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Volumn 25, Issue 6, 2006, Pages 332-341

Extracellular proteoglycans modify TGF-β bio-availability attenuating its signaling during skeletal muscle differentiation

Author keywords

Betaglycan; Biglycan; Decorin; Extracellular matrix; Myogenesis; TGF dependent signaling

Indexed keywords

BETA GLYCAN; BIGLYCAN; DECORIN; LUCIFERASE; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEOGLYCAN; RECEPTOR SUBUNIT; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 1; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 2; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 3; TRANSFORMING GROWTH FACTOR BETA1; TRANSFORMING GROWTH FACTOR BETA2; UNCLASSIFIED DRUG;

EID: 33747015300     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.matbio.2006.04.004     Document Type: Article
Times cited : (123)

References (60)
  • 1
    • 0023571274 scopus 로고
    • Inhibition of skeletal muscle satellite cell differentiation by transforming growth factor-beta
    • Allen R.E., and Boxhorn L.K. Inhibition of skeletal muscle satellite cell differentiation by transforming growth factor-beta. J. Cell. Physiol. 133 (1987) 567-572
    • (1987) J. Cell. Physiol. , vol.133 , pp. 567-572
    • Allen, R.E.1    Boxhorn, L.K.2
  • 2
    • 0036744260 scopus 로고    scopus 로고
    • Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases
    • Ameye L., and Young M.F. Mice deficient in small leucine-rich proteoglycans: novel in vivo models for osteoporosis, osteoarthritis, Ehlers-Danlos syndrome, muscular dystrophy, and corneal diseases. Glycobiology 12 (2002) 107R-116R
    • (2002) Glycobiology , vol.12
    • Ameye, L.1    Young, M.F.2
  • 3
    • 3542998048 scopus 로고    scopus 로고
    • Restoration of transforming growth factor-beta signaling through receptor RI induction by histone deacetylase activity inhibition in breast cancer cells
    • Ammanamanchi S., and Brattain M.G. Restoration of transforming growth factor-beta signaling through receptor RI induction by histone deacetylase activity inhibition in breast cancer cells. J. Biol. Chem. 279 (2004) 32620-32625
    • (2004) J. Biol. Chem. , vol.279 , pp. 32620-32625
    • Ammanamanchi, S.1    Brattain, M.G.2
  • 4
    • 0032568956 scopus 로고    scopus 로고
    • Induction of transforming growth factor-beta receptor type II expression in estrogen receptor-positive breast cancer cells through SP1 activation by 5-aza-2′-deoxycytidine
    • Ammanamanchi S., Kim S.J., Sun L.Z., and Brattain M.G. Induction of transforming growth factor-beta receptor type II expression in estrogen receptor-positive breast cancer cells through SP1 activation by 5-aza-2′-deoxycytidine. J. Biol. Chem. 273 (1998) 16527-16534
    • (1998) J. Biol. Chem. , vol.273 , pp. 16527-16534
    • Ammanamanchi, S.1    Kim, S.J.2    Sun, L.Z.3    Brattain, M.G.4
  • 5
    • 0024792629 scopus 로고
    • Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta
    • Andres J., Stanley K., Cheifetz S., and Massague J. Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta. J. Cell. Biol. 109 (1989) 3137-3145
    • (1989) J. Cell. Biol. , vol.109 , pp. 3137-3145
    • Andres, J.1    Stanley, K.2    Cheifetz, S.3    Massague, J.4
  • 6
    • 0025110119 scopus 로고
    • Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues
    • Bianco P., Fisher L.W., Young M.F., Termine J.D., and Robey P.G. Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues. J. Histochem. Cytochem. 38 (1990) 1549-1563
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1549-1563
    • Bianco, P.1    Fisher, L.W.2    Young, M.F.3    Termine, J.D.4    Robey, P.G.5
  • 8
    • 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., and Fallon J. The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle. J. Cell Biol. 148 (2000) 801-810
    • (2000) J. Cell Biol. , vol.148 , pp. 801-810
    • Bowe, M.1    Mendis, D.2    Fallon, J.3
  • 9
    • 0025913228 scopus 로고
    • The proteoglycan decorin is synthesized and secreted by differentiated myotubes
    • Brandan E., Fuentes M.E., and Andrade W. The proteoglycan decorin is synthesized and secreted by differentiated myotubes. Eur. J. Cell Biol. 55 (1991) 209-216
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 209-216
    • Brandan, E.1    Fuentes, M.E.2    Andrade, W.3
  • 10
    • 0026752005 scopus 로고
    • Decorin, a chondroitin/dermatan sulfate proteoglycan is under neural control in rat skeletal muscle
    • Brandan E., Fuentes M.E., and Andrade W. Decorin, a chondroitin/dermatan sulfate proteoglycan is under neural control in rat skeletal muscle. J. Neurosci. Res. 32 (1992) 51-59
    • (1992) J. Neurosci. Res. , vol.32 , pp. 51-59
    • Brandan, E.1    Fuentes, M.E.2    Andrade, W.3
  • 11
    • 33746987359 scopus 로고    scopus 로고
    • Brandan, E., Retamal, C., Cabello-Verrugio, C., Marzolo, M.P., submitted for publication. The low density lipoprotein receptor-related protein/ 2 macroglobulin receptor functions as an endocytic receptor for decorin. J. Biol. Chem.
