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Volumn 92, Issue 1, 2012, Pages 1-10

Review: The skeletal muscle extracellular matrix: Possible roles in the regulation of muscle development and growth

Author keywords

Extracellular matrix; Integrins; Muscle; Proteoglycans; Signal transduction

Indexed keywords


EID: 84860998689     PISSN: 00083984     EISSN: 19181825     Source Type: Journal    
DOI: 10.4141/cjas2011-098     Document Type: Review
Times cited : (15)

References (107)
  • 1
    • 0024580644 scopus 로고
    • Regulation of skeletal muscle satellite cell proliferation and differentiation by transforming growth factor-beta, insulin-like growth factor I, and fibroblast growth factor
    • Allen, R. E. and Boxhorn, L. K. 1989. Regulation of skeletal muscle satellite cell proliferation and differentiation by transforming growth factor-beta, insulin-like growth factor I, and fibroblast growth factor. J. Cell Physiol. 138: 311-315.
    • (1989) J. Cell Physiol. , vol.138 , pp. 311-315
    • Allen, R.E.1    Boxhorn, L.K.2
  • 2
    • 0028792161 scopus 로고
    • Hepatocyte growth factor activates quiescent skeletal muscle satellite cells in vitro
    • Allen, R. E., Sheehan, S. M., Taylor, R. G., Kendall, T. L. and Rice, G. M. 1995. Hepatocyte growth factor activates quiescent skeletal muscle satellite cells in vitro. J. Cell Physiol. 165: 307-312.
    • (1995) J. Cell Physiol. , vol.165 , pp. 307-312
    • Allen, R.E.1    Sheehan, S.M.2    Taylor, R.G.3    Kendall, T.L.4    Rice, G.M.5
  • 3
    • 46649120323 scopus 로고    scopus 로고
    • The ins and outs of syntenin, a multifunctional intracellular adaptor protein
    • Beekman, J. M. and Coffer, P. J. 2008. The ins and outs of syntenin, a multifunctional intracellular adaptor protein. J. Cell Sci. 121: 1349-1355.
    • (2008) J. Cell Sci. , vol.121 , pp. 1349-1355
    • Beekman, J.M.1    Coffer, P.J.2
  • 4
    • 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. 1990. Expression and localization of the two small proteoglycans biglycan and decorin in developing human skeletal and non-skeletal tissues. J. Histochem. Cytochem. 38: 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
  • 5
    • 57349141863 scopus 로고    scopus 로고
    • Mda9/Syntenin promotes metastasis in human melanoma cells by activating c-Src
    • Boukerche, H., Su, Z. Z., Prevot, C., Sarkar, D. and Fisher, P. B. 2008. Mda9/Syntenin promotes metastasis in human melanoma cells by activating c-Src. Proc. Natl. Acad. Sci. USA 105: 15914-15919.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15914-15919
    • Boukerche, H.1    Su, Z.Z.2    Prevot, C.3    Sarkar, D.4    Fisher, P.B.5
  • 6
    • 0026752005 scopus 로고
    • Decorin, a chondroitin/dermatan sulfate sproteoglycan is under neural control in rat skeletal muscle
    • Brandan, E., Fiemtes, M. E. and Andrade, W. 1992. Decorin, a chondroitin/dermatan sulfate sproteoglycan is under neural control in rat skeletal muscle. J. Neurosci. Res. 32: 51-59.
    • (1992) J. Neurosci. Res. , vol.32 , pp. 51-59
    • Brandan, E.1    Fiemtes, M.E.2    Andrade, W.3
  • 7
    • 0000052968 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans during terminal skeletal muscle differentiation Possible functions and regulation of their expression
    • Brandan, E. and Larraín, J. 1998. Heparan sulfate proteoglycans during terminal skeletal muscle differentiation. Possible functions and regulation of their expression. Basic Appl. Myol. 8: 107-113.
    • (1998) Basic Appl. Myol. , vol.8 , pp. 107-113
    • Brandan, E.1    Larraín, J.2
  • 8
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein, LRP, functions as an endocytic receptor for decorin
    • Brandan, E., Retamal, C., Cabello-Verrugio, C. and Marzolo, M. P. 2006. The low density lipoprotein receptor-related protein, LRP, 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
  • 9
    • 0025909860 scopus 로고
    • Transforming growth factor beta represses the action of myogenin through a mechanism independent of DNA binding
    • Brennan, T. J., Edmondson, D. G., Li, L. and Olson, E. N. 1991. Transforming growth factor beta represses the action of myogenin through a mechanism independent of DNA binding. Proc. Natl. Acad. Sci. USA 88: 3822-3826.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3822-3826
    • Brennan, T.J.1    Edmondson, D.G.2    Li, L.3    Olson, E.N.4
  • 10
    • 34547131835 scopus 로고    scopus 로고
    • A novel modulatory mechanism of transforming growth factor-beta signaling through decorin and LRP-1
    • Cabello-Verrugio, C. and 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
  • 12
    • 0027168757 scopus 로고
    • A lipid anchored heparan sulfate proteoglycan is present in the surface of differentiated skeletal muscle cells Isolation and biochemical characterization
    • Campos, A., Nuǔez, R., Koenig, C. S., Carey, D. J. and Brandan, E. 1993. A lipid anchored heparan sulfate proteoglycan is present in the surface of differentiated skeletal muscle cells. Isolation and biochemical characterization. Eur. J. Biochem. 216: 587-595.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 587-595
    • Campos, A.1    Nuǔez, R.2    Koenig, C.S.3    Carey, D.J.4    Brandan, E.5
  • 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. 2004. Transient up-regulation of biglycan during skeletal muscle regeneration: delayed fiber growth along with decorin increase in biglycan-deficient mice. Dev. Biol. 268: 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
    • 1942501852 scopus 로고    scopus 로고
    • Syndecan-2 regulates transforming growth factor-beta signaling
    • Chen, L., Klass, C. and Woods, A. 2004. Syndecan-2 regulates transforming growth factor-beta signaling. J. Biol. Chem. 279: 15715-15718.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15715-15718
    • Chen, L.1    Klass, C.2    Woods, A.3
  • 15
    • 79952107602 scopus 로고    scopus 로고
    • Syndecans as cell surface receptors: Unique structure equates with functional diversity
    • Choi, Y., Chung, H., Jung, H., Couchman, J. R. and Oh, E-S. 2011. Syndecans as cell surface receptors: Unique structure equates with functional diversity. Matrix Biol. 30: 93-99.
