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Volumn 48, Issue 10, 1999, Pages 1241-1247

Disruption of filamentous actin diminishes hormonally evoked Ca2+ responses in rat liver

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CYTOCHALASIN D; F ACTIN; FURA 2; GLUCAGON; MANGANESE; OXYGEN; PHALLOIDIN; VASOPRESSIN;

EID: 0032727589     PISSN: 00260495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0026-0495(99)90262-7     Document Type: Article
Times cited : (7)

References (52)
  • 1
    • 0024457508 scopus 로고
    • From signal to pseudopod. How cells control cytoplasmic actin assembly
    • Stossel TP: From signal to pseudopod. How cells control cytoplasmic actin assembly. J Biol Chem 264:18261-18264, 1989
    • (1989) J Biol Chem , vol.264 , pp. 18261-18264
    • Stossel, T.P.1
  • 2
    • 0023508472 scopus 로고
    • Interaction of the cytoskeleton with the plasma membrane
    • Niggli V, Burger MM: Interaction of the cytoskeleton with the plasma membrane. J Membr Biol 100:97-121, 1987
    • (1987) J Membr Biol , vol.100 , pp. 97-121
    • Niggli, V.1    Burger, M.M.2
  • 4
    • 0026497661 scopus 로고
    • Cytoskeleton-membrane interactions
    • Luna JE, Hitt AL: Cytoskeleton-membrane interactions. Science 258:955-964, 1992
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, J.E.1    Hitt, A.L.2
  • 5
    • 0030047838 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interactions
    • Cowin P, Burke B: Cytoskeleton-membrane interactions. Curr Opin Cell Biol 8:56-65, 1996
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 56-65
    • Cowin, P.1    Burke, B.2
  • 6
    • 0019468104 scopus 로고
    • Membrane-associated cytoskeleton and coated vesicles in cultured hepatocytes visualized by drycleaving
    • Mesland DAM, Spiele H, Roos E: Membrane-associated cytoskeleton and coated vesicles in cultured hepatocytes visualized by drycleaving. Exp Cell Res 132:169-184, 1981
    • (1981) Exp Cell Res , vol.132 , pp. 169-184
    • Mesland, D.A.M.1    Spiele, H.2    Roos, E.3
  • 7
    • 0016767907 scopus 로고
    • Ultrastructural localization of actin-like filaments in rat hepatocytes
    • French SW, Davies PL: Ultrastructural localization of actin-like filaments in rat hepatocytes. Gastroenterology 68:765-774, 1975
    • (1975) Gastroenterology , vol.68 , pp. 765-774
    • French, S.W.1    Davies, P.L.2
  • 8
    • 0016697537 scopus 로고
    • Phalloidininduced hyperplasia of actin filaments in rat hepatocytes
    • Gabbiani G, Montessano R, Tuchweber B, et al: Phalloidininduced hyperplasia of actin filaments in rat hepatocytes. Lab Invest 33:562-569, 1975
    • (1975) Lab Invest , vol.33 , pp. 562-569
    • Gabbiani, G.1    Montessano, R.2    Tuchweber, B.3
  • 9
    • 0026635134 scopus 로고
    • Localization of actin in normal human hepatocytes using fluorescent phallotoxins and immunohistochemical amplification
    • Benkoel L, Brisse J, Capo C, et al: Localization of actin in normal human hepatocytes using fluorescent phallotoxins and immunohistochemical amplification. Cell Mol Biol 38:377-383, 1992
    • (1992) Cell Mol Biol , vol.38 , pp. 377-383
    • Benkoel, L.1    Brisse, J.2    Capo, C.3
  • 10
    • 0344140186 scopus 로고
    • Cytoskeleton: Its role in cellular function
    • introduction
    • Hesketh J, Pryme IF: Cytoskeleton: Its role in cellular function. Biochem Soc Trans 19:1015, 1991 (introduction)
    • (1991) Biochem Soc Trans , vol.19 , pp. 1015
    • Hesketh, J.1    Pryme, I.F.2
  • 11
    • 0030597056 scopus 로고    scopus 로고
    • Calcium storage and release properties of F-actin: Evidence for the involvement of F-actin in cellular calcium signalling
    • Lange K, Brandt U: Calcium storage and release properties of F-actin: Evidence for the involvement of F-actin in cellular calcium signalling. FEBS Lett 395:137-142, 1996
    • (1996) FEBS Lett , vol.395 , pp. 137-142
    • Lange, K.1    Brandt, U.2
  • 12
    • 0026532680 scopus 로고
    • Direct proof that the primary site of action of cytochalasin on cell motility processes is actin
