메뉴 건너뛰기




Volumn 73, Issue 12, 2006, Pages 1541-1549

Reorganization of mouse sperm lipid rafts by capacitation

Author keywords

Capacitation; Lipid raft; Membrane organization

Indexed keywords

TRITON X 100;

EID: 33750287154     PISSN: 1040452X     EISSN: 10982795     Source Type: Journal    
DOI: 10.1002/mrd.20540     Document Type: Article
Times cited : (34)

References (49)
  • 1
    • 0036134997 scopus 로고    scopus 로고
    • Sonication of mouse sperm membranes reveals distinct protein domains
    • Baker SS, Cardullo RA, Thaler CD. 2002. Sonication of mouse sperm membranes reveals distinct protein domains. Biol Reprod 66:57-64.
    • (2002) Biol Reprod , vol.66 , pp. 57-64
    • Baker, S.S.1    Cardullo, R.A.2    Thaler, C.D.3
  • 2
    • 4143144331 scopus 로고    scopus 로고
    • Sperm membrane dynamics assessed by changes in lectin fluorescence before and after capacitation
    • Baker SS, Thomas M, Thaler CD. 2004. Sperm membrane dynamics assessed by changes in lectin fluorescence before and after capacitation. J Androl 25:744-751.
    • (2004) J Androl , vol.25 , pp. 744-751
    • Baker, S.S.1    Thomas, M.2    Thaler, C.D.3
  • 3
    • 0025674680 scopus 로고
    • Morphology of mammalian sperm membranes during differentiation, maturation, and capacitation
    • Bearer EL, Friend DS. 1990. Morphology of mammalian sperm membranes during differentiation, maturation, and capacitation. J Electron Microsc Tech 16:281-297.
    • (1990) J Electron Microsc Tech , vol.16 , pp. 281-297
    • Bearer, E.L.1    Friend, D.S.2
  • 4
    • 0034995492 scopus 로고    scopus 로고
    • Isolation and characterization of sea urchin egg lipid rafts and their possible function during fertilization
    • Belton RJ, Jr., Adams NL, Foltz KR. 2001. Isolation and characterization of sea urchin egg lipid rafts and their possible function during fertilization. Mol Reprod Dev 59:294-305.
    • (2001) Mol Reprod Dev , vol.59 , pp. 294-305
    • Belton Jr., R.J.1    Adams, N.L.2    Foltz, K.R.3
  • 5
    • 0037369769 scopus 로고    scopus 로고
    • Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction
    • Brener E, Rubinstein S, Cohen G, Shternall K, Rivlin J, Breitbart H. 2003. Remodeling of the actin cytoskeleton during mammalian sperm capacitation and acrosome reaction. Biol Reprod 68:837-845.
    • (2003) Biol Reprod , vol.68 , pp. 837-845
    • Brener, E.1    Rubinstein, S.2    Cohen, G.3    Shternall, K.4    Rivlin, J.5    Breitbart, H.6
  • 6
    • 0034741667 scopus 로고    scopus 로고
    • Microdomains, lipid rafts and caveolae
    • Brown DA, Jacobson K. 2001. Microdomains, lipid rafts and caveolae. Traffic 2:668-672.
    • (2001) Traffic , vol.2 , pp. 668-672
    • Brown, D.A.1    Jacobson, K.2
  • 7
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. 1998. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 8
    • 0141730256 scopus 로고    scopus 로고
    • The role of F-actin cytoskeleton-associated gelsolin in the guinea pig capacitation and acrosome reaction
    • Cabello-Agueros JF, Hernandez-Gonzalez EO, Mujica A. 2003. The role of F-actin cytoskeleton-associated gelsolin in the guinea pig capacitation and acrosome reaction. Cell Motil Cytoskeleton 56:94-108.