    • (2011) Matrix Biol , vol.30 , pp. 93-99
    • Choi, Y.1    Chung, H.2    Jung, H.3    Couchman, J.R.4    Oh, E.-S.5
  • 16
    • 0035018302 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans control the response of renal interstitial fibroblasts to fibroblast growth factor-2
    • Clayton, A., Thomas, J., Thomas, G. J., Davies, M. and Steadman, R. 2001. Cell surface heparan sulfate proteoglycans control the response of renal interstitial fibroblasts to fibroblast growth factor-2. Kidney Int. 59: 2084-2094.
    • (2001) Kidney Int , vol.59 , pp. 2084-2094
    • Clayton, A.1    Thomas, J.2    Thomas, G.J.3    Davies, M.4    Steadman, R.5
  • 17
    • 0035503877 scopus 로고    scopus 로고
    • Syndecan-3 and syndecan-4 specifically mark skeletal muscle satellite cells and are implicated in satellite cell maintenance and muscle regeneration
    • Cornelison, D. D., Filla, M. S., Stanley, H. M., Rapraeger, A. C. and Olwin, B. B. 2001. Syndecan-3 and syndecan-4 specifically mark skeletal muscle satellite cells and are implicated in satellite cell maintenance and muscle regeneration. Dev. Biol. 239: 79-94.
    • (2001) Dev. Biol. , vol.239 , pp. 79-94
    • Cornelison, D.D.1    Filla, M.S.2    Stanley, H.M.3    Rapraeger, A.C.4    Olwin, B.B.5
  • 18
    • 4444240885 scopus 로고    scopus 로고
    • Essential and separable roles for syndecan-3 and syndecan-4 in skeletal muscle development and regeneration
    • Cornelison, D. D., Wilcox-Adelman, S. A., Goetinck, P. F., Rauvala, H., Rapraeger, A. C. and Olwin, B. B. 2004. Essential and separable roles for syndecan-3 and syndecan-4 in skeletal muscle development and regeneration. Gens Dev. 18: 2231-2236.
    • (2004) Gens Dev , vol.18 , pp. 2231-2236
    • Cornelison, D.D.1    Wilcox-Adelman, S.A.2    Goetinck, P.F.3    Rauvala, H.4    Rapraeger, A.C.5    Olwin, B.B.6
  • 19
    • 0031044872 scopus 로고    scopus 로고
    • Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
    • Danielson, K. G., Baribault, H., Holmes, D. F., Graham, H., Kadler, K. E. and Iozzo, R. V. 1997. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 136: 729-743.
    • (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
  • 20
    • 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. and Iozzo R. V. 1996. Decorin-induced growth suppression is associated with up-regulation of p21, an inhibitor of cyclin dependent kinases. J. Biol. Chem. 271: 18961-18965.
    • (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
  • 21
    • 4444347398 scopus 로고    scopus 로고
    • Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor
    • Deepa, S. S., Yamada, S., Zako, M., Goldberg, O. and Sughara, K. 2004. Chondroitin sulfate chains on syndecan-1 and syndecan-4 from normal murine mammary gland epithelial cells are structurally and functionally distinct and cooperate with heparan sulfate chains to bind growth factors. A novel function to control binding of midkine, pleiotrophin, and basic fibroblast growth factor. J. Biol. Chem. 279: 37368-37376.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37368-37376
    • Deepa, S.S.1    Yamada, S.2    Zako, M.3    Goldberg, O.4    Sughara, K.5
  • 22
    • 0037082492 scopus 로고    scopus 로고
    • Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor binding and promotes Met signaling in multiple myeloma
    • Derksen, P. W., Keehnen, R. M., Evers, L. M., van Oers, M. H., Spaargaren, M. and Pals, S. T. 2002. Cell surface proteoglycan syndecan-1 mediates hepatocyte growth factor binding and promotes Met signaling in multiple myeloma. Blood 99: 1405-1410.
    • (2002) Blood , vol.99 , pp. 1405-1410
    • Derksen, P.W.1    Keehnen, R.M.2    Evers, L.3    van Oers, M.4    Spaargaren, M.H.M.5    Pals, S.T.6
  • 23
    • 33746918654 scopus 로고    scopus 로고
    • PKC alphadependent activation of RhoA by syndecan-4 during focal adhesion formation
    • Dovas, A., Yoneda, A. and Couchman, J. R. 2006. PKC alphadependent activation of RhoA by syndecan-4 during focal adhesion formation. J. Cell Sci. 119: 2837-2846.
