메뉴 건너뛰기




Volumn 294, Issue 1, 2008, Pages

Expression of the dystrophin-glycoprotein complex is a marker for human airway smooth muscle phenotype maturation

Author keywords

Differentiation; Laminin; Phosphatidylinositol 3 kinase; Sarcoglycans

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; BETA DYSTROGLYCAN; BETA SARCOGLYCAN; CALPONIN; DELTA SARCOGLYCAN; DYSTROPHIN; EPSILON SARCOGLYCAN; GLYCOPROTEIN; LAMININ; MYOSIN LIGHT CHAIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; WORTMANNIN;

EID: 40749148140     PISSN: 10400605     EISSN: 15221504     Source Type: Journal    
DOI: 10.1152/ajplung.00378.2007     Document Type: Article
Times cited : (34)

References (71)
  • 1
    • 4444306357 scopus 로고    scopus 로고
    • Genetic compensation for sarcoglycan loss by integrin α7β1 in muscle
    • Allikian MJ, Hack AA, Mewborn S, Mayer U, McNally EM. Genetic compensation for sarcoglycan loss by integrin α7β1 in muscle. J Cell Sci 117: 3821-3830, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 3821-3830
    • Allikian, M.J.1    Hack, A.A.2    Mewborn, S.3    Mayer, U.4    McNally, E.M.5
  • 5
    • 0034623959 scopus 로고    scopus 로고
    • Expression of gamma-sarcoglycan in smooth muscle and its interaction with the smooth muscle sarcoglycan-sarcospan complex
    • Barresi R, Moore SA, Stolle CA, Mendell JR, Campbell KP. Expression of gamma-sarcoglycan in smooth muscle and its interaction with the smooth muscle sarcoglycan-sarcospan complex. J Biol Chem 275: 38554-38560, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 38554-38560
    • Barresi, R.1    Moore, S.A.2    Stolle, C.A.3    Mendell, J.R.4    Campbell, K.P.5
  • 6
    • 33645730485 scopus 로고    scopus 로고
    • Sparks, signals and shock absorbers: How dystrophin loss causes muscular dystrophy
    • Batchelor CL, Winder SJ. Sparks, signals and shock absorbers: how dystrophin loss causes muscular dystrophy. Trends Cell Biol 16: 198-205, 2006.
    • (2006) Trends Cell Biol , vol.16 , pp. 198-205
    • Batchelor, C.L.1    Winder, S.J.2
  • 10
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell KP. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 80: 675-679, 1995.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 11
    • 23744490430 scopus 로고    scopus 로고
    • In vitro developmental expression of dystroglycan and laminin-α2 in human skeletal muscle
    • Chen L, Burgunder JM. In vitro developmental expression of dystroglycan and laminin-α2 in human skeletal muscle. Cell Biol Int 29: 506-513, 2005.
    • (2005) Cell Biol Int , vol.29 , pp. 506-513
    • Chen, L.1    Burgunder, J.M.2
  • 15
    • 0023737217 scopus 로고
    • Isolation and partial characterization of high affinity laminin receptors in neural cells
    • Douville PJ, Harvey WJ, Carbonetto S. Isolation and partial characterization of high affinity laminin receptors in neural cells. J Biol Chem 263: 14964-14969, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 14964-14969
    • Douville, P.J.1    Harvey, W.J.2    Carbonetto, S.3
  • 16
    • 34547615550 scopus 로고    scopus 로고
    • Altered biomechanical properties of carotid arteries in two mouse models of muscular dystrophy
    • Dye WW, Gleason RL, Wilson E, Humphrey JD. Altered biomechanical properties of carotid arteries in two mouse models of muscular dystrophy. J Appl Physiol 103: 664-672, 2007.
    • (2007) J Appl Physiol , vol.103 , pp. 664-672
    • Dye, W.W.1    Gleason, R.L.2    Wilson, E.3    Humphrey, J.D.4
  • 17
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122: 809-823, 1993.
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 19
    • 0024800827 scopus 로고
    • Subunit structure of a laminin-binding integrin and localization of its binding site on laminin
    • Gehlsen KR, Dickerson K, Argraves WS, Engvall E, Ruoslahti E. Subunit structure of a laminin-binding integrin and localization of its binding site on laminin. J Biol Chem 264: 19034-19038, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 19034-19038
    • Gehlsen, K.R.1    Dickerson, K.2    Argraves, W.S.3    Engvall, E.4    Ruoslahti, E.5
  • 20
    • 33747192327 scopus 로고    scopus 로고
    • Caveolar nanospaces in smooth muscle cells
    • Gherghiceanu M, Popescu LM. Caveolar nanospaces in smooth muscle cells. J Cell Mol Med 10: 519-528, 2006.
