메뉴 건너뛰기




Volumn 2, Issue 12, 1999, Pages 1070-1077

G-protein-independent signaling mediated by metabotropic glutamate receptors

Author keywords

[No Author keywords available]

Indexed keywords

GENISTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; METABOTROPIC RECEPTOR; PROTEIN TYROSINE KINASE; VANADIC ACID;

EID: 0033490463     PISSN: 10976256     EISSN: None     Source Type: Journal    
DOI: 10.1038/15996     Document Type: Article
Times cited : (144)

References (50)
  • 1
    • 0022370635 scopus 로고
    • Glutamate stimulates inositol phosphate formation in striatal neurones
    • Sladeczek, F., Pin, J. P., Recasens, M., Bockaert, J. & Weiss, S. Glutamate stimulates inositol phosphate formation in striatal neurones. Nature 317, 717-719 (1985).
    • (1985) Nature , vol.317 , pp. 717-719
    • Sladeczek, F.1    Pin, J.P.2    Recasens, M.3    Bockaert, J.4    Weiss, S.5
  • 2
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn, P. J. & Pin, J. P. Pharmacology and functions of metabotropic glutamate receptors. Annu. Rev. Toxicol. 37, 205-237 (1997).
    • (1997) Annu. Rev. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.J.1    Pin, J.P.2
  • 3
    • 0032907608 scopus 로고    scopus 로고
    • Metabotropic glutamate receptors: Electrophysiological properties and role in plasticity
    • Anwyl, R. Metabotropic glutamate receptors: electrophysiological properties and role in plasticity. Brain Res. Rev. 29, 83-120 (1999).
    • (1999) Brain Res. Rev. , vol.29 , pp. 83-120
    • Anwyl, R.1
  • 4
    • 0030014918 scopus 로고    scopus 로고
    • Perisynaptic location of metabotropic glutamate receptors mGluR1 and mGluR5 on dendrites and dendritic spines in the rat hippocampus
    • Lujan, R., Nusser, Z., Roberts, J. D., Shigemoto, R. & Somogyi, P. Perisynaptic location of metabotropic glutamate receptors mGluR1 and mGluR5 on dendrites and dendritic spines in the rat hippocampus. Eur. J. Neurosci. 8, 1488-1500 (1996).
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 1488-1500
    • Lujan, R.1    Nusser, Z.2    Roberts, J.D.3    Shigemoto, R.4    Somogyi, P.5
  • 5
    • 0027520283 scopus 로고
    • The metabotropic glutamate receptor (mGluR1α) is concentrated at perisynaptic membrane of neuronal subpopulations as detected by immunogold reaction
    • Baude, A. et al. The metabotropic glutamate receptor (mGluR1α) is concentrated at perisynaptic membrane of neuronal subpopulations as detected by immunogold reaction. Neuron 11, 771-787 (1993).
    • (1993) Neuron , vol.11 , pp. 771-787
    • Baude, A.1
  • 6
    • 0030821474 scopus 로고    scopus 로고
    • Differential presynaptic localization of metabotropic glutamate receptor subtypes in the rat hippocampus
    • Shigemoto, R. et al. Differential presynaptic localization of metabotropic glutamate receptor subtypes in the rat hippocampus. J. Neurosci. 17, 7503-7522 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 7503-7522
    • Shigemoto, R.1
  • 7
    • 0027732539 scopus 로고
    • Role of a metabotropic glutamate receptor in synaptic modulation in the accessory olfactory bulb
    • Hayashi, Y. et al. Role of a metabotropic glutamate receptor in synaptic modulation in the accessory olfactory bulb. Nature 366, 687-690 (1993).
    • (1993) Nature , vol.366 , pp. 687-690
    • Hayashi, Y.1
  • 8
    • 0031036195 scopus 로고    scopus 로고
    • Use-dependent increases in glutamate concentration activate presynaptic metabotropic glutamate receptors
    • Scanziani, M., Salin, P. A., Vogt, K. E., Malenka, R. C. & Nicoll, R. A. Use-dependent increases in glutamate concentration activate presynaptic metabotropic glutamate receptors. Nature 385, 630-634 (1997).