    • (2006) J. Cell Sci. , vol.119 , pp. 2837-2846
    • Dovas, A.1    Yoneda, A.2    Couchman, J.R.3
  • 24
    • 33747015300 scopus 로고    scopus 로고
    • Extracellular matrix proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation
    • Drougett, R., Cabello-Verrugio, C., Riquelme, C. and Brandan, E. 2006. Extracellular matrix proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation. Matrix Biol. 25: 332-341.
    • (2006) Matrix Biol , vol.25 , pp. 332-341
    • Drougett, R.1    Cabello-Verrugio, C.2    Riquelme, C.3    Brandan, E.4
  • 26
    • 0028268324 scopus 로고
    • Decorin and a large dermatan sulfate proteoglycan in bovine striated muscle
    • Eggen, K. H., Malstrøm, A. and Kolset, S. O 1994. Decorin and a large dermatan sulfate proteoglycan in bovine striated muscle. Biochem. Biophys. Acta 12: 287-297.
    • (1994) Biochem. Biophys. Acta , vol.12 , pp. 287-297
    • Eggen, K.H.1    Malstrøm, A.2    Kolset, S.O.3
  • 28
    • 0034695918 scopus 로고    scopus 로고
    • Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase
    • Fitzgerald, M. L., Wang, Z., Park, P. W., Murphy, G. and Bernfield, M. 2000. Shedding of syndecan-1 and -4 ectodomains is regulated by multiple signaling pathways and mediated by a TIMP-3-sensitive metalloproteinase. J. Cell Biol. 148: 811-824.
    • (2000) J. Cell Biol. , vol.148 , pp. 811-824
    • Fitzgerald, M.L.1    Wang, Z.2    Park, P.W.3    Murphy, G.4    Bernfield, M.5
  • 29
    • 0025836395 scopus 로고
    • Insulin-like growth factor-I stimulates terminal myogenic differentiation by induction of myogenin gene expression
    • Florini, J. R., Ewton, D. Z. and Roof, S. L. 1991. Insulin-like growth factor-I stimulates terminal myogenic differentiation by induction of myogenin gene expression. Mol. Endocrinol. 5: 718-724.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 718-724
    • Florini, J.R.1    Ewton, D.Z.2    Roof, S.L.3
  • 30
    • 0021873617 scopus 로고
    • Insulin-like growth factors and insulin: comparative aspects
    • Froesch, E. R. and Zapf, J. 1985. Insulin-like growth factors and insulin: comparative aspects. Diabetologia 28: 485-493.
    • (1985) Diabetologia , vol.28 , pp. 485-493
    • Froesch, E.R.1    Zapf, J.2
  • 31
    • 0033621470 scopus 로고    scopus 로고
    • Antisense inhibition of syndecan-3 expression during skeletal muscle differentiation accelerates myogenesis through a basic fibroblast growth factor-dependent mechanism
    • Fuentealba, L., Carey, D. J. and Brandan, E. 1999. Antisense inhibition of syndecan-3 expression during skeletal muscle differentiation accelerates myogenesis through a basic fibroblast growth factor-dependent mechanism. J. Biol. Chem. 274: 37876-37884.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37876-37884
    • Fuentealba, L.1    Carey, D.J.2    Brandan, E.3
  • 36
    • 0031001002 scopus 로고    scopus 로고
    • Enhancement of migration by protein kinase Calpha and inhibition of proliferation and cell cycle progression by protein kinase C delta in capillary endothelial cells
    • Harrington, E. O., Loffler, J., Nelson, P. R., Kent, K. C., Simons, M. and Ware, J. A. 1997. Enhancement of migration by protein kinase Calpha and inhibition of proliferation and cell cycle progression by protein kinase C delta in capillary endothelial cells. J. Biol. Chem. 272: 7390-7397.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7390-7397
    • Harrington, E.O.1    Loffler, J.2    Nelson, P.R.3    Kent, K.C.4    Simons, M.5    Ware, J.A.6
  • 38
    • 0027984873 scopus 로고
    • Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta
    • Hildebrand, A., Romarís, M., Rasmussen, L. M., Heinegård, D., Twadzik, D. R., Border, W. A. and 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    Romarís, M.2    Rasmussen, L.M.3    Heinegård, D.4    Twadzik, D.R.5    Border, W.A.6    Ruoslahti, E.7
  • 39
    • 0032080332 scopus 로고    scopus 로고
    • Regulation of syndecan-4 phosphorylation in vivo
    • Horowitz, A. and Simons, M. 1998a. Regulation of syndecan-4 phosphorylation in vivo. J. Biol. Chem. 273: 10914-10918.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10914-10918
    • Horowitz, A.1    Simons, M.2
  • 40
    • 0032475975 scopus 로고    scopus 로고
    • Phosphorylation of the cytoplasmic tail of syndecan-4 regulates activation of protein kinase C alpha
    • Horowitz, A. and Simons, M. 1998b. Phosphorylation of the cytoplasmic tail of syndecan-4 regulates activation of protein kinase C alpha. J. Biol. Chem. 273: 25548-25551.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25548-25551
    • Horowitz, A.1    Simons, M.2
  • 41
    • 0033619730 scopus 로고    scopus 로고
    • Phosphatidylinositol-4 5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C
    • Horwitz, A., Murakami, M., Gao, Y. and Simons, M. 1999. Phosphatidylinositol-4,5-bisphosphate mediates the interaction of syndecan-4 with protein kinase C. Biochemistry 38: 15871-15877.