    • (2006) J Cell Mol Med , vol.10 , pp. 519-528
    • Gherghiceanu, M.1    Popescu, L.M.2
  • 23
    • 0023518505 scopus 로고
    • A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor
    • Graf J, Ogle RC, Robey FA, Sasaki M, Martin GR, Yamada Y, Kleinman HK. A pentapeptide from the laminin B1 chain mediates cell adhesion and binds the 67,000 laminin receptor. Biochemistry 26: 6896-6900, 1987.
    • (1987) Biochemistry , vol.26 , pp. 6896-6900
    • Graf, J.1    Ogle, R.C.2    Robey, F.A.3    Sasaki, M.4    Martin, G.R.5    Yamada, Y.6    Kleinman, H.K.7
  • 24
    • 0024434199 scopus 로고
    • Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro
    • Grant DS, Tashiro K, Segui-Real B, Yamada Y, Martin GR, Kleinman HK. Two different laminin domains mediate the differentiation of human endothelial cells into capillary-like structures in vitro. Cell 58: 933-943, 1989.
    • (1989) Cell , vol.58 , pp. 933-943
    • Grant, D.S.1    Tashiro, K.2    Segui-Real, B.3    Yamada, Y.4    Martin, G.R.5    Kleinman, H.K.6
  • 25
    • 0033885496 scopus 로고    scopus 로고
    • Differential requirement for individual sarcoglycans and dystrophin in the assembly and function of the dystrophin-glycoprotein complex
    • Hack AA, Lam MY, Cordier L, Shoturma DI, Ly CT, Hadhazy MA, Hadhazy MR, Sweeney HL, McNally EM. Differential requirement for individual sarcoglycans and dystrophin in the assembly and function of the dystrophin-glycoprotein complex. J Cell Sci 113: 2535-2544, 2000.
    • (2000) J Cell Sci , vol.113 , pp. 2535-2544
    • Hack, A.A.1    Lam, M.Y.2    Cordier, L.3    Shoturma, D.I.4    Ly, C.T.5    Hadhazy, M.A.6    Hadhazy, M.R.7    Sweeney, H.L.8    McNally, E.M.9
  • 29
    • 0035164457 scopus 로고    scopus 로고
    • Molecular mechanisms of phenotypic plasticity in smooth muscle cells
    • Halayko AJ, Solway J. Molecular mechanisms of phenotypic plasticity in smooth muscle cells. J Appl Physiol 90: 358-368, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 358-368
    • Halayko, A.J.1    Solway, J.2
  • 30
    • 32544448060 scopus 로고    scopus 로고
    • The association of caveolae, actin, and the dystrophin-glycoprotein complex: A role in smooth muscle phenotype and function?
    • Halayko AJ, Stelmack GL. The association of caveolae, actin, and the dystrophin-glycoprotein complex: a role in smooth muscle phenotype and function? Can J Physiol Pharmacol 83: 877-891, 2005.
    • (2005) Can J Physiol Pharmacol , vol.83 , pp. 877-891
    • Halayko, A.J.1    Stelmack, G.L.2
  • 31
    • 0028662382 scopus 로고
    • Potential role for phenotypic modulation of bronchial smooth muscle cells in chronic asthma
    • Halayko AJ, Stephens NL. Potential role for phenotypic modulation of bronchial smooth muscle cells in chronic asthma. Can J Physiol Pharmacol 72: 1448-1457, 1994.
    • (1994) Can J Physiol Pharmacol , vol.72 , pp. 1448-1457
    • Halayko, A.J.1    Stephens, N.L.2
  • 32
    • 40749155414 scopus 로고    scopus 로고
    • Phenotype and functional plasticity of airway smooth muscle: Role of caveolae and caveolins
    • In press
    • Halayko AJ, Tran T, Gosens R. Phenotype and functional plasticity of airway smooth muscle: role of caveolae and caveolins. Proc Am Thorac Soc. In press.
    • Proc Am Thorac Soc
    • Halayko, A.J.1    Tran, T.2    Gosens, R.3
  • 33
    • 0033011344 scopus 로고    scopus 로고
    • Calcium homeostasis and ultrastructural studies in a patient with limb girdle muscular dystrophy type 2C
    • Hassoni AA, Cullen MJ. Calcium homeostasis and ultrastructural studies in a patient with limb girdle muscular dystrophy type 2C. Neuropathol Appl Neurobiol 25: 244-253, 1999.
