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Volumn 154, Issue 2, 1996, Pages 183-195

Role and source of ATP for activation of nonselective cation channels by AlF complex in guinea pig chromaffin cells

Author keywords

ATP; G protein; Glycolysis; Mitochondria; Nonselective cation channel; Phosphorylation

Indexed keywords

1 (5 ISOQUINOLINESULFONYL) 2 METHYLPIPERAZINE; 2 AMINO 2 METHYLPROPIONIC ACID; ADENOSINE TRIPHOSPHATE; CATION CHANNEL; CYANIDE; GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0029804915     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900143     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 0026638255 scopus 로고
    • ATP-dependent bacterial transporters and cystic fibrosis: Analogy between channels and transporters
    • Ames, G.F.-L., Lecar, H. 1992. ATP-dependent bacterial transporters and cystic fibrosis: analogy between channels and transporters. FASEB J. 6:2660-2666
    • (1992) FASEB J. , vol.6 , pp. 2660-2666
    • Ames, G.F.-L.1    Lecar, H.2
  • 3
    • 0026779243 scopus 로고
    • Characterization of the aluminum and beryllium fluoride species which activate transducin: Analysis of the binding and dissociation kinetics
    • Antonny, B., Chabre, M. 1992. Characterization of the aluminum and beryllium fluoride species which activate transducin: analysis of the binding and dissociation kinetics. J. Biol. Chem. 267:6710-6718
    • (1992) J. Biol. Chem. , vol.267 , pp. 6710-6718
    • Antonny, B.1    Chabre, M.2
  • 4
    • 0040613702 scopus 로고
    • Vollage-activated calcium channels that must be phosphorylated to respond to membrane depolarization
    • Armstrong, D., Eckert, R. 1987. Vollage-activated calcium channels that must be phosphorylated to respond to membrane depolarization. Proc. Natl. Acad. Sci. USA 84:2518-2522
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2518-2522
    • Armstrong, D.1    Eckert, R.2
  • 6
    • 0019558919 scopus 로고
    • The ATP substrate site of a cyclic-nucleotide-independent protein kinase from porcine liver nuclei
    • Baydoun, H., Hoppe, J., Freist, W., Wagner, K.G. 1981. The ATP substrate site of a cyclic-nucleotide-independent protein kinase from porcine liver nuclei. Eur. J. Biochem. 115:385-389
    • (1981) Eur. J. Biochem. , vol.115 , pp. 385-389
    • Baydoun, H.1    Hoppe, J.2    Freist, W.3    Wagner, K.G.4
  • 7
    • 0028174962 scopus 로고
    • Coupling of CFTR Cr channel gating to an ATP hydrolysis cycle
    • Baukrowitz. T., Hwang, T.-C., Nairn, A.C., Gadsby, D.C. 1994. Coupling of CFTR Cr channel gating to an ATP hydrolysis cycle. Neuron 12:473-482
    • (1994) Neuron , vol.12 , pp. 473-482
    • Baukrowitz, T.1    Hwang, T.-C.2    Nairn, A.C.3    Gadsby, D.C.4
  • 8
    • 0025803721 scopus 로고
    • 8 analogue inhibit potassium and calcium currents in NG108-15 neuroblastoma x glioma cells in a manner possibly unrelated to their antagonism of calmodulin
    • 8 analogue inhibit potassium and calcium currents in NG108-15 neuroblastoma x glioma cells in a manner possibly unrelated to their antagonism of calmodulin. Neurosci. Lett. 125:57-61
    • (1991) Neurosci. Lett. , vol.125 , pp. 57-61
    • Caulfield, M.P.1    Robbins, J.2    Sim, J.A.3    Brown, D.A.4    Mac Neil, S.5    Blackburn, G.M.6
  • 10
    • 0001449706 scopus 로고
    • Electron microscopic observations on the structure of the rat adrenal medulla. II. Normal innervation
    • Coupland, R.E. 1965. Electron microscopic observations on the structure of the rat adrenal medulla. II. Normal innervation. J. Anat. 99:255-272
    • (1965) J. Anat. , vol.99 , pp. 255-272
    • Coupland, R.E.1
  • 11
    • 0021891882 scopus 로고
    • Nucleoside phosphorothioates
