메뉴 건너뛰기




Volumn 344, Issue 4, 2006, Pages 1207-1215

Sulfation is required for bone morphogenetic protein 2-dependent Id1 induction

Author keywords

BMP 2; Id1; Muscle cells; Proteoglycans; Sulfation inhibitor

Indexed keywords

BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN RECEPTOR; GLYCOSAMINOGLYCAN; INHIBITOR OF DIFFERENTIATION 1; LYASE; PROTEOGLYCAN; SODIUM CHLORATE;

EID: 33646481319     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.04.029     Document Type: Article
Times cited : (7)

References (38)
  • 2
    • 13444291335 scopus 로고    scopus 로고
    • BMP signaling in skeletal development
    • Wan M., and Cao X. BMP signaling in skeletal development. Biochem. Biophys. Res. Commun. 328 (2005) 651-657
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 651-657
    • Wan, M.1    Cao, X.2
  • 5
    • 0346996450 scopus 로고    scopus 로고
    • Signal transduction of bone morphogenetic protein receptors
    • Nohe A., Keating E., Knaus P., and Petersen N.O. Signal transduction of bone morphogenetic protein receptors. Cell. Signal. 16 (2004) 291-299
    • (2004) Cell. Signal. , vol.16 , pp. 291-299
    • Nohe, A.1    Keating, E.2    Knaus, P.3    Petersen, N.O.4
  • 6
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi Y., and Massague J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 113 (2003) 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 7
    • 0036479133 scopus 로고    scopus 로고
    • Direct binding of Smad1 and Smad4 to two distinct motifs mediates bone morphogenetic protein-specific transcriptional activation of Id1 gene
    • Lopez-Rovira T., Chalaux E., Massague J., Rosa J.L., and Ventura F. Direct binding of Smad1 and Smad4 to two distinct motifs mediates bone morphogenetic protein-specific transcriptional activation of Id1 gene. J. Biol. Chem. 277 (2002) 3176-3185
    • (2002) J. Biol. Chem. , vol.277 , pp. 3176-3185
    • Lopez-Rovira, T.1    Chalaux, E.2    Massague, J.3    Rosa, J.L.4    Ventura, F.5
  • 8
    • 8544275892 scopus 로고    scopus 로고
    • Myogenin protein stability is decreased by BMP-2 through a mechanism implicating Id1
    • Vinals F., and Ventura F. Myogenin protein stability is decreased by BMP-2 through a mechanism implicating Id1. J. Biol. Chem. 279 (2004) 45766-45772
    • (2004) J. Biol. Chem. , vol.279 , pp. 45766-45772
    • Vinals, F.1    Ventura, F.2
  • 11
    • 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
  • 12
    • 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. Antisense inhibition of syndecan-3 expression during skeletal muscle differentiation accelerates myogenesis through a basic fibroblast growth factor-dependent mechanism. J. Biol. Chem. 274 (1999) 37876-37884
    • (1999) J. Biol. Chem. , vol.274 , pp. 37876-37884
    • Fuentealba, L.1    Carey, D.J.2    Brandan, E.3
  • 13
    • 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
  • 15
    • 0023429111 scopus 로고
    • Isolation of osteogenin, an extracellular matrix-associated, bone-inductive protein, by heparin affinity chromatography
    • Sampath T.K., Muthukumaran N., and Reddi A.H. Isolation of osteogenin, an extracellular matrix-associated, bone-inductive protein, by heparin affinity chromatography. Proc. Natl. Acad. Sci. USA 84 (1987) 7109-7113
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7109-7113
    • Sampath, T.K.1    Muthukumaran, N.2    Reddi, A.H.3
  • 16
    • 0042661060 scopus 로고    scopus 로고
    • Heparan sulfate is required for bone morphogenetic protein-7 signaling