    • (2003) Cell Motil Cytoskeleton , vol.56 , pp. 94-108
    • Cabello-Agueros, J.F.1    Hernandez-Gonzalez, E.O.2    Mujica, A.3
  • 9
    • 6344274550 scopus 로고    scopus 로고
    • Function of the egg's extracellular matrix
    • Hardy DM, editor. San Diego: Academic Press
    • Cardullo RA, Thaler CD. 2002. Function of the egg's extracellular matrix. In: Hardy DM, editor. Fertilization. San Diego: Academic Press. pp 119-152.
    • (2002) Fertilization , pp. 119-152
    • Cardullo, R.A.1    Thaler, C.D.2
  • 10
    • 0029155323 scopus 로고
    • Distribution and dynamics of mouse sperm surface galactosyltransferase: Implications for mammalian fertilization
    • Cardullo RA, Wolf DE. 1995. Distribution and dynamics of mouse sperm surface galactosyltransferase: Implications for mammalian fertilization. Biochemistry 34:10027-10035.
    • (1995) Biochemistry , vol.34 , pp. 10027-10035
    • Cardullo, R.A.1    Wolf, D.E.2
  • 11
    • 0442276428 scopus 로고    scopus 로고
    • Detergents as tools for the purification and classification of lipid rafts
    • Chamberlain LH. 2004. Detergents as tools for the purification and classification of lipid rafts. FEBS Lett 559:1-5.
    • (2004) FEBS Lett , vol.559 , pp. 1-5
    • Chamberlain, L.H.1
  • 12
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis
    • Chamberlain LH, Burgoyne RD, Gould GW. 2001. SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis. Proc Natl Acad Sci USA 98:5619-5624.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 13
    • 0023255879 scopus 로고
    • In vitro penetration of hamster oocyte-cumulus complexes using physiological numbers of sperm
    • Corselli J, Talbot P. 1987. In vitro penetration of hamster oocyte-cumulus complexes using physiological numbers of sperm. Dev Biol 122:227-242.
    • (1987) Dev Biol , vol.122 , pp. 227-242
    • Corselli, J.1    Talbot, P.2
  • 14
    • 0035881954 scopus 로고    scopus 로고
    • Guinea pig fertilin exhibits restricted lateral mobility in epididymal sperm and becomes freely diffusing during capacitation
    • Cowan AE, Koppel DE, Vargas LA, Hunnicutt GR. 2001. Guinea pig fertilin exhibits restricted lateral mobility in epididymal sperm and becomes freely diffusing during capacitation. Dev Biol 236:502-509.
    • (2001) Dev Biol , vol.236 , pp. 502-509
    • Cowan, A.E.1    Koppel, D.E.2    Vargas, L.A.3    Hunnicutt, G.R.4
  • 15
    • 4544342119 scopus 로고    scopus 로고
    • Reorganization of lipid rafts during capacitation of human sperm
    • Cross NL. 2004. Reorganization of lipid rafts during capacitation of human sperm. Biol Reprod 71:1367-1373.
    • (2004) Biol Reprod , vol.71 , pp. 1367-1373
    • Cross, N.L.1
  • 16
    • 11244275411 scopus 로고    scopus 로고
    • Actin polymerization in the equatorial and post-acrosomal regions of guinea pig spermatozoa during the acrosome reaction is regulated by G proteins
    • Delgado-Buenrostro NL, Hernandez-Gonzalez EO, Segura-Nieto M, Mujica A. 2005. Actin polymerization in the equatorial and post-acrosomal regions of guinea pig spermatozoa during the acrosome reaction is regulated by G proteins. Mol Reprod Dev 70:198-210.
    • (2005) Mol Reprod Dev , vol.70 , pp. 198-210
    • Delgado-Buenrostro, N.L.1    Hernandez-Gonzalez, E.O.2    Segura-Nieto, M.3    Mujica, A.4
  • 17
    • 1442358521 scopus 로고    scopus 로고
    • Membrane cholesterol and the regulation of signal transduction
    • Fielding CJ, Fielding PE. 2004. Membrane cholesterol and the regulation of signal transduction. Biochem Soc Trans 32:65-69.
