메뉴 건너뛰기




Volumn 48, Issue 4, 1995, Pages 970-984

Role of the actin cytoskeleton on epithelial Na+ channel regulation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTININ; AMILORIDE; CYTOCHALASIN D; GELSOLIN; SODIUM CHANNEL; VASOPRESSIN;

EID: 0029102078     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1038/ki.1995.379     Document Type: Conference Paper
Times cited : (111)

References (91)
  • 1
    • 0021239180 scopus 로고
    • Contribution of actin to the structure of cytomatrix
    • STOSSEL TP: Contribution of actin to the structure of cytomatrix. J Cell Biol 99(Suppl):15s-21s, 1984
    • (1984) J Cell Biol , vol.99 , Issue.SUPPL.
    • Stossel, T.P.1
  • 2
    • 0023262074 scopus 로고
    • +) ATPase and implications for the organization of membrane domains in polarized cells
    • +) ATPase and implications for the organization of membrane domains in polarized cells. Nature 328:533-536, 1987
    • (1987) Nature , vol.328 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.L.2
  • 3
    • 0025730273 scopus 로고
    • The spectrin skeleton: From red cells to brain
    • BENNETT V, LAMBERT S: The spectrin skeleton: From red cells to brain. J Clin Invest 87:1483-1489, 1991
    • (1991) J Clin Invest , vol.87 , pp. 1483-1489
    • Bennett, V.1    Lambert, S.2
  • 4
    • 0021218144 scopus 로고
    • The role of the cytoskeleton in hormone action
    • HALL PF: The role of the 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
  • 6
    • 0022411389 scopus 로고
    • Colocalization of Band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney
    • DRENCKHAHN D, SCHLUTER K, ALLEN DP, BENNETT V: Colocalization of Band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney. Science 230:1287-1290, 1985
    • (1985) Science , vol.230 , pp. 1287-1290
    • Drenckhahn, D.1    Schluter, K.2    Allen, D.P.3    Bennett, V.4
  • 8
    • 0023898489 scopus 로고
    • Identification of a 33 kD cytoskeletal protein with high affinity for the sodium channel
    • EDELSTEIN NG, CATTERAL WA, MOON RT: Identification of a 33 kD cytoskeletal protein with high affinity for the sodium channel. Biochem 27:1818-1822, 1988
    • (1988) Biochem , vol.27 , pp. 1818-1822
    • Edelstein, N.G.1    Catteral, W.A.2    Moon, R.T.3
  • 11
    • 0025834391 scopus 로고
    • Amiloride-sensitive sodium channel is linked to the cytoskeleton in renal epithelial cells
    • SMITH PR, SACCOMANI G, JOE E, ANGELIDES KJ, BENOS DJ: Amiloride-sensitive sodium channel is linked to the cytoskeleton in renal epithelial cells. Proc Natl Acad Sci USA 88:6971-6975, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6971-6975
    • Smith, P.R.1    Saccomani, G.2    Joe, E.3    Angelides, K.J.4    Benos, D.J.5
  • 13
    • 0027258451 scopus 로고
    • Calcium-induced actin depolymerization reduces NMDA channel activity
    • ROSENMUND C, WESTBROOK GL: Calcium-induced actin depolymerization reduces NMDA channel activity. Neuron 10:805-814, 1993
    • (1993) Neuron , vol.10 , pp. 805-814
    • Rosenmund, C.1    Westbrook, G.L.2
  • 15
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • POLLARD TD, COOPER JA: Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Ann Rev Biochem 55:987-1035, 1986
    • (1986) Ann Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 16
    • 0019569461 scopus 로고
    • Calcium control of microfilaments: Uncoupling of the F-actin-severing and-bundling activity of villin by limited proteolysis in vitro
    • GLENNEY JRJ, WEBER K: Calcium control of microfilaments: uncoupling of the F-actin-severing and-bundling activity of villin by limited proteolysis in vitro. Proc Natl Acad Sci USA 78:2810-2814, 1981
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2810-2814
