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Volumn 46, Issue 12, 2005, Pages 4652-4660

Absence of SPARC in murine lens epithelium leads to increased deposition of laminin-1 in lens capsule

Author keywords

[No Author keywords available]

Indexed keywords

LAMININ 1; OSTEONECTIN; SCLEROPROTEIN; LAMININ; MESSENGER RNA; PRIMER DNA;

EID: 31544449337     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.05-0460     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 0025363827 scopus 로고
    • Molecular architecture of basement membranes
    • Yurchenco PD, Schittny JC. Molecular architecture of basement membranes. FASEB J. 1990;4:1577-590.
    • (1990) FASEB J , vol.4 , pp. 1577-1590
    • Yurchenco, P.D.1    Schittny, J.C.2
  • 2
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco PD, Amenta PS, Patton BL. Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol. 2004;22:521-538.
    • (2004) Matrix Biol , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 3
    • 0023015217 scopus 로고
    • Structure, development, and molecular pathology of basement membranes
    • Timpl R, Dziadek M. Structure, development, and molecular pathology of basement membranes. Int Rev Exp Pathol. 1986;29:1-112.
    • (1986) Int Rev Exp Pathol , vol.29 , pp. 1-112
    • Timpl, R.1    Dziadek, M.2
  • 5
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • Erickson AC, Couchman JR. Still more complexity in mammalian basement membranes. J Histochem Cytochem. 2000;48:1291-1306.
    • (2000) J Histochem Cytochem , vol.48 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 6
    • 0021233712 scopus 로고
    • Growth, synthesis and regional specialization of the embryonic chicken lens capsule
    • Johnson MC, Beebe DC. Growth, synthesis and regional specialization of the embryonic chicken lens capsule. Exp Eye Res. 1984;38:579-592.
    • (1984) Exp Eye Res , vol.38 , pp. 579-592
    • Johnson, M.C.1    Beebe, D.C.2
  • 7
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N, Vatansever HS, Murray P, et al. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol. 1999;144:151-160.
    • (1999) J Cell Biol , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3
  • 8
    • 0024373738 scopus 로고
    • Structure, composition, and assembly of basement membrane
    • Leblond CP, Inoue S. Structure, composition, and assembly of basement membrane. Am J Anat. 1989;185:367-390.
    • (1989) Am J Anat , vol.185 , pp. 367-390
    • Leblond, C.P.1    Inoue, S.2
  • 9
    • 0022500639 scopus 로고
    • Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen
    • Laurie GW, Bing JT, Kleinman HK, et al. Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen. J Mol Biol. 1986;189:205-216.
    • (1986) J Mol Biol , vol.189 , pp. 205-216
    • Laurie, G.W.1    Bing, J.T.2    Kleinman, H.K.3
  • 10
    • 0345381943 scopus 로고    scopus 로고
    • Expression and biological role of laminin-1
    • Ekblom P, Lonai P, Talts JF. Expression and biological role of laminin-1. Matrix Biol. 2003;22:35-47.
    • (2003) Matrix Biol , vol.22 , pp. 35-47
    • Ekblom, P.1    Lonai, P.2    Talts, J.F.3
  • 11
    • 0031970687 scopus 로고    scopus 로고
    • Integrins and development: How might these receptors regulate differentiation of the lens
    • Menko S, Philp N, Veneziale B, Walker J. Integrins and development: how might these receptors regulate differentiation of the lens. Ann NY Acad Sci. 1998;842:36-41.
    • (1998) Ann NY Acad Sci , vol.842 , pp. 36-41
    • Menko, S.1    Philp, N.2    Veneziale, B.3    Walker, J.4
  • 12
    • 0025876747 scopus 로고
    • The roles of laminin and fibronectin in the development of the lens capsule
    • Parmigiani CM, McAvoy JW. The roles of laminin and fibronectin in the development of the lens capsule. Curr Eye Res. 1991;10:501-511.
    • (1991) Curr Eye Res , vol.10 , pp. 501-511
    • Parmigiani, C.M.1    McAvoy, J.W.2