  • 13
    • 1942518315 scopus 로고    scopus 로고
    • Transient up-regulation of biglycan during skeletal muscle regeneration: delayed fiber growth along with decorin increase in biglycan-deficient mice
    • Casar J.C., McKechnie B.A., Fallon J.R., Young M.F., and Brandan E. Transient up-regulation of biglycan during skeletal muscle regeneration: delayed fiber growth along with decorin increase in biglycan-deficient mice. Dev. Biol. 268 (2004) 358-371
    • (2004) Dev. Biol. , vol.268 , pp. 358-371
    • Casar, J.C.1    McKechnie, B.A.2    Fallon, J.R.3    Young, M.F.4    Brandan, E.5
  • 14
    • 0027468569 scopus 로고
    • Parallel regulation of procollagen I and colligin, a collagen-binding protein and a member of the serine protease inhibitor family
    • Clarke E., Jain N., Brickenden A., Lorimer I., and Sanwal B. Parallel regulation of procollagen I and colligin, a collagen-binding protein and a member of the serine protease inhibitor family. J. Cell. Biol. 121 (1993) 193-199
    • (1993) J. Cell. Biol. , vol.121 , pp. 193-199
    • Clarke, E.1    Jain, N.2    Brickenden, A.3    Lorimer, I.4    Sanwal, B.5
  • 15
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • Derynck R., and Zhang Y.E. Smad-dependent and Smad-independent pathways in TGF-beta family signalling. Nature 425 (2003) 577-584
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 16
    • 0035918274 scopus 로고    scopus 로고
    • Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation
    • Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., and Miyazono K. Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation. J. Biol. Chem. 276 (2001) 12477-12480
    • (2001) J. Biol. Chem. , vol.276 , pp. 12477-12480
    • Ebisawa, T.1    Fukuchi, M.2    Murakami, G.3    Chiba, T.4    Tanaka, K.5    Imamura, T.6    Miyazono, K.7
  • 17
    • 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 J.L., Vilchis-Landeros M.M., Okadome T., Miyazono K., and Lopez-Casillas F. 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 (2001) 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
  • 19
    • 0022914649 scopus 로고
    • Transforming growth factor-beta. A very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by Buffalo rat liver cells
    • Florini J.R., Roberts A.B., Ewton D.Z., Falen S.L., Flanders K.C., and Sporn M.B. Transforming growth factor-beta. A very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by Buffalo rat liver cells. J. Biol. Chem. 261 (1986) 16509-16513
    • (1986) J. Biol. Chem. , vol.261 , pp. 16509-16513
    • Florini, J.R.1    Roberts, A.B.2    Ewton, D.Z.3    Falen, S.L.4    Flanders, K.C.5    Sporn, M.B.6
  • 20
    • 0027375819 scopus 로고
    • Localization of transforming growth factor beta binding site in betaglycan. Comparison with small extracellular matrix proteoglycans
    • Fukushima D., Butzow R., Hildebrand A., and Ruoslahti E. Localization of transforming growth factor beta binding site in betaglycan. Comparison with small extracellular matrix proteoglycans. J. Biol. Chem. 268 (1993) 22710-22715
    • (1993) J. Biol. Chem. , vol.268 , pp. 22710-22715
    • Fukushima, D.1    Butzow, R.2    Hildebrand, A.3    Ruoslahti, E.4
  • 21
    • 0037170462 scopus 로고    scopus 로고
    • Antagonism of activin by inhibin and inhibin receptors: a functional role for betaglycan
    • Gray P., Bilezikjian L., and Vale W. Antagonism of activin by inhibin and inhibin receptors: a functional role for betaglycan. Mol. Cell. Endocrinol. 188 (2002) 254-260
    • (2002) Mol. Cell. Endocrinol. , vol.188 , pp. 254-260
    • Gray, P.1    Bilezikjian, L.2    Vale, W.3
  • 24
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta
    • Hildebrand A., Romaris M., Rasmussen L.M., Heinegard D., Twardzik D.R., Border W.A., and Ruoslahti E. Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. Biochem. J. 302 (1994) 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
  • 25
    • 0030986608 scopus 로고    scopus 로고
