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Volumn 496, Issue 2, 1996, Pages 317-329

Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscle

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BETA ESCIN; CALCIUM ION; CARBACHOL; CLOSTRIDIUM DIFFICILE TOXIN B; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); GUANOSINE TRIPHOSPHATASE; POTASSIUM ION; PROTEIN; RHO FACTOR;

EID: 0029831696     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.1996.sp021687     Document Type: Article
Times cited : (106)

References (49)
  • 1
    • 0028906470 scopus 로고
    • Activation of mitogen-activated protein kinase in porcine arteries
    • ADAM, L. P., FRANKLIN, M. T., RAFF, G. J. & HATHAWAY, D. R. (1995). Activation of mitogen-activated protein kinase in porcine arteries. Circulation Research 76, 183-190.
    • (1995) Circulation Research , vol.76 , pp. 183-190
    • Adam, L.P.1    Franklin, M.T.2    Raff, G.J.3    Hathaway, D.R.4
  • 3
    • 0023882163 scopus 로고
    • Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterisation of the ADP-ribosylation reaction in platelet membranes
    • AKTORIES, K., RÖSENER, S., BLASCHKE, U. & CHATWAL, G. S. (1988). Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterisation of the ADP-ribosylation reaction in platelet membranes. European Journal of Biochemistry 172, 445-450.
    • (1988) European Journal of Biochemistry , vol.172 , pp. 445-450
    • Aktories, K.1    Rösener, S.2    Blaschke, U.3    Chatwal, G.S.4
  • 4
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • BOURNE, H. R., SANDERS, D. A. & MCCORMICK, F. (1990). The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-131.
    • (1990) Nature , vol.348 , pp. 125-131
    • Bourne, H.R.1    Sanders, D.A.2    Mccormick, F.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • BRADFORD, M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 6
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • CHONG, L. D., TRAYNUR-KAPLAN, A., BOKOCH, G. M. & SCHWARTZ, M. A. (1994). The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79, 507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynur-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 10
    • 0023175490 scopus 로고
    • Purification of two high molecular weight toxins of Clostridium difficile which are antigenetically related
    • EICHEL-STREIBER, C., HARPERATH, U., BOSKE, D. & HADDING, U. (1987). Purification of two high molecular weight toxins of Clostridium difficile which are antigenetically related. Microbial Pathogenesis 2, 307-318.
    • (1987) Microbial Pathogenesis , vol.2 , pp. 307-318
    • Eichel-Streiber, C.1    Harperath, U.2    Boske, D.3    Hadding, U.4
  • 11
    • 0021108235 scopus 로고
    • Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts
    • FLORIN, I. & THELESTAM, M. (1983). Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts. Biochimica et Biophysica Acta 763, 383-392.
    • (1983) Biochimica et Biophysica Acta , vol.763 , pp. 383-392
    • Florin, I.1    Thelestam, M.2
  • 12
    • 0028300628 scopus 로고
    • ADP-ribosylation of Rho proteins by Clostridium botulinum exoenzyme C3 is influenced by phosphorylation of Rho-associated factors
    • FRITZ, G. & AKTORIES, K. (1994). ADP-ribosylation of Rho proteins by Clostridium botulinum exoenzyme C3 is influenced by phosphorylation of Rho-associated factors. Biochemical Journal 300, 133-139.
    • (1994) Biochemical Journal , vol.300 , pp. 133-139
    • Fritz, G.1    Aktories, K.2
  • 14
    • 0024497356 scopus 로고
    • Effects of guanosine nucleotides on skinned smooth muscle tissue of the rabbit mesenteric artery
    • FUJIWARA, T., ITOH, T., KUBOTA, Y. & KURIYAMA, H. (1989). Effects of guanosine nucleotides on skinned smooth muscle tissue of the rabbit mesenteric artery. Journal of Physiology 408, 535-547.
    • (1989) Journal of Physiology , vol.408 , pp. 535-547