    • (1997) Nature , vol.385 , pp. 630-634
    • Scanziani, M.1    Salin, P.A.2    Vogt, K.E.3    Malenka, R.C.4    Nicoll, R.A.5
  • 9
    • 0025896921 scopus 로고
    • Glutamate mediates a slow synaptic response in hippocampal slice cultures
    • Charpak, S. & Gähwiler, B. H. Glutamate mediates a slow synaptic response in hippocampal slice cultures. Proc. R. Soc. Lond. B Biol. Sci. 243, 221-226 (1991).
    • (1991) Proc. R. Soc. Lond. B Biol. Sci. , vol.243 , pp. 221-226
    • Charpak, S.1    Gähwiler, B.H.2
  • 10
    • 0027771178 scopus 로고
    • Inhibition of a slow synaptic response by a metabotropic glutamate receptor antagonist in hippocampal CA3 pyramidal cells
    • Gerber, U., Lüthi, A. & Gähwiler, B. H. Inhibition of a slow synaptic response by a metabotropic glutamate receptor antagonist in hippocampal CA3 pyramidal cells. Proc. R. Soc. Lond. B Biol. Sci. 254, 169-172 (1993).
    • (1993) Proc. R. Soc. Lond. B Biol. Sci. , vol.254 , pp. 169-172
    • Gerber, U.1    Lüthi, A.2    Gähwiler, B.H.3
  • 11
    • 0030758705 scopus 로고    scopus 로고
    • A long-lasting calcium-activated nonselective cationic current is generated by synaptic stimulation or exogenous activation of group I metabotropic glutamate receptors in CA1 pyramidal neurons
    • Congar, P., Leinekugel, X., Ben-Ari, Y. & Crépel, V. A long-lasting calcium-activated nonselective cationic current is generated by synaptic stimulation or exogenous activation of group I metabotropic glutamate receptors in CA1 pyramidal neurons. J. Neurosci. 17, 5366-5379 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 5366-5379
    • Congar, P.1    Leinekugel, X.2    Ben-Ari, Y.3    Crépel, V.4
  • 12
    • 13344294369 scopus 로고
    • G protein-coupled receptors mediate a fast excitatory postsynaptic current in CA3 pyramidal neurons in hippocampal slices
    • Pozzo Miller, L. D., Petrozzino, J. J. & Connor, J. A. G protein-coupled receptors mediate a fast excitatory postsynaptic current in CA3 pyramidal neurons in hippocampal slices. J. Neurosci. 15, 8320-8330 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 8320-8330
    • Pozzo Miller, L.D.1    Petrozzino, J.J.2    Connor, J.A.3
  • 13
    • 0033620487 scopus 로고    scopus 로고
    • Heptahelical receptor signaling: Beyond the G-protein paradigm
    • Hall, R. A., Premont, R. T. & Lefkowitz, R. J. Heptahelical receptor signaling: beyond the G-protein paradigm. J. Cell Biol. 145, 927-932 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 927-932
    • Hall, R.A.1    Premont, R.T.2    Lefkowitz, R.J.3
  • 14
    • 0029995540 scopus 로고    scopus 로고
    • Activation of metabotropic glutamate receptor type 2/3 suppresses transmission at rat hippocampal mossy fibre synapses
    • Kamiya, H., Shinozaki, H. & Yamamoto, C. Activation of metabotropic glutamate receptor type 2/3 suppresses transmission at rat hippocampal mossy fibre synapses. J. Physiol (Lond.) 493, 447-455 (1996).
