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Volumn 280, Issue 17, 2013, Pages 4109-4117

Role of proteoglycans in the regulation of the skeletal muscle fibrotic response

Author keywords

connective tissue growth factor (CTGF); fibrosis; muscular diseases; proteoglycans; transforming growth factor (TGF )

Indexed keywords

BIGLYCAN; CELL SURFACE RECEPTOR; CHONDROITIN; CONNECTIVE TISSUE GROWTH FACTOR; CREATINE KINASE; DECORIN; DERMATAN SULFATE; HSPG BETA GLYCAN; LEUCINE RICH REPEAT KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 1; MYOSIN; MYOSTATIN; PROTEOGLYCAN; PROTEOHEPARAN SULFATE; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; UNCLASSIFIED DRUG;

EID: 84882596804     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12278     Document Type: Review
Times cited : (38)

References (98)
  • 1
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • Iozzo RV, &, Schaefer L, (2010) Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans. FEBS J 277, 3864-3875.
    • (2010) FEBS J , vol.277 , pp. 3864-3875
    • Iozzo, R.V.1    Schaefer, L.2
  • 2
    • 77956641177 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel roles for proteoglycans in malignancy and their pharmacological targeting
    • Theocharis AD, Skandalis SS, Tzanakakis GN, &, Karamanos NK, (2010) Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting. FEBS J 277, 3904-3923.
    • (2010) FEBS J , vol.277 , pp. 3904-3923
    • Theocharis, A.D.1    Skandalis, S.S.2    Tzanakakis, G.N.3    Karamanos, N.K.4
  • 3
    • 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, (2008) Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy. Matrix Biol 27, 700-708.
    • (2008) Matrix Biol , vol.27 , pp. 700-708
    • Brandan, E.1    Cabello-Verrugio, C.2    Vial, C.3
  • 4
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins
    • Iozzo RV, (1999) The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins. J Biol Chem 274, 18843-18846.
    • (1999) J Biol Chem , vol.274 , pp. 18843-18846
    • Iozzo, R.V.1
  • 6
    • 30344466674 scopus 로고    scopus 로고
    • Heparan sulfates in skeletal muscle development and physiology
    • Jenniskens GJ, Veerkamp JH, &, van Kuppevelt TH, (2006) Heparan sulfates in skeletal muscle development and physiology. J Cell Physiol 206, 283-294.
    • (2006) J Cell Physiol , vol.206 , pp. 283-294
    • Jenniskens, G.J.1    Veerkamp, J.H.2    Van Kuppevelt, T.H.3
  • 7
    • 66249084507 scopus 로고    scopus 로고
    • Glypicans
    • doi: 10.1186/gb-2008-9-5-224
    • Filmus J, Capurro M, &, Rast J, (2008) Glypicans. Genome Biol 9, 224, doi: 10.1186/gb-2008-9-5-224.
    • (2008) Genome Biol , vol.9 , pp. 224
    • Filmus, J.1    Capurro, M.2    Rast, J.3
  • 8
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • Iozzo RV, &, Schaefer L, (2010) Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans. FEBS J 277, 3864-3875.
    • (2010) FEBS J , vol.277 , pp. 3864-3875
    • Iozzo, R.V.1    Schaefer, L.2
  • 9
    • 80052041196 scopus 로고    scopus 로고
    • Structure and function of the skeletal muscle extracellular matrix
    • Gillies AR, &, Lieber RL, (2011) Structure and function of the skeletal muscle extracellular matrix. Muscle Nerve 44, 318-331.
    • (2011) Muscle Nerve , vol.44 , pp. 318-331
    • Gillies, A.R.1    Lieber, R.L.2
  • 10
    • 77956637386 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Emerging concepts and future directions
    • doi: 10.1111/j.1742-4658.2010.07796.x
    • Iozzo RV, &, Karamanos N, (2010) Proteoglycans in health and disease: emerging concepts and future directions. FEBS J 277, 3863, doi: 10.1111/j.1742-4658.2010.07796.x.
    • (2010) FEBS J , vol.277 , pp. 3863
    • Iozzo, R.V.1    Karamanos, N.2
  • 12
    • 33845308607 scopus 로고    scopus 로고
    • Increase in decorin and biglycan in Duchenne muscular dystrophy: Role of fibroblasts as cell source of these proteoglycans in the disease
    • Fadic R, Mezzano V, Alvarez K, Cabrera D, Holmgren J, &, Brandan E, (2006) Increase in decorin and biglycan in Duchenne muscular dystrophy: role of fibroblasts as cell source of these proteoglycans in the disease. J Cell Mol Med 10, 758-769.
