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Volumn 46, Issue 2, 2005, Pages 568-578

Transforming growth factor-β2 modulated extracellular matrix component expression in cultured human optic nerve head astrocytes

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; COLLAGEN TYPE 3; COLLAGEN TYPE 4; CONNECTIVE TISSUE GROWTH FACTOR; FIBRONECTIN; MESSENGER RNA; PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; SMALL INTERFERING RNA; THROMBOSPONDIN; TRANSFORMING GROWTH FACTOR BETA2;

EID: 13944249469     PISSN: 01460404     EISSN: None     Source Type: Journal    
DOI: 10.1167/iovs.04-0649     Document Type: Article
Times cited : (128)

References (39)
  • 1
    • 0035021939 scopus 로고    scopus 로고
    • Transforming growth factor beta 2 levels in the aqueous humor in different types of glaucoma and the relation to filtering bleb development
    • Picht G, Welge-Luessen U, Grehn F, Lütjen-Drecoll E. Transforming growth factor beta 2 levels in the aqueous humor in different types of glaucoma and the relation to filtering bleb development. Graefes Arch Clin Exp Ophthalmol. 2001;239:199-207.
    • (2001) Graefes Arch Clin Exp Ophthalmol , vol.239 , pp. 199-207
    • Picht, G.1    Welge-Luessen, U.2    Grehn, F.3    Lütjen-Drecoll, E.4
  • 2
    • 0028592628 scopus 로고
    • Aqueous humor in glaucomatous eyes contains an increased level of TGF-beta 2
    • Tripathi RC, Li J, Chan WF, Tripathi BJ. Aqueous humor in glaucomatous eyes contains an increased level of TGF-beta 2. Exp Eye Res. 1994;59:723-727.
    • (1994) Exp Eye Res , vol.59 , pp. 723-727
    • Tripathi, R.C.1    Li, J.2    Chan, W.F.3    Tripathi, B.J.4
  • 3
    • 0033924190 scopus 로고    scopus 로고
    • Induction of tissue transglutaminase in the trabecular meshwork by TGF-beta 1 and TGF-beta2
    • Welge-Lussen U, May CA, Lütjen-Drecoll E. Induction of tissue transglutaminase in the trabecular meshwork by TGF-beta 1 and TGF-beta2. Invest Ophthalmol Vis Sci. 2000;41:2229-2238.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 2229-2238
    • Welge-Lussen, U.1    May, C.A.2    Lütjen-Drecoll, E.3
  • 5
    • 0030942119 scopus 로고    scopus 로고
    • Severity of optic nerve damage in eyes with POAG is correlated with changes in the trabecular meshwork
    • Gottanka J, Johnson DH, Martus P, Lütjen-Drecoll E. Severity of optic nerve damage in eyes with POAG is correlated with changes in the trabecular meshwork. J Glaucoma. 1997;6:123-132.
    • (1997) J Glaucoma , vol.6 , pp. 123-132
    • Gottanka, J.1    Johnson, D.H.2    Martus, P.3    Lütjen-Drecoll, E.4
  • 7
    • 0031194332 scopus 로고    scopus 로고
    • Expression of neural cell adhesion molecule (NCAM) characterizes a subpopulation of type 1 astrocytes in human optic nerve head
    • Kobayashi S, Vidal I, Pena JD, Hernandez MR. Expression of neural cell adhesion molecule (NCAM) characterizes a subpopulation of type 1 astrocytes in human optic nerve head. Glia. 1997;20:262-273.
    • (1997) Glia , vol.20 , pp. 262-273
    • Kobayashi, S.1    Vidal, I.2    Pena, J.D.3    Hernandez, M.R.4
  • 10
    • 0025021550 scopus 로고
    • Changes in the extracellular matrix of the human optic nerve head in primary open-angle glaucoma
    • Hernandez MR, Andrzejewska WM, Neufeld AH. Changes in the extracellular matrix of the human optic nerve head in primary open-angle glaucoma. Am J Ophthalmol. 1990;109:180-188.