    • (2004) Biochem Soc Trans , vol.32 , pp. 65-69
    • Fielding, C.J.1    Fielding, P.E.2
  • 18
    • 0034759226 scopus 로고    scopus 로고
    • Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane
    • Flesch FM, Brouwers JF, Nievelstein PF, Verkleij AJ, van Golde LM, Colenbrander B, Gadella BM. 2001. Bicarbonate stimulated phospholipid scrambling induces cholesterol redistribution and enables cholesterol depletion in the sperm plasma membrane. J Cell Sci 114:3543-3555.
    • (2001) J Cell Sci , vol.114 , pp. 3543-3555
    • Flesch, F.M.1    Brouwers, J.F.2    Nievelstein, P.F.3    Verkleij, A.J.4    Van Golde, L.M.5    Colenbrander, B.6    Gadella, B.M.7
  • 19
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster LJ, De Hoog CL, Mann M. 2003. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc Natl Acad Sci USA 100:5813-5818.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 20
    • 0036082781 scopus 로고    scopus 로고
    • Capacitation induces cyclic adenosine 3′,5′-monophosphate- dependent, but apoptosis-unrelated, exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells
    • Gadella BM, Harrison RA. 2002. Capacitation induces cyclic adenosine 3′,5′-monophosphate-dependent, but apoptosis-unrelated, exposure of aminophospholipids at the apical head plasma membrane of boar sperm cells. Biol Reprod 67:340-350.
    • (2002) Biol Reprod , vol.67 , pp. 340-350
    • Gadella, B.M.1    Harrison, R.A.2
  • 21
    • 5344266034 scopus 로고    scopus 로고
    • Spatial and temporal control of signaling through lipid rafts
    • Golub T, Wacha S, Caroni P. 2004. Spatial and temporal control of signaling through lipid rafts. Curr Opin Neurobiol 14:542-550.
    • (2004) Curr Opin Neurobiol , vol.14 , pp. 542-550
    • Golub, T.1    Wacha, S.2    Caroni, P.3
  • 22
    • 0034531095 scopus 로고    scopus 로고
    • Signaling through sphingolipid microdomains of the plasma membrane: The concept of signaling platform
    • Hoessli DC, Ilangumaran S, Soltermann A, Robinson PJ, Borisch B, Nasir-Ud-Din. 2000. Signaling through sphingolipid microdomains of the plasma membrane: The concept of signaling platform. Glycoconj J 17:191-197.
    • (2000) Glycoconj J , vol.17 , pp. 191-197
    • Hoessli, D.C.1    Ilangumaran, S.2    Soltermann, A.3    Robinson, P.J.4    Borisch, B.5    Nasir-Ud-Din6
  • 23
    • 0002402368 scopus 로고    scopus 로고
    • Capacitation
    • Hardy DM, editor. San Diego: Academic Press
    • Jaiswal BS, Eisenbach M. 2002. Capacitation. In: Hardy DM, editor. Fertilization. San Diego: Academic Press. pp 57-117.
    • (2002) Fertilization , pp. 57-117
    • Jaiswal, B.S.1    Eisenbach, M.2
  • 24
    • 0025340235 scopus 로고
    • Topographical rearrangement of a plasma membrane antigen during capacitation of rat spermatozoa in vitro
    • Jones R, Shalgi R, Hoyland J, Phillips DM. 1990. Topographical rearrangement of a plasma membrane antigen during capacitation of rat spermatozoa in vitro. Dev Biol 139:349-362.
    • (1990) Dev Biol , vol.139 , pp. 349-362
    • Jones, R.1    Shalgi, R.2    Hoyland, J.3    Phillips, D.M.4
  • 25
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore N, Smith KL, Graham CH, Jen A, Brady K, Hall S, Morris R. 1999. Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J 18:6917-6926.
