메뉴 건너뛰기




Volumn 12, Issue 5, 2005, Pages 415-428

PGE2 in the regulation of programmed erythrocyte death

Author keywords

Annexin; Calcium; Cell volume; Glucose depletion; Osmotic cell shrinkage

Indexed keywords

ACETYLSALICYLIC ACID; ANKYRIN; CALCIUM; CALPAIN; CALPASTATIN; CATION CHANNEL; CHLORIDE; DICLOFENAC; MEPACRINE; PHOSPHATIDYLSERINE; PHOSPHOLIPASE A2 INHIBITOR; PROSTAGLANDIN E2; THROMBOXANE;

EID: 18644375532     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401561     Document Type: Article
Times cited : (124)

References (74)
  • 1
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR and Reed JC (1998) Mitochondria and apoptosis. Science 281: 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 9
    • 0037085646 scopus 로고    scopus 로고
    • 2+-induced scrambling of various fluorescently labelled lipid analogues in red blood cells
    • 2+-induced scrambling of various fluorescently labelled lipid analogues in red blood cells. Biochem. J. 362: 741-747
    • (2002) Biochem. J. , vol.362 , pp. 741-747
    • Dekkers, D.W.1    Comfurius, F.2    Bevers, E.M.3    Zwaal, R.F.4
  • 13
    • 0033779794 scopus 로고    scopus 로고
    • New insights into the mechanism for clearance of apoptotic cells
    • Messmer UK and Pfeilschifter J (2000) New insights into the mechanism for clearance of apoptotic cells. BioEssays 22: 878-881
    • (2000) BioEssays , vol.22 , pp. 878-881
    • Messmer, U.K.1    Pfeilschifter, J.2
  • 14
    • 0032539931 scopus 로고    scopus 로고
    • Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia
    • Boas FE, Forman Land Beutler E (1998) Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia. Proc. Natl. Acad. Sci. USA 95: 3077-3081
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3077-3081
    • Boas, F.E.1    Forman Land Beutler, E.2
  • 15
    • 0036434149 scopus 로고    scopus 로고
    • Cytoadherence of malaria-infected red blood cells involves exposure of phosphatidylserine
    • Eda S and Sherman IW (2002) Cytoadherence of malaria-infected red blood cells involves exposure of phosphatidylserine. Cell. Physiol. Biochem. 12: 373-384
    • (2002) Cell Physiol. Biochem. , vol.12 , pp. 373-384
    • Eda, S.1    Sherman, I.W.2
  • 17
    • 0023063572 scopus 로고
    • Activation of calcium-dependent potassium channels in deoxygenated sickled red cells
    • Bookchin RM, Ortiz OE and Lew VL (1987) Activation of calcium-dependent potassium channels in deoxygenated sickled red cells. Prog. Clin. Biol. Res. 240: 193-200
    • (1987) Prog. Clin. Biol. Res. , vol.240 , pp. 193-200
    • Bookchin, R.M.1    Ortiz, O.E.2    Lew, V.L.3
  • 18
    • 0027275040 scopus 로고
    • Inhibition of Ca(2+)-dependent K+ transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives
    • Brugnara C, de Franceschi L and Alper SL (1993) Inhibition of Ca(2+)-dependent K+ transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives. J. Clin. Invest. 92: 520-526
    • (1993) J. Clin. Invest. , vol.92 , pp. 520-526
    • Brugnara, C.1    de Franceschi, L.2    Alper, S.L.3
  • 20
    • 0037088836 scopus 로고    scopus 로고
    • Oxidation induces a Cl(-)-dependent cation conductance in human red blood cells
    • Duranton C, Huber SM and Lang F (2002) Oxidation induces a Cl(-)-dependent cation conductance in human red blood cells. J. Physiol. 539: 847-855
    • (2002) J. Physiol. , vol.539 , pp. 847-855