    • (2006) J Cell Mol Med , vol.10 , pp. 758-769
    • Fadic, R.1    Mezzano, V.2    Alvarez, K.3    Cabrera, D.4    Holmgren, J.5    Brandan, E.6
  • 13
    • 1042268862 scopus 로고    scopus 로고
    • Temporal gene expression profiling of dystrophin-deficient (mdx) mouse diaphragm identifies conserved and muscle group-specific mechanisms in the pathogenesis of muscular dystrophy
    • Porter JD, Merriam AP, Leahy P, Gong B, Feuerman J, Cheng G, &, Khanna S, (2004) Temporal gene expression profiling of dystrophin-deficient (mdx) mouse diaphragm identifies conserved and muscle group-specific mechanisms in the pathogenesis of muscular dystrophy. Hum Mol Genet 13, 257-269.
    • (2004) Hum Mol Genet , vol.13 , pp. 257-269
    • Porter, J.D.1    Merriam, A.P.2    Leahy, P.3    Gong, B.4    Feuerman, J.5    Cheng, G.6    Khanna, S.7
  • 14
    • 22744443345 scopus 로고    scopus 로고
    • Postnatal changes in sarcolemmal organization in the mdx mouse
    • Reed P, &, Bloch RJ, (2005) Postnatal changes in sarcolemmal organization in the mdx mouse. Neuromuscul Disord 15, 552-561.
    • (2005) Neuromuscul Disord , vol.15 , pp. 552-561
    • Reed, P.1    Bloch, R.J.2
  • 15
    • 77957669313 scopus 로고    scopus 로고
    • Regulation and dysregulation of fibrosis in skeletal muscle
    • Serrano AL, &, Munoz-Canoves P, (2010) Regulation and dysregulation of fibrosis in skeletal muscle. Exp Cell Res 316, 3050-3058.
    • (2010) Exp Cell Res , vol.316 , pp. 3050-3058
    • Serrano, A.L.1    Munoz-Canoves, P.2
  • 16
    • 0036237682 scopus 로고    scopus 로고
    • Augmented synthesis and differential localization of heparan sulfate proteoglycans in Duchenne muscular dystrophy
    • Alvarez K, Fadic R, &, Brandan E, (2002) Augmented synthesis and differential localization of heparan sulfate proteoglycans in Duchenne muscular dystrophy. J Cell Biochem 85, 703-713.
    • (2002) J Cell Biochem , vol.85 , pp. 703-713
    • Alvarez, K.1    Fadic, R.2    Brandan, E.3
  • 18
    • 38549159026 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of fibrosis
    • Wynn TA, (2008) Cellular and molecular mechanisms of fibrosis. J Pathol 214, 199-210.
    • (2008) J Pathol , vol.214 , pp. 199-210
    • Wynn, T.A.1
  • 19
    • 77953633610 scopus 로고    scopus 로고
    • Signaling in fibrosis: Targeting the TGF beta, endothelin-1 and CCN2 axis in scleroderma
    • Leask A, (2009) Signaling in fibrosis: targeting the TGF beta, endothelin-1 and CCN2 axis in scleroderma. Front Biosci (Elite Ed) 1, 115-122.
    • (2009) Front Biosci (Elite Ed) , vol.1 , pp. 115-122
    • Leask, A.1
  • 23
    • 81355149683 scopus 로고    scopus 로고
    • CTGF/CCN-2 overexpression can directly induce features of skeletal muscle dystrophy
    • Morales G, Cabello-Verrugio C, Cabrera D, Goldschmeding R, &, Brandan E, (2011) CTGF/CCN-2 overexpression can directly induce features of skeletal muscle dystrophy. J Pathol 225, 490-501.
    • (2011) J Pathol , vol.225 , pp. 490-501
    • Morales, G.1    Cabello-Verrugio, C.2    Cabrera, D.3    Goldschmeding, R.4    Brandan, E.5
  • 25
    • 0042131566 scopus 로고    scopus 로고
    • Dissection of temporal gene expression signatures of affected and spared muscle groups in dystrophin-deficient (mdx) mice
    • Porter JD, Merriam AP, Leahy P, Gong B, &, Khanna S, (2003) Dissection of temporal gene expression signatures of affected and spared muscle groups in dystrophin-deficient (mdx) mice. Hum Mol Genet 12, 1813-1821.