    • (1999) Biochemistry , vol.38 , pp. 15871-15877
    • Horwitz, A.1    Murakami, M.2    Gao, Y.3    Simons, M.4
  • 42
    • 0033516558 scopus 로고    scopus 로고
    • The biology of the small leucine-rich proteoglycans Functional network of interactive proteins
    • Iozzo, R. V. 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
  • 43
    • 80053402608 scopus 로고    scopus 로고
    • Decorin antagonizes IGF-IR function by interfering with IGF-IR activity and attenuating downstream signaling
    • (in press), doi: 10.1074/jbc.M111. 262766
    • Iozzo, R. V., Buraschi, S., Genua, M., Xu, S-Q., Solomide, C. C., Peiper, S. C., Gomella, L. G., Owens, R. C. and Morrione, A. 2011. Decorin antagonizes IGF-IR function by interfering with IGF-IR activity and attenuating downstream signaling. J. Biol. Chem. (in press) doi: 10.1074/jbc.M111. 262766.
    • (2011) J. Biol. Chem.
    • Iozzo, R.V.1    Buraschi, S.2    Genua, M.3    Xu, S.-Q.4    Solomide, C.C.5    Peiper, S.C.6    Gomella, L.G.7    Owens, R.C.8    Morrione, A.9
  • 44
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • Iozzo, R. V. and 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
  • 45
    • 34547643210 scopus 로고    scopus 로고
    • PDZ domains: folding and binding
    • Jemth, P. and Gianni, S. 2007. PDZ domains: folding and binding. Biochemistry 46: 8701-8708.
    • (2007) Biochemistry , vol.46 , pp. 8701-8708
    • Jemth, P.1    Gianni, S.2
  • 46
    • 0035366676 scopus 로고    scopus 로고
    • Rat embryo fibroblasts require both the cell-binding and the heparin-binding domains of fibronectin for survival
    • Jeong, J., Han, I., Lim, Y., Kim, J., Park, I., Woods, A., Couchman, J. R. and Oh, E. S. 2001. Rat embryo fibroblasts require both the cell-binding and the heparin-binding domains of fibronectin for survival. Biochem. J. 356: 531-537.
    • (2001) Biochem. J. , vol.356 , pp. 531-537
    • Jeong, J.1    Han, I.2    Lim, Y.3    Kim, J.4    Park, I.5    Woods, A.6    Couchman, J.R.7    Oh, E.S.8
  • 47
    • 0030818314 scopus 로고    scopus 로고
    • Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle
    • Kambadur, R., Sharma, M., Smith, T. P. and Bass, J. J. 1997. Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle. Genome Res. 7: 910-916.
    • (1997) Genome Res , vol.7 , pp. 910-916
    • Kambadur, R.1    Sharma, M.2    Smith, T.P.3    Bass, J.J.4
  • 48
    • 0032985184 scopus 로고    scopus 로고
    • Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase
    • Kan, M., Wu, X., Wang, F. and McKeehan, W. L. 1999. Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase. J. Biol. Chem. 274: 15947-15952.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15947-15952
    • Kan, M.1    Wu, X.2    Wang, F.3    McKeehan, W.L.4
  • 49
    • 79953182314 scopus 로고    scopus 로고
    • Insulin-like growth factor-I: vitronectin complex-induced changes in gene expression effect breast cell survival and migration
    • Kashyap, A. S., Hollier, B. G., Manton, K. J., Satyamoorthy, K., Leavesley, D. I. and Upton, Z. 2011. Insulin-like growth factor-I: vitronectin complex-induced changes in gene expression effect breast cell survival and migration. Endocrinology 152: 1388-1401.
    • (2011) Endocrinology , vol.152 , pp. 1388-1401
    • Kashyap, A.S.1    Hollier, B.G.2    Manton, K.J.3    Satyamoorthy, K.4    Leavesley, D.I.5    Upton, Z.6
  • 50
    • 17644368573 scopus 로고    scopus 로고
    • Interleukin-6: from basic science to medicine-40 years in immunology
    • Kishimoto, T. 2005. Interleukin-6: from basic science to medicine-40 years in immunology. Annu. Rev. Immunol. 23: 1-21.
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 1-21
    • Kishimoto, T.1
  • 51
    • 42949096004 scopus 로고    scopus 로고
    • Decorin enhances the proliferation and differentiation of myogenic cells through suppressing myostatin activity
    • Kishioka, Y., Thomas, T., Wakamatsu, J., Hattori, A., Sharma, M., Kambadur, R. and Nishimura, T. 2008. Decorin enhances the proliferation and differentiation of myogenic cells through suppressing myostatin activity. J. Cell Physiol. 215: 856-867.