    • Irie A., Habuchi H., Kimata K., and Sanai Y. Heparan sulfate is required for bone morphogenetic protein-7 signaling. Biochem. Biophys. Res. Commun. 308 (2003) 858-865
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 858-865
    • Irie, A.1    Habuchi, H.2    Kimata, K.3    Sanai, Y.4
  • 17
    • 0022897789 scopus 로고
    • Chlorate-a potent inhibitor of protein sulfation in intact cells
    • Baeuerle P.A., and Huttner W.B. Chlorate-a potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Commun. 141 (1986) 870-877
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 870-877
    • Baeuerle, P.A.1    Huttner, W.B.2
  • 18
    • 0034663672 scopus 로고    scopus 로고
    • Interaction of the collagen-like tail of asymmetric acetylcholinesterase with heparin depends on triple-helical conformation, sequence and stability
    • Deprez P., Doss-Pepe E., Brodsky B., and Inestrosa N.C. Interaction of the collagen-like tail of asymmetric acetylcholinesterase with heparin depends on triple-helical conformation, sequence and stability. Biochem. J. 350 Pt. 1 (2000) 283-290
    • (2000) Biochem. J. , vol.350 , Issue.PART 1 , pp. 283-290
    • Deprez, P.1    Doss-Pepe, E.2    Brodsky, B.3    Inestrosa, N.C.4
  • 19
    • 0027276765 scopus 로고
    • Betaglycan presents ligand to the TGF beta signaling receptor
    • Lopez-Casillas F., Wrana J.L., and Massague J. Betaglycan presents ligand to the TGF beta signaling receptor. Cell 73 (1993) 1435-1444
    • (1993) Cell , vol.73 , pp. 1435-1444
    • Lopez-Casillas, F.1    Wrana, J.L.2    Massague, J.3
  • 20
    • 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
  • 21
    • 0023677430 scopus 로고
    • Chlorate: a reversible inhibitor of proteoglycan sulfation
    • Humphries D.E., and Silbert J.E. Chlorate: a reversible inhibitor of proteoglycan sulfation. Biochem. Biophys. Res. Commun. 154 (1988) 365-371
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 365-371
    • Humphries, D.E.1    Silbert, J.E.2
  • 22
    • 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
  • 23
    • 0030745802 scopus 로고    scopus 로고
    • Syndecan-1 expression is down-regulated during myoblast terminal differentiation. Modulation by growth factors and retinoic acid
    • Larrain J., Cizmeci-Smith G., Troncoso V., Stahl R.C., Carey D.J., and Brandan E. Syndecan-1 expression is down-regulated during myoblast terminal differentiation. Modulation by growth factors and retinoic acid. J. Biol. Chem. 272 (1997) 18418-18424
    • (1997) J. Biol. Chem. , vol.272 , pp. 18418-18424
    • Larrain, J.1    Cizmeci-Smith, G.2    Troncoso, V.3    Stahl, R.C.4    Carey, D.J.5    Brandan, E.6
  • 24
    • 0031213659 scopus 로고    scopus 로고
    • Expression of perlecan, a proteoglycan that binds myogenic inhibitory basic fibroblast growth factor, is down regulated during skeletal muscle differentiation
    • Larrain J., Alvarez J., Hassell J.R., and Brandan E. Expression of perlecan, a proteoglycan that binds myogenic inhibitory basic fibroblast growth factor, is down regulated during skeletal muscle differentiation. Exp. Cell Res. 234 (1997) 405-412
    • (1997) Exp. Cell Res. , vol.234 , pp. 405-412
    • Larrain, J.1    Alvarez, J.2    Hassell, J.R.3    Brandan, E.4
  • 25
    • 0029860604 scopus 로고    scopus 로고
    • Synthesis and processing of glypican during differentiation of skeletal muscle cells
    • Brandan E., Carey D.J., Larrain J., Melo F., and Campos A. Synthesis and processing of glypican during differentiation of skeletal muscle cells. Eur. J. Cell Biol. 71 (1996) 170-176