  • 13
    • 0033563308 scopus 로고    scopus 로고
    • Alpha6 integrin is regulated with lens cell differentiation by linkage to the cytoskeleton and isoform switching
    • Walker JL, Menko AS. Alpha6 integrin is regulated with lens cell differentiation by linkage to the cytoskeleton and isoform switching. Dev Biol. 1999;210:497-511.
    • (1999) Dev Biol , vol.210 , pp. 497-511
    • Walker, J.L.1    Menko, A.S.2
  • 14
    • 0036775425 scopus 로고    scopus 로고
    • Matricellular proteins: Extracellular modulators of cell function
    • Bornstein P, Sage EH. Matricellular proteins: extracellular modulators of cell function. Curr Opin Cell Biol. 2002;14:608-616.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 608-616
    • Bornstein, P.1    Sage, E.H.2
  • 15
    • 0032712968 scopus 로고    scopus 로고
    • SPARC, a matricellular glycoprotein with important biological functions
    • Yan Q, Sage EH. SPARC, a matricellular glycoprotein with important biological functions. J Histochem Cytochem. 1999;47:1495-1506.
    • (1999) J Histochem Cytochem , vol.47 , pp. 1495-1506
    • Yan, Q.1    Sage, E.H.2
  • 16
    • 0036629346 scopus 로고    scopus 로고
    • Alterations in the lens capsule contribute to cataractogenesis in SPARC-null mice
    • Yan Q, Clark JI, Wight TN, Sage EH. Alterations in the lens capsule contribute to cataractogenesis in SPARC-null mice. J Cell Sci. 2002;115:2747-2756.
    • (2002) J Cell Sci , vol.115 , pp. 2747-2756
    • Yan, Q.1    Clark, J.I.2    Wight, T.N.3    Sage, E.H.4
  • 17
    • 0037389333 scopus 로고    scopus 로고
    • Expression of the matricellular protein SPARC in murine lens: SPARC is necessary for the structural integrity of the capsular basement membrane
    • Yan Q, Blake D, Clark JI, Sage EH. Expression of the matricellular protein SPARC in murine lens: SPARC is necessary for the structural integrity of the capsular basement membrane. J Histochem Cytochem. 2003;51:503-511.
    • (2003) J Histochem Cytochem , vol.51 , pp. 503-511
    • Yan, Q.1    Blake, D.2    Clark, J.I.3    Sage, E.H.4
  • 18
    • 0033807857 scopus 로고    scopus 로고
    • Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface
    • Norose K, Lo WK, Clark JI, Sage EH, Howe CC. Lenses of SPARC-null mice exhibit an abnormal cell surface-basement membrane interface. Exp Eye Res. 2000;71:295-307.
    • (2000) Exp Eye Res , vol.71 , pp. 295-307
    • Norose, K.1    Lo, W.K.2    Clark, J.I.3    Sage, E.H.4    Howe, C.C.5
  • 19
    • 0031737501 scopus 로고    scopus 로고
    • SPARC deficiency leads to early-onset cataractogenesis
    • Norose K, Clark JI, Syed NA, et al. SPARC deficiency leads to early-onset cataractogenesis. Invest Ophthalmol Vis Sci. 1998;39:2674-2680.
    • (1998) Invest Ophthalmol Vis Sci , vol.39 , pp. 2674-2680
    • Norose, K.1    Clark, J.I.2    Syed, N.A.3
  • 20
    • 0021712863 scopus 로고
    • Localisation of laminin and fibronectin during rat lens morphogenesis
    • Parmigiani C, McAvoy J. Localisation of laminin and fibronectin during rat lens morphogenesis. Differentiation. 1984;28:53-61.
    • (1984) Differentiation , vol.28 , pp. 53-61
    • Parmigiani, C.1    McAvoy, J.2
  • 22
    • 0025271330 scopus 로고
    • Molecular cloning of SC1: A putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM40/SPARC
    • Johnston IG, Paladino T, Gurd JW, Brown IR. Molecular cloning of SC1: a putative brain extracellular matrix glycoprotein showing partial similarity to osteonectin/BM40/SPARC. Neuron. 1990;4:165-176.
    • (1990) Neuron , vol.4 , pp. 165-176
    • Johnston, I.G.1    Paladino, T.2    Gurd, J.W.3    Brown, I.R.4
  • 23
    • 0030914872 scopus 로고    scopus 로고
    • Cloning and expression of murine SC1, a gene product homologous to SPARC
    • Soderling JA, Reed MJ, Corsa A, Sage EH. Cloning and expression of murine SC1, a gene product homologous to SPARC. J Histochem Cytochem. 1997;45:823-835.