    • Duranton, C.1    Huber, S.M.2    Lang, F.3
  • 21
    • 0035141179 scopus 로고    scopus 로고
    • Chloride conductance and volume-regulatory nonselective cation conductance in human red blood cell ghosts
    • Huber SM, Gamper N and Lang F (2001) Chloride conductance and volume-regulatory nonselective cation conductance in human red blood cell ghosts. Pflugers Arch. 441: 551-558
    • (2001) Pflugers Arch. , vol.441 , pp. 551-558
    • Huber, S.M.1    Gamper, N.2    Lang, F.3
  • 22
    • 0036146457 scopus 로고    scopus 로고
    • Ion channels in the human red blood cell membrane: Their further investigation and physiological relevance
    • Kaestner L and Bernhardt I (2002) Ion channels in the human red blood cell membrane: their further investigation and physiological relevance. Bioelectrochemistry 55: 71-74
    • (2002) Bioelectrochemistry , vol.55 , pp. 71-74
    • Kaestner, L.1    Bernhardt, I.2
  • 23
    • 10444253293 scopus 로고    scopus 로고
    • 2 activates channel-mediated calcium entry in human erythrocytes: An indication of a blood clot formation supporting process
    • 2 activates channel-mediated calcium entry in human erythrocytes: An indication of a blood clot formation supporting process. Thrombosis Haemostasis 92: 1269-1272
    • (2004) Thrombosis Haemostasis , vol.92 , pp. 1269-1272
    • Kaestner, L.1    Tabellion, W.2    Lipp, P.3    Bernhardt, I.4
  • 24
    • 0015244729 scopus 로고
    • Human red blood cells: Prostaglandin E2, epinephrine, and isoproterenol alter deformability
    • Allen JE and Rasmussen H (1971) Human red blood cells: prostaglandin E2, epinephrine, and isoproterenol alter deformability. Science 174: 512-514
    • (1971) Science , vol.174 , pp. 512-514
    • Allen, J.E.1    Rasmussen, H.2
  • 25
    • 0029666477 scopus 로고    scopus 로고
    • 2+-dependent K channel in human erythrocytes and alters cell volume and filterability
    • 2+-dependent K channel in human erythrocytes and alters cell volume and filterability. J. Biol. Chem. 271: 18651-18656
    • (1996) J. Biol. Chem. , vol.271 , pp. 18651-18656
    • Li, Q.1    Jungmann, V.2    Kiyatkin, A.3    Low, P.S.4
  • 27
    • 0347995136 scopus 로고    scopus 로고
    • PLA2/PGE2 are involved in the inhibitory effect of bradykinin on the angiotensin-(1-7)-stimulated Na(+)-ATPase activity of the proximal tubule
    • Lopes AG, Soares AC, Santos DP, Fernandes MS, Leao-Ferreira LR, Quintana-Gomes E and Caruso-Neves C (2004) PLA2/PGE2 are involved in the inhibitory effect of bradykinin on the angiotensin-(1-7)-stimulated Na(+)-ATPase activity of the proximal tubule. Regul. Pept. 117: 37-41
    • (2004) Regul. Pept. , vol.117 , pp. 37-41
    • Lopes, A.G.1    Soares, A.C.2    Santos, D.P.3    Fernandes, M.S.4    Leao-Ferreira, L.R.5    Quintana-Gomes, E.6    Caruso-Neves, C.7
  • 30
    • 0029860936 scopus 로고    scopus 로고
    • Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors
    • Rosette C and Karin M (1996) Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors. Science 274: 1194-1197
    • (1996) Science , vol.274 , pp. 1194-1197
    • Rosette, C.1    Karin, M.2
  • 31
    • 0042665846 scopus 로고    scopus 로고
    • Electrophysiological properties of the Plasmodium falciparum-induced cation conductance of human erythrocytes
    • Duranton C, Huber S, Tanneur V, Lang K, Brand V, Sandu C and Lang F (2003) Electrophysiological properties of the Plasmodium falciparum-induced cation conductance of human erythrocytes. Cell. Physiol. Biochem. 13: 189-198
