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Volumn 11, Issue 2, 2011, Pages 110-128

Decorin biology, expression, function and therapy in the cornea

Author keywords

Cornea; Corneal haze scarring; Decorin; Gene therapy; Tgf beta

Indexed keywords

COLLAGEN; DECORIN; EPIDERMAL GROWTH FACTOR; TRANSFORMING GROWTH FACTOR BETA;

EID: 79952806081     PISSN: 15665240     EISSN: None     Source Type: Journal    
DOI: 10.2174/156652411794859241     Document Type: Article
Times cited : (72)

References (124)
  • 1
    • 0033773107 scopus 로고    scopus 로고
    • Extracellular matrix and cytokines: A functional unit
    • Schonherr E, Hausser HJ. Extracellular matrix and cytokines: a functional unit. Dev Immunol 2000; 7: 89-101.
    • (2000) Dev Immunol , vol.7 , pp. 89-101
    • Schonherr, E.1    Hausser, H.J.2
  • 2
    • 0035168796 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular matrix and growth control
    • Kresse H, Schonherr E. Proteoglycans of the extracellular matrix and growth control. J Cell Physiol 2001; 189: 266-74.
    • (2001) J Cell Physiol , vol.189 , pp. 266-274
    • Kresse, H.1    Schonherr, E.2
  • 3
    • 58149350127 scopus 로고    scopus 로고
    • Decorin and its galactosaminoglycan chain: Extracellular regulator of cellular function?
    • Seidler DG, Dreier R. Decorin and its galactosaminoglycan chain: extracellular regulator of cellular function? IUBMB Life 2008; 60: 729-33.
    • (2008) IUBMB Life , vol.60 , pp. 729-733
    • Seidler, D.G.1    Dreier, R.2
  • 5
    • 0027154689 scopus 로고
    • Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins
    • Rada JA, Cornuet PK, Hassell JR. Regulation of corneal collagen fibrillogenesis in vitro by corneal proteoglycan (lumican and decorin) core proteins. Exp Eye Res 1993; 56:635-48.
    • (1993) Exp Eye Res , vol.56 , pp. 635-648
    • Rada, J.A.1    Cornuet, P.K.2    Hassell, J.R.3
  • 6
    • 33747610396 scopus 로고    scopus 로고
    • A role for decorin in cutaneous wound healing and angiogenesis
    • Jarvelainen H, Puolakkainen P, Pakkanen S, et al. A role for decorin in cutaneous wound healing and angiogenesis. Wound Repair Regen 2006; 14: 443-52.
    • (2006) Wound Repair Regen , vol.14 , pp. 443-452
    • Jarvelainen, H.1    Puolakkainen, P.2    Pakkanen, S.3
  • 7
    • 77958018183 scopus 로고    scopus 로고
    • Role of transforming growth factor Beta in corneal function, biology and pathology
    • Tandon A, Tovey JC, Sharma A, Gupta R, Mohan RR. Role of transforming growth factor Beta in corneal function, biology and pathology. Curr Mol Med 2010; 10: 565-78.
    • (2010) Curr Mol Med , vol.10 , pp. 565-578
    • Tandon, A.1    Tovey, J.C.2    Sharma, A.3    Gupta, R.4    Mohan, R.R.5
  • 8
    • 77954953804 scopus 로고    scopus 로고
    • Decorin transfection suppresses profibrogenic genes and myofibroblast formation in human corneal fibroblasts
    • Mohan RR, Gupta R, Mehan MK, Cowden JW, Sinha S. Decorin transfection suppresses profibrogenic genes and myofibroblast formation in human corneal fibroblasts. Exp Eye Res 2010; 91: 238-45.
    • (2010) Exp Eye Res , vol.91 , pp. 238-245
    • Mohan, R.R.1    Gupta, R.2    Mehan, M.K.3    Cowden, J.W.4    Sinha, S.5
  • 9
    • 33846177921 scopus 로고    scopus 로고
    • Structure, metabolism, and tissue roles of chondroitin sulfate proteoglycans
    • Handley CJ, Samiric T, Ilic MZ. Structure, metabolism, and tissue roles of chondroitin sulfate proteoglycans. Adv Pharmacol 2006; 53: 219-32.
    • (2006) Adv Pharmacol , vol.53 , pp. 219-232
    • Handley, C.J.1    Samiric, T.2    Ilic, M.Z.3
  • 10
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope
    • Santra M, Reed CC, Iozzo RV. Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope. J Biol Chem 2002; 277: 35671-681.
    • (2002) J Biol Chem , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 11
    • 0029780703 scopus 로고    scopus 로고
    • Identification of a bimodal regulatory element encompassing a canonical AP-1 binding site in the proximal promoter region of the human decorin gene
    • Mauviel A, Korang K, Santra M, Tewari D, Uitto J, Iozzo RV. Identification of a bimodal regulatory element encompassing a canonical AP-1 binding site in the proximal promoter region of the human decorin gene. J Biol Chem 1996; 271: 24824-29.
    • (1996) J Biol Chem , vol.271 , pp. 24824-24829
    • Mauviel, A.1    Korang, K.2    Santra, M.3    Tewari, D.4    Uitto, J.5    Iozzo, R.V.6
  • 12
    • 0032893390 scopus 로고    scopus 로고
    • Transforming growth factor-beta and p-21: Multiple molecular targets of decorin-mediated suppression of neoplastic growth
    • Stander M, Naumann U, Wick W, Weller M. Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. Cell Tissue Res 1999; 296: 221-27.
    • (1999) Cell Tissue Res , vol.296 , pp. 221-227
    • Stander, M.1    Naumann, U.2    Wick, W.3    Weller, M.4
  • 13
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-beta by the proteoglycan decorin
    • Yamaguchi Y, Mann DM, Ruoslahti E. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature 1990; 346: 281-84.
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 14
    • 0033582415 scopus 로고    scopus 로고
    • Decorin is a biological ligand for the epidermal growth factor recepto
    • Iozzo RV, Moscatello DK, McQuillan DJ, Eichstetter I. Decorin is a biological ligand for the epidermal growth factor receptor. J Biol Chem 1999; 274: 4489-92.
    • (1999) J Biol Che , vol.27 , pp. 4489-4492
    • Iozz, R.1    Moscatell, D.2    McQuilla, D.3    Eichstette, I.4
  • 15
    • 66149095761 scopus 로고    scopus 로고
    • Decorin is a novel antagonistic ligand of the Met receptor
    • Goldoni S, Humphries A, Nystrom A, et al. Decorin is a novel antagonistic ligand of the Met receptor. J Cell Biol 2009; 185: 743-54.