    • (2008) J. Cell Physiol. , vol.215 , pp. 856-867
    • Kishioka, Y.1    Thomas, T.2    Wakamatsu, J.3    Hattori, A.4    Sharma, M.5    Kambadur, R.6    Nishimura, T.7
  • 52
  • 53
    • 0037661129 scopus 로고    scopus 로고
    • Structural and functional evidence for the interaction of insulin-like growth factors (IGFs) and IGF binding proteins with vitronectin
    • Kricker, J. A., Towne, C. L., Firth, S. M., Herington, A. C. and Upton, Z. 2003. Structural and functional evidence for the interaction of insulin-like growth factors (IGFs) and IGF binding proteins with vitronectin. Endocrinology 144: 2807-2815.
    • (2003) Endocrinology , vol.144 , pp. 2807-2815
    • Kricker, J.A.1    Towne, C.L.2    Firth, S.M.3    Herington, A.C.4    Upton, Z.5
  • 54
    • 0033610858 scopus 로고    scopus 로고
    • Syndecan-1 expression inhibits myoblast differentiation through basic fibroblast growth factor-dependent mechanisms
    • Larraín, J., Carey, D. J. and Brandan, E. 1998. Syndecan-1 expression inhibits myoblast differentiation through basic fibroblast growth factor-dependent mechanisms. J. Biol. Chem. 273: 32288-32296.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32288-32296
    • Larraín, J.1    Carey, D.J.2    Brandan, E.3
  • 55
    • 0030745802 scopus 로고    scopus 로고
    • Syndecan-1 expression is down-regulated during myoblast terminal differentiation Modulation by growth factors and retinoic acid
    • Larraín, J., Cizmeci-Smith, G., Troncoso, V., Stahl, R. C., Carey, D. J. and Brandan, E. 1997. Syndecan-1 expression is down-regulated during myoblast terminal differentiation. Modulation by growth factors and retinoic acid. J. Biol. Chem. 272: 18418-18424.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18418-18424
    • Larraín, J.1    Cizmeci-Smith, G.2    Troncoso, V.3    Stahl, R.C.4    Carey, D.J.5    Brandan, E.6
  • 56
    • 0032557438 scopus 로고    scopus 로고
    • Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4 5-bisphosphate
    • Lee, D., Oh, E. S., Woods, A., Couchman, J. R. and Lee, W. 1998. Solution structure of a syndecan-4 cytoplasmic domain and its interaction with phosphatidylinositol 4, 5-bisphosphate. J. Biol. Chem. 273: 13022-13029.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13022-13029
    • Lee, D.1    Oh, E.S.2    Woods, A.3    Couchman, J.R.4    Lee, W.5
  • 57
    • 63249091298 scopus 로고    scopus 로고
    • Effect of transforming growth factor-beta 1 on decorin expression and muscle morphology during chicken embryonic and posthatch growth and development
    • Li, X. and Velleman, S. G. 2009. Effect of transforming growth factor-beta 1 on decorin expression and muscle morphology during chicken embryonic and posthatch growth and development. Poult. Sci. 88: 387-397.
    • (2009) Poult. Sci. , vol.88 , pp. 387-397
    • Li, X.1    Velleman, S.G.2
  • 58
    • 33645734748 scopus 로고    scopus 로고
    • Effect of transforming growth factor-beta on decorin and beta 1 integrin expression during muscle development in chickens
    • Li, X., McFarland, D. C. and Velleman, S. G. 2006. Effect of transforming growth factor-beta on decorin and beta 1 integrin expression during muscle development in chickens. Poult. Sci. 85: 326-332.
    • (2006) Poult. Sci. , vol.85 , pp. 326-332
    • Li, X.1    McFarland, D.C.2    Velleman, S.G.3
  • 59
    • 50949104049 scopus 로고    scopus 로고
    • Extracellular matrix proteoglycan decorin-mediated myogenic satellite cell responsiveness to transforming growth factor-beta 1 during cell proliferation and differentiation Decorin and transforming growth factor-beta 1 in satellite cells
    • Li, X., McFarland, D. C. and Velleman, S. G. 2008. Extracellular matrix proteoglycan decorin-mediated myogenic satellite cell responsiveness to transforming growth factor-beta 1 during cell proliferation and differentiation. Decorin and transforming growth factor-beta 1 in satellite cells. Domest. Anim. Endocrinol. 35: 263-273.
    • (2008) Domest. Anim. Endocrinol. , vol.35 , pp. 263-273
    • Li, X.1    McFarland, D.C.2    Velleman, S.G.3
  • 60
    • 0032841757 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development
    • Lin, X., Buff, E. M., Perrimon, N. and Michelson, A. M. 1999. Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development. Development 126: 3715-3723.
    • (1999) Development , vol.126 , pp. 3715-3723
    • Lin, X.1    Buff, E.M.2    Perrimon, N.3    Michelson, A.M.4
  • 61
    • 33645973587 scopus 로고    scopus 로고
    • Differential expression of membrane-associated heparan sulfate proteoglycans in the skeletal muscle of turkeys with different growth rates
    • Liu, C., McFarland, D. C., Nestor, K. E. and Velleman, S. G. 2006. Differential expression of membrane-associated heparan sulfate proteoglycans in the skeletal muscle of turkeys with different growth rates. Poult. Sci. 85: 422-428.
    • (2006) Poult. Sci. , vol.85 , pp. 422-428
    • Liu, C.1    McFarland, D.C.2    Nestor, K.E.3    Velleman, S.G.4
  • 62
    • 0035890328 scopus 로고    scopus 로고
    • TGF- beta inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3
    • Liu, D., Black, B. L. and Dernck, R. 2001. TGF-beta inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3. Genes Dev. 15: 2950-2966.