    • (1990) Am J Ophthalmol , vol.109 , pp. 180-188
    • Hernandez, M.R.1    Andrzejewska, W.M.2    Neufeld, A.H.3
  • 11
    • 0028136393 scopus 로고
    • Collagen type IV gene expression in human optic nerve heads with primary open angle glaucoma
    • Hernandez MR, Ye H, Roy S. Collagen type IV gene expression in human optic nerve heads with primary open angle glaucoma. Exp Eye Res. 1994;59:41-51.
    • (1994) Exp Eye Res , vol.59 , pp. 41-51
    • Hernandez, M.R.1    Ye, H.2    Roy, S.3
  • 12
    • 0024344508 scopus 로고
    • Age-related changes in the extracellular matrix of the human optic nerve head
    • Hernandez MR, Luo XX, Andrzejewska W, Neufeld AH. Age-related changes in the extracellular matrix of the human optic nerve head. Am J Ophthalmol. 1989;107:476-484.
    • (1989) Am J Ophthalmol , vol.107 , pp. 476-484
    • Hernandez, M.R.1    Luo, X.X.2    Andrzejewska, W.3    Neufeld, A.H.4
  • 14
    • 13944270041 scopus 로고
    • Extracellular matrix of the human optic nerve head in glaucoma
    • Podos SM, et al., eds. London: Mosby-Year Book Europe
    • Hernandez MR. Extracellular matrix of the human optic nerve head in glaucoma. In: Glaucoma. Podos SM, et al., eds. London: Mosby-Year Book Europe; 1994:6.4-6.7.
    • (1994) Glaucoma
    • Hernandez, M.R.1
  • 16
    • 0036796746 scopus 로고    scopus 로고
    • Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions
    • Sottile J, Hocking DC. Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions. Mol Biol Cell. 2002;13:3546-3559.
    • (2002) Mol Biol Cell , vol.13 , pp. 3546-3559
    • Sottile, J.1    Hocking, D.C.2
  • 17
    • 0022967033 scopus 로고
    • Attachment of cells to basement membrane collagen type TV
    • Aumailley M, Timpl R. Attachment of cells to basement membrane collagen type TV. J Cell Biol. 1986;103:1569-1575.
    • (1986) J Cell Biol , vol.103 , pp. 1569-1575
    • Aumailley, M.1    Timpl, R.2
  • 18
    • 0022500639 scopus 로고
    • Localization of binding sites for laminin, heparan sulfate proteoglycan and fibronectin on basement membrane (type IV) collagen
    • Laune 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
    • Laune, G.W.1    Bing, J.T.2    Kleinman, H.K.3
  • 19
    • 0020072924 scopus 로고
    • Role of fibronectin in collagen deposition: Fab′ to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix
    • McDonald JA, Kelley DG, Broekelmann TJ. Role of fibronectin in collagen deposition: Fab′ to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix. J Cell Biol. 1982;92:485-492.
    • (1982) J Cell Biol , vol.92 , pp. 485-492
    • McDonald, J.A.1    Kelley, D.G.2    Broekelmann, T.J.3
  • 20
    • 0033956408 scopus 로고    scopus 로고
    • Connective tissue growth factor: A novel player in tissue reorganization after brain injury?
    • Hertel M, Tretter Y, Alzheimer C, Werner S. Connective tissue growth factor: a novel player in tissue reorganization after brain injury? Eur J Neurosci. 2000;12:376-380.
    • (2000) Eur J Neurosci , vol.12 , pp. 376-380
    • Hertel, M.1    Tretter, Y.2    Alzheimer, C.3    Werner, S.4
  • 21
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg CS, Birckbichler PJ, Rice RH. Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues. Faseb J. 1991;5:3071-3077.
    • (1991) Faseb J , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 22
    • 0025261220 scopus 로고
    • Highly sulfated glycosaminoglycans augment the cross-linking of vitronectin by guinea pig liver transglutaminase: Functional studies of the cross-linked vitronectin multimers
    • Sane DC, Moser TL, Parker CJ, Seiffert D, Loskutoff DJ, Greenberg CS. Highly sulfated glycosaminoglycans augment the cross-linking of vitronectin by guinea pig liver transglutaminase: functional studies of the cross-linked vitronectin multimers. J Biol Chem. 1990;265:3543-3548.
