메뉴 건너뛰기




Volumn 15, Issue 8, 2011, Pages 1788-1796

Fibrotic response in fibroblasts from congenital disorders of glycosylation

Author keywords

CDG; Collagen; Fibroblast; IGFBP5; Transcriptome

Indexed keywords

BIGLYCAN; CARTILAGE MATRIX PROTEIN; COLLAGEN TYPE 1; GLYCOPROTEIN; RECOMBINANT PROTEIN; SCLEROPROTEIN; SOMATOMEDIN BINDING PROTEIN 5; TRANSFORMING GROWTH FACTOR BETA;

EID: 79960338992     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2010.01187.x     Document Type: Article
Times cited : (12)

References (58)
  • 1
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda P, Aebi M. The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta. 1999; 1426: 239-57.
    • (1999) Biochim Biophys Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 2
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology. 2002; 12: 43R-56R.
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 3
    • 0025321793 scopus 로고
    • Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect
    • Kretz KA, Carson GS, Morimoto S, et al. Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect. Proc Natl Acad Sci USA. 1990; 87: 2541-4.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2541-2544
    • Kretz, K.A.1    Carson, G.S.2    Morimoto, S.3
  • 4
    • 0033564273 scopus 로고    scopus 로고
    • Familial overexpression of beta antithrombin caused by an Asn135Thr substitution
    • Bayston TA, Tripodi A, Mannucci PM, et al. Familial overexpression of beta antithrombin caused by an Asn135Thr substitution. Blood. 1999; 93: 4242-7.
    • (1999) Blood , vol.93 , pp. 4242-4247
    • Bayston, T.A.1    Tripodi, A.2    Mannucci, P.M.3
  • 5
    • 0025151012 scopus 로고
    • Heerlen polymorphism of protein S, an immunologic polymorphism due to dimorphism of residue 460
    • Bertina RM, Ploos van Amstel HK, van Wijngaarden A, et al. Heerlen polymorphism of protein S, an immunologic polymorphism due to dimorphism of residue 460. Blood. 1990; 76: 538-48.
    • (1990) Blood , vol.76 , pp. 538-548
    • Bertina, R.M.1    Ploos van Amstel, H.K.2    van Wijngaarden, A.3
  • 6
    • 0031474374 scopus 로고    scopus 로고
    • A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI Zbristol) associated with novel electrophoretic properties
    • Lovegrove JU, Jeremiah S, Gillett GT, et al. A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI Zbristol) associated with novel electrophoretic properties. Ann Hum Genet. 1997; 61: 385-91.
    • (1997) Ann Hum Genet , vol.61 , pp. 385-391
    • Lovegrove, J.U.1    Jeremiah, S.2    Gillett, G.T.3
  • 7
    • 22844449795 scopus 로고    scopus 로고
    • Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations
    • Vogt G, Chapgier A, Yang K, et al. Gains of glycosylation comprise an unexpectedly large group of pathogenic mutations. Nat Genet. 2005; 37: 692-700.
    • (2005) Nat Genet , vol.37 , pp. 692-700
    • Vogt, G.1    Chapgier, A.2    Yang, K.3
  • 8
    • 0035279221 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: genetic model systems lead the way
    • Aebi M, Hennet T. Congenital disorders of glycosylation: genetic model systems lead the way. Trends Cell Biol. 2001; 11: 136-41.
    • (2001) Trends Cell Biol , vol.11 , pp. 136-141
    • Aebi, M.1    Hennet, T.2
  • 9
    • 35548972537 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: a rapidly expanding disease family
    • Jaeken J, Matthijs G. Congenital disorders of glycosylation: a rapidly expanding disease family. Annu Rev Genomics Hum Genet. 2007; 8: 261-78.
    • (2007) Annu Rev Genomics Hum Genet , vol.8 , pp. 261-278
    • Jaeken, J.1    Matthijs, G.2
  • 10
    • 33745381312 scopus 로고    scopus 로고
    • Genetic defects in the human glycome
    • Freeze HH. Genetic defects in the human glycome. Nat Rev Genet. 2006; 7: 537-51.