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 170-176
    • Brandan, E.1    Carey, D.J.2    Larrain, J.3    Melo, F.4    Campos, A.5
  • 26
    • 28444461805 scopus 로고    scopus 로고
    • Changes in secreted and cell associated proteoglycan synthesis during conversion of myoblasts to osteoblasts in response to bone morphogenetic protein-2: role of decorin in cell response to BMP-2
    • Gutierrez J., Osses N., and Brandan E. Changes in secreted and cell associated proteoglycan synthesis during conversion of myoblasts to osteoblasts in response to bone morphogenetic protein-2: role of decorin in cell response to BMP-2. J. Cell. Physiol. 206 (2006) 58-67
    • (2006) J. Cell. Physiol. , vol.206 , pp. 58-67
    • Gutierrez, J.1    Osses, N.2    Brandan, E.3
  • 27
    • 2942706108 scopus 로고    scopus 로고
    • The small leucine-rich proteoglycan biglycan modulates BMP-4-induced osteoblast differentiation
    • Chen X.D., Fisher L.W., Robey P.G., and Young M.F. The small leucine-rich proteoglycan biglycan modulates BMP-4-induced osteoblast differentiation. FASEB J. 18 (2004) 948-958
    • (2004) FASEB J. , vol.18 , pp. 948-958
    • Chen, X.D.1    Fisher, L.W.2    Robey, P.G.3    Young, M.F.4
  • 28
    • 0024312346 scopus 로고
    • Inhibition of proteoglycan synthesis alters extracellular matrix deposition, proliferation, and cytoskeletal organization of rat aortic smooth muscle cells in culture
    • Hamati H.F., Britton E.L., and Carey D.J. Inhibition of proteoglycan synthesis alters extracellular matrix deposition, proliferation, and cytoskeletal organization of rat aortic smooth muscle cells in culture. J. Cell. Biol. 108 (1989) 2495-2505
    • (1989) J. Cell. Biol. , vol.108 , pp. 2495-2505
    • Hamati, H.F.1    Britton, E.L.2    Carey, D.J.3
  • 29
    • 2642609494 scopus 로고    scopus 로고
    • JunB is involved in the inhibition of myogenic differentiation by bone morphogenetic protein-2
    • Chalaux E., Lopez-Rovira T., Rosa J.L., Bartrons R., and Ventura F. JunB is involved in the inhibition of myogenic differentiation by bone morphogenetic protein-2. J. Biol. Chem. 273 (1998) 537-543
    • (1998) J. Biol. Chem. , vol.273 , pp. 537-543
    • Chalaux, E.1    Lopez-Rovira, T.2    Rosa, J.L.3    Bartrons, R.4    Ventura, F.5
  • 30
    • 0031577571 scopus 로고    scopus 로고
    • Smad1 and smad5 act downstream of intracellular signalings of BMP-2 that inhibits myogenic differentiation and induces osteoblast differentiation in C2C12 myoblasts
    • Yamamoto N., Akiyama S., Katagiri T., Namiki M., Kurokawa T., and Suda T. Smad1 and smad5 act downstream of intracellular signalings of BMP-2 that inhibits myogenic differentiation and induces osteoblast differentiation in C2C12 myoblasts. Biochem. Biophys. Res. Commun. 238 (1997) 574-580
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 574-580
    • Yamamoto, N.1    Akiyama, S.2    Katagiri, T.3    Namiki, M.4    Kurokawa, T.5    Suda, T.6
  • 31
    • 0028295710 scopus 로고
    • Inhibition of protein and lipid sulfation in oligodendrocytes blocks biological responses to FGF-2 and retards cytoarchitectural maturation, but not developmental lineage progression
    • Bansal R., and Pfeiffer S.E. Inhibition of protein and lipid sulfation in oligodendrocytes blocks biological responses to FGF-2 and retards cytoarchitectural maturation, but not developmental lineage progression. Dev. Biol. 162 (1994) 511-524
    • (1994) Dev. Biol. , vol.162 , pp. 511-524