    • Glenney, J.R.J.1    Weber, K.2
  • 18
    • 0020044056 scopus 로고
    • Action of cytochalasin D on cytoskeletal networks
    • SCHLIWA M: Action of cytochalasin D on cytoskeletal networks. J Cell Biol 92:79-91, 1982
    • (1982) J Cell Biol , vol.92 , pp. 79-91
    • Schliwa, M.1
  • 19
    • 0024095187 scopus 로고
    • Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone
    • FORSCHER P, SMITH SJ: Actions of cytochalasins on the organization of actin filaments and microtubules in a neuronal growth cone. J Cell Biol 107:1505-1516, 1988
    • (1988) J Cell Biol , vol.107 , pp. 1505-1516
    • Forscher, P.1    Smith, S.J.2
  • 20
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • KORN ED, CARLIER MF, PANTALONI D: Actin polymerization and ATP hydrolysis. Science 238:638-644, 1987
    • (1987) Science , vol.238 , pp. 638-644
    • Korn, E.D.1    Carlier, M.F.2    Pantaloni, D.3
  • 22
    • 0020493159 scopus 로고
    • Actin-binding proteins-regulators of cell architecture and motility
    • WEEDS A: Actin-binding proteins-regulators of cell architecture and motility. Nature 296:811-816, 1982
    • (1982) Nature , vol.296 , pp. 811-816
    • Weeds, A.1
  • 23
    • 0021243964 scopus 로고
    • Interaction of actin filaments with microtubules
    • POLLARD TD, SELDEN SC, MAUPIN P: Interaction of actin filaments with microtubules. J Cell Biol 99:33s-37s, 1984
    • (1984) J Cell Biol , vol.99
    • Pollard, T.D.1    Selden, S.C.2    Maupin, P.3
  • 24
    • 0022408470 scopus 로고
    • Microfilament-membrane interactions
    • GEIGER B: Microfilament-membrane interactions. Trends Biochem Sci 10:456-461, 1985
    • (1985) Trends Biochem Sci , vol.10 , pp. 456-461
    • Geiger, B.1
  • 25
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • HITT AL, LUNA EJ: Membrane interactions with the actin cytoskeleton. Curr Opin Cell Biol 1994:120-130, 1994
    • (1994) Curr Opin Cell Biol , vol.1994 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 26
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • CARLSSON L, NYSTROM L-E, SUNDKVIST I, MARKEY F, LINDEBERG U: Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 115:465-483, 1977
    • (1977) J Mol Biol , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.-E.2    Sundkvist, I.3    Markey, F.4    Lindeberg, U.5
  • 27
    • 0018140092 scopus 로고
    • Human platelets contain profilin, a potential regulator of actin polymerisability
    • MARKEY F, LINDBERT U, ERIKSSON L: Human platelets contain profilin, a potential regulator of actin polymerisability. FEBS Lett 75-79, 1978
    • (1978) FEBS Lett , pp. 75-79
    • Markey, F.1    Lindbert, U.2    Eriksson, L.3
  • 29
    • 0021814573 scopus 로고
    • The filamins: Properties and functions
    • WEIHING RR: The filamins: Properties and functions. Can J Biochem Cell Biol 63:397-413, 1985
    • (1985) Can J Biochem Cell Biol , vol.63 , pp. 397-413
    • Weihing, R.R.1
  • 30
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • MATSUDAIRA P: Modular organization of actin crosslinking proteins. Trends Biol Sci 16:87-92, 1991
    • (1991) Trends Biol Sci , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 31
    • 0017089064 scopus 로고
    • Purification and properties of filamin, an actin binding protein from chicken gizzard
    • SHIZUTA Y, SHIZUTA H, GALLO M, DAVIES P, PASTAN I: Purification and properties of filamin, an actin binding protein from chicken gizzard. J Biol Chem 251:6562-6567, 1976
    • (1976) J Biol Chem , vol.251 , pp. 6562-6567
    • Shizuta, Y.1    Shizuta, H.2    Gallo, M.3    Davies, P.4    Pastan, I.5
  • 33
    • 0025943943 scopus 로고
    • Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (FcγRI)