    • Eckstein, F. 1985. Nucleoside phosphorothioates. Annu. Rev. Biochem. 54:367-402
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 367-402
    • Eckstein, F.1
  • 13
    • 0021325696 scopus 로고
    • ATP analogue specificity of cAMP-dependent protein kinase, cGMP-dependent protein kinase, and phosphorylase kinase
    • Flockhart, D.A., Freist, W., Hoppe, J., Lincoln, T.M., Corbin, J.D. 1984. ATP analogue specificity of cAMP-dependent protein kinase, cGMP-dependent protein kinase, and phosphorylase kinase. Eur. J. Biochem. 140:289-295
    • (1984) Eur. J. Biochem. , vol.140 , pp. 289-295
    • Flockhart, D.A.1    Freist, W.2    Hoppe, J.3    Lincoln, T.M.4    Corbin, J.D.5
  • 15
    • 0015139015 scopus 로고
    • Nucleotide requirements for sodium-sodium exchange catalysed by the sodium pump in human red cells
    • Glynn, I.M., Hoffman, J.F. 1971. Nucleotide requirements for sodium-sodium exchange catalysed by the sodium pump in human red cells. J. Physiol. 218:239-256
    • (1971) J. Physiol. , vol.218 , pp. 239-256
    • Glynn, I.M.1    Hoffman, J.F.2
  • 16
    • 0021118719 scopus 로고
    • NMR studies of intracellular metal ions in intact cells and tissues
    • Gupta, R.K., Gupta, P. 1984. NMR studies of intracellular metal ions in intact cells and tissues. Annu. Rev. Biophys. Bioeng. 13:221-246
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 221-246
    • Gupta, R.K.1    Gupta, P.2
  • 17
    • 0021751197 scopus 로고
    • Isoquinoline-sulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C
    • Hidaka, H., Inagaki, M., Kawamoto, S., Sasaki, Y. 1984. Isoquinoline-sulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C. Biochemistry 23:5036-5041
    • (1984) Biochemistry , vol.23 , pp. 5036-5041
    • Hidaka, H.1    Inagaki, M.2    Kawamoto, S.3    Sasaki, Y.4
  • 18
    • 0027174570 scopus 로고
    • ATP depletion induces an increase in the assembly of a labile pool of polymerized actin in endothelial cells
    • Hinshaw, D.B., Burger, J.M., Miller, M.T., Adams, J.A., Beals, T.F., Omann, G.M. 1993. ATP depletion induces an increase in the assembly of a labile pool of polymerized actin in endothelial cells. Am. J. Physiol. 264:C1171-C1179
    • (1993) Am. J. Physiol. , vol.264
    • Hinshaw, D.B.1    Burger, J.M.2    Miller, M.T.3    Adams, J.A.4    Beals, T.F.5    Omann, G.M.6
  • 19
    • 0028983157 scopus 로고
    • 2+-dependent phosphatase as an inhibitory mediator of the nonselective cation current induced by aluminum fluoride in guinea-pig chromaffin cells
    • 2+-dependent phosphatase as an inhibitory mediator of the nonselective cation current induced by aluminum fluoride in guinea-pig chromaffin cells. Brain Res 687:199-204
    • (1995) Brain Res , vol.687 , pp. 199-204
    • Inoue, M.1    Fujishiro, N.2    Imanaga, I.3
  • 20
    • 0027219290 scopus 로고
    • Phosphorylation-dependent regulation of nonselective cation channels in guinea pig chromaffin cells
    • Inoue, M., Imanaga, I. 1993. Phosphorylation-dependent regulation of nonselective cation channels in guinea pig chromaffin cells. Am. J. Physiol. 265:C343-C348
    • (1993) Am. J. Physiol. , vol.265
    • Inoue, M.1    Imanaga, I.2
  • 21
    • 0028961825 scopus 로고
    • + currents in guinea pig chromaffin cells
    • + currents in guinea pig chromaffin cells. J. Gen Physiol. 105:249-266
    • (1995) J. Gen Physiol. , vol.105 , pp. 249-266
    • Inoue, M.1    Imanaga, I.2
  • 22
    • 0028883274 scopus 로고
    • 4 muscarinic receptor in guinea-pig chromaffin cells
    • 4 muscarinic receptor in guinea-pig chromaffin cells. Br. J. Pharmacol. 114:419-427
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 419-427
    • Inoue, M.1    Imanaga, I.2
