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Volumn 71, Issue 5, 1998, Pages 1978-1986

Role of calcineurin in Ca2+-induced release of catecholamines and neuropeptides

Author keywords

Dynamin I; Exocytosis; Phosphatase; Rat

Indexed keywords

CALCINEURIN; CALCIUM ION; CATECHOLAMINE; CHOLECYSTOKININ OCTAPEPTIDE; DYNAMIN; MARCKS PROTEIN; NEUROMODULIN; NEUROPEPTIDE; NORADRENALIN; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; SYNAPSIN; SYNAPTOTAGMIN; BACTERIAL PROTEIN; CALCIUM; ENZYME INHIBITOR; IMMUNOGLOBULIN G; PHOSPHATASE; STREPTOLYSIN; STREPTOLYSIN O;

EID: 0031595657     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.71051978.x     Document Type: Article
Times cited : (23)

References (68)
  • 1
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • Aderem A. (1992) The MARCKS brothers: a family of protein kinase C substrates. Cell 71, 713-716.
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 2
    • 0024368011 scopus 로고
    • Poration by α-toxin and streptolysin O: An approach to analyze intracellular processes
    • Ahnert-Hilger G., Mach W., Föhr K. J., and Gratzl M. (1989) Poration by α-toxin and streptolysin O: an approach to analyze intracellular processes. Methods Cell Biol. 31, 63-90.
    • (1989) Methods Cell Biol. , vol.31 , pp. 63-90
    • Ahnert-Hilger, G.1    Mach, W.2    Föhr, K.J.3    Gratzl, M.4
  • 3
    • 0020618174 scopus 로고
    • Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes
    • Andreasen T. J., Luetje C. W., Heideman W., and Storm D. R. (1983) Purification of a novel calmodulin binding protein from bovine cerebral cortex membranes. Biochemistry 22, 4615-4618.
    • (1983) Biochemistry , vol.22 , pp. 4615-4618
    • Andreasen, T.J.1    Luetje, C.W.2    Heideman, W.3    Storm, D.R.4
  • 4
    • 0023878754 scopus 로고
    • Quantitative subcellular localization of calmodulin-dependent phosphatase in chick forebrain
    • Anthony F. A., Winkler M. A., Edwards H. H., and Cheung W. Y. (1988) Quantitative subcellular localization of calmodulin-dependent phosphatase in chick forebrain. J. Neurosci. 8, 1245-1253.
    • (1988) J. Neurosci. , vol.8 , pp. 1245-1253
    • Anthony, F.A.1    Winkler, M.A.2    Edwards, H.H.3    Cheung, W.Y.4
  • 5
    • 0027274857 scopus 로고
    • Inhibitory role for calcineurin in stimulus-secretion coupling revealed by FK506 and cyclosporin A in pituitary corticotrope tumor cells
    • Antoni F. C., Shipston M. J., and Smith S. M. (1993) Inhibitory role for calcineurin in stimulus-secretion coupling revealed by FK506 and cyclosporin A in pituitary corticotrope tumor cells. Biochem. Biophys. Res. Commun. 194, 226-233.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 226-233
    • Antoni, F.C.1    Shipston, M.J.2    Smith, S.M.3
  • 7
    • 0027511827 scopus 로고
    • Casein kinase II phosphorylates the synaptic vesicle protein p65
    • Bennett M. K., Miller K. G., and Scheller R. H. (1993) Casein kinase II phosphorylates the synaptic vesicle protein p65. J. Neurosci. 13, 1701-1707.
    • (1993) J. Neurosci. , vol.13 , pp. 1701-1707
    • Bennett, M.K.1    Miller, K.G.2    Scheller, R.H.3
  • 8
    • 0021718482 scopus 로고
    • Isolation and identification of two hemolytic forms of streptolysin-O
    • Bhakdi S., Roth M., Sziegoliet A., and Tranum-Jensen J. (1984) Isolation and identification of two hemolytic forms of streptolysin-O. Infect. Immun. 46, 394-400.
    • (1984) Infect. Immun. , vol.46 , pp. 394-400
    • Bhakdi, S.1    Roth, M.2    Sziegoliet, A.3    Tranum-Jensen, J.4
  • 9
    • 0023691731 scopus 로고
    • Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases: Specificity and kinetics
    • Bialojan C. and Takai A. (1988) Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases: specificity and kinetics. Biochem. J. 256, 283-290.