    • (2006) Nat Rev Genet , vol.7 , pp. 537-551
    • Freeze, H.H.1
  • 11
    • 33646135550 scopus 로고    scopus 로고
    • The congenital disorders of glycosylation: a multifaceted group of syndromes
    • Eklund EA, Freeze HH. The congenital disorders of glycosylation: a multifaceted group of syndromes. NeuroRx. 2006; 3: 254-63.
    • (2006) NeuroRx , vol.3 , pp. 254-263
    • Eklund, E.A.1    Freeze, H.H.2
  • 12
    • 37549056201 scopus 로고    scopus 로고
    • Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2
    • Kornak U, Reynders E, Dimopoulou A, et al. Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2. Nat Genet. 2008; 40: 32-4.
    • (2008) Nat Genet , vol.40 , pp. 32-34
    • Kornak, U.1    Reynders, E.2    Dimopoulou, A.3
  • 13
    • 0035213149 scopus 로고    scopus 로고
    • MPDU1mutations underlie a novel human congenital disorder of glycosylation (CDG), designated type If
    • Schenk B, Imbach T, Frank CG, et al. MPDU1mutations underlie a novel human congenital disorder of glycosylation (CDG), designated type If. J Clin Invest. 2001; 108: 1687-95.
    • (2001) J Clin Invest , vol.108 , pp. 1687-1695
    • Schenk, B.1    Imbach, T.2    Frank, C.G.3
  • 14
    • 0033636903 scopus 로고    scopus 로고
    • Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation
    • Westphal V, Murch S, Kim S, et al. Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation. Am J Pathol. 2000; 157: 1917-25.
    • (2000) Am J Pathol , vol.157 , pp. 1917-1925
    • Westphal, V.1    Murch, S.2    Kim, S.3
  • 15
    • 33947724303 scopus 로고    scopus 로고
    • Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation
    • Lau KS, Partridge EA, Grigorian A, et al. Complex N-glycan number and degree of branching cooperate to regulate cell proliferation and differentiation. Cell. 2007; 129: 123-34.
    • (2007) Cell , vol.129 , pp. 123-134
    • Lau, K.S.1    Partridge, E.A.2    Grigorian, A.3
  • 16
    • 29244449332 scopus 로고    scopus 로고
    • Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes
    • Ohtsubo K, Takamatsu S, Minowa MT, et al. Dietary and genetic control of glucose transporter 2 glycosylation promotes insulin secretion in suppressing diabetes. Cell. 2005; 123: 1307-21.
    • (2005) Cell , vol.123 , pp. 1307-1321
    • Ohtsubo, K.1    Takamatsu, S.2    Minowa, M.T.3
  • 17
    • 6044239186 scopus 로고    scopus 로고
    • Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis
    • Partridge EA, Le Roy C, Di Guglielmo GM, et al. Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science. 2004; 306: 120-4.
    • (2004) Science , vol.306 , pp. 120-124
    • Partridge, E.A.1    Le Roy, C.2    Di Guglielmo, G.M.3
  • 18
    • 27644439090 scopus 로고    scopus 로고
    • Dysregulation of TGF-beta1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice
    • Wang X, Inoue S, Gu J, et al. Dysregulation of TGF-beta1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice. Proc Natl Acad Sci USA. 2005; 102: 15791-6.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15791-15796
    • Wang, X.1    Inoue, S.2    Gu, J.3
  • 19
    • 0035887188 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation type I leads to altered processing of N-linked glycans, as well as underglycosylation
    • Mills P, Mills K, Clayton P, et al. Congenital disorders of glycosylation type I leads to altered processing of N-linked glycans, as well as underglycosylation. Biochem J. 2001; 359: 249-54.
    • (2001) Biochem J , vol.359 , pp. 249-254
    • Mills, P.1    Mills, K.2    Clayton, P.3
  • 20
    • 0038732507 scopus 로고    scopus 로고
    • Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I
    • Callewaert N, Schollen E, Vanhecke A, et al. Increased fucosylation and reduced branching of serum glycoprotein N-glycans in all known subtypes of congenital disorder of glycosylation I. Glycobiology. 2003; 13: 367-75.
    • (2003) Glycobiology , vol.13 , pp. 367-375
    • Callewaert, N.1    Schollen, E.2    Vanhecke, A.3
  • 21
    • 2142646426 scopus 로고    scopus 로고
    • TGF-beta signaling and the fibrotic response
    • Leask A, Abraham DJ. TGF-beta signaling and the fibrotic response. FASEB J. 2004; 18: 816-27.