    • (1996) J. Physiol (Lond.) , vol.493 , pp. 447-455
    • Kamiya, H.1    Shinozaki, H.2    Yamamoto, C.3
  • 16
    • 0033587709 scopus 로고    scopus 로고
    • Inhibition of uptake unmasks rapid extracellular turnover of glutamate of nonvesicular origin
    • Jabaudon, D. et al. Inhibition of uptake unmasks rapid extracellular turnover of glutamate of nonvesicular origin. Proc. Natl. Acad. Sci. USA 96, 8733-8738 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8733-8738
    • Jabaudon, D.1
  • 17
    • 0029133818 scopus 로고
    • Phenylglycine derivatives discriminate between mGluR1-and mGluR5-mediated responses
    • Brabet, I., Mary, S., Bockaert, J. & Pin, J. P. Phenylglycine derivatives discriminate between mGluR1-and mGluR5-mediated responses. Neuropharmacology 34, 895-903 (1995).
    • (1995) Neuropharmacology , vol.34 , pp. 895-903
    • Brabet, I.1    Mary, S.2    Bockaert, J.3    Pin, J.P.4
  • 18
    • 8244251426 scopus 로고    scopus 로고
    • Pharmacological characterization of 1-aminoindan-1,5-dicarboxylic acid, a potent mGluR1 antagonist
    • Moroni, F. et al. Pharmacological characterization of 1-aminoindan-1,5-dicarboxylic acid, a potent mGluR1 antagonist. J. Pharmacol Exp. Ther. 281, 721-729 (1997).
    • (1997) J. Pharmacol Exp. Ther. , vol.281 , pp. 721-729
    • Moroni, F.1
  • 19
    • 0032853255 scopus 로고    scopus 로고
    • 2-Methyl-6-(phenylethynyl)-pyridine (MPEP), a potent, selective and systemically active mGlu5 receptor antagonist
    • Gasparini, F. et al. 2-Methyl-6-(phenylethynyl)-pyridine (MPEP), a potent, selective and systemically active mGlu5 receptor antagonist. Neuropharmacology 38, 1493-1503 (1999).
    • (1999) Neuropharmacology , vol.38 , pp. 1493-1503
    • Gasparini, F.1
  • 20
    • 0030894148 scopus 로고    scopus 로고
    • (RS)-2-chloro-5-hydroxyphenylglycine (CHPG) activates mGlu5, but not mGlu1, receptors expressed in CHO cells and potentiates NMDA responses in the hippocampus
    • Doherty, A. L, Palmer, M. J., Henley, J. M., Collingridge, G. L. & Jane, D. E. (RS)-2-chloro-5-hydroxyphenylglycine (CHPG) activates mGlu5, but not mGlu1, receptors expressed in CHO cells and potentiates NMDA responses in the hippocampus. Neuropharmacology 36, 265-267 (1997).
    • (1997) Neuropharmacology , vol.36 , pp. 265-267
    • Doherty, A.L.1    Palmer, M.J.2    Henley, J.M.3    Collingridge, G.L.4    Jane, D.E.5
  • 21
    • 0023186677 scopus 로고
    • Reactive sulfhydryl groups of α39, a guanine nucleotide-binding protein from brain. Location and function
    • Winslow, J. W., Bradley, J. D., Smith, J. A. & Neer, E. J. Reactive sulfhydryl groups of α39, a guanine nucleotide-binding protein from brain. Location and function. J. Biol. Chem. 262, 4501-4507 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 4501-4507
    • Winslow, J.W.1    Bradley, J.D.2    Smith, J.A.3    Neer, E.J.4
  • 22
    • 0028143024 scopus 로고
    • 2+ channels by PTX-sensitive G-proteins is blocked by N-ethylmaleimide in rat sympathetic neurons
    • 2+ channels by PTX-sensitive G-proteins is blocked by N-ethylmaleimide in rat sympathetic neurons. J. Neurosci. 14, 7109-7116 (1994).
    • (1994) J. Neurosci. , vol.14 , pp. 7109-7116
    • Shapiro, M.S.1    Wollmuth, L.P.2    Hille, B.3
  • 23
    • 0022272328 scopus 로고
    • Adenosine increases synaptic facilitation in the in vitro rat hippocampus: Evidence for a presynaptic site of action
    • Dunwiddie, T. V. & Haas, H. L. Adenosine increases synaptic facilitation in the in vitro rat hippocampus: evidence for a presynaptic site of action. J. Physiol. (Lond.) 369, 365-377 (1985).