    • (1988) Biochem. J. , vol.256 , pp. 283-290
    • Bialojan, C.1    Takai, A.2
  • 10
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss T. V. P. and Collingridge G. L. (1993) A synaptic model of memory: long-term potentiation in the hippocampus. Nature 361, 31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.P.1    Collingridge, G.L.2
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0029985418 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle endocytosis and recycling
    • De Camilli P. and Takei K. (1996) Molecular mechanisms in synaptic vesicle endocytosis and recycling. Neuron 16, 481-486.
    • (1996) Neuron , vol.16 , pp. 481-486
    • De Camilli, P.1    Takei, K.2
  • 16
    • 0026347085 scopus 로고
    • Transmitter release: Target of regulation by protein kinase C?
    • Dekker L. V., De Graan P. N. E., and Gispen W. H. (1991) Transmitter release: target of regulation by protein kinase C? Prog. Brain Res. 89, 209-233.
    • (1991) Prog. Brain Res. , vol.89 , pp. 209-233
    • Dekker, L.V.1    De Graan, P.N.E.2    Gispen, W.H.3
  • 18
    • 0027200739 scopus 로고
    • Calculation and control of free divalent cations in solutions used for membrane fusion studies
    • Föhr K. J., Warchol W., and Gratzl M. (1993) Calculation and control of free divalent cations in solutions used for membrane fusion studies. Methods Enzymol. 221, 149-157.
    • (1993) Methods Enzymol. , vol.221 , pp. 149-157
    • Föhr, K.J.1    Warchol, W.2    Gratzl, M.3
  • 20
    • 0028921368 scopus 로고
    • 2+/calmodulin- And cAMP-dependent protein kinases in vitro
    • 2+/calmodulin-and cAMP-dependent protein kinases in vitro. J. Neurosci. 15, 2385-2395.
    • (1995) J. Neurosci. , vol.15 , pp. 2385-2395
    • Fykse, E.M.1    Li, C.2    Südhof, T.C.3
  • 21
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P., Valtorta F., Czernik A. J., and Benfenati F. (1993) Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 259, 780-785.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 22
    • 0028175820 scopus 로고
    • 2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells
    • 2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells. J. Biol. Chem. 269, 15111-15117.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15111-15117
    • Groblewski, G.E.1    Wagner, A.C.C.2    Williams, J.A.3
  • 24
    • 0025129228 scopus 로고
    • Activation of NMDA receptors induces dephosphorylation of DARPP-32 in rat striatal slices
    • Halpain S., Girault J.-A., and Greengard P. (1990) Activation of NMDA receptors induces dephosphorylation of DARPP-32 in rat striatal slices. Nature 343, 369-372.
    • (1990) Nature , vol.343 , pp. 369-372
    • Halpain, S.1    Girault, J.-A.2    Greengard, P.3
  • 30
    • 0029922172 scopus 로고    scopus 로고
    • Evidence for a role of calmodulin in calcium-induced noradrenaline release from permeated synaptosomes: Effects of calmodulin antibodies and antagonists
    • Hens J. J. H., Oestreicher A. B., De Wit M., Marquart A., Gispen W.-H., and De Graan P. N. E. (1996) Evidence for a role of calmodulin in calcium-induced noradrenaline release from permeated synaptosomes: effects of calmodulin antibodies and antagonists. J. Neurochem. 66, 1933-1942.
    • (1996) J. Neurochem. , vol.66 , pp. 1933-1942
    • Hens, J.J.H.1    Oestreicher, A.B.2    De Wit, M.3    Marquart, A.4    Gispen, W.-H.5    De Graan, P.N.E.6
  • 31
    • 0027263007 scopus 로고
    • Synaptic vesicle traffic: Rush hour in the nerve terminal
    • Jahn R. and Südhof T. C. (1993) Synaptic vesicle traffic: rush hour in the nerve terminal. J. Neurochem. 61, 12-21.