    • The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth
    • Iozzo R.V. The family of the small leucine-rich proteoglycans: key regulators of matrix assembly and cellular growth. Crit. Rev. Biochem. Mol. Biol. 32 (1997) 141-174
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 141-174
    • Iozzo, R.V.1
  • 26
    • 0027293284 scopus 로고
    • Expression of hepatocyte growth factor in growing and regenerating rat skeletal muscle
    • Jennische E., Ekberg S., and Matejka G. Expression of hepatocyte growth factor in growing and regenerating rat skeletal muscle. Am. J. Physiol. 265 (1993) C122-C128
    • (1993) Am. J. Physiol. , vol.265
    • Jennische, E.1    Ekberg, S.2    Matejka, G.3
  • 27
    • 0034517389 scopus 로고    scopus 로고
    • Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation
    • Kavsak P., Rasmussen R.K., Causing C.G., Bonni S., Zhu H., Thomsen G.H., and Wrana J.L. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol. Cell 6 (2000) 1365-1375
    • (2000) Mol. Cell , vol.6 , pp. 1365-1375
    • Kavsak, P.1    Rasmussen, R.K.2    Causing, C.G.3    Bonni, S.4    Zhu, H.5    Thomsen, G.H.6    Wrana, J.L.7
  • 28
    • 0030965611 scopus 로고    scopus 로고
    • Processing of the transforming growth factor beta type I and II receptors. Biosynthesis and ligand-induced regulation
    • Koli K.M., and Arteaga C.L. Processing of the transforming growth factor beta type I and II receptors. Biosynthesis and ligand-induced regulation. J. Biol. Chem. 272 (1997) 6423-6427
    • (1997) J. Biol. Chem. , vol.272 , pp. 6423-6427
    • Koli, K.M.1    Arteaga, C.L.2
  • 29
    • 0018850985 scopus 로고
    • A simple, rapid, and sensitive DNA assay procedure
    • Labarca C., and Paigen K. A simple, rapid, and sensitive DNA assay procedure. Anal. Biochem. 102 (1980) 344-352
    • (1980) Anal. Biochem. , vol.102 , pp. 344-352
    • Labarca, C.1    Paigen, K.2
  • 30
    • 0033610858 scopus 로고    scopus 로고
    • Syndecan-1 expression inhibits myoblast differentiation through a basic fibroblast growth factor-dependent mechanism
    • Larrain J., Carey D.J., and Brandan E. Syndecan-1 expression inhibits myoblast differentiation through a basic fibroblast growth factor-dependent mechanism. J. Biol. Chem. 273 (1998) 32288-32296
    • (1998) J. Biol. Chem. , vol.273 , pp. 32288-32296
    • Larrain, J.1    Carey, D.J.2    Brandan, E.3
  • 31
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • Le Roy C., and Wrana J.L. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev., Mol. Cell Biol. 6 (2005) 112-126
    • (2005) Nat. Rev., Mol. Cell Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 32
    • 0035947646 scopus 로고    scopus 로고
    • Differential functions of members of the low density lipoprotein receptor family suggested by their distinct endocytosis rates
    • Li Y., Lu W., Marzolo M.P., and Bu G. Differential functions of members of the low density lipoprotein receptor family suggested by their distinct endocytosis rates. J. Biol. Chem. 276 (2001) 18000-18006
    • (2001) J. Biol. Chem. , vol.276 , pp. 18000-18006
    • Li, Y.1    Lu, W.2    Marzolo, M.P.3    Bu, G.4
  • 33
    • 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 B.M., Chan Y., Prisk V., Tang Y., Cummins J., and Huard J. 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 (2004) 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
  • 34
    • 0033257926 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of TGF-beta-activated smad2
    • Lo R.S., and Massague J. Ubiquitin-dependent degradation of TGF-beta-activated smad2. Nat. Cell Biol. 1 (1999) 472-478
    • (1999) Nat. Cell Biol. , vol.1 , pp. 472-478
    • Lo, R.S.1    Massague, J.2
  • 35
    • 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 J.L., Lane W.S., and Massague J. Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system. Cell 67 (1991) 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
  • 36