    • (2003) Cell Physiol. Biochem. , vol.13 , pp. 189-198
    • Duranton, C.1    Huber, S.2    Tanneur, V.3    Lang, K.4    Brand, V.5    Sandu, C.6    Lang, F.7
  • 32
    • 0029966766 scopus 로고    scopus 로고
    • Dehydration of transferrin receptor-positive sickle reticulocytes during continuous or cyclic deoxygenation: Role of KCl cotransport and extracellular calcium
    • Franco RS, Palascak M, Thompson H, Rucknagel DL and Joiner CH (1996) Dehydration of transferrin receptor-positive sickle reticulocytes during continuous or cyclic deoxygenation: role of KCl cotransport and extracellular calcium. Blood 88: 4359-4365
    • (1996) Blood , vol.88 , pp. 4359-4365
    • Franco, R.S.1    Palascak, M.2    Thompson, H.3    Rucknagel, D.L.4    Joiner, C.H.5
  • 35
    • 0027468927 scopus 로고
    • Ca(2+)-activated K+ transport in erythrocytes. Comparison of binding and transport inhibition by scorpion toxins
    • Brugnara C, de Franceschi L and Alper SL (1993) Ca(2+)-activated K+ transport in erythrocytes. Comparison of binding and transport inhibition by scorpion toxins. J. Biol. Chem. 268: 8760-8768
    • (1993) J. Biol. Chem. , vol.268 , pp. 8760-8768
    • Brugnara, C.1    de Franceschi, L.2    Alper, S.L.3
  • 36
    • 0028944824 scopus 로고
    • Oral administration of clotrimazole and blockade of human erythrocyte Ca(++)-activated K+ channel: The imidazole ring is not required for inhibitory activity
    • Brugnara C, Armsby CC, Sakamoto M, Rifai N, Alper SL and Platt O (1995) Oral administration of clotrimazole and blockade of human erythrocyte Ca(++)-activated K+ channel: the imidazole ring is not required for inhibitory activity. J. Pharmacol. Exp. Ther. 273: 266-272
    • (1995) J. Pharmacol. Exp. Ther. , vol.273 , pp. 266-272
    • Brugnara, C.1    Armsby, C.C.2    Sakamoto, M.3    Rifai, N.4    Alper, S.L.5    Platt, O.6
  • 38
    • 0033618445 scopus 로고    scopus 로고
    • Caspase independent/dependent regulation of K(+), cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis
    • Bortner CD and Cidlowski JA (1999) Caspase independent/dependent regulation of K(+), cell shrinkage, and mitochondrial membrane potential during lymphocyte apoptosis. J. Biol. Chem. 274: 21953-21962
    • (1999) J. Biol. Chem. , vol.274 , pp. 21953-21962
    • Bortner, C.D.1    Cidlowski, J.A.2
  • 41
    • 0345240928 scopus 로고    scopus 로고
    • Potassium is a critical regulator of apoptotic enzymes in vitro and in vivo
    • Hughes Jr FM and Cidlowski JA (1999) Potassium is a critical regulator of apoptotic enzymes in vitro and in vivo. Adv. Enzyme Regul. 39: 157-171
    • (1999) Adv. Enzyme Regul. , vol.39 , pp. 157-171
    • Hughes Jr., F.M.1    Cidlowski, J.A.2
  • 42
    • 0032834460 scopus 로고    scopus 로고
    • A necessary role for reduced intracellular potassium during the DNA degradation phase of apoptosis
    • Montague JW, Bortner CD, Hughes Jr FM and Cidlowski JA (1999) A necessary role for reduced intracellular potassium during the DNA degradation phase of apoptosis. Steroids 64: 563-569
    • (1999) Steroids , vol.64 , pp. 563-569
    • Montague, J.W.1    Bortner, C.D.2    Hughes Jr., F.M.3    Cidlowski, J.A.4
  • 43
    • 0033755773 scopus 로고    scopus 로고
    • Identification of potassium-dependent and -independent components of the apoptotic machinery in mouse ovarian germ cells and granulosa cells