    • (1993) J. Neurochem. , vol.61 , pp. 12-21
    • Jahn, R.1    Südhof, T.C.2
  • 32
    • 0027419032 scopus 로고
    • Storage and release of neurotransmitters
    • Kelly R. B. (1993) Storage and release of neurotransmitters. Cell 72/Neuron 10 (Suppl.), 43-53.
    • (1993) Cell 72/Neuron , vol.10 , Issue.SUPPL. , pp. 43-53
    • Kelly, R.B.1
  • 33
    • 0020491337 scopus 로고
    • Calcium-activated, phospholipid-dependent protein kinase from rat brain. Subcellular distribution, purification and properties
    • Kikkawa U., Takai Y., Minakuchi R., Inohara S., and Nishizuka Y. (1982) Calcium-activated, phospholipid-dependent protein kinase from rat brain. Subcellular distribution, purification and properties. J. Biol. Chem. 257, 13341-13348.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13341-13348
    • Kikkawa, U.1    Takai, Y.2    Minakuchi, R.3    Inohara, S.4    Nishizuka, Y.5
  • 34
    • 0023774750 scopus 로고
    • Preparation, characterization, and properties of affinity-purified antibodies to calmodulin-dependent cyclic nucleotide phosphodiesterase and the protein phosphatase calcineurin
    • Kincaid R. L. (1988) Preparation, characterization, and properties of affinity-purified antibodies to calmodulin-dependent cyclic nucleotide phosphodiesterase and the protein phosphatase calcineurin. Methods Enzymol. 159, 627-652.
    • (1988) Methods Enzymol. , vol.159 , pp. 627-652
    • Kincaid, R.L.1
  • 36
    • 0019929469 scopus 로고
    • Evidence that the synaptic phosphoprotein B-50 is localized exclusively in nerve tissue
    • Kristjansson G. I., Zwiers H., Oestreicher A. B., and Gispen W. H. (1982) Evidence that the synaptic phosphoprotein B-50 is localized exclusively in nerve tissue. J. Neurochem. 39, 371-378.
    • (1982) J. Neurochem. , vol.39 , pp. 371-378
    • Kristjansson, G.I.1    Zwiers, H.2    Oestreicher, A.B.3    Gispen, W.H.4
  • 37
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J., Farmer J. D., Lane W. S., Friedman J., Weissman I., and Schreiber S. L. (1991) Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66, 807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 38
    • 0027998457 scopus 로고
    • Calcineurin inhibition of dynamin I GTPase activity coupled to nerve terminal depolarization
    • Liu J.-P., Sim A. T. R., and Robinson P. J. (1994a) Calcineurin inhibition of dynamin I GTPase activity coupled to nerve terminal depolarization. Science 265, 970-973.
    • (1994) Science , vol.265 , pp. 970-973
    • Liu, J.-P.1    Sim, A.T.R.2    Robinson, P.J.3
  • 39
    • 0028169455 scopus 로고
    • 2+-sensitive phospholipid-binding protein with very high affinity for protein kinase C
    • 2+-sensitive phospholipid-binding protein with very high affinity for protein kinase C. J. Biol. Chem. 269, 21043-21050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21043-21050
    • Liu, J.-P.1    Powell, K.A.2    Südhof, T.C.3    Robinson, P.J.4
  • 40
    • 0027469980 scopus 로고
    • Long-term depression: Not so depressing after all
    • Malenka R. C. (1993) Long-term depression: not so depressing after all. Proc. Natl. Acad. Sci. USA 90, 3121-3123.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3121-3123
    • Malenka, R.C.1
  • 41
    • 0032498227 scopus 로고    scopus 로고
    • Restricted and regulated overexpression reveals calcineurin as a key component in the transition from short-term to long-term memory
    • Mansuy I. M., Mayford M., Jacob B., Kandel E. R., and Bach M. E. (1998) Restricted and regulated overexpression reveals calcineurin as a key component in the transition from short-term to long-term memory. Cell 92, 39-49.
    • (1998) Cell , vol.92 , pp. 39-49
    • Mansuy, I.M.1    Mayford, M.2    Jacob, B.3    Kandel, E.R.4    Bach, M.E.5
  • 42
    • 0025098050 scopus 로고
    • Glutamate and aspartate loading of synaptosomes: A reevaluation of effects on calcium-dependent excitatory amino acid release
    • McMahon H. T. and Nicholls D. G. (1990) Glutamate and aspartate loading of synaptosomes: a reevaluation of effects on calcium-dependent excitatory amino acid release. J. Neurochem. 54, 373-380.