    • (1999) Neuropathol Appl Neurobiol , vol.25 , pp. 244-253
    • Hassoni, A.A.1    Cullen, M.J.2
  • 34
    • 0032582808 scopus 로고    scopus 로고
    • Differentiated phenotype of smooth muscle cells depends on signaling pathways through insulin-like growth factors and phosphatidylinositol 3-kinase
    • Hayashi K, Saga H, Chimori Y, Kimura K, Yamanaka Y, Sobue K. Differentiated phenotype of smooth muscle cells depends on signaling pathways through insulin-like growth factors and phosphatidylinositol 3-kinase. J Biol Chem 273: 28860-28867, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 28860-28867
    • Hayashi, K.1    Saga, H.2    Chimori, Y.3    Kimura, K.4    Yamanaka, Y.5    Sobue, K.6
  • 35
    • 28844506745 scopus 로고    scopus 로고
    • Dystroglycan: A multifunctional adaptor protein
    • Higginson JR, Winder SJ. Dystroglycan: a multifunctional adaptor protein. Biochem Soc Trans 33: 1254-1255, 2005.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1254-1255
    • Higginson, J.R.1    Winder, S.J.2
  • 37
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation
    • Ilsley JL, Sudol M, Winder SJ. The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. Cell Signal 13: 625-632, 2001.
    • (2001) Cell Signal , vol.13 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 39
    • 0023492076 scopus 로고    scopus 로고
    • Iwamoto Y, Robey FA, Graf J, Sasaki M, Kleinman HK, Yamada Y, Martin GR. YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science 238: 1132-1134, 1987.
    • Iwamoto Y, Robey FA, Graf J, Sasaki M, Kleinman HK, Yamada Y, Martin GR. YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science 238: 1132-1134, 1987.
  • 40
    • 0025102960 scopus 로고
    • Symptoms of upper gastrointestinal dysfunction in Duchenne muscular dystrophy: Case-control study
    • Jaffe KM, McDonald CM, Ingman E, Haas J. Symptoms of upper gastrointestinal dysfunction in Duchenne muscular dystrophy: case-control study. Arch Phys Med Rehabil 71: 742-744, 1990.
    • (1990) Arch Phys Med Rehabil , vol.71 , pp. 742-744
    • Jaffe, K.M.1    McDonald, C.M.2    Ingman, E.3    Haas, J.4
  • 41
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells
    • Langenbach KJ, Rando TA. Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells. Muscle Nerve 26: 644-653, 2002.
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2
  • 42
    • 2342621479 scopus 로고    scopus 로고
    • The dystrophin glycoprotein complex: Signaling strength and integrity for the sarcolemma
    • Lapidos KA, Kakkar R, McNally EM. The dystrophin glycoprotein complex: signaling strength and integrity for the sarcolemma. Circ Res 94: 1023-1031, 2004.
    • (2004) Circ Res , vol.94 , pp. 1023-1031
    • Lapidos, K.A.1    Kakkar, R.2    McNally, E.M.3
  • 44
    • 0032831526 scopus 로고    scopus 로고
    • Mechanical properties of smooth muscle portal vein in normal and dystrophin-deficient (mdx) mice
    • Mancinelli R, Tonali P, Romani R, Tringali A, Vargiu R, Azzena GB. Mechanical properties of smooth muscle portal vein in normal and dystrophin-deficient (mdx) mice. Exp Physiol 84: 929-940, 1999.
    • (1999) Exp Physiol , vol.84 , pp. 929-940
    • Mancinelli, R.1    Tonali, P.2    Romani, R.3    Tringali, A.4    Vargiu, R.5    Azzena, G.B.6
  • 45
    • 0023010323 scopus 로고
    • Effects of dystrophy and age on hamster tracheal smooth muscle function
    • Mardini IA, Schlenker EH, Burbach JA. Effects of dystrophy and age on hamster tracheal smooth muscle function. Respir Physiol 66: 157-170, 1986.
    • (1986) Respir Physiol , vol.66 , pp. 157-170
    • Mardini, I.A.1    Schlenker, E.H.2    Burbach, J.A.3
  • 46
    • 0028047235 scopus 로고
    • Dystrophin-glycoprotein complex: Its role in the molecular pathogenesis of muscular dystrophies
    • Matsumura K, Campbell KP. Dystrophin-glycoprotein complex: its role in the molecular pathogenesis of muscular dystrophies. Muscle Nerve 17: 2-15, 1994.