    • Perez GI, Maravei DV, Trbovich AM, Cidlowski JA, Tilly JL and Hughes Jr FM. (2000) Identification of potassium-dependent and -independent components of the apoptotic machinery in mouse ovarian germ cells and granulosa cells. Biol. Reprod. 63: 1358-1369
    • (2000) Biol. Reprod. , vol.63 , pp. 1358-1369
    • Perez, G.I.1    Maravei, D.V.2    Trbovich, A.M.3    Cidlowski, J.A.4    Tilly, J.L.5    Hughes Jr., F.M.6
  • 45
    • 0019311634 scopus 로고
    • The effect of endogenous proteases on the spectrin binding proteins of human erythrocytes
    • Siegel DL, Goodman SR and Branton D (1980) The effect of endogenous proteases on the spectrin binding proteins of human erythrocytes. Biochim. Biophys. Acta 598: 517-527
    • (1980) Biochim. Biophys. Acta , vol.598 , pp. 517-527
    • Siegel, D.L.1    Goodman, S.R.2    Branton, D.3
  • 46
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall TG and Bennett V (1987) Regulatory domains of erythrocyte ankyrin. J. Biol. Chem. 262: 10537-10545
    • (1987) J. Biol. Chem. , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 47
    • 0037181167 scopus 로고    scopus 로고
    • Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
    • Mandal D, Moitra PK, Saha S and Basu J (2002) Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes. FEBS Lett. 513:184-188
    • (2002) FEBS Lett. , vol.513 , pp. 184-188
    • Mandal, D.1    Moitra, P.K.2    Saha, S.3    Basu, J.4
  • 48
    • 0347993072 scopus 로고    scopus 로고
    • Caspase 3-mediated proteolysis of the N-terminal cytoplasmic domain of the human erythroid anion exchanger 1 (band 3)
    • Mandal D, Baudin-Creuza V, Bhattacharyya A, Pathak S, Delaunay J, Kundu M and Basu J (2003) Caspase 3-mediated proteolysis of the N-terminal cytoplasmic domain of the human erythroid anion exchanger 1 (band 3). J. Biol. Chem. 278: 52551-52558
    • (2003) J. Biol. Chem. , vol.278 , pp. 52551-52558
    • Mandal, D.1    Baudin-Creuza, V.2    Bhattacharyya, A.3    Pathak, S.4    Delaunay, J.5    Kundu, M.6    Basu, J.7
  • 49
  • 52
    • 84939666375 scopus 로고
    • The pathophysiology of ischaemic acute renal failure. A new hypothesis about the initiation phase
    • Mason J (1986) The pathophysiology of ischaemic acute renal failure. A new hypothesis about the initiation phase. Renal Physiol. 9:129-147
    • (1986) Renal Physiol. , vol.9 , pp. 129-147
    • Mason, J.1
  • 53
    • 0027513049 scopus 로고
    • Cation transport and volume regulation in sickle red blood cells
    • Joiner CH (1993) Cation transport and volume regulation in sickle red blood cells. Am. J. Physiol. 264: C251-C270
    • (1993) Am. J. Physiol. , vol.264
    • Joiner, C.H.1
  • 55
    • 0034074414 scopus 로고    scopus 로고
    • Prevalence of hypochromia (without microcytosis) vs microcytosis (without hypochromia) in iron deficiency
    • Jolobe CM (2000) Prevalence of hypochromia (without microcytosis) vs microcytosis (without hypochromia) in iron deficiency. Clin. Lab. Haematol. 22: 79-80
    • (2000) Clin. Lab. Haematol. , vol.22 , pp. 79-80
    • Jolobe, C.M.1
  • 57
    • 0001803529 scopus 로고
    • The adhesiveness of human blood platelets in vitro
    • Hellem AJ (1960) The adhesiveness of human blood platelets in vitro. Scand. J. Clin. Lab. Invest. 12 (Suppl): 1-117
    • (1960) Scand. J. Clin. Lab. Invest. , vol.12 , Issue.SUPPL. , pp. 1-117