    • (2009) J Cell Biol , vol.185 , pp. 743-754
    • Goldoni, S.1    Humphries, A.2    Nystrom, A.3
  • 16
    • 0029098129 scopus 로고
    • Decorin-binding sites for collagen type I are mainly located in leucine-rich repeats 4-5
    • Svensson L, Heinegard D, Oldberg A. Decorin-binding sites for collagen type I are mainly located in leucine-rich repeats 4-5. J Biol Chem 1995; 270: 20712-16.
    • (1995) J Biol Chem , vol.270 , pp. 20712-20716
    • Svensson, L.1    Heinegard, D.2    Oldberg, A.3
  • 17
    • 34447536155 scopus 로고    scopus 로고
    • The decorin sequence SYIRIADTNIT binds collagen type I
    • Kalamajski S, Aspberg A, Oldberg A. The decorin sequence SYIRIADTNIT binds collagen type I. J Biol Chem 2007; 282: 16062-67.
    • (2007) J Biol Chem , vol.282 , pp. 16062-16067
    • Kalamajski, S.1    Aspberg, A.2    Oldberg, A.3
  • 18
    • 0021715115 scopus 로고
    • Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon
    • Vogel KG, Paulsson M, Heinegard D. Specific inhibition of type I and type II collagen fibrillogenesis by the small proteoglycan of tendon. Biochem J 1984; 223: 587-597.
    • (1984) Biochem J , vol.223 , pp. 587-597
    • Vogel, K.G.1    Paulsson, M.2    Heinegard, D.3
  • 20
    • 0030297999 scopus 로고    scopus 로고
    • Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin
    • Font B, Eichenberger D, Rosenberg LM, van der Rest M. Characterization of the interactions of type XII collagen with two small proteoglycans from fetal bovine tendon, decorin and fibromodulin. Matrix Biol 1996; 15: 341-348.
    • (1996) Matrix Biol , vol.15 , pp. 341-348
    • Font, B.1    Eichenberger, D.2    Rosenberg, L.M.3    van der, R.M.4
  • 21
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo RV. Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 1998; 67: 609-52.
    • (1998) Annu Rev Biochem , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 22
    • 33746536017 scopus 로고    scopus 로고
    • Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development
    • Zhang G, Ezura Y, Chervoneva I, et al. Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development. J Cell Biochem 2006; 98: 1436-49.
    • (2006) J Cell Biochem , vol.98 , pp. 1436-1449
    • Zhang, G.1    Ezura, Y.2    Chervoneva, I.3
  • 23
    • 0023603301 scopus 로고
    • Glycosaminoglycan- free small proteoglycan core protein is secreted by fibroblasts from a patient with a syndrome resembling progeroid
    • Kresse H, Rosthoj S, Quentin E, et al. Glycosaminoglycan- free small proteoglycan core protein is secreted by fibroblasts from a patient with a syndrome resembling progeroid. Am J Hum Genet 1987; 41: 436-53.
    • (1987) Am J Hum Genet , vol.41 , pp. 436-453
    • Kresse, H.1    Rosthoj, S.2    Quentin, E.3
  • 24
    • 0033237149 scopus 로고    scopus 로고
    • TGFbeta isoforms and decorin gene expression are modified in fibroblasts obtained from non-syndromic cleft lip and palate subjects
    • Bodo M, Baroni T, Carinci F, et al. TGFbeta isoforms and decorin gene expression are modified in fibroblasts obtained from non-syndromic cleft lip and palate subjects. J Dent Res 1999; 78: 1783-90.
    • (1999) J Dent Res , vol.78 , pp. 1783-1790
    • Bodo, M.1    Baroni, T.2    Carinci, F.3
  • 25
    • 0027185252 scopus 로고
    • Spatial and temporal patterns of gene expression for the proteoglycans biglycan and decorin and for transforming growth factor-beta 1 revealed by in situ hybridization during experimentally induced liver fibrosis in the rat
    • Krull NB, Zimmermann T, Gressner AM. Spatial and temporal patterns of gene expression for the proteoglycans biglycan and decorin and for transforming growth factor-beta 1 revealed by in situ hybridization during experimentally induced liver fibrosis in the rat. Hepatology 1993; 18: 581-89.
    • (1993) Hepatology , vol.18 , pp. 581-589
    • Krull, N.B.1    Zimmermann, T.2    Gressner, A.M.3
  • 26
    • 0028925505 scopus 로고
    • Role of transforming growth factor beta and decorin in controlling fibrosis
    • Harper JR, Spiro RC, Gaarde WA, et al. Role of transforming growth factor beta and decorin in controlling fibrosis. Methods Enzymol 1994; 245: 241-54.
    • (1994) Methods Enzymol , vol.245 , pp. 241-254
    • Harper, J.R.1    Spiro, R.C.2    Gaarde, W.A.3
  • 27
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta
    • Hildebrand A, Romarís M, Rasmussen LM, et al. Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. Biochem J 1994; 302: 527-34.
    • (1994) Biochem J , vol.302 , pp. 527-534
    • Hildebrand, A.1    Romarís, M.2    Rasmussen, L.M.3
  • 28
    • 72449168557 scopus 로고    scopus 로고
    • Decorin deficiency in diabetic mice: Aggravation of nephropathy due to overexpression of profibrotic factors, enhanced apoptosis and mononuclear cell infiltration
    • Merline R, Lazaroski S, Babelova A, et al. Decorin deficiency in diabetic mice: aggravation of nephropathy due to overexpression of profibrotic factors, enhanced apoptosis and mononuclear cell infiltration. J Physiol Pharmacol 2009; 60: 5-13.
    • (2009) J Physiol Pharmacol , vol.60 , pp. 5-13
    • Merline, R.1    Lazaroski, S.2    Babelova, A.3
  • 29
    • 8744221615 scopus 로고    scopus 로고
    • Involvement of membrane-type matrix metalloproteinases (MT-MMPs) in capillary tube formation by human endometrial microvascular endothelial cells: Role of MT3-MMP
    • Plaisier M, Kapiteijn K, Koolwijk P, et al. Involvement of membrane-type matrix metalloproteinases (MT-MMPs) in capillary tube formation by human endometrial microvascular endothelial cells: role of MT3-MMP. J Clin Endocrinol Metab 2004; 89: 5828-36.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 5828-5836
    • Plaisier, M.1    Kapiteijn, K.2    Koolwijk, P.3
  • 30
    • 77955842202 scopus 로고    scopus 로고
    • The molecular basis of corneal transparency
    • Hassell JR, Birk DE. The molecular basis of corneal transparency. Exp Eye Res 2010; 91: 326-35.
    • (2010) Exp Eye Res , vol.91 , pp. 326-335
    • Hassell, J.R.1    Birk, D.E.2
  • 31
    • 0042326281 scopus 로고    scopus 로고
    • Collagens and proteoglycans of the corneal extracellular matrix
    • Michelacci YM. Collagens and proteoglycans of the corneal extracellular matrix. Braz J Med Biol Res 2003; 36: 1037-46.