    • OHTA Y, STOSSEL TP, HARTWIG JH: Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (FcγRI). Cell 67:1-20, 1991
    • (1991) Cell , vol.67 , pp. 1-20
    • Ohta, Y.1    Stossel, T.P.2    Hartwig, J.H.3
  • 35
    • 0018890176 scopus 로고
    • The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization
    • BRENNER SL, KORN ED: The effects of cytochalasins on actin polymerization and actin ATPase provide insights into the mechanism of polymerization. J Biol Chem 255:841-844, 1980
    • (1980) J Biol Chem , vol.255 , pp. 841-844
    • Brenner, S.L.1    Korn, E.D.2
  • 36
    • 0022994966 scopus 로고
    • The kinetics of cytochalasin D binding to monomeric actin
    • GODDETTE DW, FRIEDEN C: The kinetics of cytochalasin D binding to monomeric actin. J Biol Chem 261:15970-15973, 1986
    • (1986) J Biol Chem , vol.261 , pp. 15970-15973
    • Goddette, D.W.1    Frieden, C.2
  • 37
    • 0019321610 scopus 로고
    • 2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation
    • 2+ control of actin gelation. Interaction of gelsolin with actin filaments and regulation of actin gelation. J Biol Chem 255:9494-9500, 1980
    • (1980) J Biol Chem , vol.255 , pp. 9494-9500
    • Yin, H.L.1    Zaner, K.S.2    Stossel, T.P.3
  • 38
    • 0019751470 scopus 로고
    • 2+-dependent regulatory protein of actin gel-sol transformation, and its intracellular distribution in a variery of cells and tissues
    • 2+-dependent regulatory protein of actin gel-sol transformation, and its intracellular distribution in a variery of cells and tissues. J Cell Bol 91:901-908, 1981
    • (1981) J Cell Bol , vol.91 , pp. 901-908
    • Yin, H.L.1    Albretch, J.H.2    Fattoum, A.3
  • 39
    • 0021287115 scopus 로고
    • Stretch-activated single ion channel currents in tissue-cultured embryonic chick skeletal muscle
    • GUHARAY F, SACHS F: Stretch-activated single ion channel currents in tissue-cultured embryonic chick skeletal muscle. J Physiol 352:685-701, 1984
    • (1984) J Physiol , vol.352 , pp. 685-701
    • Guharay, F.1    Sachs, F.2
  • 40
    • 0023755321 scopus 로고
    • Ion channels activated by osmotic and mechanical stress in membranes of opossum kidney cells
    • UBL J, MURER H, KOLB HA: Ion channels activated by osmotic and mechanical stress in membranes of opossum kidney cells. J Membr Biol 104:223-232, 1988
    • (1988) J Membr Biol , vol.104 , pp. 223-232
    • Ubl, J.1    Murer, H.2    Kolb, H.A.3
  • 41
    • 0024582447 scopus 로고
    • + channel sensitive to cell volume
    • + channel sensitive to cell volume. Proc Natl Acad Sci USA 86:1731-1735, 1989
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1731-1735
    • Sackin, H.1
  • 43
    • 0027320184 scopus 로고
    • Vasopressin and protein kinase A activate G protein-sensitive Na channels
    • PRAT AG, AUSIELLO DA, CANTIELLO HF: Vasopressin and protein kinase A activate G protein-sensitive Na channels. Am J Physiol 265:C218-C223, 1993
    • (1993) Am J Physiol , vol.265
    • Prat, A.G.1    Ausiello, D.A.2    Cantiello, H.F.3
  • 45
    • 0019615083 scopus 로고
    • Transport properties of toad kidney epithelia in culture
    • PERKINS FM, HANDLER JS: Transport properties of toad kidney epithelia in culture. Am J Physiol 241:C154-C159, 1981
    • (1981) Am J Physiol , vol.241
    • Perkins, F.M.1    Handler, J.S.2
  • 46
    • 0022115717 scopus 로고
    • Single-channel recordings from amiloride-sensitive epithelial sodium channel
    • HAMILTON KL, EATON DC: Single-channel recordings from amiloride-sensitive epithelial sodium channel. Am J Physiol 249:C200-C207, 1985
    • (1985) Am J Physiol , vol.249
    • Hamilton, K.L.1    Eaton, D.C.2
  • 47