    • (2003) Hum Mol Genet , vol.12 , pp. 1813-1821
    • Porter, J.D.1    Merriam, A.P.2    Leahy, P.3    Gong, B.4    Khanna, S.5
  • 26
    • 0035793550 scopus 로고    scopus 로고
    • Antisense inhibition of decorin expression in myoblasts decreases cell responsiveness to transforming growth factor beta and accelerates skeletal muscle differentiation
    • Riquelme C, Larrain J, Schonherr E, Henriquez JP, Kresse H, &, Brandan E, (2001) Antisense inhibition of decorin expression in myoblasts decreases cell responsiveness to transforming growth factor beta and accelerates skeletal muscle differentiation. J Biol Chem 276, 3589-3596.
    • (2001) J Biol Chem , vol.276 , pp. 3589-3596
    • Riquelme, C.1    Larrain, J.2    Schonherr, E.3    Henriquez, J.P.4    Kresse, H.5    Brandan, E.6
  • 27
    • 0011899697 scopus 로고
    • Type beta transforming growth factor is an inhibitor of myogenic differentiation
    • Massague J, Cheifetz S, Endo T, &, Nadal-Ginard B, (1986) Type beta transforming growth factor is an inhibitor of myogenic differentiation. Proc Natl Acad Sci USA 83, 8206-8210.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8206-8210
    • Massague, J.1    Cheifetz, S.2    Endo, T.3    Nadal-Ginard, B.4
  • 28
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-beta signals
    • Massague J, (2000) How cells read TGF-beta signals. Nat Rev Mol Cell Biol 1, 169-178.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 169-178
    • Massague, J.1
  • 29
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • Derynck R, &, Zhang YE, (2003) Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 425, 577-584.
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 30
    • 0032787927 scopus 로고    scopus 로고
    • The connective tissue growth factor/cysteine-rich 61/nephroblastoma overexpressed (CCN) family
    • Brigstock DR, (1999) The connective tissue growth factor/cysteine-rich 61/nephroblastoma overexpressed (CCN) family. Endocr Rev 20, 189-206.
    • (1999) Endocr Rev , vol.20 , pp. 189-206
    • Brigstock, D.R.1
  • 31
    • 33845906843 scopus 로고    scopus 로고
    • All in the CCN family: Essential matricellular signaling modulators emerge from the bunker
    • Leask A, &, Abraham DJ, (2006) All in the CCN family: essential matricellular signaling modulators emerge from the bunker. J Cell Sci 119, 4803-4810.
    • (2006) J Cell Sci , vol.119 , pp. 4803-4810
    • Leask, A.1    Abraham, D.J.2
  • 32
    • 0029996247 scopus 로고    scopus 로고
    • Connective tissue growth factor gene expression in tissue sections from localized scleroderma, keloid, and other fibrotic skin disorders
    • Igarashi A, Nashiro K, Kikuchi K, Sato S, Ihn H, Fujimoto M, Grotendorst GR, &, Takehara K, (1996) Connective tissue growth factor gene expression in tissue sections from localized scleroderma, keloid, and other fibrotic skin disorders. J Invest Dermatol 106, 729-733.
    • (1996) J Invest Dermatol , vol.106 , pp. 729-733
    • Igarashi, A.1    Nashiro, K.2    Kikuchi, K.3    Sato, S.4    Ihn, H.5    Fujimoto, M.6    Grotendorst, G.R.7    Takehara, K.8
  • 39
    • 56949085767 scopus 로고    scopus 로고
    • Skeletal muscle repair and regeneration
    • In 3 (Stienen, G.J.M. ed), 379. Springer, New York
    • Schiaffino S, &, Partridge T, (2008) Skeletal muscle repair and regeneration. In Advances in Muscle Research Vol. 3 (, Stienen, GJM, ed), pp. 379. Springer, New York.
    • (2008) Advances in Muscle Research
    • Schiaffino, S.1    Partridge, T.2
  • 40
    • 0034695928 scopus 로고    scopus 로고
    • The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle
    • Bowe M, Mendis D, &, Fallon J, (2000) The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle. J Cell Biol 148, 801-810.
    • (2000) J Cell Biol , vol.148 , pp. 801-810
    • Bowe, M.1    Mendis, D.2    Fallon, J.3
  • 42
    • 33645993621 scopus 로고    scopus 로고
    • Cell surface and gene expression regulation molecules in dystrophinopathy: Mdx vs. Duchenne
    • Fadic R, (2005) Cell surface and gene expression regulation molecules in dystrophinopathy: mdx vs. Duchenne. Biol Res 38, 375-380.