    • (2004) FASEB J , vol.18 , pp. 816-827
    • Leask, A.1    Abraham, D.J.2
  • 22
    • 0042855012 scopus 로고    scopus 로고
    • The CCN family: a new stimulus package
    • Brigstock DR. The CCN family: a new stimulus package. J Endocrinol. 2003; 178: 169-75.
    • (2003) J Endocrinol , vol.178 , pp. 169-175
    • Brigstock, D.R.1
  • 23
    • 0035234139 scopus 로고    scopus 로고
    • SPARC, a matricellular protein: at the crossroads of cell-matrix communication
    • Brekken RA, Sage EH. SPARC, a matricellular protein: at the crossroads of cell-matrix communication. Matrix Biol. 2001; 19: 816-27.
    • (2001) Matrix Biol , vol.19 , pp. 816-827
    • Brekken, R.A.1    Sage, E.H.2
  • 24
    • 0033968250 scopus 로고    scopus 로고
    • Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie
    • Imbach T, Schenk B, Schollen E, et al. Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie. J Clin Invest. 2000; 105: 233-9.
    • (2000) J Clin Invest , vol.105 , pp. 233-239
    • Imbach, T.1    Schenk, B.2    Schollen, E.3
  • 25
    • 0033977322 scopus 로고    scopus 로고
    • Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)
    • Kim S, Westphal V, Srikrishna G, et al. Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie). J Clin Invest. 2000; 105: 191-8.
    • (2000) J Clin Invest , vol.105 , pp. 191-198
    • Kim, S.1    Westphal, V.2    Srikrishna, G.3
  • 26
    • 0037106328 scopus 로고    scopus 로고
    • ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg
    • Grubenmann CE, Frank CG, Kjaergaard S, et al. ALG12 mannosyltransferase defect in congenital disorder of glycosylation type lg. Hum Mol Genet. 2002; 11: 2331-9.
    • (2002) Hum Mol Genet , vol.11 , pp. 2331-2339
    • Grubenmann, C.E.1    Frank, C.G.2    Kjaergaard, S.3
  • 27
    • 0036799549 scopus 로고    scopus 로고
    • Deficiency of dolichyl-P-Man: Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig
    • Thiel C, Schwarz M, Hasilik M, et al. Deficiency of dolichyl-P-Man: Man7GlcNAc2-PP-dolichyl mannosyltransferase causes congenital disorder of glycosylation type Ig. Biochem J. 2002; 367: 195-201.
    • (2002) Biochem J , vol.367 , pp. 195-201
    • Thiel, C.1    Schwarz, M.2    Hasilik, M.3
  • 28
    • 18544384105 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose: Man7GlcNAc2-PP-dolichyl mannosyltransferase
    • Chantret I, Dupre T, Delenda C, et al. Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose: Man7GlcNAc2-PP-dolichyl mannosyltransferase. J Biol Chem. 2002; 277: 25815-22.
    • (2002) J Biol Chem , vol.277 , pp. 25815-25822
    • Chantret, I.1    Dupre, T.2    Delenda, C.3
  • 29
    • 0033536073 scopus 로고    scopus 로고
    • A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic
    • Imbach T, Burda P, Kuhnert P, et al. A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic. Proc Natl Acad Sci USA. 1999; 96: 6982-7.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6982-6987
    • Imbach, T.1    Burda, P.2    Kuhnert, P.3
  • 30
    • 13244265807 scopus 로고    scopus 로고
    • Genome-wide analysis of the unfolded protein response in fibroblasts from congenital disorders of glycosylation type-I patients
    • Lecca MR, Wagner U, Patrignani A, et al. Genome-wide analysis of the unfolded protein response in fibroblasts from congenital disorders of glycosylation type-I patients. FASEB J. 2005; 19: 240-2.
    • (2005) FASEB J , vol.19 , pp. 240-242
    • Lecca, M.R.1    Wagner, U.2    Patrignani, A.3
  • 31
    • 0036947892 scopus 로고    scopus 로고
    • Robust estimators for expression analysis
    • Hubbell E, Liu WM, Mei R. Robust estimators for expression analysis. Bioinformatics. 2002; 18: 1585-92.