    • Hellem, A.J.1
  • 58
    • 72949135166 scopus 로고
    • The role of red cells in haemostasis: The relation between haematocrit, bleeding time and platelet adhesiveness
    • Hellem AJ, Borchgrevink CF and Ames SB (1961) The role of red cells in haemostasis: the relation between haematocrit, bleeding time and platelet adhesiveness. Br. J. Haematol. 7: 42-50
    • (1961) Br. J. Haematol. , vol.7 , pp. 42-50
    • Hellem, A.J.1    Borchgrevink, C.F.2    Ames, S.B.3
  • 59
    • 0026082088 scopus 로고
    • Enhancement of platelet reactivity and modulation of eicosanoid production by intact erythrocytes. A new approach to platelet activation and recruitment
    • Santos MT, Valles J, Marcus AJ, Safier LB, Broekman MJ, Islam N, Ullman HL, Eiroa AM and Aznar J (1991) Enhancement of platelet reactivity and modulation of eicosanoid production by intact erythrocytes. A new approach to platelet activation and recruitment. J. Clin. Invest. 87: 571-580
    • (1991) J. Clin. Invest. , vol.87 , pp. 571-580
    • Santos, M.T.1    Valles, J.2    Marcus, A.J.3    Safier, L.B.4    Broekman, M.J.5    Islam, N.6    Ullman, H.L.7    Eiroa, A.M.8    Aznar, J.9
  • 60
    • 0025776841 scopus 로고
    • Erythrocytes metabolically enhance collagen-induced platelet responsiveness via increased thromboxane production, adenosine diphosphate release, and recruitment
    • Valles J, Santos MT, Aznar J, Marcus AJ, Martinez-Sales V, Portoles M, Broekman MJ and Safier LB (1991) Erythrocytes metabolically enhance collagen-induced platelet responsiveness via increased thromboxane production, adenosine diphosphate release, and recruitment. Blood 78: 154-162
    • (1991) Blood , vol.78 , pp. 154-162
    • Valles, J.1    Santos, M.T.2    Aznar, J.3    Marcus, A.J.4    Martinez-Sales, V.5    Portoles, M.6    Broekman, M.J.7    Safier, L.B.8
  • 61
    • 0041328097 scopus 로고    scopus 로고
    • Role of eicosanoids in structural degradation in osteoarthritis
    • Laufer S (2003) Role of eicosanoids in structural degradation in osteoarthritis. Curr. Opin. Rheumatol. 15: 623-627
    • (2003) Curr. Opin. Rheumatol. , vol.15 , pp. 623-627
    • Laufer, S.1
  • 62
    • 0028123552 scopus 로고
    • Effect of ion composition on the changes in membrane potential induced with several stimuli in rat mast cells
    • Cabado AG, Vieytes MR and Botana LM (1994) Effect of ion composition on the changes in membrane potential induced with several stimuli in rat mast cells. J. Cell. Physiol. 158: 309-316
    • (1994) J. Cell Physiol. , vol.158 , pp. 309-316
    • Cabado, A.G.1    Vieytes, M.R.2    Botana, L.M.3
  • 63
    • 0034494205 scopus 로고    scopus 로고
    • Cell volume-sensitive sodium channels upregulated by glucocorticoids in U937 macrophages
    • Gamper N, Huber SM, Badawi K and Lang F (2000) Cell volume-sensitive sodium channels upregulated by glucocorticoids in U937 macrophages. Pflugers Arch. 441: 281-286
    • (2000) Pflugers Arch. , vol.441 , pp. 281-286
    • Gamper, N.1    Huber, S.M.2    Badawi, K.3    Lang, F.4
  • 64
    • 0032998641 scopus 로고    scopus 로고
    • Osmotic shrinkage activates nonselective cation (NSC) channels in various cell types
    • Koch J and Korbmacher C (1999) Osmotic shrinkage activates nonselective cation (NSC) channels in various cell types. J. Membr. Biol. 168: 131-139
    • (1999) J. Membr. Biol. , vol.168 , pp. 131-139