    • (2005) Biol Res , vol.38 , pp. 375-380
    • Fadic, R.1
  • 43
    • 56949092670 scopus 로고    scopus 로고
    • Constitutively activated dystrophic muscle fibroblasts show a paradoxical response to TGF-beta and CTGF/CCN2
    • Mezzano V, Cabrera D, Vial C, &, Brandan E, (2007) Constitutively activated dystrophic muscle fibroblasts show a paradoxical response to TGF-beta and CTGF/CCN2. J Cell Commun Signal 1, 205-217.
    • (2007) J Cell Commun Signal , vol.1 , pp. 205-217
    • Mezzano, V.1    Cabrera, D.2    Vial, C.3    Brandan, E.4
  • 45
    • 33747015300 scopus 로고    scopus 로고
    • Extracellular proteoglycans modifies TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation
    • Droguett R, Cabello-Verrugio C, Riquelme C, &, Brandan E, (2006) Extracellular proteoglycans modifies TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation. Matrix Biol 25, 332-341.
    • (2006) Matrix Biol , vol.25 , pp. 332-341
    • Droguett, R.1    Cabello-Verrugio, C.2    Riquelme, C.3    Brandan, E.4
  • 47
    • 79957582013 scopus 로고    scopus 로고
    • Integrin expression and function in the response of primary culture hepatic stellate cells to connective tissue growth factor (CCN2)
    • Huang G, &, Brigstock DR, (2011) Integrin expression and function in the response of primary culture hepatic stellate cells to connective tissue growth factor (CCN2). J Cell Mol Med 15, 1087-1095.
    • (2011) J Cell Mol Med , vol.15 , pp. 1087-1095
    • Huang, G.1    Brigstock, D.R.2
  • 48
    • 59649107705 scopus 로고    scopus 로고
    • Functions and mechanisms of action of CCN matricellular proteins
    • Chen CC, &, Lau LF, (2009) Functions and mechanisms of action of CCN matricellular proteins. Int J Biochem Cell Biol 41, 771-783.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 771-783
    • Chen, C.C.1    Lau, L.F.2
  • 49
    • 0242690484 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein (LRP) is a heparin-dependent adhesion receptor for connective tissue growth factor (CTGF) in rat activated hepatic stellate cells
    • Gao R, &, Brigstock DR, (2003) Low density lipoprotein receptor-related protein (LRP) is a heparin-dependent adhesion receptor for connective tissue growth factor (CTGF) in rat activated hepatic stellate cells. Hepatol Res 27, 214-220.
    • (2003) Hepatol Res , vol.27 , pp. 214-220
    • Gao, R.1    Brigstock, D.R.2
  • 50
    • 40949152810 scopus 로고    scopus 로고
    • Skeletal muscle cells express the profibrotic cytokine connective tissue growth factor (CTGF/CCN2), which induces their dedifferentiation
    • Vial C, Zuniga LM, Cabello-Verrugio C, Canon P, Fadic R, &, Brandan E, (2008) Skeletal muscle cells express the profibrotic cytokine connective tissue growth factor (CTGF/CCN2), which induces their dedifferentiation. J Cell Physiol 215, 410-421.
    • (2008) J Cell Physiol , vol.215 , pp. 410-421
    • Vial, C.1    Zuniga, L.M.2    Cabello-Verrugio, C.3    Canon, P.4    Fadic, R.5    Brandan, E.6
  • 51
    • 79959865250 scopus 로고    scopus 로고
    • Decorin interacts with CTGF/CCN2 through LRR12 inhibiting its biological activity
    • Vial C, Gutiérrez J, Santander C, Cabrera D, &, Brandan E, (2011) Decorin interacts with CTGF/CCN2 through LRR12 inhibiting its biological activity. J Biol Chem 286, 24242-24252.
    • (2011) J Biol Chem , vol.286 , pp. 24242-24252
    • Vial, C.1    Gutiérrez, J.2    Santander, C.3    Cabrera, D.4    Brandan, E.5
  • 53
    • 4444381213 scopus 로고    scopus 로고
    • Profibrotic effects of endothelin-1 via the ET(A) receptor in cultured human cardiac fibroblasts
    • Hafizi S, Wharton J, Chester A, &, Yacoub M, (2004) Profibrotic effects of endothelin-1 via the ET(A) receptor in cultured human cardiac fibroblasts. Cell Physiol Biochem 14, 285-292.
    • (2004) Cell Physiol Biochem , vol.14 , pp. 285-292
    • Hafizi, S.1    Wharton, J.2    Chester, A.3    Yacoub, M.4
  • 56
    • 40749107501 scopus 로고    scopus 로고
    • Regulation and function of connective tissue growth factor/CCN2 in tissue repair, scarring and fibrosis
    • Shi-Wen X, Leask A, &, Abraham D, (2008) Regulation and function of connective tissue growth factor/CCN2 in tissue repair, scarring and fibrosis. Cytokine Growth Factor Rev 19, 133-144.