    • 0024336798 scopus 로고
    • + channels in A6 cells, a regulatory role for protein kinase C
    • + channels in A6 cells, a regulatory role for protein kinase C. Am J Physiol 256:F1094-F1103, 1989
    • (1989) Am J Physiol , vol.256
    • Ling, B.N.1    Eaton, D.C.2
  • 49
    • 0023007962 scopus 로고
    • Actin polymerization. The mechanism of action of cytochalasin D
    • GODDETTE DW, FRIEDEN C: Actin polymerization. The mechanism of action of cytochalasin D. J Biol Chem 261:15974-15980, 1986
    • (1986) J Biol Chem , vol.261 , pp. 15974-15980
    • Goddette, D.W.1    Frieden, C.2
  • 50
    • 0023211638 scopus 로고
    • Baroreceptor mechanisms at the cellular level
    • SACHS F: Baroreceptor mechanisms at the cellular level. Fed Proc 46:12-16, 1987
    • (1987) Fed Proc , vol.46 , pp. 12-16
    • Sachs, F.1
  • 51
    • 0020492978 scopus 로고
    • Investigation of the actin-deoxyribonuclease I interaction using a pyrene-conjugated actin derivative
    • PINDER JC, GRATZER WB: Investigation of the actin-deoxyribonuclease I interaction using a pyrene-conjugated actin derivative. Biochemistry 21:4886-4890, 1982
    • (1982) Biochemistry , vol.21 , pp. 4886-4890
    • Pinder, J.C.1    Gratzer, W.B.2
  • 52
    • 0023772655 scopus 로고
    • How actin binds and assembles onto plasma membranes from Dictyostelium discoideum
    • SCHWARTZ MA, LUNA EJ: How actin binds and assembles onto plasma membranes from Dictyostelium discoideum. J Cell Biol 107: 201-209, 1988
    • (1988) J Cell Biol , vol.107 , pp. 201-209
    • Schwartz, M.A.1    Luna, E.J.2
  • 53
    • 0021923779 scopus 로고
    • Diacylglycerol in large α-actinin/actin complexes and in the cytoskeleton of activated platelets
    • BURN P, ROTMAN A, MEYER RK, BURGER MM: Diacylglycerol in large α-actinin/actin complexes and in the cytoskeleton of activated platelets. Nature 314:469-474, 1985
    • (1985) Nature , vol.314 , pp. 469-474
    • Burn, P.1    Rotman, A.2    Meyer, R.K.3    Burger, M.M.4
  • 57
    • 0001748454 scopus 로고
    • The mechanism of Na uptake through Na-selective channels in the epithelium of frog skin
    • New York, Raven
    • LINDEMANN B, VAN DRIESSCHE W: The mechanism of Na uptake through Na-selective channels in the epithelium of frog skin, in Membrane Transport Processes, New York, Raven, 1978, pp 155-178
    • (1978) Membrane Transport Processes , pp. 155-178
    • Lindemann, B.1    Van Driessche, W.2
  • 58
    • 0025728956 scopus 로고
    • Effects of vasopressin and cAMP on single amiloride-blockable Na channels
    • MARUNAKA Y, EATON D: Effects of vasopressin and cAMP on single amiloride-blockable Na channels. Am J Physiol 260:C1071-C1084, 1991
    • (1991) Am J Physiol , vol.260
    • Marunaka, Y.1    Eaton, D.2
  • 59
    • 0024212415 scopus 로고
    • Single-channel recordings from the apical membrane of the toad urinary bladder epithelial cell
    • FRINGS S, PURVES RD, MACKNIGHT ADC: Single-channel recordings from the apical membrane of the toad urinary bladder epithelial cell. J Membr Biol 106:157-172, 1988
    • (1988) J Membr Biol , vol.106 , pp. 157-172
    • Frings, S.1    Purves, R.D.2    Macknight, A.D.C.3
  • 60
    • 0023877650 scopus 로고
    • Characterization of cAMP-induced activation of epithelial sodium channels
    • LESTER DS, ASHER C, GARTY H: Characterization of cAMP-induced activation of epithelial sodium channels. Am J Physiol 254:C802-C808, 1988
    • (1988) Am J Physiol , vol.254
    • Lester, D.S.1    Asher, C.2    Garty, H.3
  • 61
    • 85030134217 scopus 로고
    • Purification of an epithelial sodium channel: Vasopressin-dependent subunit phosphorylation
    • Paris, Colloque INSERM/John Libbey Eurotext Ltd.