    • (2003) Braz J Med Biol Res , vol.36 , pp. 1037-1046
    • Michelacci, Y.M.1
  • 33
    • 0029743832 scopus 로고    scopus 로고
    • Induction of alpha-smooth muscle actin expression and myofibroblast transformation in cultured corneal keratocytes
    • Jester JV, Barry-Lane PA, Cavanagh HD, Petroll WM. Induction of alpha-smooth muscle actin expression and myofibroblast transformation in cultured corneal keratocytes. Cornea 1996; 15: 505-16.
    • (1996) Cornea , vol.15 , pp. 505-516
    • Jester, J.V.1    Barry-Lane, P.A.2    Cavanagh, H.D.3    Petroll, W.M.4
  • 34
    • 0014697087 scopus 로고
    • Solubility of collagen fibrils formed in vitro in the presence of sulphated acid mucopolysaccharide-protein
    • Toole BP. Solubility of collagen fibrils formed in vitro in the presence of sulphated acid mucopolysaccharide-protein. Nature 1969; 222: 872-73.
    • (1969) Nature , vol.222 , pp. 872-873
    • Toole, B.P.1
  • 35
    • 52049122865 scopus 로고    scopus 로고
    • Biological functions of the small leucine-rich proteoglycans: From genetics to signal transduction
    • Schaefer L, Iozzo RV. Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction. J Biol Chem 2008; 283: 21305-09.
    • (2008) J Biol Chem , vol.283 , pp. 21305-21309
    • Schaefer, L.1    Iozzo, R.V.2
  • 36
    • 0029778529 scopus 로고    scopus 로고
    • Model structure of decorin and implications for collagen fibrillogenesis
    • Weber IT, Harrison RW, Iozzo RV. Model structure of decorin and implications for collagen fibrillogenesis. J Biol Chem 1996; 271: 31767-70.
    • (1996) J Biol Chem , vol.271 , pp. 31767-31770
    • Weber, I.T.1    Harrison, R.W.2    Iozzo, R.V.3
  • 37
    • 8144221077 scopus 로고    scopus 로고
    • Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
    • Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J. Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. Proc Natl Acad Sci USA 2004; 101: 15633-8.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15633-15638
    • Scott, P.G.1    McEwan, P.A.2    Dodd, C.M.3    Bergmann, E.M.4    Bishop, P.N.5    Bella, J.6
  • 38
    • 33845407527 scopus 로고    scopus 로고
    • The structure and function of cartilage proteoglycans
    • Roughley PJ. The structure and function of cartilage proteoglycans. Eur Cell Mater 2006; 12: 92-101.
    • (2006) Eur Cell Mater , vol.12 , pp. 92-101
    • Roughley, P.J.1
  • 39
    • 0022404219 scopus 로고
    • Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate
    • Chopra RK. Pearson CH, Pringle GA, Fackre DS, Scott PG. Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate. Biochem J 1985; 232: 77.
    • (1985) Biochem J , vol.232 , pp. 77
    • Chopra, R.K.1    Pearson, C.H.2    Pringle, G.A.3    Fackre, D.S.4    Scott, P.G.5
  • 40
    • 0024550294 scopus 로고
    • Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species
    • Fisher LW, Termine JD, Young MF. Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species. J Biol Chem 1989; 264: 4571-76.
    • (1989) J Biol Chem , vol.264 , pp. 4571-4576
    • Fisher, L.W.1    Termine, J.D.2    Young, M.F.3
  • 41
    • 33747781400 scopus 로고    scopus 로고
    • Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans
    • McEwan PA, Scott PG, Bishop PN, Bella J. Structural correlations in the family of small leucine-rich repeat proteins and proteoglycans. J Struct Biol 2006; 155: 294-305.
    • (2006) J Struct Biol , vol.155 , pp. 294-305
    • McEwan, P.A.1    Scott, P.G.2    Bishop, P.N.3    Bella, J.4
  • 42
    • 70349330118 scopus 로고    scopus 로고
    • Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding
    • Orgel JP, Eid A, Antipova O, Bella J, Scott JE. Decorin core protein (decoron) shape complements collagen fibril surface structure and mediates its binding. PLoS One 2009; 4: e7028.
    • (2009) PLoS One , vol.4
    • Orgel, J.P.1    Eid, A.2    Antipova, O.3    Bella, J.4    Scott, J.E.5
  • 43
    • 0029143935 scopus 로고
    • The human lumican gene. Organization, chromosomal location, and expression in articular cartilage
    • Grover J, Chen X-N, Korenberg JR, Roughley PJ. The human lumican gene. Organization, chromosomal location, and expression in articular cartilage. J Biol Chem 1995; 270:21942-49.
    • (1995) J Biol Chem , vol.270 , pp. 21942-21949
    • Grover, J.1    Chen, X.-N.2    Korenberg, J.R.3    Roughley, P.J.4
  • 46
    • 36048958903 scopus 로고    scopus 로고
    • Growth factor binding to the pericellular matrix and its importance in tissue engineering
    • Macri L, Silverstein D, Clark RA. Growth factor binding to the pericellular matrix and its importance in tissue engineering. Adv Drug Deliv Rev 2007; 59: 1366-81.
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 1366-1381
    • Macri, L.1    Silverstein, D.2    Clark, R.A.3
  • 47
    • 0029852530 scopus 로고    scopus 로고
    • Distinct isoforms of chicken decorin contain either one or two dermatan sulfate chains
    • Blaschke UK, Hedbom E, Bruckner P. Distinct isoforms of chicken decorin contain either one or two dermatan sulfate chains. J Biol Chem 1996; 271: 30347-53.
    • (1996) J Biol Chem , vol.271 , pp. 30347-30353
    • Blaschke, U.K.1    Hedbom, E.2    Bruckner, P.3
  • 48
    • 0027159325 scopus 로고
    • Mapping the locations of the epitopes of five monoclonal antibodies to the core protein of dermatan sulfate proteoglycan II (decorin)
    • Scott PG, Dodd CM, Pringle GA. Mapping the locations of the epitopes of five monoclonal antibodies to the core protein of dermatan sulfate proteoglycan II (decorin). J Biol Chem 1993; 268: 11558-64.
    • (1993) J Biol Chem , vol.268 , pp. 11558-11564
    • Scott, P.G.1    Dodd, C.M.2    Pringle, G.A.3
  • 49
    • 0030016013 scopus 로고    scopus 로고
    • Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen
    • Scott JE. Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry 1996; 35: 8795-99.