    • (1997) J Histochem Cytochem , vol.45 , pp. 823-835
    • Soderling, J.A.1    Reed, M.J.2    Corsa, A.3    Sage, E.H.4
  • 24
    • 2542610616 scopus 로고    scopus 로고
    • Expression and characterization of murine hevin (SC1), a member of the SPARC family of matricellular proteins
    • Brekken RA, Sullivan MM, Workman G, et al. Expression and characterization of murine hevin (SC1), a member of the SPARC family of matricellular proteins. J Histochem Cytochem. 2004;52:735-748.
    • (2004) J Histochem Cytochem , vol.52 , pp. 735-748
    • Brekken, R.A.1    Sullivan, M.M.2    Workman, G.3
  • 25
    • 0023377705 scopus 로고
    • Laminin-nidogen complex: Extraction with chelating agents and structural characterization
    • Paulsson M, Aumailley M, Deutzmann R, Timpl R, Beck K, Engel J. Laminin-nidogen complex: extraction with chelating agents and structural characterization. Eur J Biochem. 1987;166:11-19.
    • (1987) Eur J Biochem , vol.166 , pp. 11-19
    • Paulsson, M.1    Aumailley, M.2    Deutzmann, R.3    Timpl, R.4    Beck, K.5    Engel, J.6
  • 26
    • 0026742984 scopus 로고
    • Regulation of gene expression by SPARC during angiogenesis in vitro: Changes in fibronectin, thrombospondin-1, and plasminogen activator inhibitor-1
    • Lane TF, Iruela-Arispe ML, Sage EH. Regulation of gene expression by SPARC during angiogenesis in vitro: changes in fibronectin, thrombospondin-1, and plasminogen activator inhibitor-1. J Biol Chem. 1992;267:16736-16745.
    • (1992) J Biol Chem , vol.267 , pp. 16736-16745
    • Lane, T.F.1    Iruela-Arispe, M.L.2    Sage, E.H.3
  • 27
    • 0028356296 scopus 로고
    • Osteonectin/SPARC regulates cellular secretion rates of fibronectin and laminin extracellular matrix proteins
    • Kamihagi K, Katayama M, Ouchi R, Kato I. Osteonectin/SPARC regulates cellular secretion rates of fibronectin and laminin extracellular matrix proteins. Biochem Biophys Res Commun. 1994;200:423-428.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 423-428
    • Kamihagi, K.1    Katayama, M.2    Ouchi, R.3    Kato, I.4
  • 28
    • 0025772967 scopus 로고
    • SPARC induces the expression of type 1 plasminogen activator inhibitor in cultured bovine aortic endothelial cells
    • Hasselaar P, Loskutoff DJ, Sawdey M, Sage EH. SPARC induces the expression of type 1 plasminogen activator inhibitor in cultured bovine aortic endothelial cells. J Biol Chem. 1991;266:13178-13184.
    • (1991) J Biol Chem , vol.266 , pp. 13178-13184
    • Hasselaar, P.1    Loskutoff, D.J.2    Sawdey, M.3    Sage, E.H.4
  • 29
    • 0027297962 scopus 로고
    • SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway
    • Tremble PM, Lane TF, Sage EH, Werb Z. SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway. J Cell Biol. 1993;121:1433-1444.
    • (1993) J Cell Biol , vol.121 , pp. 1433-1444
    • Tremble, P.M.1    Lane, T.F.2    Sage, E.H.3    Werb, Z.4
  • 30
    • 0037791886 scopus 로고    scopus 로고
    • SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength
    • Bradshaw AD, Puolakkainen P, Dasgupta J, Davidson JM, Wight TN, Sage EH. SPARC-null mice display abnormalities in the dermis characterized by decreased collagen fibril diameter and reduced tensile strength. J Invest Dermatol. 2003;120:949-955.
    • (2003) J Invest Dermatol , vol.120 , pp. 949-955
    • Bradshaw, A.D.1    Puolakkainen, P.2    Dasgupta, J.3    Davidson, J.M.4    Wight, T.N.5    Sage, E.H.6
  • 32
    • 0345016887 scopus 로고    scopus 로고
    • Leukocyte, rather than tumor-produced SPARC, determines stroma and collagen type IV deposition in mammary carcinoma
    • Sangaletti S, Stoppacciaro A, Guiducci C, Torrisi MR, Colombo MP. Leukocyte, rather than tumor-produced SPARC, determines stroma and collagen type IV deposition in mammary carcinoma. J Exp Med. 2003;198:1475-1485.
    • (2003) J Exp Med , vol.198 , pp. 1475-1485