    • (2002) Bioinformatics , vol.18 , pp. 1585-1592
    • Hubbell, E.1    Liu, W.M.2    Mei, R.3
  • 32
    • 12244313858 scopus 로고    scopus 로고
    • Analysis of high density expression microarrays with signed-rank call algorithms
    • Liu WM, Mei R, Di X, et al. Analysis of high density expression microarrays with signed-rank call algorithms. Bioinformatics. 2002; 18: 1593-9.
    • (2002) Bioinformatics , vol.18 , pp. 1593-1599
    • Liu, W.M.1    Mei, R.2    Di, X.3
  • 33
    • 0035829361 scopus 로고    scopus 로고
    • Controlling the false discovery rate in behavior genetics research
    • Benjamini Y, Drai D, Elmer G, et al. Controlling the false discovery rate in behavior genetics research. Behav Brain Res. 2001; 125: 279-84.
    • (2001) Behav Brain Res , vol.125 , pp. 279-284
    • Benjamini, Y.1    Drai, D.2    Elmer, G.3
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA. 1979; 76: 4350-4.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0028821581 scopus 로고
    • Molecular cloning and expression of carcinoembryonic antigen gene family members
    • Thompson JA. Molecular cloning and expression of carcinoembryonic antigen gene family members. Tumour Biol. 1995; 16: 10-6.
    • (1995) Tumour Biol , vol.16 , pp. 10-16
    • Thompson, J.A.1
  • 36
    • 0343485045 scopus 로고    scopus 로고
    • Expression profile viewer (ExProView): a software tool for transcriptome analysis
    • Larsson M, Stahl S, Uhlen M, et al. Expression profile viewer (ExProView): a software tool for transcriptome analysis. Genomics. 2000; 63: 341-53.
    • (2000) Genomics , vol.63 , pp. 341-353
    • Larsson, M.1    Stahl, S.2    Uhlen, M.3
  • 37
    • 0037047426 scopus 로고    scopus 로고
    • Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II
    • Guerrero-Esteo M, Sanchez-Elsner T, Letamendia A, et al. Extracellular and cytoplasmic domains of endoglin interact with the transforming growth factor-beta receptors I and II. J Biol Chem. 2002; 277: 29197-209.
    • (2002) J Biol Chem , vol.277 , pp. 29197-29209
    • Guerrero-Esteo, M.1    Sanchez-Elsner, T.2    Letamendia, A.3
  • 38
    • 34447309766 scopus 로고    scopus 로고
    • The myofibroblast: one function, multiple origins
    • Hinz B, Phan SH, Thannickal VJ, et al. The myofibroblast: one function, multiple origins. Am J Pathol. 2007; 170: 1807-16.
    • (2007) Am J Pathol , vol.170 , pp. 1807-1816
    • Hinz, B.1    Phan, S.H.2    Thannickal, V.J.3
  • 39
    • 13244254138 scopus 로고    scopus 로고
    • Insulin-like growth factor binding proteins 3 and 5 are overexpressed in idiopathic pulmonary fibrosis and contribute to extracellular matrix deposition
    • Pilewski JM, Liu L, Henry AC, et al. Insulin-like growth factor binding proteins 3 and 5 are overexpressed in idiopathic pulmonary fibrosis and contribute to extracellular matrix deposition. Am J Pathol. 2005; 166: 399-407.
    • (2005) Am J Pathol , vol.166 , pp. 399-407
    • Pilewski, J.M.1    Liu, L.2    Henry, A.C.3
  • 40
    • 0031814087 scopus 로고    scopus 로고
    • Intestinal, pancreatic and hepatic involvement in carbohydrate-deficient glycoprotein syndrome type I
    • Kristiansson B, Borulf S, Conradi N, et al. Intestinal, pancreatic and hepatic involvement in carbohydrate-deficient glycoprotein syndrome type I. J Pediatr Gastroenterol Nutr. 1998; 27: 23-9.
    • (1998) J Pediatr Gastroenterol Nutr , vol.27 , pp. 23-29
    • Kristiansson, B.1    Borulf, S.2    Conradi, N.3
  • 41
    • 34447130291 scopus 로고    scopus 로고
    • The liver in congenital disorders of glycosylation: ultrastructural features
    • Iancu TC, Mahajnah M, Manov I, et al. The liver in congenital disorders of glycosylation: ultrastructural features. Ultrastruct Pathol. 2007; 31: 189-97.