    • (1994) Muscle Nerve , vol.17 , pp. 2-15
    • Matsumura, K.1    Campbell, K.P.2
  • 47
    • 0031018436 scopus 로고    scopus 로고
    • The role of dystroglycan, a novel receptor of laminin and agrin, in cell differentiation
    • Matsumura K, Yamada H, Saito F, Sunada Y, Shimizu T. The role of dystroglycan, a novel receptor of laminin and agrin, in cell differentiation. Histol Histopathol 12: 195-203, 1997.
    • (1997) Histol Histopathol , vol.12 , pp. 195-203
    • Matsumura, K.1    Yamada, H.2    Saito, F.3    Sunada, Y.4    Shimizu, T.5
  • 48
    • 2442700500 scopus 로고    scopus 로고
    • Decreased expression of ryanodine receptors alters calcium-induced calcium release mechanism in mdx duodenal myocytes
    • Morel JL, Rakotoarisoa L, Jeyakumar LH, Fleischer S, Mironneau C, Mironneau J. Decreased expression of ryanodine receptors alters calcium-induced calcium release mechanism in mdx duodenal myocytes. J Biol Chem 279: 21287-21293, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 21287-21293
    • Morel, J.L.1    Rakotoarisoa, L.2    Jeyakumar, L.H.3    Fleischer, S.4    Mironneau, C.5    Mironneau, J.6
  • 50
    • 0027476106 scopus 로고
    • Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle
    • North AJ, Galazkiewicz B, Byers TJ, Glenney JR Jr, Small JV. Complementary distributions of vinculin and dystrophin define two distinct sarcolemma domains in smooth muscle. J Cell Biol 120: 1159-1167, 1993.
    • (1993) J Cell Biol , vol.120 , pp. 1159-1167
    • North, A.J.1    Galazkiewicz, B.2    Byers, T.J.3    Glenney Jr, J.R.4    Small, J.V.5
  • 51
    • 0029048550 scopus 로고
    • Regulation of differentiation of vascular smooth muscle cells
    • Owens GK. Regulation of differentiation of vascular smooth muscle cells. Physiol Rev 75: 487-517, 1995.
    • (1995) Physiol Rev , vol.75 , pp. 487-517
    • Owens, G.K.1
  • 53
    • 0032832968 scopus 로고    scopus 로고
    • Purification and characterization of an alpha-actinin-binding PDZ-LIM protein that is up-regulated during muscle differentiation
    • Pomies P, Macalma T, Beckerle MC. Purification and characterization of an alpha-actinin-binding PDZ-LIM protein that is up-regulated during muscle differentiation. J Biol Chem 274: 29242-29250, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 29242-29250
    • Pomies, P.1    Macalma, T.2    Beckerle, M.C.3
  • 54
    • 33748515008 scopus 로고    scopus 로고
    • IL-17A induces eotaxin-1/CC chemokine ligand 11 expression in human airway smooth muscle cells: Role of MAPK (Erk1/2, JNK, and p38) pathways
    • Rahman MS, Yamasaki A, Yang J, Shan L, Halayko AJ, Gounni AS. IL-17A induces eotaxin-1/CC chemokine ligand 11 expression in human airway smooth muscle cells: role of MAPK (Erk1/2, JNK, and p38) pathways. J Immunol 177: 4064-4071, 2006.
    • (2006) J Immunol , vol.177 , pp. 4064-4071
    • Rahman, M.S.1    Yamasaki, A.2    Yang, J.3    Shan, L.4    Halayko, A.J.5    Gounni, A.S.6
  • 55
    • 13244286597 scopus 로고    scopus 로고
    • Expression analysis of the SG-SSPN complex in smooth muscle and endothelial cells of human umbilical cord vessels
    • Ramirez-Sanchez I, Rosas-Vargas H, Ceballos-Reyes G, Salamanca F, Coral-Vazquez RM. Expression analysis of the SG-SSPN complex in smooth muscle and endothelial cells of human umbilical cord vessels. J Vasc Res 42: 1-7, 2005.
    • (2005) J Vasc Res , vol.42 , pp. 1-7
    • Ramirez-Sanchez, I.1    Rosas-Vargas, H.2    Ceballos-Reyes, G.3    Salamanca, F.4    Coral-Vazquez, R.M.5
  • 57
    • 0033552596 scopus 로고    scopus 로고
    • Cell elongation induces laminin alpha2 chain expression in mouse embryonic mesenchymal cells: Role in visceral myogenesis
    • Relan NK, Yang Y, Beqaj S, Miner JH, Schuger L. Cell elongation induces laminin alpha2 chain expression in mouse embryonic mesenchymal cells: role in visceral myogenesis. J Cell Biol 147: 1341-1350, 1999.