    • Fujiwara, T.1    Itoh, T.2    Kubota, Y.3    Kuriyama, H.4
  • 15
    • 0028944568 scopus 로고
    • Clostridium difficile toxin B activates calcium influx required for actin disassembly during cytotoxicity
    • GILBERT, R. J., POTHOULAKIS, C., LAMONT, J. T. & YAKUBOVICH, M. (1995). Clostridium difficile toxin B activates calcium influx required for actin disassembly during cytotoxicity. American Journal of Physiology 268, G487-495.
    • (1995) American Journal of Physiology , vol.268
    • Gilbert, R.J.1    Pothoulakis, C.2    Lamont, J.T.3    Yakubovich, M.4
  • 17
    • 0020493109 scopus 로고
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • 2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography. Biochemical and Biophysical Research Communications 104, 830-836.
    • (1982) Biochemical and Biophysical Research Communications , vol.104 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 18
    • 0023858610 scopus 로고
    • Free calcium and force transients during depolarization and pharmacomechanical coupling in guinea-pig smooth muscle
    • HIMPENS, B. & SOMLYO, A. P. (1988). Free calcium and force transients during depolarization and pharmacomechanical coupling in guinea-pig smooth muscle. Journal of Physiology 395, 507-530.
    • (1988) Journal of Physiology , vol.395 , pp. 507-530
    • Himpens, B.1    Somlyo, A.P.2
  • 21
    • 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., VAN CURVEN, E. J., HENGEVELD, T., MORII, N., NARUMIYA, S. & MOOLENAAR, W. H. (1994). Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. Journal of Cell Biology 126, 801-810.
    • (1994) Journal of Cell Biology , vol.126 , pp. 801-810
    • Jalink, K.1    Van Curven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 31
    • 0027496730 scopus 로고
    • ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3TU cells
    • KUMAGI, N., MORII, N., FUJISAWA, K., NEMOTO, Y. & NARUMIYA, S. (1993). ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3TU cells. Journal of Biological Chemistry 268, 24535-24538.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 24535-24538
    • Kumagi, N.1    Morii, N.2    Fujisawa, K.3    Nemoto, Y.4    Narumiya, S.5
  • 32
    • 0026541143 scopus 로고
    • Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein
    • LEEVERS, S. J. & MARSHALL, C. J. (1992). Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein. EMBO Journal 11, 569-574.
    • (1992) EMBO Journal , vol.11 , pp. 569-574
    • Leevers, S.J.1    Marshall, C.J.2
  • 33
    • 0028980248 scopus 로고
    • Involvement of rho in GTPyS-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: Inhibition of phosphatase activity
    • NODA, M., YASUDA-FUKUZAWA, C, MORIISHI, K., KATO, T, OKUDA, T, KUROKAWA, K. & TAKUWA, Y. (1995). Involvement of rho in GTPyS-induced enhancement of phosphorylation of 20 kDa myosin light chain in vascular smooth muscle cells: inhibition of phosphatase activity. FEBS Letters 367, 246-250.
    • (1995) FEBS Letters , vol.367 , pp. 246-250
    • Noda, M.1    Yasuda-Fukuzawa, C.2    Moriishi, K.3    Kato, T.4    Okuda, T.5    Kurokawa, K.6    Takuwa, Y.7
  • 34
    • 85035175340 scopus 로고
    • Inhibition of intact and permeabilized smooth muscle by toxin B from C. difficile
    • OTTO, B., TROSCHKA, M., JUST, I., AKTORIES, K. & PFITZER, G. (1995). Inhibition of intact and permeabilized smooth muscle by toxin B from C. difficile. Pflügers Archiv 429, A263.
    • (1995) Pflügers Archiv , vol.429
    • Otto, B.1    Troschka, M.2    Just, I.3    Aktories, K.4    Pfitzer, G.5
  • 35
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21 rho induces rapid changes in cell morphology
    • PATERSON, H., SELF, A. J., GARRET, M. D. & JUST, J. (1990). Microinjection of recombinant p21 rho induces rapid changes in cell morphology. Journal of Cell Biology 111, 1001-1007.