    • (1990) J Biol Chem , vol.265 , pp. 3543-3548
    • Sane, D.C.1    Moser, T.L.2    Parker, C.J.3    Seiffert, D.4    Loskutoff, D.J.5    Greenberg, C.S.6
  • 23
    • 0025823541 scopus 로고
    • Cross-linking of laminin-nidogen complexes by tissue transglutaminase: A novel mechanism for basement membrane stabilization
    • Aeschlimann D, Paulsson M. Cross-linking of laminin-nidogen complexes by tissue transglutaminase: a novel mechanism for basement membrane stabilization. J Biol Chem. 1991;266:15308-15317.
    • (1991) J Biol Chem , vol.266 , pp. 15308-15317
    • Aeschlimann, D.1    Paulsson, M.2
  • 24
    • 0026612802 scopus 로고
    • Identification of Gln726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes
    • Aeschlimann D, Paulsson M, Mann K. Identification of Gln726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes. J Biol Chem. 1992;267: 11316-11321.
    • (1992) J Biol Chem , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 25
    • 0023139866 scopus 로고
    • Identification of a substrate site for liver transglutaminase on the aminopropeptide of type III collagen
    • Bowness JM, Folk JE, Timpl R. Identification of a substrate site for liver transglutaminase on the aminopropeptide of type III collagen. J Biol Chem. 1987;262:1022-1024.
    • (1987) J Biol Chem , vol.262 , pp. 1022-1024
    • Bowness, J.M.1    Folk, J.E.2    Timpl, R.3
  • 26
    • 0018691962 scopus 로고
    • Changes in transglutaminase activity in an experimental model of pulmonary fibrosis induced by paraquat
    • Griffin M, Smith LL, Wynne J. Changes in transglutaminase activity in an experimental model of pulmonary fibrosis induced by paraquat. Br J Exp Pathol. 1979;60:653-661.
    • (1979) Br J Exp Pathol , vol.60 , pp. 653-661
    • Griffin, M.1    Smith, L.L.2    Wynne, J.3
  • 27
    • 0024320762 scopus 로고
    • Transglutaminase-catalysed cross-linking: A potential mechanism for the interaction of fibrinogen, low density lipoprotein and arterial type III procollagen
    • Bowness JM, Tarr AH, Wiebe RI. Transglutaminase-catalysed cross-linking: a potential mechanism for the interaction of fibrinogen, low density lipoprotein and arterial type III procollagen. Thromb Res. 1989;54:357-367.
    • (1989) Thromb Res , vol.54 , pp. 357-367
    • Bowness, J.M.1    Tarr, A.H.2    Wiebe, R.I.3
  • 28
    • 0025075724 scopus 로고
    • Lipoprotein binding of crosslinked type III collagen aminopropeptide and fractions of its antigen in blood
    • Bowness JM, Tarr AH. Lipoprotein binding of crosslinked type III collagen aminopropeptide and fractions of its antigen in blood. Biochem Biophys Res Commun. 1990;170:519-525.
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 519-525
    • Bowness, J.M.1    Tarr, A.H.2
  • 29
    • 0028170881 scopus 로고
    • Increase in epsilon-(gamma-glutamyl)lysine crosslinks in atherosclerotic aortas
    • Bowness JM, Venditti M, Tarr AH, Taylor JR. Increase in epsilon-(gamma-glutamyl)lysine crosslinks in atherosclerotic aortas. Atherosclerosis. 1994;111:247-253.
    • (1994) Atherosclerosis , vol.111 , pp. 247-253
    • Bowness, J.M.1    Venditti, M.2    Tarr, A.H.3    Taylor, J.R.4
  • 30
    • 0029808645 scopus 로고    scopus 로고
    • A novel transforming growth factor beta response element controls the expression of the connective tissue growth factor gene
    • Grotendorst GR, Okochi H, Hayashi N. A novel transforming growth factor beta response element controls the expression of the connective tissue growth factor gene. Cell Growth Differ. 1996;7:469-480.
    • (1996) Cell Growth Differ , vol.7 , pp. 469-480
    • Grotendorst, G.R.1    Okochi, H.2    Hayashi, N.3
  • 31
    • 0142124407 scopus 로고    scopus 로고
    • Increased expression of connective tissue growth factor in amyotrophic lateral sclerosis human spinal cord
    • Spliet WG, Aronica E, Ramkema M, Aten J, Troost D. Increased expression of connective tissue growth factor in amyotrophic lateral sclerosis human spinal cord. Acta Neuropathol (Berl). 2003;106:449-457.