    • (1985) J. Physiol. (Lond.) , vol.369 , pp. 365-377
    • Dunwiddie, T.V.1    Haas, H.L.2
  • 24
    • 0023434169 scopus 로고
    • Dependence of an adenosine-activated potassium current on a GTP-binding protein in mammalian central neurons
    • Trussell, L. O. & Jackson, M. B. Dependence of an adenosine-activated potassium current on a GTP-binding protein in mammalian central neurons. J. Neurosci. 7, 3306-3316 (1987).
    • (1987) J. Neurosci. , vol.7 , pp. 3306-3316
    • Trussell, L.O.1    Jackson, M.B.2
  • 25
    • 0018564618 scopus 로고
    • Guanosine 5′-O-(2-thiodiphosphate). An inhibitor of adenylate cyclase stimulation by guanine nucleotides and fluoride ions
    • Eckstein, R, Cassel, D., Levkovitz, H., Lowe, M. & Selinger, Z. Guanosine 5′-O-(2-thiodiphosphate). An inhibitor of adenylate cyclase stimulation by guanine nucleotides and fluoride ions. J. Biol Chem. 254, 9829-9834 (1979).
    • (1979) J. Biol Chem. , vol.254 , pp. 9829-9834
    • Eckstein, R.1    Cassel, D.2    Levkovitz, H.3    Lowe, M.4    Selinger, Z.5
  • 26
    • 0029840588 scopus 로고    scopus 로고
    • Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase β (PYK2/CAKβ) and pp125(FAK) by glutamate and depolarization in rat hippocampus
    • Siciliano, J. C., Toutant, M., Derkinderen, P., Sasaki, T. & Girault, J. A. Differential regulation of proline-rich tyrosine kinase 2/cell adhesion kinase β (PYK2/CAKβ) and pp125(FAK) by glutamate and depolarization in rat hippocampus. J. Biol. Chem. 271, 28942-28946 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 28942-28946
    • Siciliano, J.C.1    Toutant, M.2    Derkinderen, P.3    Sasaki, T.4    Girault, J.A.5
  • 27
    • 0031724144 scopus 로고    scopus 로고
    • Phosphorylation of mitogen-activated protein kinase in cultured rat cortical glia by stimulation of metabotropic glutamate receptors
    • Peavy, R. D. & Conn, P. J. Phosphorylation of mitogen-activated protein kinase in cultured rat cortical glia by stimulation of metabotropic glutamate receptors. J. Neurochem. 71, 603-612 (1998).
    • (1998) J. Neurochem. , vol.71 , pp. 603-612
    • Peavy, R.D.1    Conn, P.J.2
  • 28
    • 0031866285 scopus 로고    scopus 로고
    • Tyrosine kinases and synaptic transmission
    • Boxall, A. R. & Lancaster, B. Tyrosine kinases and synaptic transmission. Eur. J. Neurosci. 10, 2-7 (1998).
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2-7
    • Boxall, A.R.1    Lancaster, B.2
  • 29
    • 0030029143 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck-and FynT-dependent T cell activation
    • Hanke, J. H. et al. Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck-and FynT-dependent T cell activation. J. Biol. Chem. 271, 695-701 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 695-701
    • Hanke, J.H.1
  • 30
    • 0020479192 scopus 로고
    • Phosphotyrosyl-protein phosphatase of TCRC-2 cells
    • Swarup, G., Speeg, K. V. J., Cohen, S. & Garbers, D. L. Phosphotyrosyl-protein phosphatase of TCRC-2 cells. J. Biol. Chem. 257, 7298-7301 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 7298-7301
    • Swarup, G.1    Speeg, K.V.J.2    Cohen, S.3    Garbers, D.L.4
  • 31
    • 0027288978 scopus 로고
    • Regulation of c-Src tyrosine kinase activity by the Src SH2 domain
    • Liu, X. et al. Regulation of c-Src tyrosine kinase activity by the Src SH2 domain. Oncogene 8, 1119-1126 (1993).