    • (2008) Cytokine Growth Factor Rev , vol.19 , pp. 133-144
    • Shi-Wen, X.1    Leask, A.2    Abraham, D.3
  • 57
    • 84856695092 scopus 로고    scopus 로고
    • PAI-1-regulated miR-21 defines a novel age-associated fibrogenic pathway in muscular dystrophy
    • Ardite E, Perdiguero E, Vidal B, Gutarra S, Serrano AL, &, Munoz-Canoves P, (2012) PAI-1-regulated miR-21 defines a novel age-associated fibrogenic pathway in muscular dystrophy. J Cell Biol 196, 163-175.
    • (2012) J Cell Biol , vol.196 , pp. 163-175
    • Ardite, E.1    Perdiguero, E.2    Vidal, B.3    Gutarra, S.4    Serrano, A.L.5    Munoz-Canoves, P.6
  • 61
    • 34548072165 scopus 로고    scopus 로고
    • Decorin gene transfer promotes muscle cell differentiation and muscle regeneration
    • Li Y, Li J, Zhu J, Sun B, Branca M, Tang Y, Foster W, Xiao X, &, Huard J, (2007) Decorin gene transfer promotes muscle cell differentiation and muscle regeneration. Mol Ther 15, 1616-1622.
    • (2007) Mol Ther , vol.15 , pp. 1616-1622
    • Li, Y.1    Li, J.2    Zhu, J.3    Sun, B.4    Branca, M.5    Tang, Y.6    Foster, W.7    Xiao, X.8    Huard, J.9
  • 62
    • 78650501005 scopus 로고    scopus 로고
    • Prevention of muscle fibrosis and myonecrosis in mdx mice by suramin, a TGF-beta1 blocker
    • Taniguti AP, Pertille A, Matsumura CY, Santo Neto H, &, Marques MJ, (2011) Prevention of muscle fibrosis and myonecrosis in mdx mice by suramin, a TGF-beta1 blocker. Muscle Nerve 43, 82-87.
    • (2011) Muscle Nerve , vol.43 , pp. 82-87
    • Taniguti, A.P.1    Pertille, A.2    Matsumura, C.Y.3    Santo Neto, H.4    Marques, M.J.5
  • 63
    • 79952764909 scopus 로고    scopus 로고
    • Targeting the activin type IIB receptor to improve muscle mass and function in the mdx mouse model of Duchenne muscular dystrophy
    • Pistilli EE, Bogdanovich S, Goncalves MD, Ahima RS, Lachey J, Seehra J, &, Khurana T, (2011) Targeting the activin type IIB receptor to improve muscle mass and function in the mdx mouse model of Duchenne muscular dystrophy. Am J Pathol 178, 1287-1297.
    • (2011) Am J Pathol , vol.178 , pp. 1287-1297
    • Pistilli, E.E.1    Bogdanovich, S.2    Goncalves, M.D.3    Ahima, R.S.4    Lachey, J.5    Seehra, J.6    Khurana, T.7
  • 65
    • 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, (2001) The use of an antifibrosis agent to improve muscle recovery after laceration. Am J Sports Med 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
  • 66
    • 1242293760 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 induces the differentiation of myogenic cells into fibrotic cells in injured skeletal muscle: A key event in muscle fibrogenesis
    • Li Y, Foster W, Deasy BM, Chan Y, Prisk V, Tang Y, Cummins J, &, Huard J, (2004) Transforming growth factor-beta1 induces the differentiation of myogenic cells into fibrotic cells in injured skeletal muscle: a key event in muscle fibrogenesis. Am J Pathol 164, 1007-1019.
    • (2004) Am J Pathol , vol.164 , pp. 1007-1019
    • Li, Y.1    Foster, W.2    Deasy, B.M.3    Chan, Y.4    Prisk, V.5    Tang, Y.6    Cummins, J.7    Huard, J.8
  • 68
    • 34548492947 scopus 로고    scopus 로고
    • Relationships between transforming growth factor-beta1, myostatin, and decorin: Implications for skeletal muscle fibrosis
    • Zhu J, Li Y, Shen W, Qiao C, Ambrosio F, Lavasani M, Nozaki M, Branca MF, &, Huard J, (2007) Relationships between transforming growth factor-beta1, myostatin, and decorin: implications for skeletal muscle fibrosis. J Biol Chem 282, 25852-25863.