    • BENOS DJ: Purification of an epithelial sodium channel: Vasopressin-dependent subunit phosphorylation, in Vasopressin, Paris, Colloque INSERM/John Libbey Eurotext Ltd., 1991, pp 125-134
    • (1991) Vasopressin , pp. 125-134
    • Benos, D.J.1
  • 63
    • 0011343924 scopus 로고
    • Microfilament organization and vasopressin action
    • edited by SCHRIER RW, New York, Raven Press
    • AUSIELLO DA, HARTWIG JH: Microfilament organization and vasopressin action, in Vasopressin, edited by SCHRIER RW, New York, Raven Press, 1985, pp 89-96
    • (1985) Vasopressin , pp. 89-96
    • Ausiello, D.A.1    Hartwig, J.H.2
  • 64
    • 0025965365 scopus 로고
    • Vasopressin depolymerizes F-actin in toad bladder epithelial cells
    • DING G, FRANKI N, CONDEELIS J, HAYS RM: Vasopressin depolymerizes F-actin in toad bladder epithelial cells. Am J Physiol 260:C9-C16, 1991
    • (1991) Am J Physiol , vol.260
    • Ding, G.1    Franki, N.2    Condeelis, J.3    Hays, R.M.4
  • 65
    • 0022628244 scopus 로고
    • A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase
    • CHENG H-C, KEMP BE, PEARSON RB, ET AL: A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase. J Biol Chem 261:989-992, 1986
    • (1986) J Biol Chem , vol.261 , pp. 989-992
    • Cheng, H.-C.1    Kemp, B.E.2    Pearson, R.B.3
  • 66
    • 0020170017 scopus 로고
    • Dihydrocytochalasin B disorganizes actin cytoarchitecture and inhibits initiation of DNA synthesis in 3T3 cells
    • MANESS PF, WALSH RC JR: Dihydrocytochalasin B disorganizes actin cytoarchitecture and inhibits initiation of DNA synthesis in 3T3 cells. Cell 30:253-262, 1982
    • (1982) Cell , vol.30 , pp. 253-262
    • Maness, P.F.1    Walsh Jr., R.C.2
  • 67
    • 0022589972 scopus 로고
    • Cytochalasin releases mRNA from the cytoskeletal framework and inhibits protein synthesis
    • ORNELLES DA, FEY EG, PENMAN S: Cytochalasin releases mRNA from the cytoskeletal framework and inhibits protein synthesis. Mol Cell Biol 6:1650-1662, 1986
    • (1986) Mol Cell Biol , vol.6 , pp. 1650-1662
    • Ornelles, D.A.1    Fey, E.G.2    Penman, S.3
  • 69
    • 0027276953 scopus 로고
    • Cytoskeleton and ion movements during volume regulation in cultured PC12 cells
    • CORNET M, UBL J, KOLB HA: Cytoskeleton and ion movements during volume regulation in cultured PC12 cells. J Membr Biol 133:161-170, 1993
    • (1993) J Membr Biol , vol.133 , pp. 161-170
    • Cornet, M.1    Ubl, J.2    Kolb, H.A.3
  • 71
    • 0026578868 scopus 로고
    • Hypotonicity and cell volume regulation in shark rectal gland: Role of organic osmolytes and F-actin
    • ZIYADEH FN, MILLS JW, KLEINZELLER A: Hypotonicity and cell volume regulation in shark rectal gland: Role of organic osmolytes and F-actin. Am J Physiol 262:F468-F479, 1992
    • (1992) Am J Physiol , vol.262
    • Ziyadeh, F.N.1    Mills, J.W.2    Kleinzeller, A.3
  • 72
    • 84940623044 scopus 로고
    • Volume regulation in non-epithelial cells
    • REUSS L: Volume regulation in non-epithelial cells. Renal Physiol Biochem 3-5:187-201, 1988
    • (1988) Renal Physiol Biochem , vol.3-5 , pp. 187-201
    • Reuss, L.1
  • 73
    • 0027636705 scopus 로고