    • Sangaletti, S.1    Stoppacciaro, A.2    Guiducci, C.3    Torrisi, M.R.4    Colombo, M.P.5
  • 33
    • 0036938372 scopus 로고    scopus 로고
    • Evolutionary conservation and association of SPARC with the basal lamina in Drosophila
    • Martinek N, Zou R, Berg M, Sodek J, Ringuette M. Evolutionary conservation and association of SPARC with the basal lamina in Drosophila. Dev Genes Evol. 2002;212:124-133.
    • (2002) Dev Genes Evol , vol.212 , pp. 124-133
    • Martinek, N.1    Zou, R.2    Berg, M.3    Sodek, J.4    Ringuette, M.5
  • 34
    • 0022542156 scopus 로고
    • Endothelial cell injury in vitro is associated with increased secretion of an Mr 43,000 glycoprotein ligand
    • Sage H, Tupper J, Bramson R. Endothelial cell injury in vitro is associated with increased secretion of an Mr 43,000 glycoprotein ligand. J Cell Physiol. 1986;127:373-387.
    • (1986) J Cell Physiol , vol.127 , pp. 373-387
    • Sage, H.1    Tupper, J.2    Bramson, R.3
  • 35
    • 0028306966 scopus 로고
    • Two collagen-binding proteins, osteonectin and HSP47, are coordinately induced in transformed keratinocytes by heat and other stresses
    • Kudo H, Hirayoshi K, Kitagawa Y, Imamura S, Nagata K. Two collagen-binding proteins, osteonectin and HSP47, are coordinately induced in transformed keratinocytes by heat and other stresses. Exp Cell Res. 1994;212:219-224.
    • (1994) Exp Cell Res , vol.212 , pp. 219-224
    • Kudo, H.1    Hirayoshi, K.2    Kitagawa, Y.3    Imamura, S.4    Nagata, K.5
  • 36
    • 0026547680 scopus 로고
    • Heat-shock response in cultured chick embryo chondrocytes. Osteonectin is a secreted heat-shock protein
    • Neri M, Descalzi-Cancedda F, Cancedda R. Heat-shock response in cultured chick embryo chondrocytes. Osteonectin is a secreted heat-shock protein. Eur J Biochem. 1992;205:569-574.
    • (1992) Eur J Biochem , vol.205 , pp. 569-574
    • Neri, M.1    Descalzi-Cancedda, F.2    Cancedda, R.3
  • 37
    • 14744279741 scopus 로고    scopus 로고
    • Matricellular protein SPARC is translocated to the nuclei of immortalized murine lens epithelial cells
    • Yan Q, Weaver M, Perdue N, Sage EH. Matricellular protein SPARC is translocated to the nuclei of immortalized murine lens epithelial cells. J Cell Physiol. 2005;203:286-294.
    • (2005) J Cell Physiol , vol.203 , pp. 286-294
    • Yan, Q.1    Weaver, M.2    Perdue, N.3    Sage, E.H.4
  • 38
    • 0033814869 scopus 로고    scopus 로고
    • Association of SPARC (osteonectin, BM-40) with extracellular and intracellular components of the ciliated surface ectoderm of Xenopus embryos
    • Huynh MH, Hong H, Delovitch S, Desser S, Ringuette M. Association of SPARC (osteonectin, BM-40) with extracellular and intracellular components of the ciliated surface ectoderm of Xenopus embryos. Cell Motil Cytoskeleton. 2000;47:154-162.
    • (2000) Cell Motil Cytoskeleton , vol.47 , pp. 154-162
    • Huynh, M.H.1    Hong, H.2    Delovitch, S.3    Desser, S.4    Ringuette, M.5
  • 40
    • 0032984442 scopus 로고    scopus 로고
    • Cell cycle-dependent nuclear location of the matricellular protein SPARC: Association with the nuclear matrix
    • Gooden MD, Vernon RB, Bassuk JA, Sage EH. Cell cycle-dependent nuclear location of the matricellular protein SPARC: association with the nuclear matrix. J Cell Biochem. 1999;74:152-167.
    • (1999) J Cell Biochem , vol.74 , pp. 152-167
    • Gooden, M.D.1    Vernon, R.B.2    Bassuk, J.A.3    Sage, E.H.4
  • 41
    • 0021049422 scopus 로고
    • Immunohistochemical localization of entactin and laminin in mouse embryos and fetuses
    • Wu TC, Wan YJ, Chung AE, Damjanov I. Immunohistochemical localization of entactin and laminin in mouse embryos and fetuses. Dev Biol. 1983;100:496-505.
    • (1983) Dev Biol , vol.100 , pp. 496-505
    • Wu, T.C.1    Wan, Y.J.2    Chung, A.E.3    Damjanov, I.4


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