    • (2003) Acta Neuropathol (Berl) , vol.106 , pp. 449-457
    • Spliet, W.G.1    Aronica, E.2    Ramkema, M.3    Aten, J.4    Troost, D.5
  • 32
    • 0029586571 scopus 로고
    • Transforming growth factor-beta: Neuronal and glial expression in CNS degenerative diseases
    • Lippa CF, Smith TW, Flanders KC. Transforming growth factor-beta: neuronal and glial expression in CNS degenerative diseases. Neurodegeneration. 1995;4:425-432.
    • (1995) Neurodegeneration , vol.4 , pp. 425-432
    • Lippa, C.F.1    Smith, T.W.2    Flanders, K.C.3
  • 33
    • 0029879741 scopus 로고    scopus 로고
    • Increased expression of TGF-beta 1 in brain tissue after ischemie stroke in humans
    • Krupinski J, Kumar P, Kumar S, Kaluza J. Increased expression of TGF-beta 1 in brain tissue after ischemie stroke in humans. Stroke. 1996;27:852-857.
    • (1996) Stroke , vol.27 , pp. 852-857
    • Krupinski, J.1    Kumar, P.2    Kumar, S.3    Kaluza, J.4
  • 35
    • 0029816069 scopus 로고    scopus 로고
    • Stimulation of fibroblast cell growth, matrix production, and granulation tissue formation by connective tissue growth factor
    • Frazier K, Williams S, Kothapalli D, Klapper H, Grotendorst GR. Stimulation of fibroblast cell growth, matrix production, and granulation tissue formation by connective tissue growth factor. J Invest Dermatol. 1996;107:404-411.
    • (1996) J Invest Dermatol , vol.107 , pp. 404-411
    • Frazier, K.1    Williams, S.2    Kothapalli, D.3    Klapper, H.4    Grotendorst, G.R.5
  • 36
    • 0027175464 scopus 로고
    • Establishment of an astrocyte progenitor cell line: Induction of glial fibrillary acidic protein and fibronectin by transforming growth factor-beta 1
    • Yoshida T, Takeuchi M. Establishment of an astrocyte progenitor cell line: induction of glial fibrillary acidic protein and fibronectin by transforming growth factor-beta 1. J Neurosci Res. 199335: 129-137.
    • (1993) J Neurosci Res , vol.35 , pp. 129-137
    • Yoshida, T.1    Takeuchi, M.2
  • 37
    • 0027569648 scopus 로고
    • Effects of transforming growth factor-beta 1 on the extracellular matrix and cytoskeleton of cultured astrocytes
    • Baghdassarian D, Toru-Delbauffe D, Gavaret JM, Pierre M. Effects of transforming growth factor-beta 1 on the extracellular matrix and cytoskeleton of cultured astrocytes. Glia. 1993;7:193-202.
    • (1993) Glia , vol.7 , pp. 193-202
    • Baghdassarian, D.1    Toru-Delbauffe, D.2    Gavaret, J.M.3    Pierre, M.4
  • 38
    • 0034109215 scopus 로고    scopus 로고
    • Activation of latent TGF-beta by trombospondin-1: Mechanisms and physiology
    • Murphy-Ullrich JE, Poczatek M. Activation of latent TGF-beta by trombospondin-1: mechanisms and physiology. Cytokine Growth Factor Rev. 2000;11:59-69.
    • (2000) Cytokine Growth Factor Rev , vol.11 , pp. 59-69
    • Murphy-Ullrich, J.E.1    Poczatek, M.2
  • 39
    • 0242594633 scopus 로고    scopus 로고
    • The effect of TGF-beta2 on human trabecular meshwork extracellular proteolytic system
    • Fuchshofer R, Welge-Lussen U, Lütjen-Drecoll E. The effect of TGF-beta2 on human trabecular meshwork extracellular proteolytic system. Exp Eye Res. 2003;77:757-765.
    • (2003) Exp Eye Res , vol.77 , pp. 757-765
    • Fuchshofer, R.1    Welge-Lussen, U.2    Lütjen-Drecoll, E.3


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