    • 0027976511 scopus 로고
    • Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites
    • Lopez-Casillas F., Payne H.M., Andres J.L., and Massague J. Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites. J. Cell. Biol. 124 (1994) 557-568
    • (1994) J. Cell. Biol. , vol.124 , pp. 557-568
    • Lopez-Casillas, F.1    Payne, H.M.2    Andres, J.L.3    Massague, J.4
  • 38
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague J. TGF-beta signal transduction. Annu. Rev. Biochem. 67 (1998) 753-791
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 39
    • 0034644472 scopus 로고    scopus 로고
    • TGFbeta signaling in growth control, cancer, and heritable disorders
    • Massague J., Blain S., and Lo R. TGFbeta signaling in growth control, cancer, and heritable disorders. Cell 103 (2000) 295-309
    • (2000) Cell , vol.103 , pp. 295-309
    • Massague, J.1    Blain, S.2    Lo, R.3
  • 40
  • 41
    • 0027379217 scopus 로고
    • Localisation of transforming growth factor beta 1 in developing muscles: implications for connective tissue and fiber type pattern formation
    • McLennan I.S. Localisation of transforming growth factor beta 1 in developing muscles: implications for connective tissue and fiber type pattern formation. Dev. Dyn. 197 (1993) 281-290
    • (1993) Dev. Dyn. , vol.197 , pp. 281-290
    • McLennan, I.S.1
  • 42
    • 0032543988 scopus 로고    scopus 로고
    • The non-synaptic expression of transforming growth factor-beta 2 is neurally regulated and varies between skeletal muscle fibre types
    • McLennan I.S., Koishi K., Zhang M., and Murakami N. The non-synaptic expression of transforming growth factor-beta 2 is neurally regulated and varies between skeletal muscle fibre types. Neuroscience 87 (1998) 845-853
    • (1998) Neuroscience , vol.87 , pp. 845-853
    • McLennan, I.S.1    Koishi, K.2    Zhang, M.3    Murakami, N.4
  • 43
    • 0029823186 scopus 로고    scopus 로고
    • Extracellular matrix is required for skeletal muscle differentiation but not myogenin expression
    • Melo F., Carey D.J., and Brandan E. Extracellular matrix is required for skeletal muscle differentiation but not myogenin expression. J. Cell. Biochem. 62 (1996) 227-239
    • (1996) J. Cell. Biochem. , vol.62 , pp. 227-239
    • Melo, F.1    Carey, D.J.2    Brandan, E.3
  • 45
    • 0036086733 scopus 로고    scopus 로고
    • ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression
    • Osses N., and Brandan E. ECM is required for skeletal muscle differentiation independently of muscle regulatory factor expression. Am. J. Physiol., Cell Physiol. 282 (2002) C383-C394
    • (2002) Am. J. Physiol., Cell Physiol. , vol.282
    • Osses, N.1    Brandan, E.2
  • 46
    • 0033135695 scopus 로고    scopus 로고
    • Ectodomain cleavage and shedding of the type III transforming growth factor-beta receptor in lung membranes effect of temperature, ligand binding and membrane solubilization
    • Philip A., Hannah R., and O'Connor-McCourt M.D. Ectodomain cleavage and shedding of the type III transforming growth factor-beta receptor in lung membranes effect of temperature, ligand binding and membrane solubilization. Eur. J. Biochem. 261 (1999) 618-628
    • (1999) Eur. J. Biochem. , vol.261 , pp. 618-628
    • Philip, A.1    Hannah, R.2    O'Connor-McCourt, M.D.3
  • 47
    • 0032763469 scopus 로고    scopus 로고
    • Specificity, diversity, and regulation in TGF-beta superfamily signaling
    • Piek E., Heldin C., and Ten Dijke P. Specificity, diversity, and regulation in TGF-beta superfamily signaling. FASEB J. 13 (1999) 2105-2124
    • (1999) FASEB J. , vol.13 , pp. 2105-2124
    • Piek, E.1    Heldin, C.2    Ten Dijke, P.3
  • 48
    • 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 J.D., Merriam A.P., Leahy P., Gong B., Feuerman J., Cheng G., and Khanna S. 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 (2004) 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
  • 49