    • (1990) Journal of Cell Biology , vol.111 , pp. 1001-1007
    • Paterson, H.1    Self, A.J.2    Garret, M.D.3    Just, J.4
  • 36
    • 0028912216 scopus 로고
    • Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction
    • PAVALKO, F. M., ADAM, L. P., WU, M. F., WALKER, T. L. & GUNST, S. J. (1995). Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction. American Journal of Physiology 268, C563-571.
    • (1995) American Journal of Physiology , vol.268
    • Pavalko, F.M.1    Adam, L.P.2    Wu, M.F.3    Walker, T.L.4    Gunst, S.J.5
  • 37
    • 0013493438 scopus 로고
    • Permeabilized smooth muscle
    • ed. BARANY, M., Academic Press
    • PFITZER, G. (1995). Permeabilized smooth muscle. In The Biochemistry of Smooth Muscle Contraction, ed. BARANY, M., pp. 191-199. Academic Press.
    • (1995) The Biochemistry of Smooth Muscle Contraction , pp. 191-199
    • Pfitzer, G.1
  • 39
    • 0027944638 scopus 로고
    • Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125FAK and paxillin induced by bombesin and endothelin
    • RANKIN, S., MORII, N., NARUMIYA, S. & ROZENGURT, E. (1994). Botulinum C3 exoenzyme blocks the tyrosine phosphorylation of p125FAK and paxillin induced by bombesin and endothelin. FEBS Letters 354, 315-319.
    • (1994) FEBS Letters , vol.354 , pp. 315-319
    • Rankin, S.1    Morii, N.2    Narumiya, S.3    Rozengurt, E.4
  • 40
    • 0025197314 scopus 로고
    • 2+ sensitivity of myasin phosphorylation in intact swine arterial smooth muscle
    • 2+ sensitivity of myasin phosphorylation in intact swine arterial smooth muscle. Journal of Physiology 429, 77-94.
    • (1990) Journal of Physiology , vol.429 , pp. 77-94
    • Rembold, C.M.1
  • 41
    • 0028894787 scopus 로고
    • Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells
    • RIDLEY, A. J., COMOGLIO, P. M. & HALL, A. (1995). Regulation of scatter factor/hepatocyte growth factor responses by Ras, Rac, and Rho in MDCK cells. Molecular and Cellular Biolngy 15, 1110-1122.
    • (1995) Molecular and Cellular Biolngy , vol.15 , pp. 1110-1122
    • Ridley, A.J.1    Comoglio, P.M.2    Hall, A.3
  • 42
    • 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. & HALL, A. (1992). 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) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 43
    • 0027969286 scopus 로고
    • 2+-sensitization of coronary artery contraction in genetically hypertensive rats: Evidence for altered signal transduction in the coronary smooth muscle cell
    • 2+-sensitization of coronary artery contraction in genetically hypertensive rats: evidence for altered signal transduction in the coronary smooth muscle cell. Journal of Clinical Investigation 94, 1397-1403.
    • (1994) Journal of Clinical Investigation , vol.94 , pp. 1397-1403
    • Satoh, S.1    Kreutz, R.2    Wilm, C.3    Ganten, D.4    Pfitzer, G.5
  • 45
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • SOMLYO, A. P. & SOMLYO, A. V. (1994). Signal transduction and regulation in smooth muscle. Nature 372, 231-236.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 48
    • 0027952703 scopus 로고
    • Involvement of rho p21 small GTP-binding protein and its regulator in HGF-induced cell motility
    • TAKAISHI, K., SASAKI, T., KATO, M., YAMOCHI, W., KURODA, S., NAKAMURA, T., TAKEICHI, M. & TAKAI, Y. (1994). Involvement of rho p21 small GTP-binding protein and its regulator in HGF-induced cell motility. Oncogene 9, 273-279.
    • (1994) Oncogene , vol.9 , pp. 273-279
    • Takaishi, K.1    Sasaki, T.2    Kato, M.3    Yamochi, W.4    Kuroda, S.5    Nakamura, T.6    Takeichi, M.7    Takai, Y.8
  • 49
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • VOJTEK, A. B. & COOPER, J. A. (1995). Rho family members: activators of MAP kinase cascades. Cell 82, 527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2


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