  • 23
    • 0025796686 scopus 로고
    • Muscarinic receptor is coupled with a cation channel through a GTP-binding protein in guinea-pig chromaffin cells
    • Inoue, M., Kuriyama, H. 1991. Muscarinic receptor is coupled with a cation channel through a GTP-binding protein in guinea-pig chromaffin cells. J. Physiol. 436:511-529
    • (1991) J. Physiol. , vol.436 , pp. 511-529
    • Inoue, M.1    Kuriyama, H.2
  • 24
    • 0024327843 scopus 로고
    • Evidence for compartmentation of high energy phosphagens in smooth muscle
    • R.J. Paul, G. Elzinga, and K. Yamada, editors. Alan R. Liss, New York
    • Ishida, Y., Paul, R.J. 1989. Evidence for compartmentation of high energy phosphagens in smooth muscle. In: Muscle Energetics, R.J. Paul, G. Elzinga, and K. Yamada, editors. pp. 417-428. Alan R. Liss, New York
    • (1989) Muscle Energetics , pp. 417-428
    • Ishida, Y.1    Paul, R.J.2
  • 26
    • 0025296423 scopus 로고
    • Effects of calmodulin antagonists on calcium-activated potassium channels in pregnant rat myometrium
    • Kihira, M., Matsuzawa, K., Tokuno, H., Tomita, T. 1990. Effects of calmodulin antagonists on calcium-activated potassium channels in pregnant rat myometrium. Br. J. Pharmacol. 100:353-359
    • (1990) Br. J. Pharmacol. , vol.100 , pp. 353-359
    • Kihira, M.1    Matsuzawa, K.2    Tokuno, H.3    Tomita, T.4
  • 27
    • 0028324395 scopus 로고
    • Modulation of ion channels by protein phosphorylation and dephosphorylation
    • Levitan, I.B. 1994. Modulation of ion channels by protein phosphorylation and dephosphorylation. Annu. Rev. Physiol. 56:193-212
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 193-212
    • Levitan, I.B.1
  • 28
    • 0018856838 scopus 로고
    • Vanadium-an element in search of a role
    • Macara, I.G. 1980. Vanadium-an element in search of a role. Trends Biochem. Sci. 5:92-94
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 92-94
    • Macara, I.G.1
  • 29
    • 0019847313 scopus 로고
    • Membrane-bound ATP fuels the Na/K pump: Studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes
    • Mercer, R.W., Dunham, P.B. 1981. Membrane-bound ATP fuels the Na/K pump: studies on membrane-bound glycolytic enzymes on inside-out vesicles from human red cell membranes. J. Gen. Physiol. 78:547-568
    • (1981) J. Gen. Physiol. , vol.78 , pp. 547-568
    • Mercer, R.W.1    Dunham, P.B.2
  • 30
    • 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) Nature , vol.328 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.J.2
  • 31
    • 0021086270 scopus 로고
    • + channels in cardiac muscle
    • + channels in cardiac muscle. Nature 305:147-148
    • (1983) Nature , vol.305 , pp. 147-148
    • Noma, A.1
  • 33
    • 0026545458 scopus 로고
    • Effects of the constitutively active proteolytic fragment of protein kinase C on the contractile properties of demembranated smooth muscle fibers
    • Parente, J.E., Walsh, M.P., Kerrick, W.G.L., Hoar, P.E. 1992. Effects of the constitutively active proteolytic fragment of protein kinase C on the contractile properties of demembranated smooth muscle fibers. J. Muscle Res. Cell Mot. 13:90-99
    • (1992) J. Muscle Res. Cell Mot. , vol.13 , pp. 90-99
    • Parente, J.E.1    Walsh, M.P.2    Kerrick, W.G.L.3    Hoar, P.E.4
  • 35
    • 0023858163 scopus 로고
    • Rates of diffusional exchange between small cells and a measuring patch pipette
    • Pusch, M., Neher, E. 1988. Rates of diffusional exchange between small cells and a measuring patch pipette. Pfluegers Arch. 411:204-211
    • (1988) Pfluegers Arch. , vol.411 , pp. 204-211
    • Pusch, M.1    Neher, E.2
  • 36
    • 0023036604 scopus 로고