    • Koch, J.1    Korbmacher, C.2
  • 65
    • 0029088906 scopus 로고
    • Hypertonicity activates nonselective cation channels in mouse cortical collecting duct cells
    • Volk T, Fromter E and Korbmacher C (1995) Hypertonicity activates nonselective cation channels in mouse cortical collecting duct cells. Proc. Natl. Acad. Sci. USA 92: 8478-8482
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8478-8482
    • Volk, T.1    Fromter, E.2    Korbmacher, C.3
  • 67
    • 0034534732 scopus 로고    scopus 로고
    • The hypertonicity-induced Na(+) conductance of rat hepatocytes: Physiological significance and molecular correlate
    • Wehner F, Böhmer C, Heinzinger H, van den BF and Tinel H (2000) The hypertonicity-induced Na(+) conductance of rat hepatocytes: physiological significance and molecular correlate. Cell. Physiol. Biochem. 10: 335-340
    • (2000) Cell Physiol. Biochem. , vol.10 , pp. 335-340
    • Wehner, F.1    Böhmer, C.2    Heinzinger, H.3    van den, B.F.4    Tinel, H.5
  • 69
    • 0034662989 scopus 로고    scopus 로고
    • Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis
    • Maeno E, Ishizaki Y, Kanaseki T, Hazama A and Okada Y (2000) Normotonic cell shrinkage because of disordered volume regulation is an early prerequisite to apoptosis. Proc. Natl. Acad. Sci. USA 97: 9487-9492
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9487-9492
    • Maeno, E.1    Ishizaki, Y.2    Kanaseki, T.3    Hazama, A.4    Okada, Y.5
  • 70
    • 0033607549 scopus 로고    scopus 로고
    • Cell shrinkage triggers the activation of mitogen-activated protein kinases by hypertonicity in the rat kidney medullary thick ascending limb of the Henle's loop. Requirement of p38 kinase for the regulatory volume increase response
    • Roger F, Martin PY, Rousselot M, Favre H and Feraille E (1999) Cell shrinkage triggers the activation of mitogen-activated protein kinases by hypertonicity in the rat kidney medullary thick ascending limb of the Henle's loop. Requirement of p38 kinase for the regulatory volume increase response. J. Biol. Chem. 274: 34103-34110
    • (1999) J. Biol. Chem. , vol.274 , pp. 34103-34110
    • Roger, F.1    Martin, P.Y.2    Rousselot, M.3    Favre, H.4    Feraille, E.5
  • 71
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill OP, Marty A, Neher E, Sakmann B and Sigeorth FJ (1981) Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches. Pflügers Arch. 391: 85-100
    • (1981) Pflügers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigeorth, F.J.5
  • 72
    • 0025774354 scopus 로고
    • Liquid junction potentials and small cell effects in patch-clamp analysis
    • Barry PH and Lynch JW (1991) Liquid junction potentials and small cell effects in patch-clamp analysis. J. Membr. Biol. 121: 101-117
    • (1991) J. Membr. Biol. , vol.121 , pp. 101-117
    • Barry, P.H.1    Lynch, J.W.2
  • 74
    • 0036838529 scopus 로고    scopus 로고
    • Phorbol ester stimulates a protein kinase C-mediated agatoxin-TK-sensitive calcium permeability pathway in human red blood cells
    • Andrews DA, Yang L and Low PS (2002) Phorbol ester stimulates a protein kinase C-mediated agatoxin-TK-sensitive calcium permeability pathway in human red blood cells. Blood 100: 3392-3399
    • (2002) Blood , vol.100 , pp. 3392-3399
    • Andrews, D.A.1    Yang, L.2    Low, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.