    • (2007) J Biol Chem , vol.282 , pp. 25852-25863
    • Zhu, J.1    Li, Y.2    Shen, W.3    Qiao, C.4    Ambrosio, F.5    Lavasani, M.6    Nozaki, M.7    Branca, M.F.8    Huard, J.9
  • 69
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta
    • Hildebrand A, Romaris M, Rasmussen LM, Heinegard D, Twardzik DR, Border WA, &, Ruoslahti E, (1994) Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. Biochem J 302, 527-534.
    • (1994) Biochem J , vol.302 , pp. 527-534
    • Hildebrand, A.1    Romaris, M.2    Rasmussen, L.M.3    Heinegard, D.4    Twardzik, D.R.5    Border, W.A.6    Ruoslahti, E.7
  • 70
    • 0038259506 scopus 로고    scopus 로고
    • Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type i collagen
    • Schonherr E, Broszat M, Brandan E, Bruckner P, &, Kresse H, (1998) Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen. Arch Biochem Biophys 355, 241-248.
    • (1998) Arch Biochem Biophys , vol.355 , pp. 241-248
    • Schonherr, E.1    Broszat, M.2    Brandan, E.3    Bruckner, P.4    Kresse, H.5
  • 71
    • 0030986608 scopus 로고    scopus 로고
    • The family of the small leucine-rich proteoglycans: Key regulators of matrix assembly and cellular growth
    • Iozzo RV, (1997) The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth. Crit Rev Biochem Mol Biol 32, 141-174.
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 141-174
    • Iozzo, R.V.1
  • 72
    • 0025913228 scopus 로고
    • The proteoglycan decorin is synthesized and secreted by differentiated myotubes
    • Brandan E, Fuentes ME, &, Andrade W, (1991) The proteoglycan decorin is synthesized and secreted by differentiated myotubes. Eur J Cell Biol 55, 209-216.
    • (1991) Eur J Cell Biol , vol.55 , pp. 209-216
    • Brandan, E.1    Fuentes, M.E.2    Andrade, W.3
  • 73
    • 0026067041 scopus 로고
    • Hormones, growth factors, and myogenic differentiation
    • Florini JR, Ewton DZ, &, Magri KA, (1991) Hormones, growth factors, and myogenic differentiation. Annu Rev Physiol 53, 201-216.
    • (1991) Annu Rev Physiol , vol.53 , pp. 201-216
    • Florini, J.R.1    Ewton, D.Z.2    Magri, K.A.3
  • 74
    • 34547131835 scopus 로고    scopus 로고
    • A novel modulatory mechanism of transforming growth factor-beta signaling through decorin and LRP-1
    • Cabello-Verrugio C, &, Brandan E, (2007) A novel modulatory mechanism of transforming growth factor-beta signaling through decorin and LRP-1. J Biol Chem 282, 18842-18850.
    • (2007) J Biol Chem , vol.282 , pp. 18842-18850
    • Cabello-Verrugio, C.1    Brandan, E.2
  • 75
    • 84857479041 scopus 로고    scopus 로고
    • The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-beta-dependent signaling, and inhibits TGF-beta-dependent fibrotic response in skeletal muscles
    • Cabello-Verrugio C, Santander C, Cofre C, Acuna MJ, Melo F, &, Brandan E, (2012) The internal region leucine-rich repeat 6 of decorin interacts with low density lipoprotein receptor-related protein-1, modulates transforming growth factor (TGF)-beta-dependent signaling, and inhibits TGF-beta-dependent fibrotic response in skeletal muscles. J Biol Chem 287, 6773-6787.
    • (2012) J Biol Chem , vol.287 , pp. 6773-6787
    • Cabello-Verrugio, C.1    Santander, C.2    Cofre, C.3    Acuna, M.J.4    Melo, F.5    Brandan, E.6
  • 76
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin
    • Brandan E, Retamal C, Cabello-Verrugio C, &, Marzolo MP, (2006) The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin. J Biol Chem 281, 31562-31571.
    • (2006) J Biol Chem , vol.281 , pp. 31562-31571
    • Brandan, E.1    Retamal, C.2    Cabello-Verrugio, C.3    Marzolo, M.P.4
  • 79
    • 0035805505 scopus 로고    scopus 로고
    • Ligand binding and functional properties of betaglycan, a co-receptor of the transforming growth factor-beta superfamily. Specialized binding regions for transforming growth factor-beta and inhibin A
    • Esparza-Lopez J, Montiel JL, Vilchis-Landeros MM, Okadome T, Miyazono K, &, Lopez-Casillas F, (2001) Ligand binding and functional properties of betaglycan, a co-receptor of the transforming growth factor-beta superfamily. Specialized binding regions for transforming growth factor-beta and inhibin A. J Biol Chem 276, 14588-14596.