    • Molecular clues to mechanosensitivity
    • HAMILL O, MCBRIDE D: Molecular clues to mechanosensitivity. Biophys J 66:17-18, 1993
    • (1993) Biophys J , vol.66 , pp. 17-18
    • Hamill, O.1    Mcbride, D.2
  • 74
    • 0026781144 scopus 로고
    • Rapid adaptation of the mechanosensitive channel in Xenopus oocytes
    • HAMILL OP, MCBRIDE DW: Rapid adaptation of the mechanosensitive channel in Xenopus oocytes. Proc Natl Acad Sci USA 89:7462-7466, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7462-7466
    • Hamill, O.P.1    Mcbride, D.W.2
  • 75
    • 0026042464 scopus 로고
    • Dual modulation of renal ATP-sensitive K-channel by protein kinase A and C
    • WANG W, GIEBISCH G: Dual modulation of renal ATP-sensitive K-channel by protein kinase A and C. Proc Natl Acad Sci USA 88:9722-9725, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9722-9725
    • Wang, W.1    Giebisch, G.2
  • 76
    • 0027506454 scopus 로고
    • Vasopressin increases the density of apical low-conductance K channel in rat CCD
    • CASSOLA AC, GIEBISCH G, WANG W: Vasopressin increases the density of apical low-conductance K channel in rat CCD. Am J Physiol 264:F502-F509, 1993
    • (1993) Am J Physiol , vol.264
    • Cassola, A.C.1    Giebisch, G.2    Wang, W.3
  • 77
    • 0027992930 scopus 로고
    • Involvement of actin cytoskeleton in modulation of apical K channel activity in rat collecting duct
    • WANG W-H, CASSOLA A, GIEBISH G: Involvement of actin cytoskeleton in modulation of apical K channel activity in rat collecting duct. Am J Physiol 267:F592-F598, 1994
    • (1994) Am J Physiol , vol.267
    • Wang, W.-H.1    Cassola, A.2    Giebish, G.3
  • 78
    • 0026482525 scopus 로고
    • Association of a receptor and G-protein-regulated phospholipase C with the cytoskeleton
    • VAZIRI C, DOWNES CP: Association of a receptor and G-protein-regulated phospholipase C with the cytoskeleton. J Biol Chem 267: 22973-22981, 1992
    • (1992) J Biol Chem , vol.267 , pp. 22973-22981
    • Vaziri, C.1    Downes, C.P.2
  • 79
    • 0027399438 scopus 로고
    • Evidence for an increase in the association of cytosolic phospholipase A2 with the cytoskeleton of stimulated rabbit platelets
    • AKIBA S, SATO T, FUJII T: Evidence for an increase in the association of cytosolic phospholipase A2 with the cytoskeleton of stimulated rabbit platelets. J Biochem (Tokyo) 113:4-6, 1993
    • (1993) J Biochem (Tokyo) , vol.113 , pp. 4-6
    • Akiba, S.1    Sato, T.2    Fujii, T.3
  • 80
    • 0027483065 scopus 로고
    • Epithelial sodium channel related to proteins involved in neurodegeneration
    • CANESSA CM, HORISBERGER J-D, ROSSIER BC: Epithelial sodium channel related to proteins involved in neurodegeneration. Nature 361:467-470, 1993
    • (1993) Nature , vol.361 , pp. 467-470
    • Canessa, C.M.1    Horisberger, J.-D.2    Rossier, B.C.3
  • 81
    • 0027958441 scopus 로고
    • + channel is made of three homologous subunits
    • + channel is made of three homologous subunits. Nature 367:463-467, 1994
    • (1994) Nature , vol.367 , pp. 463-467
    • Canessa, C.M.1    Schild, L.2    Buell, G.3
  • 82
    • 0027470203 scopus 로고
    • The structural and functional diversity of dystrophin