    • (2007) Ultrastruct Pathol , vol.31 , pp. 189-197
    • Iancu, T.C.1    Mahajnah, M.2    Manov, I.3
  • 42
    • 70249148051 scopus 로고    scopus 로고
    • The clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib
    • de Lonlay P, Seta N. The clinical spectrum of phosphomannose isomerase deficiency, with an evaluation of mannose treatment for CDG-Ib. Biochim Biophys Acta. 2009; 1792: 841-3.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 841-843
    • de Lonlay, P.1    Seta, N.2
  • 43
    • 70349089028 scopus 로고    scopus 로고
    • The clinical spectrum of phosphomannomutase 2 deficiency (CDG-Ia)
    • Grunewald S. The clinical spectrum of phosphomannomutase 2 deficiency (CDG-Ia). Biochim Biophys Acta. 2009; 1792: 827-34.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 827-834
    • Grunewald, S.1
  • 44
    • 33646567848 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein is overexpressed by scleroderma dermal fibroblasts
    • Farina G, Lemaire R, Korn JH, et al. Cartilage oligomeric matrix protein is overexpressed by scleroderma dermal fibroblasts. Matrix Biol. 2006; 25: 213-22.
    • (2006) Matrix Biol , vol.25 , pp. 213-222
    • Farina, G.1    Lemaire, R.2    Korn, J.H.3
  • 45
    • 0036158006 scopus 로고    scopus 로고
    • The involvement of matrix glycoproteins in vascular calcification and fibrosis: an immunohistochemical study
    • Canfield AE, Farrington C, Dziobon MD, et al. The involvement of matrix glycoproteins in vascular calcification and fibrosis: an immunohistochemical study. J Pathol. 2002; 196: 228-34.
    • (2002) J Pathol , vol.196 , pp. 228-234
    • Canfield, A.E.1    Farrington, C.2    Dziobon, M.D.3
  • 46
    • 0347367032 scopus 로고    scopus 로고
    • COMP is selectively up-regulated in degenerating acinar cells in chronic pancreatitis and in chronic-pancreatitis-like lesions in pancreatic cancer
    • Liao Q, Kleeff J, Xiao Y, et al. COMP is selectively up-regulated in degenerating acinar cells in chronic pancreatitis and in chronic-pancreatitis-like lesions in pancreatic cancer. Scand J Gastroenterol. 2003; 38: 207-15.
    • (2003) Scand J Gastroenterol , vol.38 , pp. 207-215
    • Liao, Q.1    Kleeff, J.2    Xiao, Y.3
  • 47
    • 0029035708 scopus 로고
    • Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia
    • Hecht JT, Nelson LD, Crowder E, et al. Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia. Nat Genet. 1995; 10: 325-9.
    • (1995) Nat Genet , vol.10 , pp. 325-329
    • Hecht, J.T.1    Nelson, L.D.2    Crowder, E.3
  • 48
    • 0033503210 scopus 로고    scopus 로고
    • Identification of multiple, differentially expressed messenger RNAs in dermal fibroblasts from patients with systemic sclerosis
    • Feghali CA, Wright TM. Identification of multiple, differentially expressed messenger RNAs in dermal fibroblasts from patients with systemic sclerosis. Arthritis Rheum. 1999; 42: 1451-7.
    • (1999) Arthritis Rheum , vol.42 , pp. 1451-1457
    • Feghali, C.A.1    Wright, T.M.2
  • 49
    • 33749347078 scopus 로고    scopus 로고
    • Insulin-like growth factor binding protein 5 induces skin fibrosis: a novel murine model for dermal fibrosis
    • Yasuoka H, Jukic DM, Zhou Z, et al. Insulin-like growth factor binding protein 5 induces skin fibrosis: a novel murine model for dermal fibrosis. Arthritis Rheum. 2006; 54: 3001-10.