    • (1999) EMBO J , vol.18 , pp. 6917-6926
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 26
    • 0037235101 scopus 로고    scopus 로고
    • Developmental association of the synaptic activity-regulated protein arc with the mouse acrosomal organelle and the sperm tail
    • Maier B, Medrano S, Sleight SB, Visconti PE, Scrable H. 2003. Developmental association of the synaptic activity-regulated protein arc with the mouse acrosomal organelle and the sperm tail. Biol Reprod 68:67-76.
    • (2003) Biol Reprod , vol.68 , pp. 67-76
    • Maier, B.1    Medrano, S.2    Sleight, S.B.3    Visconti, P.E.4    Scrable, H.5
  • 27
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default
    • Oh P, Schnitzer JE. 2001. Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default. Mol Biol Cell 12:685-698.
    • (2001) Mol Biol Cell , vol.12 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 28
    • 0023198755 scopus 로고
    • A two-step procedure for efficient electrotransfer of both high-molecular-weight (greater than 400,000) and low-molecular weight (less than 20,000) proteins
    • Otter T, King SM, Witman GB. 1988. A two-step procedure for efficient electrotransfer of both high-molecular-weight (greater than 400,000) and low-molecular weight (less than 20,000) proteins. Anal Biochem 162:370-377.
    • (1988) Anal Biochem , vol.162 , pp. 370-377
    • Otter, T.1    King, S.M.2    Witman, G.B.3
  • 29
    • 0022379986 scopus 로고
    • The mammalian spermatozoon: A model for the study of regional specificity in plasma membrane organization and function
    • Peterson RN, Russell LD. 1985. The mammalian spermatozoon: A model for the study of regional specificity in plasma membrane organization and function. Tissue Cell 17:769-791.
    • (1985) Tissue Cell , vol.17 , pp. 769-791
    • Peterson, R.N.1    Russell, L.D.2
  • 30
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior IA, Harding A, Yan J, Sluimer J, Parton RG, Hancock JF. 2001. GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat Cell Biol 3:368-375.
    • (2001) Nat Cell Biol , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton, R.G.5    Hancock, J.F.6
  • 31
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaun C, James DJ, Chamberlain LH. 2004. Lipid rafts and the regulation of exocytosis. Traffic 5:255-264.
    • (2004) Traffic , vol.5 , pp. 255-264
    • Salaun, C.1    James, D.J.2    Chamberlain, L.H.3
  • 32
    • 12544252686 scopus 로고    scopus 로고
    • The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells: Regulation by distinct cysteine-rich domains
    • Salaun C, Gould GW, Chamberlain LH. 2005. The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells: Regulation by distinct cysteine-rich domains. J Biol Chem 280:1236-1240.
    • (2005) J Biol Chem , vol.280 , pp. 1236-1240
    • Salaun, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 33
    • 0022977415 scopus 로고
    • Changes in the organization of surface antigens during in-vitro capacitation of boar spermatozoa as detected by monoclonal antibodies
    • Saxena N, Peterson RN, Sharif S, Saxena NK, Russell LD. 1986. Changes in the organization of surface antigens during in-vitro capacitation of boar spermatozoa as detected by monoclonal antibodies. J Reprod Fertil 178:601-614.
    • (1986) J Reprod Fertil , vol.178 , pp. 601-614
    • Saxena, N.1    Peterson, R.N.2    Sharif, S.3    Saxena, N.K.4    Russell, L.D.5
  • 34
    • 0029014820 scopus 로고
    • Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases
    • Schnitzer JE, Liu J, Oh P. 1995a. Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases. J Biol Chem 270:14399-14404.
    • (1995) J Biol Chem , vol.270 , pp. 14399-14404
    • Schnitzer, J.E.1    Liu, J.2    Oh, P.3
  • 35
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer JE, McIntosh DP, Dvorak AM, Liu J, Oh P. 1995b. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 269:1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 37
    • 3142724785 scopus 로고    scopus 로고
    • Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa
    • Shadan S, James PS, Howes EA, Jones R. 2004. Cholesterol efflux alters lipid raft stability and distribution during capacitation of boar spermatozoa. Biol Reprod 71:253-265.