    • (2001) Genes Dev , vol.15 , pp. 2950-2966
    • Liu, D.1    Black, B.L.2    Dernck, R.3
  • 63
    • 39349089905 scopus 로고    scopus 로고
    • Increasing alpha 7 beta 1-integrin promotes muscle cell proliferation, adhesion, and resistance to apoptosis without changing gene expression
    • Liu, J., Burkin, D. J. and Kaufman, S. J. 2008. Increasing alpha 7 beta 1-integrin promotes muscle cell proliferation, adhesion, and resistance to apoptosis without changing gene expression. Am. J. Cell Physiol. 294: C627-C640.
    • (2008) Am. J. Cell Physiol. , vol.294
    • Liu, J.1    Burkin, D.J.2    Kaufman, S.J.3
  • 64
    • 1642341404 scopus 로고    scopus 로고
    • Developmental regulated expression of syndecan-1 and glypican in pectoralis major muscle in turkeys with different growth rates
    • Liu, X., McFarland, D. C., Nestor, K. E. and Velleman, S. G. 2004. Developmental regulated expression of syndecan-1 and glypican in pectoralis major muscle in turkeys with different growth rates. Dev. Growth Diff. 46: 37-51.
    • (2004) Dev. Growth Diff. , vol.46 , pp. 37-51
    • Liu, X.1    McFarland, D.C.2    Nestor, K.E.3    Velleman, S.G.4
  • 65
    • 0000642664 scopus 로고
    • Satellite cell of skeletal muscle fibers
    • Mauro, A. 1961. Satellite cell of skeletal muscle fibers. J. Biophys. Biochem. Cytol. 9: 493-495.
    • (1961) J. Biophys. Biochem. Cytol. , vol.9 , pp. 493-495
    • Mauro, A.1
  • 67
    • 0030840359 scopus 로고    scopus 로고
    • Double muscling in cattle due to mutations in the myostatin gene
    • McPherron, A. C. and Lee, S. J. 1997. Double muscling in cattle due to mutations in the myostatin gene. Proc. Natl. Acad. Sci. USA 94: 12457-12461.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12457-12461
    • McPherron, A.C.1    Lee, S.J.2
  • 68
    • 0036965929 scopus 로고    scopus 로고
    • TGF- beta and Smad signal transduction pathway
    • Mehra, A. and Wrana, J. L. 2002. TGF-beta and Smad signal transduction pathway. Biochem. Cell Biol. 80: 605-622.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 605-622
    • Mehra, A.1    Wrana, J.L.2
  • 70
    • 0014279946 scopus 로고
    • The relationship between the dimensions of the fibers and the number of nuclei during normal growth of skeletal muscle in domestic fowl
    • Moss, F. P. 1968. The relationship between the dimensions of the fibers and the number of nuclei during normal growth of skeletal muscle in domestic fowl. Am. J. Anat. 122: 555-563.
    • (1968) Am. J. Anat. , vol.122 , pp. 555-563
    • Moss, F.P.1
  • 71
    • 33748077106 scopus 로고    scopus 로고
    • Binding of internalized receptors to the PDZ domain of GIPC/synectin recruits myosin VI to endocytic vesicles
    • Naccache, S. N., Hasson, T. and Horowitz, A. 2006. Binding of internalized receptors to the PDZ domain of GIPC/synectin recruits myosin VI to endocytic vesicles. Proc. Natl. Acad. Sci. USA 103: 12735-12740.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12735-12740
    • Naccache, S.N.1    Hasson, T.2    Horowitz, A.3
  • 72
    • 0021285134 scopus 로고
    • Partial purification and characterization of hepatocyte growth factor from serum of hepatectomized rats
    • Nakamura, T., Nawa, K. and Ichihara, A. 1984. Partial purification and characterization of hepatocyte growth factor from serum of hepatectomized rats. Biochem. Biophys. Res. Commun. 122: 1450-1459.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1450-1459
    • Nakamura, T.1    Nawa, K.2    Ichihara, A.3
  • 73
    • 0035816723 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces fibronectin synthesis in coronary artery smooth muscle cells by a nitric oxide-dependent posttranscriptional mechanism
    • O'Blenes, C. A., Kinnear, C. and Rabinovitch, M. 2001. Tumor necrosis factor-alpha induces fibronectin synthesis in coronary artery smooth muscle cells by a nitric oxide-dependent posttranscriptional mechanism. Circ. Res. 89: 26-32.
    • (2001) Circ. Res. , vol.89 , pp. 26-32
    • O'Blenes, C.A.1    Kinnear, C.2    Rabinovitch, M.3
  • 74
    • 0030889054 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
    • Oh, E. S., Woods, A. and Couchman, J. R. 1997a. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. J. Biol. Chem. 272: 8133-8136.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8133-8136
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 75
    • 0030911243 scopus 로고    scopus 로고
    • Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C
    • Oh, E. S., Woods, A. and Couchman, J. R. 1997b. Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C. J. Biol. Chem. 272: 11805-11811.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11805-11811
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 76
    • 0032562706 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4 5-bisphosphate coordinately regulate protein kinase C activity
    • Oh, E. S., Woods, A., Lim, S. T., Theibert, A. W. and Couchman, J. R. 1998. Syndecan-4 proteoglycan cytoplasmic domain and phosphatidylinositol 4, 5-bisphosphate coordinately regulate protein kinase C activity. J. Biol. Chem. 273: 10624-10629.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10624-10629
    • Oh, E.S.1    Woods, A.2    Lim, S.T.3    Theibert, A.W.4    Couchman, J.R.5
  • 77
    • 0023191706 scopus 로고
    • Isolation and characterization of a low molecular weight chondroitin sulfate proteoglycan from rabbit skeletal muscle
    • Parthasarathy, N. and Tanzer, M. L. 1987. Isolation and characterization of a low molecular weight chondroitin sulfate proteoglycan from rabbit skeletal muscle. Biochemistry 26: 3149-3156.