    • 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 J.P., Kresse H., and Brandan E. Antisense inhibition of decorin expression in myoblasts decreases cell responsiveness to transforming growth factor beta and accelerates skeletal muscle differentiation. J. Biol. Chem. 276 (2001) 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
  • 50
    • 0033974649 scopus 로고    scopus 로고
    • The adaptive response of transforming growth factor-beta 2 and-beta RII in the overloaded, regenerating and denervated muscles of rats
    • Sakuma K., Watanabe K., Sano M., Kitajima S., Sakamoto K., Uramoto I., and Totsuka T. The adaptive response of transforming growth factor-beta 2 and-beta RII in the overloaded, regenerating and denervated muscles of rats. Acta Neuropathol. (Berl.) 99 (2000) 177-185
    • (2000) Acta Neuropathol. (Berl.) , vol.99 , pp. 177-185
    • Sakuma, K.1    Watanabe, K.2    Sano, M.3    Kitajima, S.4    Sakamoto, K.5    Uramoto, I.6    Totsuka, T.7
  • 51
    • 0037832412 scopus 로고    scopus 로고
    • The basement membrane/basal lamina of skeletal muscle
    • Sanes J.R. The basement membrane/basal lamina of skeletal muscle. J. Biol. Chem. 278 (2003) 12601-12604
    • (2003) J. Biol. Chem. , vol.278 , pp. 12601-12604
    • Sanes, J.R.1
  • 52
    • 33746941572 scopus 로고    scopus 로고
    • Santander, C., and Brandan, E., in press. Betaglycan induces TGF-beta signaling in a ligand-independent manner, through activation of the p38 pathway. Cell Signal.
  • 53
    • 0032006325 scopus 로고    scopus 로고
    • HGF/SF is present in normal adult skeletal muscle and is capable of activating satellite cells
    • Tatsumi R., Anderson J., Nevoret C., Halevy O., and Allen R. HGF/SF is present in normal adult skeletal muscle and is capable of activating satellite cells. Dev. Biol. 194 (1998) 114-128
    • (1998) Dev. Biol. , vol.194 , pp. 114-128
    • Tatsumi, R.1    Anderson, J.2    Nevoret, C.3    Halevy, O.4    Allen, R.5
  • 54
    • 33745830812 scopus 로고    scopus 로고
    • Transforming growth factor β signaling is regulated by electrical activity in skeletal muscle cells: TGF-β type I receptor is transciptionally regulated by myotubes excitability
    • Ugarte G., and Brandan E. Transforming growth factor β signaling is regulated by electrical activity in skeletal muscle cells: TGF-β type I receptor is transciptionally regulated by myotubes excitability. J. Biol. Chem. (2006) 281
    • (2006) J. Biol. Chem. , pp. 281
    • Ugarte, G.1    Brandan, E.2
  • 55
    • 1542289879 scopus 로고    scopus 로고
    • The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1
    • Velasco-Loyden G., Arribas J., and Lopez-Casillas F. The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1. J. Biol. Chem. 279 (2004) 7721-7733
    • (2004) J. Biol. Chem. , vol.279 , pp. 7721-7733
    • Velasco-Loyden, G.1    Arribas, J.2    Lopez-Casillas, F.3
  • 56
    • 0030967203 scopus 로고    scopus 로고
    • Biosynthesis of the type I and type II TGF-beta receptors. Implications for complex formation
    • Wells R.G., Yankelev H., Lin H.Y., and Lodish H.F. Biosynthesis of the type I and type II TGF-beta receptors. Implications for complex formation. J. Biol. Chem. 272 (1997) 11444-11451
    • (1997) J. Biol. Chem. , vol.272 , pp. 11444-11451
    • Wells, R.G.1    Yankelev, H.2    Lin, H.Y.3    Lodish, H.F.4
  • 58
    • 0017759258 scopus 로고
    • Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle
    • Yaffe D., and Saxel O. Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature 270 (1977) 725-727
    • (1977) Nature , vol.270 , pp. 725-727
    • Yaffe, D.1    Saxel, O.2
  • 59
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-beta by the proteoglycan decorin
    • Yamaguchi Y., Mann D., and Ruoslahti E. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature 346 (1990) 281-284
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.2    Ruoslahti, E.3


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