    • (1996) Biochemistry , vol.35 , pp. 8795-8799
    • Scott, J.E.1
  • 50
    • 0028032085 scopus 로고
    • Structural and functional characterization of the human decorin gene promoter. A homopurine-homopyrimidine S1 nuclease-sensitive region is involved in transcriptional control
    • Santra M, Danielson KG, Iozzo RV. Structural and functional characterization of the human decorin gene promoter. A homopurine-homopyrimidine S1 nuclease-sensitive region is involved in transcriptional control. J Biol Chem 1994; 269: 579-87.
    • (1994) J Biol Chem , vol.269 , pp. 579-587
    • Santra, M.1    Danielson, K.G.2    Iozzo, R.V.3
  • 51
    • 0029056591 scopus 로고
    • Transcriptional regulation of decorin gene expression. Induction by quiescence and repression by tumor necrosis factor-alpha
    • Mauviel A, Santra M, Chen YQ, Uitto J, Iozzo RV. Transcriptional regulation of decorin gene expression. Induction by quiescence and repression by tumor necrosis factor-alpha. J Biol Chem 1995; 270: 11692-700.
    • (1995) J Biol Chem , vol.270 , pp. 11692-11700
    • Mauviel, A.1    Santra, M.2    Chen, Y.Q.3    Uitto, J.4    Iozzo, R.V.5
  • 52
    • 0025138512 scopus 로고
    • Transforming growth factor-beta regulates production of proteoglycans by mesangial cells
    • Border WA, Okuda S, Languino LR, Ruoslahti E. Transforming growth factor-beta regulates production of proteoglycans by mesangial cells. Kidney Int 1990; 37: 689-95.
    • (1990) Kidney Int , vol.37 , pp. 689-695
    • Border, W.A.1    Okuda, S.2    Languino, L.R.3    Ruoslahti, E.4
  • 54
    • 0030799830 scopus 로고    scopus 로고
    • Biosynthesis of the proteoglycan decorin-identification of intermediates in galactosaminoglycan assembly
    • Moses J, Oldberg A, Eklund E, Fransson LA. Biosynthesis of the proteoglycan decorin -- identification of intermediates in galactosaminoglycan assembly. Eur J Biochem 1997; 248:767-74.
    • (1997) Eur J Biochem , vol.248 , pp. 767-774
    • Moses, J.1    Oldberg, A.2    Eklund, E.3    Fransson, L.A.4
  • 55
    • 0028079838 scopus 로고
    • Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues
    • Cheng F, Heinegard D, Malmstrom A, Schmidtchen A, Yoshida K, Fransson LA. Patterns of uronosyl epimerization and 4-/6-O-sulphation in chondroitin/dermatan sulphate from decorin and biglycan of various bovine tissues. Glycobiology 1994; 4: 685-96.
    • (1994) Glycobiology , vol.4 , pp. 685-696
    • Cheng, F.1    Heinegard, D.2    Malmstrom, A.3    Schmidtchen, A.4    Yoshida, K.5    Fransson, L.A.6
  • 56
    • 70449112926 scopus 로고    scopus 로고
    • Dermatan sulfate epimerase 1- deficient mice have reduced content and changed distribution of iduronic acids in dermatan sulfate and an altered collagen structure in skin
    • Maccarana M, Kalamajski S, Kongsgaard M, Magnusson SP, Oldberg A, Malmstrom A. Dermatan sulfate epimerase 1- deficient mice have reduced content and changed distribution of iduronic acids in dermatan sulfate and an altered collagen structure in skin. Mol Cell Biol 2009; 29: 5517-28.
    • (2009) Mol Cell Biol , vol.29 , pp. 5517-5528
    • Maccarana, M.1    Kalamajski, S.2    Kongsgaard, M.3    Magnusson, S.P.4    Oldberg, A.5    Malmstrom, A.6
  • 57
    • 0020544568 scopus 로고
    • Specific association of iduronic acid-rich dermatan sulphate with the extracellular matrix of human skin fibroblasts cultured on collagen gels
    • Gallagher JT, Gasiunas N, Schor SL. Specific association of iduronic acid-rich dermatan sulphate with the extracellular matrix of human skin fibroblasts cultured on collagen gels. Biochem J 1983; 215: 107-16.
    • (1983) Biochem J , vol.215 , pp. 107-116
    • Gallagher, J.T.1    Gasiunas, N.2    Schor, S.L.3
  • 58
    • 77952550108 scopus 로고    scopus 로고
    • The role of small leucine-rich proteoglycans in collagen fibrillogenesis
    • Kalamajski S, Oldberg A. The role of small leucine-rich proteoglycans in collagen fibrillogenesis. Matrix Biol 2010; 29: 248-53.
    • (2010) Matrix Biol , vol.29 , pp. 248-253
    • Kalamajski, S.1    Oldberg, A.2
  • 60
    • 0023764681 scopus 로고
    • Dermatan sulphate proteoglycan from human articular cartilage. Variation in its content with age and its structural comparison with a small chondroitin sulphate proteoglycan from pig laryngeal cartilage
    • Sampaio Lde O, Bayliss MT, Hardingham TE, Muir H. Dermatan sulphate proteoglycan from human articular cartilage. Variation in its content with age and its structural comparison with a small chondroitin sulphate proteoglycan from pig laryngeal cartilage. Biochem J 1988; 254: 757-64.
    • (1988) Biochem J , vol.254 , pp. 757-764
    • Sampaio, L.O.1    Bayliss, M.T.2    Hardingham, T.E.3    Muir, H.4
  • 61
    • 0025042428 scopus 로고
    • Immunoelectron microscopic localization of the core protein of decorin near the d and e bands of tendon collagen fibrils by use of monoclonal antibodies
    • Pringle GA, Dodd CM. Immunoelectron microscopic localization of the core protein of decorin near the d and e bands of tendon collagen fibrils by use of monoclonal antibodies. J Histochem Cytochem 1990; 38: 1405-11.
    • (1990) J Histochem Cytochem , vol.38 , pp. 1405-1411
    • Pringle, G.A.1    Dodd, C.M.2
  • 62
    • 56949083199 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy
    • Brandan E, Cabello-Verrugio C, Vial C. Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy. Matrix Biol 2008; 27: 700-8.
    • (2008) Matrix Biol , vol.27 , pp. 700-708
    • Brandan, E.1    Cabello-Verrugio, C.2    Vial, C.3
  • 63
    • 78049238210 scopus 로고    scopus 로고
    • Regulation of intracellular decorin via proteasome degradation in rat mesangial cells
    • Wu H, Jiang W, Zhang Y, et al. Regulation of intracellular decorin via proteasome degradation in rat mesangial cells. J Cell Biochem 2010; 111: 1010-9.
    • (2010) J Cell Biochem , vol.111 , pp. 1010-1019
    • Wu, H.1    Jiang, W.2    Zhang, Y.3
  • 64
    • 0036278883 scopus 로고    scopus 로고
    • The expression of decorin in human ovarian tumors
    • Nash MA, Deavers MT, Freedman RS. The expression of decorin in human ovarian tumors. Clin Cancer Res 2002; 8: 1754-60.