    • (1987) Biochemistry , vol.26 , pp. 3149-3156
    • Parthasarathy, N.1    Tanzer, M.L.2
  • 80
    • 0141864365 scopus 로고    scopus 로고
    • Myostatin signals trhough a transforming growth factor beta-like signaling pathway to block adipogenesis
    • Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J. and Attisano, L. 2003. Myostatin signals trhough a transforming growth factor beta-like signaling pathway to block adipogenesis. Mol. Cell Biol. 23: 7230-7242.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7230-7242
    • Rebbapragada, A.1    Benchabane, H.2    Wrana, J.L.3    Celeste, A.J.4    Attisano, L.5
  • 81
    • 0026643352 scopus 로고
    • The enzymatic and non-enzymatic crosslinking of collagen and elastin
    • Reiser, J. M., McCormick, R. J. and Rucker, R. B. 1992. The enzymatic and non-enzymatic crosslinking of collagen and elastin. FASEB J. 6: 2439-2449.
    • (1992) FASEB J , vol.6 , pp. 2439-2449
    • Reiser, J.M.1    McCormick, R.J.2    Rucker, R.B.3
  • 82
    • 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., Larraín, J., Schönherr, E., Henriquez, J. P., Kresse, H. and 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    Larraín, J.2    Schönherr, E.3    Henriquez, J.P.4    Kresse, H.5    Brandan, E.6
  • 83
    • 0033553417 scopus 로고    scopus 로고
    • Activated protein kinase C isoforms target to cardiomyocyte caveolae: Stimulation of local protein phosphorylation
    • Rybin, V. O., Xu, X. and Steinberg, S. F. 1999. Activated protein kinase C isoforms target to cardiomyocyte caveolae: Stimulation of local protein phosphorylation. Circ. Res. 84: 980-988.
    • (1999) Circ. Res. , vol.84 , pp. 980-988
    • Rybin, V.O.1    Xu, X.2    Steinberg, S.F.3
  • 84
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGFbinding epitope
    • Santra, M., Reed, C. C. and Iozzo, R. V. 2002. Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGFbinding epitope. J. Biol. Chem. 277: 35671-35681.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 87
    • 37449022587 scopus 로고    scopus 로고
    • Interleukin-6 is an essential regulator of satellite cell-mediated skeletal muscle hypertrophy
    • Serrano, A. L., Baeza-Raja, B., Perdiguero, E., Jardí M. and Muñoz-Cánoves, P. 2008. Interleukin-6 is an essential regulator of satellite cell-mediated skeletal muscle hypertrophy. Cell Metab. 7: 33-44.
    • (2008) Cell Metab , vol.7 , pp. 33-44
    • Serrano, A.L.1    Baeza-Raja, B.2    Perdiguero, E.3    Jardí, M.4    Muñoz-Cánoves, P.5
  • 88
    • 0007852442 scopus 로고
    • Relation of body size to muscle cell size and number in the chicken
    • Smith, J. H. 1963. Relation of body size to muscle cell size and number in the chicken. Poult. Sci. 42: 283-290.
    • (1963) Poult. Sci. , vol.42 , pp. 283-290
    • Smith, J.H.1
  • 89
    • 72249099026 scopus 로고    scopus 로고
    • Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness
    • Song, Y., Nestor, K. E., McFarland, D. C. and Velleman, S. G. 2010. Effect of glypican-1 covalently attached chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Poult. Sci. 89: 123-134.
    • (2010) Poult. Sci. , vol.89 , pp. 123-134
    • Song, Y.1    Nestor, K.E.2    McFarland, D.C.3    Velleman, S.G.4
  • 90
    • 0032558391 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans control intracellular processing of bFGF in vascular smooth muscle cells
    • Sperinde, G. V. and Nugent, M. A. 1998. Heparan sulfate proteoglycans control intracellular processing of bFGF in vascular smooth muscle cells. Biochemistry 37: 13153-13164.
    • (1998) Biochemistry , vol.37 , pp. 13153-13164
    • Sperinde, G.V.1    Nugent, M.A.2
  • 91
    • 0029878968 scopus 로고    scopus 로고
    • Stimulation of fibroblast growth factor receptor-1 occupancy and signaling by cell surface associated syndecans and glypican
    • Steinfeld, R., Van Den Berghe, H. and David, G. 1996. Stimulation of fibroblast growth factor receptor-1 occupancy and signaling by cell surface associated syndecans and glypican. J. Cell Biol. 133: 405-416.
    • (1996) J. Cell Biol. , vol.133 , pp. 405-416
    • Steinfeld, R.1    Van Den Berghe, H.2    David, G.3
  • 92
    • 0030916062 scopus 로고    scopus 로고
    • Delayed myogenesis associated with muscle fiber hyperplasia in high-growth mice
    • Summers, P. J. and Medrano, J. F. 1997. Delayed myogenesis associated with muscle fiber hyperplasia in high-growth mice. Proc. Soc. Exp. Biol. Med. 214: 380-385.