    • AHN AH, KUNKEL LM: The structural and functional diversity of dystrophin. Nature Genet 3:283-291, 1993
    • (1993) Nature Genet , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 84
    • 85030134423 scopus 로고    scopus 로고
    • Actin filaments regulate epithelial sodium, potassium ATPase activity
    • in press
    • CANTIELLO HF: Actin filaments regulate epithelial sodium, potassium ATPase activity. Am J Physiol (in press)
    • Am J Physiol
    • Cantiello, H.F.1
  • 85
    • 0023942464 scopus 로고
    • Polymerization of actin by positively charge liposomes
    • LALIBERTE A, GICQUAUD C: Polymerization of actin by positively charge liposomes. J Cell Biol 106:1221-1227, 1988
    • (1988) J Cell Biol , vol.106 , pp. 1221-1227
    • Laliberte, A.1    Gicquaud, C.2
  • 86
    • 0025007608 scopus 로고
    • Enhanced polymerization of polar macromolecules by an applied electric field with application to mitosis
    • MEGGS W: Enhanced polymerization of polar macromolecules by an applied electric field with application to mitosis. J Theor Biol 145:245-255, 1990
    • (1990) J Theor Biol , vol.145 , pp. 245-255
    • Meggs, W.1
  • 87
    • 0025809627 scopus 로고
    • Osmotically induced electrical signals from actin filaments
    • CANTIELLO HF, PATENAUDE CR, ZANER KS: Osmotically induced electrical signals from actin filaments. Biophys J 59:1284-1289, 1991
    • (1991) Biophys J , vol.59 , pp. 1284-1289
    • Cantiello, H.F.1    Patenaude, C.R.2    Zaner, K.S.3
  • 88
    • 0027430107 scopus 로고
    • A novel method to study the electrodynamic behavior of actin filaments. Evidence for cable-like properties of actin
    • LIN E, CANTIELLO HF: A novel method to study the electrodynamic behavior of actin filaments. Evidence for cable-like properties of actin. Biophys J 65:1371-1378, 1993
    • (1993) Biophys J , vol.65 , pp. 1371-1378
    • Lin, E.1    Cantiello, H.F.2
  • 89
    • 85030131672 scopus 로고
    • Actin phosphorylation by protein kinases a and C effects epithelial sodium channel regulation
    • PRAT AG, CANTIELLO HF: Actin phosphorylation by protein kinases A and C effects epithelial sodium channel regulation. (abstract) Biophys J 66:A244, 1994
    • (1994) Biophys J , vol.66
    • Prat, A.G.1    Cantiello, H.F.2
  • 90
    • 0023645738 scopus 로고
    • Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability
    • OHTA Y, AKIYAMA T, NISHIDA E, SAKAI H: Protein kinase C and cAMP-dependent protein kinase induce opposite effects on actin polymerizability. FEBS Lett 222:305-310, 1987
    • (1987) FEBS Lett , vol.222 , pp. 305-310
    • Ohta, Y.1    Akiyama, T.2    Nishida, E.3    Sakai, H.4
  • 91
    • 43849100830 scopus 로고
    • The vasopressin-mediated regulation of renal sodium transport. Role of the actin cytoskeleton in hormone action
    • Paris, John Libbey Eurotext
    • CANTIELLO HF: The vasopressin-mediated regulation of renal sodium transport. Role of the actin cytoskeleton in hormone action, in Vasopressin, Paris, John Libbey Eurotext, 1993, pp 357-370
    • (1993) Vasopressin , pp. 357-370
    • Cantiello, H.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.