    • (2006) Arthritis Rheum , vol.54 , pp. 3001-3010
    • Yasuoka, H.1    Jukic, D.M.2    Zhou, Z.3
  • 50
    • 70349332328 scopus 로고    scopus 로고
    • IGFBP-5 induces epithelial and fibroblast responses consistent with the fibrotic response
    • Sureshbabu A, Okajima H, Yamanaka D, et al. IGFBP-5 induces epithelial and fibroblast responses consistent with the fibrotic response. Biochem Soc Trans. 2009; 37: 882-5.
    • (2009) Biochem Soc Trans , vol.37 , pp. 882-885
    • Sureshbabu, A.1    Okajima, H.2    Yamanaka, D.3
  • 51
    • 33645560435 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein-5 (IGFBP-5): a critical member of the IGF axis
    • Beattie J, Allan GJ, Lochrie JD, et al. Insulin-like growth factor-binding protein-5 (IGFBP-5): a critical member of the IGF axis. Biochem J. 2006; 395: 1-19.
    • (2006) Biochem J , vol.395 , pp. 1-19
    • Beattie, J.1    Allan, G.J.2    Lochrie, J.D.3
  • 52
    • 0036905115 scopus 로고    scopus 로고
    • Cellular actions of the insulin-like growth factor binding proteins
    • Firth SM, Baxter RC. Cellular actions of the insulin-like growth factor binding proteins. Endocr Rev. 2002; 23: 824-54.
    • (2002) Endocr Rev , vol.23 , pp. 824-854
    • Firth, S.M.1    Baxter, R.C.2
  • 53
    • 0034974302 scopus 로고    scopus 로고
    • IGF-I receptor signalling in transformation and differentiation
    • Valentinis B, Baserga R. IGF-I receptor signalling in transformation and differentiation. Mol Pathol. 2001; 54: 133-7.
    • (2001) Mol Pathol , vol.54 , pp. 133-137
    • Valentinis, B.1    Baserga, R.2
  • 54
    • 0027160032 scopus 로고
    • Extracellular matrix contains insulin-like growth factor binding protein-5: potentiation of the effects of IGF-I
    • Jones JI, Gockerman A, Busby WH Jr., et al. Extracellular matrix contains insulin-like growth factor binding protein-5: potentiation of the effects of IGF-I. J Cell Biol. 1993; 121: 679-87.
    • (1993) J Cell Biol , vol.121 , pp. 679-687
    • Jones, J.I.1    Gockerman, A.2    Busby Jr., W.H.3
  • 55
    • 0028029340 scopus 로고
    • Heparin, heparan sulfate, and dermatan sulfate regulate formation of the insulin-like growth factor-I and insulin-like growth factor-binding protein complexes
    • Arai T, Parker A, Busby W Jr., et al. Heparin, heparan sulfate, and dermatan sulfate regulate formation of the insulin-like growth factor-I and insulin-like growth factor-binding protein complexes. J Biol Chem. 1994; 269: 20388-93.
    • (1994) J Biol Chem , vol.269 , pp. 20388-20393
    • Arai, T.1    Parker, A.2    Busby Jr., W.3
  • 56
    • 56849118244 scopus 로고    scopus 로고
    • Epithelial injury induces an innate repair mechanism linked to cellular senescence and fibrosis involving IGF-binding protein-5
    • Allan GJ, Beattie J, Flint DJ. Epithelial injury induces an innate repair mechanism linked to cellular senescence and fibrosis involving IGF-binding protein-5. J Endocrinol. 2008; 199: 155-64.
    • (2008) J Endocrinol , vol.199 , pp. 155-164
    • Allan, G.J.1    Beattie, J.2    Flint, D.J.3
  • 57
    • 34548843398 scopus 로고    scopus 로고
    • A polymorphism in the CTGF promoter region associated with systemic sclerosis
    • Fonseca C, Lindahl GE, Ponticos M, et al. A polymorphism in the CTGF promoter region associated with systemic sclerosis. N Engl J Med. 2007; 357: 1210-20.
    • (2007) N Engl J Med , vol.357 , pp. 1210-1220
    • Fonseca, C.1    Lindahl, G.E.2    Ponticos, M.3
  • 58
    • 77949351029 scopus 로고    scopus 로고
    • New insights into epithelial-mesenchymal transition in kidney fibrosis
    • Liu Y. New insights into epithelial-mesenchymal transition in kidney fibrosis. J Am Soc Nephrol. 2010; 21: 212-22.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 212-222
    • Liu, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.