    • (2001) J Biol Chem , vol.276 , pp. 14588-14596
    • Esparza-Lopez, J.1    Montiel, J.L.2    Vilchis-Landeros, M.M.3    Okadome, T.4    Miyazono, K.5    Lopez-Casillas, F.6
  • 80
    • 0025987832 scopus 로고
    • Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system
    • Lopez-Casillas F, Cheifetz S, Doody J, Andres JL, Lane WS, &, Massague J, (1991) Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system. Cell 67, 785-795.
    • (1991) Cell , vol.67 , pp. 785-795
    • Lopez-Casillas, F.1    Cheifetz, S.2    Doody, J.3    Andres, J.L.4    Lane, W.S.5    Massague, J.6
  • 81
    • 33744784611 scopus 로고    scopus 로고
    • Betaglycan induces TGF-beta signaling in a ligand-independent manner, through activation of the p38 pathway
    • Santander C, &, Brandan E, (2006) Betaglycan induces TGF-beta signaling in a ligand-independent manner, through activation of the p38 pathway. Cell Signal 18, 1492-1491.
    • (2006) Cell Signal , vol.18 , pp. 1492-1491
    • Santander, C.1    Brandan, E.2
  • 82
    • 84866350456 scopus 로고    scopus 로고
    • Angiotensin II receptor type 1 blockade decreases CTGF/CCN2-mediated damage and fibrosis in normal and dystrophic skeletal muscles
    • Cabello-Verrugio C, Morales G, Cabrera D, Vio CP, &, Brandan E, (2011) Angiotensin II receptor type 1 blockade decreases CTGF/CCN2-mediated damage and fibrosis in normal and dystrophic skeletal muscles. J Cell Mol Med 16, 752-764.
    • (2011) J Cell Mol Med , vol.16 , pp. 752-764
    • Cabello-Verrugio, C.1    Morales, G.2    Cabrera, D.3    Vio, C.P.4    Brandan, E.5
  • 83
    • 33847133425 scopus 로고    scopus 로고
    • Connective tissue growth factor binds to fibronectin through the type i repeat modules and enhances the affinity of fibronectin to fibrin
    • Yoshida K, &, Munakata H, (2007) Connective tissue growth factor binds to fibronectin through the type I repeat modules and enhances the affinity of fibronectin to fibrin. Biochim Biophys Acta 1770, 672-680.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 672-680
    • Yoshida, K.1    Munakata, H.2
  • 84
    • 0036051343 scopus 로고    scopus 로고
    • Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-beta
    • Abreu JG, Ketpura NI, Reversade B, &, De Robertis EM, (2002) Connective-tissue growth factor (CTGF) modulates cell signalling by BMP and TGF-beta. Nat Cell Biol 4, 599-604.
    • (2002) Nat Cell Biol , vol.4 , pp. 599-604
    • Abreu, J.G.1    Ketpura, N.I.2    Reversade, B.3    De Robertis, E.M.4
  • 85
    • 20444384532 scopus 로고    scopus 로고
    • Connective tissue growth factor CCN2 interacts with and activates the tyrosine kinase receptor TrkA
    • Wahab NA, Weston BS, &, Mason RM, (2005) Connective tissue growth factor CCN2 interacts with and activates the tyrosine kinase receptor TrkA. J Am Soc Nephrol 16, 340-351.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 340-351
    • Wahab, N.A.1    Weston, B.S.2    Mason, R.M.3
  • 86
    • 0035798710 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein/alpha2-macroglobulin receptor is a receptor for connective tissue growth factor
    • Segarini PR, Nesbitt JE, Li D, Hays LG, Yates JR III, &, Carmichael DF, (2001) The low density lipoprotein receptor-related protein/alpha2- macroglobulin receptor is a receptor for connective tissue growth factor. J Biol Chem 276, 40659-40667.
    • (2001) J Biol Chem , vol.276 , pp. 40659-40667
    • Segarini, P.R.1    Nesbitt, J.E.2    Li, D.3    Hays, L.G.4    Yates III, J.R.5    Carmichael, D.F.6
  • 87
    • 84872500380 scopus 로고    scopus 로고
    • Fell-Muir lecture: Connective tissue growth factor (CCN2) - A pernicious and pleiotropic player in the development of kidney fibrosis
    • Mason RM, (2013) Fell-Muir lecture: connective tissue growth factor (CCN2)-a pernicious and pleiotropic player in the development of kidney fibrosis. Int J Exp Pathol 94, 1-16.