    • Ohmori H, Toyama S, Toyama S: Direct proof that the primary site of action of cytochalasin on cell motility processes is actin. J Cell Biol 116:933-941, 1992
    • (1992) J Cell Biol , vol.116 , pp. 933-941
    • Ohmori, H.1    Toyama, S.2    Toyama, S.3
  • 14
    • 0027751653 scopus 로고
    • 3 receptor with the plasma membrane: Relevance to mode of action
    • 3 receptor with the plasma membrane: Relevance to mode of action. Am J Physiol 265:C1588-C1596,1993
    • (1993) Am J Physiol , vol.265
    • Feng, L.1    Kraus-Friedmann, N.2
  • 16
    • 0021184806 scopus 로고
    • Alterations in intracellular calcium compartmentation following the inhibition of calcium efflux from isolated hepatocytes
    • Bellomo G, Nicotera P, Orrenius S: Alterations in intracellular calcium compartmentation following the inhibition of calcium efflux from isolated hepatocytes. Eur J Biochem 144:19-23, 1984
    • (1984) Eur J Biochem , vol.144 , pp. 19-23
    • Bellomo, G.1    Nicotera, P.2    Orrenius, S.3
  • 17
    • 0019277497 scopus 로고
    • Role of the cytoskeleton in glycogenolysis stimulation by glucagon in primary cultures of adult hepatocytes
    • Tomomura A, Nakamura T, Ichihara A: Role of the cytoskeleton in glycogenolysis stimulation by glucagon in primary cultures of adult hepatocytes. Biochem Biophys Res Commun 97:1276-1282, 1980
    • (1980) Biochem Biophys Res Commun , vol.97 , pp. 1276-1282
    • Tomomura, A.1    Nakamura, T.2    Ichihara, A.3
  • 18
    • 0014965085 scopus 로고
    • Calcium, manganese and hepatic gluconeogenesis
    • Friedmann N, Rasmussen H: Calcium, manganese and hepatic gluconeogenesis. Biochim Biophys Acta 222:41-52, 1970
    • (1970) Biochim Biophys Acta , vol.222 , pp. 41-52
    • Friedmann, N.1    Rasmussen, H.2
  • 19
    • 0026724636 scopus 로고
    • Demonstration of ryanodineinduced metabolic effects in rat liver
    • Pereira B, Feng L, Bazotte R, et al: Demonstration of ryanodineinduced metabolic effects in rat liver. Biochem Pharmacol 44:413-416, 1992
    • (1992) Biochem Pharmacol , vol.44 , pp. 413-416
    • Pereira, B.1    Feng, L.2    Bazotte, R.3
  • 20
    • 0014645531 scopus 로고
    • High-yield preparation of isolated rat liver parenchymal cells. A biochemical and structural study
    • Berry MN, Friends DS: High-yield preparation of isolated rat liver parenchymal cells. A biochemical and structural study. J Cell Biol 43:506-520, 1969
    • (1969) J Cell Biol , vol.43 , pp. 506-520
    • Berry, M.N.1    Friends, D.S.2
  • 21
    • 0026043996 scopus 로고
    • Effects of ryanodine on calcium sequestration in rat liver
    • Bazotte RB, Pereira B, Higham S, et al: Effects of ryanodine on calcium sequestration in rat liver. Biochem Pharmacol 42:1799-1803, 1991
    • (1991) Biochem Pharmacol , vol.42 , pp. 1799-1803
    • Bazotte, R.B.1    Pereira, B.2    Higham, S.3
  • 22
    • 0028004310 scopus 로고
    • 2+ levels in liver by the immunosuppressant FK506
    • 2+ levels in liver by the immunosuppressant FK506. Biochem Pharmacol 42:2157-2162, 1994
    • (1994) Biochem Pharmacol , vol.42 , pp. 2157-2162
    • Kraus-Friedmann, N.1    Feng, L.2
  • 24
    • 0021895138 scopus 로고
    • 2- indicators with greatly improved fluorescence properties
    • 2- indicators with greatly improved fluorescence properties. J Biol Chem 260:3440-3450, 1985
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Ponie, M.2    Tsien, R.Y.3
  • 25
    • 0024997044 scopus 로고
    • Receptor-operated calcium influx in hepatocytes
    • Kass GEN, Llopis J, Chow SC, et al: Receptor-operated calcium influx in hepatocytes. J Biol Chem 265:17486-17492, 1990
    • (1990) J Biol Chem , vol.265 , pp. 17486-17492
    • Kass, G.E.N.1    Llopis, J.2    Chow, S.C.3
  • 26
    • 0028169313 scopus 로고
    • 2+ influx in rat hepatocytes: Comparison of cells loaded with fura-2 ester and cells microinjected with fura-2 salts
    • 2+ influx in rat hepatocytes: Comparison of cells loaded with fura-2 ester and cells microinjected with fura-2 salts. Biochem J 302:5-9, 1994