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.214 , pp. 380-385
    • Summers, P.J.1    Medrano, J.F.2
  • 95
    • 0024315692 scopus 로고
    • Fibroblast growth factor and transforming growth factor beta repress transcription of the myogenic regulatory MyoD1
    • Vaidya, T. B., Rhodes, S. J., Taparowsky, E. J. and Konieczny, S. F. 1989. Fibroblast growth factor and transforming growth factor beta repress transcription of the myogenic regulatory MyoD1. Mol. Cell Biol. 9: 3576-3579.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 3576-3579
    • Vaidya, T.B.1    Rhodes, S.J.2    Taparowsky, E.J.3    Konieczny, S.F.4
  • 96
    • 0025792023 scopus 로고
    • Collagen family proteins
    • Van der Rest, M. and Garrone, R. 1991. Collagen family proteins. FASEB J. 5: 2814-2823.
    • (1991) FASEB J , vol.5 , pp. 2814-2823
    • Van der Rest, M.1    Garrone, R.2
  • 97
    • 0033226918 scopus 로고    scopus 로고
    • Developmental regulation of proteoglycan synthesis and decorin expression during turkey embryonic skeletal muscle formation
    • Velleman, S. G., Liu, X., Eggen, K. H. and Nestor, K. E. 1999. Developmental regulation of proteoglycan synthesis and decorin expression during turkey embryonic skeletal muscle formation. Poult. Sci. 78: 1619-1626.
    • (1999) Poult. Sci. , vol.78 , pp. 1619-1626
    • Velleman, S.G.1    Liu, X.2    Eggen, K.H.3    Nestor, K.E.4
  • 98
    • 0033588024 scopus 로고    scopus 로고
    • The role of syndecan cytoplasmic domain in basic fibroblast growth factor-dependent signal transduction
    • Volk, R., Schwartz, J. J., Li, J., Rosenberg, R. D. and Simons, M. 1999. The role of syndecan cytoplasmic domain in basic fibroblast growth factor-dependent signal transduction. J. Biol. Chem. 274: 24417-24424.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24417-24424
    • Volk, R.1    Schwartz, J.J.2    Li, J.3    Rosenberg, R.D.4    Simons, M.5
  • 100
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-beta by the proteoglycan decorin
    • Yamaguichi, Y., Mann, D. M. and Ruoslahti, E. 1990. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature 346: 281-284.
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguichi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 101
    • 0346847627 scopus 로고    scopus 로고
    • Functional characterization of recombinant myostatin and its inhibitory role to chicken muscle development Acta
    • Yang, W., Wang, K., Chen, Y., Zhang, Y., Huang, B. and Zhu, D. 2003. Functional characterization of recombinant myostatin and its inhibitory role to chicken muscle development Acta. Biochem. Biophys. Sin. 35: 1016-1022.
    • (2003) Biochem. Biophys. Sin. , vol.35 , pp. 1016-1022
    • Yang, W.1    Wang, K.2    Chen, Y.3    Zhang, Y.4    Huang, B.5    Zhu, D.6
  • 102
    • 0025259478 scopus 로고
    • Changes in synthesis of sulfated glyconconjugates during muscle development, maturation and aging in embryonic to senescent CBF-1 mouse
    • Young, H. E., Carrino, D. A. and Caplan, A. I. 1990. Changes in synthesis of sulfated glyconconjugates during muscle development, maturation and aging in embryonic to senescent CBF-1 mouse. Mech. Ageing Dev. 53: 179-193.
    • (1990) Mech. Ageing Dev. , vol.53 , pp. 179-193
    • Young, H.E.1    Carrino, D.A.2    Caplan, A.I.3
  • 104
    • 35348905401 scopus 로고    scopus 로고
    • The effect of glypican-1 glycosaminoglycan chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness
    • Zhang, X., Liu, C., Nestor, K. E., McFarland, D. C. and Velleman, S. G. 2007. The effect of glypican-1 glycosaminoglycan chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Poult. Sci. 86: 2020-2028.
    • (2007) Poult. Sci. , vol.86 , pp. 2020-2028
    • Zhang, X.1    Liu, C.2    Nestor, K.E.3    McFarland, D.C.4    Velleman, S.G.5
  • 105
    • 54249163330 scopus 로고    scopus 로고
    • The role of syndecan-4 and attached glycosaminoglycan chains on myogenic satellite cell growth
    • Zhang, X., Nestor, K. E., McFarland, D. C. and Velleman, S. G. 2008. The role of syndecan-4 and attached glycosaminoglycan chains on myogenic satellite cell growth. Matrix Biol. 27: 619-630.
    • (2008) Matrix Biol , vol.27 , pp. 619-630
    • Zhang, X.1    Nestor, K.E.2    McFarland, D.C.3    Velleman, S.G.4
  • 106
    • 2942536234 scopus 로고    scopus 로고
    • Myostatin signaling through Smad2 Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism
    • Zhu, X., Topouzis, S., Liang, L. F. and Stotish, R. L. 2004. Myostatin signaling through Smad2, Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism. Cytokine 26: ???-???.
    • (2004) Cytokine , vol.26
    • Zhu, X.1    Topouzis, S.2    Liang, L.F.3    Stotish, R.L.4


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