    • (1993) Oncogene , vol.8 , pp. 1119-1126
    • Liu, X.1
  • 32
    • 0030790285 scopus 로고    scopus 로고
    • The synaptic activation of kainate receptors
    • Vignes, M. & Collingridge, G. L. The synaptic activation of kainate receptors. Nature 388, 179-182 (1997).
    • (1997) Nature , vol.388 , pp. 179-182
    • Vignes, M.1    Collingridge, G.L.2
  • 33
    • 0030742265 scopus 로고    scopus 로고
    • Kainate receptors mediate a slow postsynaptic current in hippocampal CA3 neurons
    • Castillo, P. E., Malenka, R. C. & Nicoll, R. A. Kainate receptors mediate a slow postsynaptic current in hippocampal CA3 neurons. Nature 388, 182-186 (1997).
    • (1997) Nature , vol.388 , pp. 182-186
    • Castillo, P.E.1    Malenka, R.C.2    Nicoll, R.A.3
  • 34
    • 0028124594 scopus 로고
    • + conductance increase in Aplysia neurons that appears to be independent of G proteins
    • + conductance increase in Aplysia neurons that appears to be independent of G proteins. Neuron 13, 691-702 (1994).
    • (1994) Neuron , vol.13 , pp. 691-702
    • Kehoe, J.1
  • 35
    • 0029061652 scopus 로고
    • Activation of a nonselective cationic conductance by metabotropic glutamatergic and muscarinic agonists in CA3 pyramidal neurons of the rat hippocampus
    • Guérineau, N. C., Bossu, J. L., Gähwiler, B. H. & Gerber, U. Activation of a nonselective cationic conductance by metabotropic glutamatergic and muscarinic agonists in CA3 pyramidal neurons of the rat hippocampus. J. Neurosci. 15, 4395-4407 (1995).
    • (1995) J. Neurosci. , vol.15 , pp. 4395-4407
    • Guérineau, N.C.1    Bossu, J.L.2    Gähwiler, B.H.3    Gerber, U.4
  • 36
    • 0029113134 scopus 로고
    • 1S,3R-ACPD-preferring inward current in rat dorsolateral septal neurons is mediated by a novel excitatory amino acid receptor
    • Zheng, F., Hasuo, H. & Gallagher, J. P. 1S,3R-ACPD-preferring inward current in rat dorsolateral septal neurons is mediated by a novel excitatory amino acid receptor. Neuropharmacology 34, 905-917 (1995).
    • (1995) Neuropharmacology , vol.34 , pp. 905-917
    • Zheng, F.1    Hasuo, H.2    Gallagher, J.P.3
  • 37
    • 0033613938 scopus 로고    scopus 로고
    • β-Arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes
    • Luttrell, L. M. et al. β-arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes. Science 283, 655-661 (1999).
    • (1999) Science , vol.283 , pp. 655-661
    • Luttrell, L.M.1
  • 38
    • 0033166537 scopus 로고    scopus 로고
    • Coupling of mGluR/Homer and PSD-95 complexes by the shank family of postsynaptic density proteins
    • Tu, J. C. et al. Coupling of mGluR/Homer and PSD-95 complexes by the shank family of postsynaptic density proteins. Neuron 23, 583-592 (1999).
    • (1999) Neuron , vol.23 , pp. 583-592
    • Tu, J.C.1
  • 39
    • 0032192487 scopus 로고    scopus 로고
    • 3 receptors
    • 3 receptors. Neuron 21, 717-726 (1998).
    • (1998) Neuron , vol.21 , pp. 717-726
    • Tu, J.C.1
  • 40
    • 0030176232 scopus 로고    scopus 로고
    • Regulation of potassium channels by protein kinases
    • Jonas, E. A. & Kaczmarek, L. K. Regulation of potassium channels by protein kinases. Curr. Opin. Neurobiol. 6, 318-323 (1996).