    • Bansal, R.1    Pfeiffer, S.E.2
  • 32
    • 0034721843 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 stimulation of p42/44 MAPK phosphorylation and IkappaB degradation is regulated by heparan sulfate/heparin in rat mammary fibroblasts
    • Delehedde M., Seve M., Sergeant N., Wartelle I., Lyon M., Rudland P.S., and Fernig D.G. Fibroblast growth factor-2 stimulation of p42/44 MAPK phosphorylation and IkappaB degradation is regulated by heparan sulfate/heparin in rat mammary fibroblasts. J. Biol. Chem. 275 (2000) 33905-33910
    • (2000) J. Biol. Chem. , vol.275 , pp. 33905-33910
    • Delehedde, M.1    Seve, M.2    Sergeant, N.3    Wartelle, I.4    Lyon, M.5    Rudland, P.S.6    Fernig, D.G.7
  • 33
    • 4544228455 scopus 로고    scopus 로고
    • Under-sulfation by PAPS synthetase inhibition modulates the expression of ECM molecules during chondrogenesis
    • Cho Y.R., Lee S.J., Jeon H.B., Park Z.Y., Chun J.S., and Yoo Y.J. Under-sulfation by PAPS synthetase inhibition modulates the expression of ECM molecules during chondrogenesis. Biochem. Biophys. Res. Commun. 323 (2004) 769-775
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 769-775
    • Cho, Y.R.1    Lee, S.J.2    Jeon, H.B.3    Park, Z.Y.4    Chun, J.S.5    Yoo, Y.J.6
  • 34
    • 0037085287 scopus 로고    scopus 로고
    • The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways
    • Nohe A., Hassel S., Ehrlich M., Neubauer F., Sebald W., Henis Y.I., and Knaus P. The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways. J. Biol. Chem. 277 (2002) 5330-5338
    • (2002) J. Biol. Chem. , vol.277 , pp. 5330-5338
    • Nohe, A.1    Hassel, S.2    Ehrlich, M.3    Neubauer, F.4    Sebald, W.5    Henis, Y.I.6    Knaus, P.7
  • 35
    • 1942470528 scopus 로고    scopus 로고
    • Kinetic model for FGF, FGFR, and proteoglycan signal transduction complex assembly
    • Ibrahimi O.A., Zhang F., Hrstka S.C., Mohammadi M., and Linhardt R.J. Kinetic model for FGF, FGFR, and proteoglycan signal transduction complex assembly. Biochemistry 43 (2004) 4724-4730
    • (2004) Biochemistry , vol.43 , pp. 4724-4730
    • Ibrahimi, O.A.1    Zhang, F.2    Hrstka, S.C.3    Mohammadi, M.4    Linhardt, R.J.5
  • 36
    • 0029985256 scopus 로고    scopus 로고
    • Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity
    • Ruppert R., Hoffmann E., and Sebald W. Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity. Eur. J. Biochem. 237 (1996) 295-302
    • (1996) Eur. J. Biochem. , vol.237 , pp. 295-302
    • Ruppert, R.1    Hoffmann, E.2    Sebald, W.3
  • 37
    • 0037022121 scopus 로고    scopus 로고
    • Action range of BMP is defined by its N-terminal basic amino acid core
    • Ohkawara B., Iemura S., ten Dijke P., and Ueno N. Action range of BMP is defined by its N-terminal basic amino acid core. Curr. Biol. 12 (2002) 205-209
    • (2002) Curr. Biol. , vol.12 , pp. 205-209
    • Ohkawara, B.1    Iemura, S.2    ten Dijke, P.3    Ueno, N.4
  • 38
    • 0034666302 scopus 로고    scopus 로고
    • Interaction and functional cooperation of NF-kappa B with Smads. Transcriptional regulation of the junB promoter
    • Lopez-Rovira T., Chalaux E., Rosa J.L., Bartrons R., and Ventura F. Interaction and functional cooperation of NF-kappa B with Smads. Transcriptional regulation of the junB promoter. J. Biol. Chem. 275 (2000) 28937-28946
    • (2000) J. Biol. Chem. , vol.275 , pp. 28937-28946
    • Lopez-Rovira, T.1    Chalaux, E.2    Rosa, J.L.3    Bartrons, R.4    Ventura, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.