    • (2002) Clin Cancer Res , vol.8 , pp. 1754-1760
    • Nash, M.A.1    Deavers, M.T.2    Freedman, R.S.3
  • 65
    • 0030958072 scopus 로고    scopus 로고
    • Degradation of decorin by matrix metalloproteinases: Identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release
    • Imai K, Hiramatsu A, Fukushima D, Pierschbacher MD, Okada Y. Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-beta1 release. Biochem J 1997; 322: 809-14.
    • (1997) Biochem J , vol.322 , pp. 809-814
    • Imai, K.1    Hiramatsu, A.2    Fukushima, D.3    Pierschbacher, M.D.4    Okada, Y.5
  • 66
    • 0035798706 scopus 로고    scopus 로고
    • Decorin-mediated signal transduction in endothelial cells. Involvement of Akt/protein kinase B in up-regulation of p21(WAF1/CIP1) but not p27(KIP1)
    • Schonherr E, Levkau B, Schaefer L, Kresse H, Walsh K. Decorin-mediated signal transduction in endothelial cells. Involvement of Akt/protein kinase B in up-regulation of p21(WAF1/CIP1) but not p27(KIP1). J Biol Chem 2001; 276: 40687-92.
    • (2001) J Biol Chem , vol.276 , pp. 40687-40692
    • Schonherr, E.1    Levkau, B.2    Schaefer, L.3    Kresse, H.4    Walsh, K.5
  • 67
    • 0029785662 scopus 로고    scopus 로고
    • Decorin-induced growth suppression is associated with up-regulation of p21, an inhibitor of cyclin-dependent kinases
    • De Luca A, Santra M, Baldi A, Giordano A, Iozzo RV. Decorin-induced growth suppression is associated with up- regulation of p21, an inhibitor of cyclin-dependent kinases. J Biol Chem 1996; 271: 18961-65.
    • (1996) J Biol Chem , vol.271 , pp. 18961-18965
    • de Luca, A.1    Santra, M.2    Baldi, A.3    Giordano, A.4    Iozzo, R.V.5
  • 68
    • 31144462147 scopus 로고    scopus 로고
    • Focus on molecules: Keratocan (KERA)
    • Chakravarti S. Focus on molecules: keratocan (KERA). Exp Eye Res 2006; 82: 183-14.
    • (2006) Exp Eye Res , vol.82 , pp. 183-114
    • Chakravarti, S.1
  • 69
    • 0026657581 scopus 로고
    • Isolation and partial characterization of lumican and decorin from adult chicken corneas. A keratan sulfate-containing isoform of decorin is developmentally regulated
    • Blochberger TC, Cornuet PK, Hassell JR. Isolation and partial characterization of lumican and decorin from adult chicken corneas. A keratan sulfate-containing isoform of decorin is developmentally regulated. J Biol Chem 1992; 267: 20613-19.
    • (1992) J Biol Chem , vol.267 , pp. 20613-20619
    • Blochberger, T.C.1    Cornuet, P.K.2    Hassell, J.R.3
  • 70
    • 0037311082 scopus 로고    scopus 로고
    • Neonatal corneal stromal development in the normal and lumican-deficient mouse
    • Song J, Lee YG, Houston J, et al. Neonatal corneal stromal development in the normal and lumican-deficient mouse. Invest Ophthalmol Vis Sci 2003; 44: 548-57.
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 548-557
    • Song, J.1    Lee, Y.G.2    Houston, J.3
  • 71
    • 21844451940 scopus 로고    scopus 로고
    • Expression of a chondroitin sulfate proteoglycan, versican (PG-M), during development of rat cornea
    • Koga T, Inatani M, Hirata A, et al. Expression of a chondroitin sulfate proteoglycan, versican (PG-M), during development of rat cornea. Curr Eye Res 2005; 30: 455-63.
    • (2005) Curr Eye Res , vol.30 , pp. 455-463
    • Koga, T.1    Inatani, M.2    Hirata, A.3
  • 72
    • 0024599079 scopus 로고
    • Proteoglycans of rabbit corneas with nonperforating wounds
    • Funderburgh JL, Chandler JW. Proteoglycans of rabbit corneas with nonperforating wounds. Invest Ophthalmol Vis Sci 1989; 30: 435-42.
    • (1989) Invest Ophthalmol Vis Sci , vol.30 , pp. 435-442
    • Funderburgh, J.L.1    Chandler, J.W.2
  • 73
    • 67649745754 scopus 로고    scopus 로고
    • Genetic evidence for the coordinated regulation of collagen fibrillogenesis in the cornea by decorin and biglycan
    • Zhang G, Chen S, Goldoni S, et al. Genetic evidence for the coordinated regulation of collagen fibrillogenesis in the cornea by decorin and biglycan. J Biol Chem 2009; 284: 8888-97.
    • (2009) J Biol Chem , vol.284 , pp. 8888-8897
    • Zhang, G.1    Chen, S.2    Goldoni, S.3
  • 74
    • 50849117808 scopus 로고    scopus 로고
    • Differential gene expression patterns of the developing and adult mouse cornea compared to the lens and tendon
    • Wu F, Lee S, Schumacher M, Jun A, Chakravarti S. Differential gene expression patterns of the developing and adult mouse cornea compared to the lens and tendon. Exp Eye Res 2008; 87: 214-25.
    • (2008) Exp Eye Res , vol.87 , pp. 214-225
    • Wu, F.1    Lee, S.2    Schumacher, M.3    Jun, A.4    Chakravarti, S.5
  • 75
    • 67649424445 scopus 로고    scopus 로고
    • MT1-MMP-mediated cleavage of decorin in corneal angiogenesis
    • Mimura T, Han KY, Onguchi T, et al. MT1-MMP-mediated cleavage of decorin in corneal angiogenesis. J Vasc Res 2009; 46: 541-50.
    • (2009) J Vasc Res , vol.46 , pp. 541-550
    • Mimura, T.1    Han, K.Y.2    Onguchi, T.3
  • 76
    • 39149129400 scopus 로고    scopus 로고
    • A novel method for generating corneal haze in anterior stroma of the mouse eye with the excimer laser
    • Mohan RR, Stapleton WM, Sinha S, Netto MV, Wilson SE. A novel method for generating corneal haze in anterior stroma of the mouse eye with the excimer laser. Exp Eye Res 2008; 86: 235-40.
    • (2008) Exp Eye Res , vol.86 , pp. 235-240
    • Mohan, R.R.1    Stapleton, W.M.2    Sinha, S.3    Netto, M.V.4    Wilson, S.E.5
  • 77
    • 68049137063 scopus 로고    scopus 로고
    • Stem cell therapy restores transparency to defective murine corneas
    • Du Y, Carlson EC, Funderburgh ML, et al. Stem cell therapy restores transparency to defective murine corneas. Stem Cells 2009; 27: 1635-42.