    • (1999) J Cell Biol , vol.147 , pp. 1341-1350
    • Relan, N.K.1    Yang, Y.2    Beqaj, S.3    Miner, J.H.4    Schuger, L.5
  • 60
    • 0026019355 scopus 로고
    • Inhibition of angiogenesis and tumor growth by a synthetic laminin peptide, CDPGYIGSRNH2
    • Sakamoto N, Iwahana M, Tanaka NG, Osada Y. Inhibition of angiogenesis and tumor growth by a synthetic laminin peptide, CDPGYIGSRNH2. Cancer Res 51: 903-906, 1991.
    • (1991) Cancer Res , vol.51 , pp. 903-906
    • Sakamoto, N.1    Iwahana, M.2    Tanaka, N.G.3    Osada, Y.4
  • 62
    • 33744934776 scopus 로고    scopus 로고
    • Zeta-sarcoglycan is a functional homologue of gamma-sarcoglycan in the formation of the sarcoglycan complex
    • Shiga K, Yoshioka H, Matsumiya T, Kimura I, Takeda S, Imamura M. Zeta-sarcoglycan is a functional homologue of gamma-sarcoglycan in the formation of the sarcoglycan complex. Exp Cell Res 312: 2083-2092, 2006.
    • (2006) Exp Cell Res , vol.312 , pp. 2083-2092
    • Shiga, K.1    Yoshioka, H.2    Matsumiya, T.3    Kimura, I.4    Takeda, S.5    Imamura, M.6
  • 64
    • 2942604709 scopus 로고    scopus 로고
    • Dystroglycan, a scaffold for the ERK-MAP kinase cascade
    • Spence HJ, Dhillon AS, James M, Winder SJ. Dystroglycan, a scaffold for the ERK-MAP kinase cascade. EMBO Rep 5: 484-489, 2004.
    • (2004) EMBO Rep , vol.5 , pp. 484-489
    • Spence, H.J.1    Dhillon, A.S.2    James, M.3    Winder, S.J.4
  • 65
    • 0033600605 scopus 로고    scopus 로고
    • ε-Sarcoglycan replaces α-sarcoglycan in smooth muscle to form a unique dystrophin-glycoprotein complex
    • Straub V, Ettinger AJ, Durbeej M, Venzke DP, Cutshall S, Sanes JR, Campbell KP. ε-Sarcoglycan replaces α-sarcoglycan in smooth muscle to form a unique dystrophin-glycoprotein complex. J Biol Chem 274: 27989-27996, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 27989-27996
    • Straub, V.1    Ettinger, A.J.2    Durbeej, M.3    Venzke, D.P.4    Cutshall, S.5    Sanes, J.R.6    Campbell, K.P.7
  • 67
    • 33749256297 scopus 로고    scopus 로고
    • Endogenous laminin is required for human airway smooth muscle cell maturation
    • Tran T, McNeill KD, Gerthoffer WT, Unruh H, Halayko AJ. Endogenous laminin is required for human airway smooth muscle cell maturation. Respir Res 7: 117, 2006.
    • (2006) Respir Res , vol.7 , pp. 117
    • Tran, T.1    McNeill, K.D.2    Gerthoffer, W.T.3    Unruh, H.4    Halayko, A.J.5
  • 68
    • 33750262034 scopus 로고    scopus 로고
    • Culture of human skeletal muscle myoblasts: Timing appearance and localization of dystrophin-glycoprotein complex and vinculin-talin-integrin complex
    • Trimarchi F, Favaloro A, Fulle S, Magaudda L, Puglielli C, Di Mauro D. Culture of human skeletal muscle myoblasts: timing appearance and localization of dystrophin-glycoprotein complex and vinculin-talin-integrin complex. Cells Tissues Organs 183: 87-98, 2006.
    • (2006) Cells Tissues Organs , vol.183 , pp. 87-98
    • Trimarchi, F.1    Favaloro, A.2    Fulle, S.3    Magaudda, L.4    Puglielli, C.5    Di Mauro, D.6
  • 70
    • 0030835890 scopus 로고    scopus 로고
    • Functional expression of the alpha 7 integrin receptor in differentiated smooth muscle cells
    • Yao CC, Breuss J, Pytela R, Kramer RH. Functional expression of the alpha 7 integrin receptor in differentiated smooth muscle cells. J Cell Sci 110: 1477-1487, 1997.
    • (1997) J Cell Sci , vol.110 , pp. 1477-1487
    • Yao, C.C.1    Breuss, J.2    Pytela, R.3    Kramer, R.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.