    • (2013) Int J Exp Pathol , vol.94 , pp. 1-16
    • Mason, R.M.1
  • 88
    • 67649400810 scopus 로고    scopus 로고
    • MMP-2 deficient fibroblasts exhibit an alteration in the fibrotic response to CTGF/CCN2 due to an increase in the levels of endogenous fibronectin
    • Droppelmann C, Gutierrez J, Vial C, &, Brandan E, (2009) MMP-2 deficient fibroblasts exhibit an alteration in the fibrotic response to CTGF/CCN2 due to an increase in the levels of endogenous fibronectin. J Biol Chem 284, 13551-13561.
    • (2009) J Biol Chem , vol.284 , pp. 13551-13561
    • Droppelmann, C.1    Gutierrez, J.2    Vial, C.3    Brandan, E.4
  • 89
    • 0036775425 scopus 로고    scopus 로고
    • Matricellular proteins: Extracellular modulators of cell function
    • Bornstein P, &, Sage EH, (2002) Matricellular proteins: extracellular modulators of cell function. Curr Opin Cell Biol 14, 608-616.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 608-616
    • Bornstein, P.1    Sage, E.H.2
  • 90
    • 67349168833 scopus 로고    scopus 로고
    • Connective tissue growth factor: Context-dependent functions and mechanisms of regulation
    • Cicha I, &, Goppelt-Struebe M, (2009) Connective tissue growth factor: context-dependent functions and mechanisms of regulation. BioFactors 35, 200-208.
    • (2009) BioFactors , vol.35 , pp. 200-208
    • Cicha, I.1    Goppelt-Struebe, M.2
  • 91
    • 33746265975 scopus 로고    scopus 로고
    • Inhibition of connective tissue growth factor by siRNA prevents liver fibrosis in rats
    • Li G, Xie Q, Shi Y, Li D, Zhang M, Jiang S, Zhou H, Lu H, &, Jin Y, (2006) Inhibition of connective tissue growth factor by siRNA prevents liver fibrosis in rats. J Gene Med 8, 889-900.
    • (2006) J Gene Med , vol.8 , pp. 889-900
    • Li, G.1    Xie, Q.2    Shi, Y.3    Li, D.4    Zhang, M.5    Jiang, S.6    Zhou, H.7    Lu, H.8    Jin, Y.9
  • 92
    • 35248841125 scopus 로고    scopus 로고
    • Specific down-regulation of connective tissue growth factor attenuates progression of nephropathy in mouse models of type 1 and type 2 diabetes
    • Guha M, Xu ZG, Tung D, Lanting L, &, Natarajan R, (2007) Specific down-regulation of connective tissue growth factor attenuates progression of nephropathy in mouse models of type 1 and type 2 diabetes. FASEB J 21, 3355-3368.
    • (2007) FASEB J , vol.21 , pp. 3355-3368
    • Guha, M.1    Xu, Z.G.2    Tung, D.3    Lanting, L.4    Natarajan, R.5
  • 96
    • 80055014533 scopus 로고    scopus 로고
    • CCN2/decorin interactions: A novel approach to combating fibrosis?
    • Leask A, (2011) CCN2/decorin interactions: a novel approach to combating fibrosis? J Cell Commun Signal 5, 249-250.
    • (2011) J Cell Commun Signal , vol.5 , pp. 249-250
    • Leask, A.1
  • 97
    • 0023665170 scopus 로고
    • Membrane binding characteristics of two forms of transforming growth factor-beta
    • Segarini P, Roberts A, Rosen D, &, Seyedin S, (1987) Membrane binding characteristics of two forms of transforming growth factor-beta. J Biol Chem 262, 14655-14662.
    • (1987) J Biol Chem , vol.262 , pp. 14655-14662
    • Segarini, P.1    Roberts, A.2    Rosen, D.3    Seyedin, S.4
  • 98
    • 0037844869 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein complexes with cell surface heparan sulfate proteoglycans to regulate proteoglycan-mediated lipoprotein catabolism
    • Wilsie LC, &, Orlando RA, (2003) The low density lipoprotein receptor-related protein complexes with cell surface heparan sulfate proteoglycans to regulate proteoglycan-mediated lipoprotein catabolism. J Biol Chem 278, 15758-15764.
    • (2003) J Biol Chem , vol.278 , pp. 15758-15764
    • Wilsie, L.C.1    Orlando, R.A.2


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