    • (2009) Stem Cells , vol.27 , pp. 1635-1642
    • Du, Y.1    Carlson, E.C.2    Funderburgh, M.L.3
  • 78
    • 0003682024 scopus 로고    scopus 로고
    • The Extracellular Matrix Facts Book
    • San Diego: Academic Press
    • Ayad S, Boot-handford RP, Humpries MJ. The Extracellular Matrix Facts Book. San Diego: Academic Press, 1998.
    • (1998)
    • Ayad, S.1    Boot-Handford, R.P.2    Humpries, M.J.3
  • 79
    • 0342465598 scopus 로고
    • Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA
    • Krusius T, Ruoslahti E. Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA. Proc Natl Acad Sci USA 1986; 83: 7683-87.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7683-7687
    • Krusius, T.1    Ruoslahti, E.2
  • 80
    • 0024150891 scopus 로고
    • Structure and biology of proteoglycans
    • Ruoslahti E. Structure and biology of proteoglycans. Annu Rev Cell Biol 1988; 4: 229-55.
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 229-255
    • Ruoslahti, E.1
  • 81
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J Cell Biol 1997; 136: 729-43.
    • (1997) J Cell Biol , vol.136 , pp. 729-743
    • Danielson, K.G.1    Baribault, H.2    Holmes, D.F.3    Graham, H.4    Kadler, K.E.5    Iozzo, R.V.6
  • 82
    • 20444423668 scopus 로고    scopus 로고
    • A physiologic three-dimensional cell culture system to investigate the role of decorin in matrix organisation and cell survival
    • Seidler DG, Schaefer L, Robenek H, Iozzo RV, Kresse H, Schonherr E. A physiologic three-dimensional cell culture system to investigate the role of decorin in matrix organisation and cell survival. Biochem Biophys Res Commun 2005; 332: 1162-70.
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 1162-1170
    • Seidler, D.G.1    Schaefer, L.2    Robenek, H.3    Iozzo, R.V.4    Kresse, H.5    Schonherr, E.6
  • 83
    • 0026473155 scopus 로고
    • Interactions between thrombospondin and the small proteoglycan decorin: Interference with cell attachment
    • Winnemoller M, Schon P, Vischer P, Kresse H. Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment. Eur J Cell Biol 1992; 59: 47-55.
    • (1992) Eur J Cell Biol , vol.59 , pp. 47-55
    • Winnemoller, M.1    Schon, P.2    Vischer, P.3    Kresse, H.4
  • 85
    • 33750977810 scopus 로고    scopus 로고
    • SLRP interaction can protect collagen fibrils from cleavage by collagenases
    • Geng Y, McQuillan D, Roughley PJ. SLRP interaction can protect collagen fibrils from cleavage by collagenases. Matrix Biol 2006; 25: 484-491.
    • (2006) Matrix Biol , vol.25 , pp. 484-491
    • Geng, Y.1    McQuillan, D.2    Roughley, P.J.3
  • 86
    • 34547796856 scopus 로고    scopus 로고
    • The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis
    • Ruhland C, Schonherr E, Robenek H, et al. The glycosaminoglycan chain of decorin plays an important role in collagen fibril formation at the early stages of fibrillogenesis. FEBS J 2007; 274: 4246-55.
    • (2007) FEBS J , vol.274 , pp. 4246-4255
    • Ruhland, C.1    Schonherr, E.2    Robenek, H.3
  • 87
    • 0032101311 scopus 로고    scopus 로고
    • Lumican regulates collagen fibril assembly: Skin fragility and corneal opacity in the absence of lumican
    • Chakravarti S, Magnuson T, Lass JH, Jepsen KJ, LaMantia C, Carroll H. Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican. J Cell Biol 1998; 141: 1277-86.
    • (1998) J Cell Biol , vol.141 , pp. 1277-1286
    • Chakravarti, S.1    Magnuson, T.2    Lass, J.H.3    Jepsen, K.J.4    Lamantia, C.5    Carroll, H.6
  • 88
    • 0035941233 scopus 로고    scopus 로고
    • Proteoglycan expression during transforming growth factor beta-induced keratocyte-myofibroblast transdifferentiation
    • Funderburgh JL, Funderburgh ML, Mann MM, Corpuz L, Roth MR. Proteoglycan expression during transforming growth factor beta-induced keratocyte-myofibroblast transdifferentiation. J Biol Chem 2001; 276: 44173-8.
    • (2001) J Biol Chem , vol.276 , pp. 44173-44178
    • Funderburgh, J.L.1    Funderburgh, M.L.2    Mann, M.M.3    Corpuz, L.4    Roth, M.R.5
  • 90
    • 1842530296 scopus 로고    scopus 로고
    • Causes and prevalence of visual impairment among adults in the United States
    • Congdon N, O'Colmain B, Klaver CC, et al. Causes and prevalence of visual impairment among adults in the United States. Arch Ophthalmol 2004; 122: 477-85.
    • (2004) Arch Ophthalmol , vol.122 , pp. 477-485
    • Congdon, N.1    O'Colmain, B.2    Klaver, C.C.3
  • 91
    • 29244485881 scopus 로고    scopus 로고
    • The Impact of Vision 2020 on Global Blindness
    • Foster A, Resnikoff S. The Impact of Vision 2020 on Global Blindness. Eye 2005; 19: 1133-5.
    • (2005) Eye , vol.19 , pp. 1133-1135
    • Foster, A.1    Resnikoff, S.2
  • 92
    • 34748905918 scopus 로고    scopus 로고
    • Refractive surgery: The future of perfect vision?
    • Fong CS. Refractive surgery: the future of perfect vision? Singapore Med J 2007; 48: 709-18.
    • (2007) Singapore Med J , vol.48 , pp. 709-718
    • Fong, C.S.1
  • 93
    • 33646128024 scopus 로고    scopus 로고
    • Laser eye surgery for refractive errors
    • Sakimoto T, Rosenblatt MI, Azar DT. Laser eye surgery for refractive errors. Lancet 2006; 367: 1432-47.
    • (2006) Lancet , vol.367 , pp. 1432-1447
    • Sakimoto, T.1    Rosenblatt, M.I.2    Azar, D.T.3
  • 94
    • 0029160918 scopus 로고
    • Excimer laser photorefractive keratectomy
    • Seiler T, McDonnell PJ. Excimer laser photorefractive keratectomy. Surv Ophthalmol 1995; 40: 89-118.