    • (1994) Biochem J , vol.302 , pp. 5-9
    • Kass, G.E.N.1    Webb, D.L.2    Chow, S.C.3
  • 27
    • 0024445033 scopus 로고
    • Microfilaments and cellular signal transduction: Effect of cytochalasin D on the production of cAMP, inositol phosphates, and on calcium movements in rat parotid glands
    • Huleux C, Dreux C, Imhoff V, et al: Microfilaments and cellular signal transduction: Effect of cytochalasin D on the production of cAMP, inositol phosphates, and on calcium movements in rat parotid glands. Biol Cell 67:185-193, 1989
    • (1989) Biol Cell , vol.67 , pp. 185-193
    • Huleux, C.1    Dreux, C.2    Imhoff, V.3
  • 28
    • 0028264160 scopus 로고
    • Luminal communication between intracellular calcium stores modulated by GTP and the cytoskeleton
    • Hajnoczky G, Lin C, Thomas AP: Luminal communication between intracellular calcium stores modulated by GTP and the cytoskeleton. J Biol Chem 269:10280-10287, 1994
    • (1994) J Biol Chem , vol.269 , pp. 10280-10287
    • Hajnoczky, G.1    Lin, C.2    Thomas, A.P.3
  • 29
    • 0028224822 scopus 로고
    • Inositol 1,4,5-trisphosphate activates receptor-mediated calcium entry by two different pathways in hepatocytes
    • Striggow F, Bohnensack R: Inositol 1,4,5-trisphosphate activates receptor-mediated calcium entry by two different pathways in hepatocytes. Eur J Biochem 222:229-234, 1994
    • (1994) Eur J Biochem , vol.222 , pp. 229-234
    • Striggow, F.1    Bohnensack, R.2
  • 30
    • 0024453294 scopus 로고
    • Inositol phosphates and cell signalling
    • Berridge MJ, Irvine RF: Inositol phosphates and cell signalling. Nature 341:197-205, 1989
    • (1989) Nature , vol.341 , pp. 197-205
    • Berridge, M.J.1    Irvine, R.F.2
  • 31
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge MJ: Capacitative calcium entry. Biochem J 312:1-11, 1995
    • (1995) Biochem J , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 32
    • 0030004471 scopus 로고    scopus 로고
    • The role of intracellular calcium in the regulation of gluconeogenesis
    • Kraus-Friedmann N, Feng L: The role of intracellular calcium in the regulation of gluconeogenesis. Metabolism 45:389-403, 1996
    • (1996) Metabolism , vol.45 , pp. 389-403
    • Kraus-Friedmann, N.1    Feng, L.2
  • 33
    • 0017331962 scopus 로고
    • On the role of calcium as a second messenger in liver for hormonally-induced activation of glycogen phosphorylase
    • Keppens S, Vandenheede JR, Wulf H: On the role of calcium as a second messenger in liver for hormonally-induced activation of glycogen phosphorylase. Biochim Biophys Acta 496:448-457, 1977
    • (1977) Biochim Biophys Acta , vol.496 , pp. 448-457
    • Keppens, S.1    Vandenheede, J.R.2    Wulf, H.3
  • 34
    • 0022445402 scopus 로고
    • 2+ influx and polyphosphoinositide metabolism in isolated hepatocytes
    • 2+ influx and polyphosphoinositide metabolism in isolated hepatocytes. Biochem J 235:663-669, 1986
    • (1986) Biochem J , vol.235 , pp. 663-669
    • Poggioli, J.1    Mauger, J.P.2    Claret, M.3
  • 37
    • 0027288899 scopus 로고
    • 2+ inflow is an early action of glucagon and dibutyryl cyclic AMP in rat hepatocytes
    • 2+ inflow is an early action of glucagon and dibutyryl cyclic AMP in rat hepatocytes. Biochem J 292:19-22, 1993
    • (1993) Biochem J , vol.292 , pp. 19-22
    • Bygrave, F.L.1    Gamberucci, A.2    Fulceri, R.3
  • 39
    • 0028986864 scopus 로고
    • 2+-mobilizing actions of Jurkat cell extract of mammalian cells and Xenopus laevis oocytes
    • 2+-mobilizing actions of Jurkat cell extract of mammalian cells and Xenopus laevis oocytes. J Biol Chem 270:8050-8055, 1995
    • (1995) J Biol Chem , vol.270 , pp. 8050-8055
    • Gilon, P.1    Bird, G.S.J.2    Bian, X.3
  • 40
    • 0028067857 scopus 로고
    • Signal transduction and calcium: A suggested role for the cytoskeleton in inositol 1,4,5-trisphosphate action
    • Kraus-Friedmann N: Signal transduction and calcium: A suggested role for the cytoskeleton in inositol 1,4,5-trisphosphate action. Cell Motil Cytoskeleton 28:279-284, 1994