    • (2004) Biol Reprod , vol.71 , pp. 253-265
    • Shadan, S.1    James, P.S.2    Howes, E.A.3    Jones, R.4
  • 38
    • 25144513384 scopus 로고    scopus 로고
    • Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: Evidence for dissociation of lipid rafts during capacitation
    • 2005
    • Sleight SB, Miranda PV, Plaskett NW, Maier B, Lysiak J, Scrable H, Herr JC, Visconti PE. 2005. Isolation and proteomic analysis of mouse sperm detergent-resistant membrane fractions: Evidence for dissociation of lipid rafts during capacitation. Biol Reprod 2005.; 73:721-729.
    • (2005) Biol Reprod , vol.73 , pp. 721-729
    • Sleight, S.B.1    Miranda, P.V.2    Plaskett, N.W.3    Maier, B.4    Lysiak, J.5    Scrable, H.6    Herr, J.C.7    Visconti, P.E.8
  • 39
    • 0035923728 scopus 로고    scopus 로고
    • Distinction between signaling mechanisms in lipid rafts vs. caveolae
    • Sowa G, Pypaert M, Sessa WC. 2001. Distinction between signaling mechanisms in lipid rafts vs. caveolae. Proc Natl Acad Sci USA 98:14072-14077.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14072-14077
    • Sowa, G.1    Pypaert, M.2    Sessa, W.C.3
  • 40
    • 0022405229 scopus 로고
    • Sperm penetration through oocyte investments in mammals
    • Talbot P. 1985. Sperm penetration through oocyte investments in mammals. Am J Anat 174:331-346.
    • (1985) Am J Anat , vol.174 , pp. 331-346
    • Talbot, P.1
  • 42
    • 0035976822 scopus 로고    scopus 로고
    • Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm
    • Trevino CL, Serrano CJ, Beltran C, Felix R, Darszon A. 2001. Identification of mouse trp homologs and lipid rafts from spermatogenic cells and sperm. FEBS Lett 509:119-125.
    • (2001) FEBS Lett , vol.509 , pp. 119-125
    • Trevino, C.L.1    Serrano, C.J.2    Beltran, C.3    Felix, R.4    Darszon, A.5
  • 44
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS. 1995a. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 121:1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 45
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL, Leclerc P, Connors SA, Pan D, Olds-Clarke P, Kopf GS. 1995b. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121:1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6    Olds-Clarke, P.7    Kopf, G.S.8
  • 47
    • 0033613867 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm. beta-cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation
    • Visconti PE, Galantino-Homer H, Ning X, Moore GD, Valenzuela JP, Jorgez CJ, Alvarez JG, Kopf GS. 1999a. Cholesterol efflux-mediated signal transduction in mammalian sperm. beta-cyclodextrins initiate transmembrane signaling leading to an increase in protein tyrosine phosphorylation and capacitation. J Biol Chem 274:3235-3242.
    • (1999) J Biol Chem , vol.274 , pp. 3235-3242
    • Visconti, P.E.1    Galantino-Homer, H.2    Ning, X.3    Moore, G.D.4    Valenzuela, J.P.5    Jorgez, C.J.6    Alvarez, J.G.7    Kopf, G.S.8
  • 48
    • 0033570112 scopus 로고    scopus 로고
    • Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation
    • Visconti PE, Ning X, Fornes MW, Alvarez JG, Stein P, Connors SA, Kopf GS. 1999b. Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation. Dev Biol 214:429-443.
    • (1999) Dev Biol , vol.214 , pp. 429-443
    • Visconti, P.E.1    Ning, X.2    Fornes, M.W.3    Alvarez, J.G.4    Stein, P.5    Connors, S.A.6    Kopf, G.S.7
  • 49
    • 0027297159 scopus 로고
    • Molecular events mediating sperm activation
    • Ward CR, Kopf GS. 1993. Molecular events mediating sperm activation. Dev Biol 158:9-34.
    • (1993) Dev Biol , vol.158 , pp. 9-34
    • Ward, C.R.1    Kopf, G.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.