    • (1995) Surv Ophthalmol , vol.40 , pp. 89-118
    • Seiler, T.1    McDonnell, P.J.2
  • 95
    • 0033064004 scopus 로고    scopus 로고
    • Corneal stromal wound healing in refractive surgery: The role of myofibroblasts
    • Jester JV, Petroll WM, Cavanagh HD. Corneal stromal wound healing in refractive surgery: the role of myofibroblasts. Prog Retin Eye Res 1999, 18: 311-56.
    • (1999) Prog Retin Eye Res , vol.18 , pp. 311-356
    • Jester, J.V.1    Petroll, W.M.2    Cavanagh, H.D.3
  • 98
    • 0033732919 scopus 로고    scopus 로고
    • Influence of decorin expression on transforming growth factor-beta- mediated collagen gel retraction and biglycan induction
    • Markmann A, Hausser H, Schonherr E, Kresse H. Influence of decorin expression on transforming growth factor-beta- mediated collagen gel retraction and biglycan induction. Matrix Biol 2000; 19: 631-6.
    • (2000) Matrix Biol , vol.19 , pp. 631-636
    • Markmann, A.1    Hausser, H.2    Schonherr, E.3    Kresse, H.4
  • 99
    • 33748850603 scopus 로고    scopus 로고
    • A second decorin frame shift mutation in a family with congenital stromal corneal dystrophy
    • Rodahl E, Van Ginderdeuren R, Knappskog PM, Bredrup C, Boman H. A second decorin frame shift mutation in a family with congenital stromal corneal dystrophy. Am J Ophthalmol 2006; 142: 520-1.
    • (2006) Am J Ophthalmol , vol.142 , pp. 520-521
    • Rodahl, E.1    van Ginderdeuren, R.2    Knappskog, P.M.3    Bredrup, C.4    Boman, H.5
  • 100
    • 79952782111 scopus 로고    scopus 로고
    • Decorin accumulation contributes to the stromal opacities found in congenital stromal corneal dystrophy
    • Bredrup C, Stang E, Bruland O, et al. Decorin accumulation contributes to the stromal opacities found in congenital stromal corneal dystrophy. Invest Ophthalmol Vis Sci 2010; 51: 5578-82.
    • (2010) Invest Ophthalmol Vis Sci , vol.51 , pp. 5578-5582
    • Bredrup, C.1    Stang, E.2    Bruland, O.3
  • 101
    • 33646370762 scopus 로고    scopus 로고
    • Beta ig-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation, and participates in ternary complexing with these macromolecules
    • Reinboth B, Thomas J, Hanssen E, Gibson MA. Beta ig-h3 interacts directly with biglycan and decorin, promotes collagen VI aggregation, and participates in ternary complexing with these macromolecules. J Biol Chem 2006; 281: 7816-24.
    • (2006) J Biol Chem , vol.281 , pp. 7816-7824
    • Reinboth, B.1    Thomas, J.2    Hanssen, E.3    Gibson, M.A.4
  • 102
    • 0035955705 scopus 로고    scopus 로고
    • Altered fine structures of corneal and skeletal keratan sulfate and chondroitin/dermatan sulfate in macular corneal dystrophy
    • Plaas AH, West LA, Thonar EJ, et al. Altered fine structures of corneal and skeletal keratan sulfate and chondroitin/dermatan sulfate in macular corneal dystrophy. J Biol Chem 2001; 276: 39788-96.
    • (2001) J Biol Chem , vol.276 , pp. 39788-39796
    • Plaas, A.H.1    West, L.A.2    Thonar, E.J.3
  • 104
    • 33751349523 scopus 로고    scopus 로고
    • Structural change in decorin with skin aging
    • Nomura Y. Structural change in decorin with skin aging. Connect Tissue Res 2006; 47: 249-55.
    • (2006) Connect Tissue Res , vol.47 , pp. 249-255
    • Nomura, Y.1
  • 105
    • 0028220220 scopus 로고
    • Changes in the expression of decorin and biglycan in human articular cartilage with age and regulation by TGF-beta
    • Roughley PJ, Melching LI, Recklies AD. Changes in the expression of decorin and biglycan in human articular cartilage with age and regulation by TGF-beta. Matrix Biol 1994; 14: 51-9.
    • (1994) Matrix Biol , vol.14 , pp. 51-59
    • Roughley, P.J.1    Melching, L.I.2    Recklies, A.D.3
  • 106
    • 0031420122 scopus 로고    scopus 로고
    • Transforming growth factor-beta 1 overexpression produces drug resistance in vivo: Reversal by decorin
    • Teicher BA, Ikebe M, Ara G, Keyes SR, Herbst RS. Transforming growth factor-beta 1 overexpression produces drug resistance in vivo: reversal by decorin. In vivo 1997; 11: 463-472.
    • (1997) In Vivo , vol.11 , pp. 463-472
    • Teicher, B.A.1    Ikebe, M.2    Ara, G.3    Keyes, S.R.4    Herbst, R.S.5
  • 108
    • 0029088680 scopus 로고
    • De novo decorin gene expression suppresses the malignant phenotype in human colon cancer cells
    • Santra M, Skorski T, Calabretta B, Lattime EC, Iozzo RV. De novo decorin gene expression suppresses the malignant phenotype in human colon cancer cells. Proc Natl Acad Sci USA 1995; 92: 7016-20.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7016-7020
    • Santra, M.1    Skorski, T.2    Calabretta, B.3    Lattime, E.C.4    Iozzo, R.V.5
  • 109
    • 0037161919 scopus 로고    scopus 로고
    • Suppression of tumorigenicity by adenovirus-mediated gene transfer of decorin
    • Reed CC, Gauldie J, Iozzo RV. Suppression of tumorigenicity by adenovirus-mediated gene transfer of decorin. Oncogene 2002; 21: 3688-95.
    • (2002) Oncogene , vol.21 , pp. 3688-3695
    • Reed, C.C.1    Gauldie, J.2    Iozzo, R.V.3
  • 110
    • 0026676859 scopus 로고
    • Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease
    • Border WA, Noble NA, Yamamoto T, et al. Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Nature 1992; 360: 361-64.
    • (1992) Nature , vol.360 , pp. 361-364
    • Border, W.A.1    Noble, N.A.2    Yamamoto, T.3
  • 111
    • 0029905441 scopus 로고    scopus 로고
    • Gene therapy by skeletal muscle expression of decorin prevents fibrotic disease in rat kidney
    • Isaka Y, Brees DK, Ikegaya K, et al. Gene therapy by skeletal muscle expression of decorin prevents fibrotic disease in rat kidney. Nat Med 1996; 2: 418-423.