    • (1990) J. Neurochem. , vol.54 , pp. 373-380
    • McMahon, H.T.1    Nicholls, D.G.2
  • 43
    • 0028229610 scopus 로고
    • Nitric oxide stimulates calcium-independent synaptic vesicle release
    • Meffert M. K., Premack B. A., and Schulman H. (1994) Nitric oxide stimulates calcium-independent synaptic vesicle release. Neuron 12, 1235-1244.
    • (1994) Neuron , vol.12 , pp. 1235-1244
    • Meffert, M.K.1    Premack, B.A.2    Schulman, H.3
  • 44
    • 0023376810 scopus 로고
    • Exocytosis induction of Paramecium tetraurelia cells by exogenous phosphoprotein phosphatase in vivo and in vitro: Possible involvement of calcineurin in exocytotic membrane fusion
    • Momayezi M., Lumpert C. J., Kersken H., Gras U., Plattner H., Krinks M. H., and Klee C. B. (1987) Exocytosis induction of Paramecium tetraurelia cells by exogenous phosphoprotein phosphatase in vivo and in vitro: possible involvement of calcineurin in exocytotic membrane fusion. J. Cell Biol. 105, 181-189.
    • (1987) J. Cell Biol. , vol.105 , pp. 181-189
    • Momayezi, M.1    Lumpert, C.J.2    Kersken, H.3    Gras, U.4    Plattner, H.5    Krinks, M.H.6    Klee, C.B.7
  • 45
    • 0027934706 scopus 로고
    • Calcineurin-mediated protein dephosphorylation in brain nerve terminals regulates the release of glutamate
    • Nichols R. A., Suplick G. R., and Brown J. M. (1994) Calcineurin-mediated protein dephosphorylation in brain nerve terminals regulates the release of glutamate. J. Biol. Chem. 269, 23817-23823.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23817-23823
    • Nichols, R.A.1    Suplick, G.R.2    Brown, J.M.3
  • 46
    • 0030051609 scopus 로고    scopus 로고
    • Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel
    • Nicolli A., Basso E., Petronilli V., Wenger R. M., and Bernardi P. (1996) Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel. J. Biol. Chem. 271, 2185-2192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2185-2192
    • Nicolli, A.1    Basso, E.2    Petronilli, V.3    Wenger, R.M.4    Bernardi, P.5
  • 48
    • 0028143054 scopus 로고
    • Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphatase
    • Park I.-K. and DePaoli-Roach A. A. (1994) Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphatase. J. Biol. Chem. 269, 28919-28928.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28919-28928
    • Park, I.-K.1    DePaoli-Roach, A.A.2
  • 50
    • 0026291394 scopus 로고
    • The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release
    • Robinson P. J. (1991) The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release. Mol. Neurobiol. 5, 87-130.
    • (1991) Mol. Neurobiol. , vol.5 , pp. 87-130
    • Robinson, P.J.1
  • 53
    • 0029058492 scopus 로고
    • Membrane trafficking in the presynaptic nerve terminal
    • Scheller R. H. (1995) Membrane trafficking in the presynaptic nerve terminal. Neuron 14, 893-897.
    • (1995) Neuron , vol.14 , pp. 893-897
    • Scheller, R.H.1
  • 55
    • 0028913606 scopus 로고
    • From vesicle docking to endocytosis: Intermediate reactions of exocytosis
    • Schweizer F. E., Betz H., and Augustine G. J. (1995) From vesicle docking to endocytosis: intermediate reactions of exocytosis. Neuron 14, 689-696.
    • (1995) Neuron , vol.14 , pp. 689-696
    • Schweizer, F.E.1    Betz, H.2    Augustine, G.J.3
  • 56
    • 0027391983 scopus 로고
    • Mechanisms in the regulation of neurotransmitter release from brain nerve terminals: Current hypotheses
    • Sihra T. S. and Nichols R. A. (1993) Mechanisms in the regulation of neurotransmitter release from brain nerve terminals: current hypotheses. Neurochem. Res. 18, 47-58.