    • Receptor interconversion model of hormone action: II. nucleotide-mediated conversion of estrogen receptors from nonsteroid binding to the lower affinity binding state
    • Raymoure, W.J., McNaught, R.W., Greene, G.L., Smith, R.G. 1986. Receptor interconversion model of hormone action: II. nucleotide-mediated conversion of estrogen receptors from nonsteroid binding to the lower affinity binding state. J. Biol. Chem. 261:17018-17025
    • (1986) J. Biol. Chem. , vol.261 , pp. 17018-17025
    • Raymoure, W.J.1    McNaught, R.W.2    Greene, G.L.3    Smith, R.G.4
  • 38
    • 0025996310 scopus 로고
    • Protein phosphatases: Recent progress
    • P. Greengard and G.A. Robison, editors. Raven Press, New York
    • Shenolikar, S., Nairn, A.C. 1991. Protein phosphatases: recent progress. In: Advances in Second Messenger and Phosphoprotein Research, P. Greengard and G.A. Robison, editors. Vol. 23, pp. 1-121. Raven Press, New York
    • (1991) Advances in Second Messenger and Phosphoprotein Research , vol.23 , pp. 1-121
    • Shenolikar, S.1    Nairn, A.C.2
  • 40
    • 0023161936 scopus 로고
    • Studies of the unitary properties of adenosine-5′-triphosphate-regulated potassium channels of frog skeletal muscle
    • Spruce, A.E., Standen, N.B., Stanfield, P.R. 1987. Studies of the unitary properties of adenosine-5′-triphosphate-regulated potassium channels of frog skeletal muscle. J. Physiol. 382:213-236
    • (1987) J. Physiol. , vol.382 , pp. 213-236
    • Spruce, A.E.1    Standen, N.B.2    Stanfield, P.R.3
  • 41
    • 0023948543 scopus 로고
    • Ankyrin and spectrin associate with voltage-dependent sodium channels in brain
    • Srinivasan, Y., Elmer, L., Davis, J., Bennett, V., Angelides, K. 1988. Ankyrin and spectrin associate with voltage-dependent sodium channels in brain. Nature 333:177-180
    • (1988) Nature , vol.333 , pp. 177-180
    • Srinivasan, Y.1    Elmer, L.2    Davis, J.3    Bennett, V.4    Angelides, K.5
  • 42
    • 0019332186 scopus 로고
    • Affinity purification of newly phosphorylated protein molecules: Thiophosphorylation and recovery of histones H1, H2B, and H3 and the high mobility group protein HMG-1 using adenosine 5′-O-(3-thiotriphosphate) and cyclic AMP-dependent protein kinase
    • Sun, I.Y.-C., Johnson, E.M., Allfrey, V.G. 1980. Affinity purification of newly phosphorylated protein molecules: thiophosphorylation and recovery of histones H1, H2B, and H3 and the high mobility group protein HMG-1 using adenosine 5′-O-(3-thiotriphosphate) and cyclic AMP-dependent protein kinase. J. Biol. Chem. 255:742-747
    • (1980) J. Biol. Chem. , vol.255 , pp. 742-747
    • Sun, I.Y.-C.1    Johnson, E.M.2    Allfrey, V.G.3
  • 44
    • 0025248527 scopus 로고
    • The innervation of the adrenal gland. IV. Innervation of the rat adrenal medulla from birth to old age. A descriptive and quantitative morphometric and biochemical study of the innervation of chromaffin cells and adrenal medullary neurons in Wistar rats
    • Tomlinson, A., Coupland, R.E. 1990. The innervation of the adrenal gland. IV. Innervation of the rat adrenal medulla from birth to old age. A descriptive and quantitative morphometric and biochemical study of the innervation of chromaffin cells and adrenal medullary neurons in Wistar rats. J. Anat. 169:209-236
    • (1990) J. Anat. , vol.169 , pp. 209-236
    • Tomlinson, A.1    Coupland, R.E.2
  • 46
    • 0024444850 scopus 로고
    • + channels: Evidence for preferential regulation by glycolysis
    • + channels: evidence for preferential regulation by glycolysis. J. Gen. Physiol. 94:911-935
    • (1989) J. Gen. Physiol. , vol.94 , pp. 911-935
    • Weiss, J.N.1    Lamp, S.T.2


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