    • (1996) Nat Med , vol.2 , pp. 418-423
    • Isaka, Y.1    Brees, D.K.2    Ikegaya, K.3
  • 112
    • 0034979153 scopus 로고    scopus 로고
    • Proteoglycans decorin and biglycan differentially modulate TGF-beta- mediated fibrotic responses in the lun
    • Kolb M, Margetts PJ, Sime PJ, Gauldie J. Proteoglycans decorin and biglycan differentially modulate TGF-beta- mediated fibrotic responses in the lung. Am J Physiol Lung Cell Mol Physiol 2001; 280: L1327-34.
    • (2001) Am J Physiol Lung Cell Mol Physio , vol.280
    • Kolb, M.1    Margetts, P.J.2    Sime, P.J.3    Gauldie, J.4
  • 113
    • 0033844151 scopus 로고    scopus 로고
    • The decorin high glucose response element and mechanism of its activation in human mesangial cells
    • Wahab NA, Parker S, Sraer JD, Mason RM. The decorin high glucose response element and mechanism of its activation in human mesangial cells. J Am Soc Nephrol 2000; 11: 1607-19.
    • (2000) J Am Soc Nephrol , vol.11 , pp. 1607-1619
    • Wahab, N.A.1    Parker, S.2    Sraer, J.D.3    Mason, R.M.4
  • 114
    • 36348995969 scopus 로고    scopus 로고
    • Decorin deficiency enhances progressive nephropathy in diabetic mice
    • Williams KJ, Qiu G, Usui HK, et al. Decorin deficiency enhances progressive nephropathy in diabetic mice. Am J Pathol 2007; 171: 1441-50.
    • (2007) Am J Pathol , vol.171 , pp. 1441-1450
    • Williams, K.J.1    Qiu, G.2    Usui, H.K.3
  • 115
    • 0035292906 scopus 로고    scopus 로고
    • Small proteoglycans in human diabetic nephropathy: Discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin
    • Schaefer L, Raslik I, Grone HJ, et al. Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin. FASEB J 2001; 15: 559-61.
    • (2001) FASEB J , vol.15 , pp. 559-561
    • Schaefer, L.1    Raslik, I.2    Grone, H.J.3
  • 116
    • 0031834175 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor p27 Kip1 safeguards against inflammatory injury
    • Ophascharoensuk V, Fero ML, Hughes J, Roberts JM, Shankland SJ. The cyclin-dependent kinase inhibitor p27 Kip1 safeguards against inflammatory injury. Nat Med 1998; 4: 575-80.
    • (1998) Nat Med , vol.4 , pp. 575-580
    • Ophascharoensuk, V.1    Fero, M.L.2    Hughes, J.3    Roberts, J.M.4    Shankland, S.J.5
  • 117
    • 48249087988 scopus 로고    scopus 로고
    • Fragmentation of decorin, biglycan, lumican and keratocan is elevated in degenerate human meniscus, knee and hip articular cartilages compared with age-matched macroscopically normal and control tissues
    • Melrose J, Fuller ES, Roughley PJ, et al. Fragmentation of decorin, biglycan, lumican and keratocan is elevated in degenerate human meniscus, knee and hip articular cartilages compared with age-matched macroscopically normal and control tissues. Arthritis Res Ther 2008; 10: R79.
    • (2008) Arthritis Res Ther , vol.10
    • Melrose, J.1    Fuller, E.S.2    Roughley, P.J.3
  • 118
    • 0034945607 scopus 로고    scopus 로고
    • The use of an antifibrosis agent to improve muscle recovery after laceration
    • Fukushima K, Badlani N, Usas A, Riano F, Fu F, Huard J. The use of an antifibrosis agent to improve muscle recovery after laceration. Am J Sports Med 2001; 29: 394-402.
    • (2001) Am J Sports Med , vol.29 , pp. 394-402
    • Fukushima, K.1    Badlani, N.2    Usas, A.3    Riano, F.4    Fu, F.5    Huard, J.6
  • 119
    • 79952798628 scopus 로고
    • Adjuvant Decorin Therapy For Wound Healing Suppression After Filtrating Glaucoma Surgery
    • Invest Ophthalmol Vis Sci 2003; 44: E-Abstract
    • Szurman P, Grisanti S, Ziemssen F, et al. Adjuvant decorin therapy for wound healing suppression after filtrating glaucoma surgery. Invest Ophthalmol Vis Sci 2003; 44: E-Abstract 1202.
    • (1202)
    • Szurman, P.1    Grisanti, S.2    Ziemssen, F.3
  • 120
    • 11144346920 scopus 로고    scopus 로고
    • Decorin modulates wound healing in experimental glaucoma filtration surgery: A pilot study
    • Grisanti S, Szurman P, Warga M, et al. Decorin modulates wound healing in experimental glaucoma filtration surgery: a pilot study. Invest Ophthalmol Vis Sci 2005; 46: 191-6.
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 191-196
    • Grisanti, S.1    Szurman, P.2    Warga, M.3
  • 121
    • 73949158120 scopus 로고    scopus 로고
    • Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1)
    • von Marschall Z, Fisher LW. Decorin is processed by three isoforms of bone morphogenetic protein-1 (BMP1). Biochem Biophys Res Commun 2010; 391: 1374-8.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1374-1378
    • von, M.Z.1    Fisher, L.W.2
  • 122
    • 2342627322 scopus 로고    scopus 로고
    • Extracellular matrix glycoprotein biglycan enhances vascular smooth muscle cell proliferation and migration
    • Shimizu-Hirota R, Sasamura H, Kuroda M, Kobayashi E, Hayashi M, Saruta T. Extracellular matrix glycoprotein biglycan enhances vascular smooth muscle cell proliferation and migration. Circ Res 2004; 94: 1067-74.
    • (2004) Circ Res , vol.94 , pp. 1067-1074
    • Shimizu-Hirota, R.1    Sasamura, H.2    Kuroda, M.3    Kobayashi, E.4    Hayashi, M.5    Saruta, T.6
  • 123
    • 8444229365 scopus 로고    scopus 로고
    • Effects of ectopic decorin in modulating intracranial glioma progression in vivo, in a rat syngeneic model
    • Biglari A, Bataille D, Naumann U, et al. Effects of ectopic decorin in modulating intracranial glioma progression in vivo, in a rat syngeneic model. Cancer Gene Ther 2004; 11: 721-32.
    • (2004) Cancer Gene Ther , vol.11 , pp. 721-732
    • Biglari, A.1    Bataille, D.2    Naumann, U.3
  • 124
    • 0032212812 scopus 로고    scopus 로고
    • Retroviral vector- mediated gene transfer into keratocytes in vitro and in vivo
    • Seitz B, Moreira L, Baktanian E, et al. Retroviral vector- mediated gene transfer into keratocytes in vitro and in vivo. Am J Ophthalmol 1998; 126: 630-9.
    • (1998) Am J Ophthalmol , vol.126 , pp. 630-639
    • Seitz, B.1    Moreira, L.2    Baktanian, E.3


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