    • (1993) Neurochem. Res. , vol.18 , pp. 47-58
    • Sihra, T.S.1    Nichols, R.A.2
  • 57
  • 59
    • 0024660445 scopus 로고
    • Cellular and molecular biology of neuropeptide processing and packaging
    • Sossin W. S., Fischer J. M., and Scheller R. H. (1989) Cellular and molecular biology of neuropeptide processing and packaging. Neuron 2, 1407-1417.
    • (1989) Neuron , vol.2 , pp. 1407-1417
    • Sossin, W.S.1    Fischer, J.M.2    Scheller, R.H.3
  • 60
    • 0026471769 scopus 로고
    • Noradrenaline release from permeabilized synaptosomes is inhibited by the light chain of tetanus toxin
    • Stecher B., Hens J. J. H., Weller U., Gratzl M., Gispen W. H., and De Graan P. N. E. (1992) Noradrenaline release from permeabilized synaptosomes is inhibited by the light chain of tetanus toxin. FEBS Lett. 312, 192-194.
    • (1992) FEBS Lett. , vol.312 , pp. 192-194
    • Stecher, B.1    Hens, J.J.H.2    Weller, U.3    Gratzl, M.4    Gispen, W.H.5    De Graan, P.N.E.6
  • 62
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof T. C. (1995) The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 63
    • 0025804129 scopus 로고
    • Displacement of endogenous glutamate with D-aspartate: An effective strategy for reducing the calcium-independent component of glutamate release from synaptosomes
    • Terrian D. M., Dorman R. V., Damron D. S., and Gannon R. L. (1991) Displacement of endogenous glutamate with D-aspartate: an effective strategy for reducing the calcium-independent component of glutamate release from synaptosomes. Neurochem. Res. 16, 35-41.
    • (1991) Neurochem. Res. , vol.16 , pp. 35-41
    • Terrian, D.M.1    Dorman, R.V.2    Damron, D.S.3    Gannon, R.L.4
  • 65
    • 0024395212 scopus 로고
    • Chains and fragments of tetanus toxin. Separation, reassociation and pharmacological properties
    • Weller U., Dauzenroth M.-E., Meyer zu Heringdorf D., and Habermann E. (1989) Chains and fragments of tetanus toxin. Separation, reassociation and pharmacological properties. Eur. J. Biochem. 182, 649-656.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 649-656
    • Weller, U.1    Dauzenroth, M.-E.2    Meyer Zu Heringdorf, D.3    Habermann, E.4
  • 66
    • 0032498272 scopus 로고    scopus 로고
    • Genetic and pharmacological evidence for a novel, intermediate phase of long-term potentiation suppressed by calcineurin
    • Winder D. G., Mansuy I. M., Osman M., Moallem T. M., and Kandel E. R. (1998) Genetic and pharmacological evidence for a novel, intermediate phase of long-term potentiation suppressed by calcineurin. Cell 92, 25-37.
    • (1998) Cell , vol.92 , pp. 25-37
    • Winder, D.G.1    Mansuy, I.M.2    Osman, M.3    Moallem, T.M.4    Kandel, E.R.5
  • 67
    • 0030887172 scopus 로고    scopus 로고
    • Calcineurin regulation of synaptic function: From ion channels to transmitter release and gene transcription
    • Yakel J. L. (1997) Calcineurin regulation of synaptic function: from ion channels to transmitter release and gene transcription. Trends Pharmacol. Sci. 18, 124-134.
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 124-134
    • Yakel, J.L.1
  • 68
    • 0021959565 scopus 로고
    • Resolution of rat brain synaptic phosphoprotein B-50 into multiple forms by two-dimensional electrophoresis: Evidence for multisite phosphorylation
    • Zwiers H., Verhaagen J., van Dongen C. J., De Graan P. N. E., and Gispen W. H. (1985) Resolution of rat brain synaptic phosphoprotein B-50 into multiple forms by two-dimensional electrophoresis: evidence for multisite phosphorylation. J. Neurochem. 44, 1083-1090.
    • (1985) J. Neurochem. , vol.44 , pp. 1083-1090
    • Zwiers, H.1    Verhaagen, J.2    Van Dongen, C.J.3    De Graan, P.N.E.4    Gispen, W.H.5


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