    • (1994) Cell Motil Cytoskeleton , vol.28 , pp. 279-284
    • Kraus-Friedmann, N.1
  • 43
    • 0030583550 scopus 로고    scopus 로고
    • Expression of photoreceptor cyclic-nucleotide-gated cation channel subunit (CNGC) in the liver and skeletal muscle
    • Feng L, Subbaraya I, Yamamoto NS, et al: Expression of photoreceptor cyclic-nucleotide-gated cation channel subunit (CNGC) in the liver and skeletal muscle. FEBS Lett 395:77-81, 1996
    • (1996) FEBS Lett , vol.395 , pp. 77-81
    • Feng, L.1    Subbaraya, I.2    Yamamoto, N.S.3
  • 44
    • 0032544624 scopus 로고    scopus 로고
    • Molecular cloning of cDNA encoding the α unit of CNGC gene from human fetal heart
    • Gong L, Kraus N: Molecular cloning of cDNA encoding the α unit of CNGC gene from human fetal heart. Life Sci 63:1555-1562, 1998
    • (1998) Life Sci , vol.63 , pp. 1555-1562
    • Gong, L.1    Kraus, N.2
  • 45
    • 0026579804 scopus 로고
    • Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes
    • Shariff A, Luna EJ: Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes. Science 256:245-247, 1992
    • (1992) Science , vol.256 , pp. 245-247
    • Shariff, A.1    Luna, E.J.2
  • 46
    • 0021218144 scopus 로고
    • The role of cytoskeleton in hormone action
    • Hall PF: The role of cytoskeleton in hormone action. Can J Biochem Cell Biol 62:653-665, 1984
    • (1984) Can J Biochem Cell Biol , vol.62 , pp. 653-665
    • Hall, P.F.1
  • 47
    • 0025987518 scopus 로고
    • High molecular mass complexes of the regulatory subunits of cyclic AMP-dependent protein kinases
    • Haarik J, Fauske B, Flatmark T, et al: High molecular mass complexes of the regulatory subunits of cyclic AMP-dependent protein kinases. Biochem Soc Trans 19:1163-1165, 1991
    • (1991) Biochem Soc Trans , vol.19 , pp. 1163-1165
    • Haarik, J.1    Fauske, B.2    Flatmark, T.3
  • 48
    • 0026515691 scopus 로고
    • 2+-mediated secretion in parotid acinar cells is associated with reversible changes in the organization of the cytoskeleton
    • 2+-mediated secretion in parotid acinar cells is associated with reversible changes in the organization of the cytoskeleton. J Cell Biol 116:127-137, 1992
    • (1992) J Cell Biol , vol.116 , pp. 127-137
    • Perrin, D.1    Moller, K.2    Hanke, K.3
  • 49
    • 0028081499 scopus 로고
    • Regulation of motility and cytoskeletal organization of rat bladder carcinoma cells by cyclic-AMP
    • Morton DM, Tchao R: Regulation of motility and cytoskeletal organization of rat bladder carcinoma cells by cyclic-AMP. Cell Motil Cytoskeleton 29:375-382, 1994
    • (1994) Cell Motil Cytoskeleton , vol.29 , pp. 375-382
    • Morton, D.M.1    Tchao, R.2
  • 50
    • 0005188452 scopus 로고
    • Vasopressin depolymerizes apical F-actin in rat inner medullary collecting duct
    • Simon H, Gao Y, Franki N, et al: Vasopressin depolymerizes apical F-actin in rat inner medullary collecting duct. Am J Physiol 265:C757-C762, 1993
    • (1993) Am J Physiol , vol.265
    • Simon, H.1    Gao, Y.2    Franki, N.3
  • 51
    • 85030368689 scopus 로고
    • Cytoskeletal changes in endothelial cells exposed to 8-bromo cAMP
    • abstr
    • Merkle CJ, Shaeffer RC Jr: Cytoskeletal changes in endothelial cells exposed to 8-bromo cAMP. Mol Biol Cell 61:161a, 1995 (abstr)
    • (1995) Mol Biol Cell , vol.61
    • Merkle, C.J.1    Shaeffer Jr., R.C.2
  • 52
    • 0024317027 scopus 로고
    • Cyclic AMP-mediated cytoskeletal effects in adrenal cells are modified by serum insulin, insulin-like growth factor-I, and an antibody against urokinase plasminogen activator
    • Horsby PJ, Maghsoudlon SS, Cheng V, et al: Cyclic AMP-mediated cytoskeletal effects in adrenal cells are modified by serum insulin, insulin-like growth factor-I, and an antibody against urokinase plasminogen activator. Mol Cell Endocrinol 67:185-193, 1989
    • (1989) Mol Cell Endocrinol , vol.67 , pp. 185-193
    • Horsby, P.J.1    Maghsoudlon, S.S.2    Cheng, V.3


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