    • (1996) Curr. Opin. Neurobiol. , vol.6 , pp. 318-323
    • Jonas, E.A.1    Kaczmarek, L.K.2
  • 41
    • 0028360327 scopus 로고
    • Regulation of NMDA receptors by tyrosine kinases and phosphatases
    • Wang, Y. T. & Salter, M. W. Regulation of NMDA receptors by tyrosine kinases and phosphatases. Nature 369, 233-235 (1994).
    • (1994) Nature , vol.369 , pp. 233-235
    • Wang, Y.T.1    Salter, M.W.2
  • 42
    • 0001048711 scopus 로고    scopus 로고
    • Src activation in the induction of long-term potentiation in CA1 hippocampal neurons
    • Lu, Y. M., Roder, J. C, Davidow, J. & Salter, M. W. Src activation in the induction of long-term potentiation in CA1 hippocampal neurons. Science 279, 1363-1367 (1998).
    • (1998) Science , vol.279 , pp. 1363-1367
    • Lu, Y.M.1    Roder, J.C.2    Davidow, J.3    Salter, M.W.4
  • 43
    • 0032518695 scopus 로고    scopus 로고
    • Signal transduction by the Wnt family of ligands
    • Dale, T. C. Signal transduction by the Wnt family of ligands. Biochem. J. 329, 209-223 (1998).
    • (1998) Biochem. J. , vol.329 , pp. 209-223
    • Dale, T.C.1
  • 44
    • 0030631376 scopus 로고    scopus 로고
    • Chemoattractant receptor signaling: G protein-dependent and -independent pathways
    • Milne, J. L., Kim, J. Y. & Devreotes, P. N. Chemoattractant receptor signaling: G protein-dependent and -independent pathways. Adv. Second Messenger Phosphoprotein Res. 31, 83-104 (1997).
    • (1997) Adv. Second Messenger Phosphoprotein Res. , vol.31 , pp. 83-104
    • Milne, J.L.1    Kim, J.Y.2    Devreotes, P.N.3
  • 45
    • 0029019246 scopus 로고
    • 1 receptor
    • 1 receptor. Nature 375, 247-250 (1995).
    • (1995) Nature , vol.375 , pp. 247-250
    • Marrero, M.B.1
  • 46
    • 0032568416 scopus 로고    scopus 로고
    • Rhodopsin-family receptors associate with small G-proteins to activate phospholipase D
    • Mitchell, R. et al. Rhodopsin-family receptors associate with small G-proteins to activate phospholipase D. Nature 392, 411-414 (1998).
    • (1998) Nature , vol.392 , pp. 411-414
    • Mitchell, R.1
  • 47
    • 0018642422 scopus 로고
    • Ionotropic and metabotropic neurotransmission
    • Eccles, J. C. & McGeer, P. L. Ionotropic and metabotropic neurotransmission. Trends Neurosci. 2, 39-40 (1979).
    • (1979) Trends Neurosci. , vol.2 , pp. 39-40
    • Eccles, J.C.1    McGeer, P.L.2
  • 49
    • 0031813687 scopus 로고    scopus 로고
    • A peptide activator of endogenous tyrosine kinase enhances synaptic currents mediated by NMDA receptors
    • Lancaster, B. & Rogers, M. V. A peptide activator of endogenous tyrosine kinase enhances synaptic currents mediated by NMDA receptors. Eur. J. Neurosci. 10, 2302-2308 (1998).
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 2302-2308
    • Lancaster, B.1    Rogers, M.V.2
  • 50
    • 0025905753 scopus 로고
    • Mechanism of vanadate-induced activation of tyrosine phosphorylation and of the respiratory burst in HL60 cells. Role of reduced oxygen metabolites
    • Trudel, S., Paquet, M. R. & Grinstein, S. Mechanism of vanadate-induced activation of tyrosine phosphorylation and of the respiratory burst in HL60 cells. Role of reduced oxygen metabolites. Biochem. I. 276, 611-619 (1991).
    • (1991) Biochem. J. , vol.276 , pp. 611-619
    • Trudel, S.1    Paquet, M.R.2    Grinstein, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.