just, I.3    Aktories, K.4    Pfitzer, G.5
  • 28
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21 rho induces rapid changes in cell morphology
    • Paterson, H. F., A. J. Self, M. D. Garrett, I. Just, K. Aktories, and A. Hall. Microinjection of recombinant p21 rho induces rapid changes in cell morphology. J. Cell Biol. 111: 1001-1007, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 1001-1007
    • Paterson, H.F.1    Self, A.J.2    Garrett, M.D.3    Just, I.4    Aktories, K.5    Hall, A.6
  • 29
    • 0029900434 scopus 로고    scopus 로고
    • G protein-coupled receptors and signaling pathways regulating growth responses
    • Post, G. R, and J. H. Brown. G protein-coupled receptors and signaling pathways regulating growth responses. FASEB J. 10: 741-749, 1996.
    • (1996) FASEB J. , vol.10 , pp. 741-749
    • Post, G.R.1    Brown, J.H.2
  • 30
    • 0028578072 scopus 로고
    • Signal transduction through the GTP-binding proteins Rac and Rho
    • Ridley, A. J. Signal transduction through the GTP-binding proteins Rac and Rho. J. Cell Sci. 18: 127-131, 1994.
    • (1994) J. Cell Sci. , vol.18 , pp. 127-131
    • Ridley, A.J.1
  • 31
    • 0028894787 scopus 로고
    • Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells
    • Ridley, A. J., P. M. Comoglio, and A. Hall. Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells. Mol. Cell. Biol. 15: 1110-1122, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1110-1122
    • Ridley, A.J.1    Comoglio, P.M.2    Hall, A.3
  • 32
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70: 389-399, 1992.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 33
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating Rho-mediated stress fibre formation: Requirement for a tyrosine kinase
    • Ridley, A. J., 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, A.J.1    Hall, A.2
  • 39
    • 17544377292 scopus 로고    scopus 로고
    • ADP-ribosylation of the G protein Rho inhibits integrin regulation of tumor cell growth
    • Udagawa, T., and B. W. McIntyre. ADP-ribosylation of the G protein Rho inhibits integrin regulation of tumor cell growth. J. Biol. Chem. 271: 12542-12548, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12542-12548
    • Udagawa, T.1    McIntyre, B.W.2


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