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Volumn 22, Issue 12, 2008, Pages 2689-2702

Proteomic identification and functional validation of activins and bone morphogenetic protein 11 as candidate novel muscle mass regulators

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN; ACTIVIN A; ACTIVIN RECEPTOR 2; BONE MORPHOGENETIC PROTEIN; BONE MORPHOGENETIC PROTEIN 10; BONE MORPHOGENETIC PROTEIN 11; BONE MORPHOGENETIC PROTEIN 9; LIGAND; MYELOPID; MYOSTATIN; TRANSFORMING GROWTH FACTOR BETA; UNCLASSIFIED DRUG;

EID: 56749170664     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2008-0290     Document Type: Article
Times cited : (121)

References (62)
  • 1
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • McPherron AC, Lawler AM, Lee SJ 1997 Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature 387:83-90
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 2
    • 0030840359 scopus 로고    scopus 로고
    • Double muscling in cattle due to mutations in the myostatin gene
    • McPherron AC, Lee SJ 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
  • 5
    • 34548414546 scopus 로고    scopus 로고
    • Gross muscle hypertrophy in whippet dogs is caused by a mutation in the myostatin gene
    • Shelton GD, Engvall E 2007 Gross muscle hypertrophy in whippet dogs is caused by a mutation in the myostatin gene. Neuromuscul Disord 17:721-722
    • (2007) Neuromuscul Disord , vol.17 , pp. 721-722
    • Shelton, G.D.1    Engvall, E.2
  • 9
    • 39749114099 scopus 로고    scopus 로고
    • Myostatin blockade improves function but not histopathology in a murine model of limb-girdle muscular dystrophy 2C
    • Bogdanovich S, McNally EM, Khurana TS 2008 Myostatin blockade improves function but not histopathology in a murine model of limb-girdle muscular dystrophy 2C. Muscle Nerve 37:308-316
    • (2008) Muscle Nerve , vol.37 , pp. 308-316
    • Bogdanovich, S.1    McNally, E.M.2    Khurana, T.S.3
  • 11
    • 0037174939 scopus 로고    scopus 로고
    • The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum
    • Hill JJ, Davies MV, Pearson AA, Wang JH, Hewick RM, Wolfman NM, Qiu Y 2002 The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J Biol Chem 277:40735-40741
    • (2002) J Biol Chem , vol.277 , pp. 40735-40741
    • Hill, J.J.1    Davies, M.V.2    Pearson, A.A.3    Wang, J.H.4    Hewick, R.M.5    Wolfman, N.M.6    Qiu, Y.7
  • 12
    • 0037841469 scopus 로고    scopus 로고
    • Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: A novel protein with protease inhibitor and follistatin domains
    • Hill JJ, Qiu Y, Hewick RM, Wolfman NM 2003 Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: a novel protein with protease inhibitor and follistatin domains. Mol Endocrinol 17:1144-1154
    • (2003) Mol Endocrinol , vol.17 , pp. 1144-1154
    • Hill, J.J.1    Qiu, Y.2    Hewick, R.M.3    Wolfman, N.M.4
  • 13
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee SJ, McPherron AC 2001 Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci USA 98:9306-9311
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 17
    • 0141864365 scopus 로고    scopus 로고
    • Myostatin signals through a transforming growth factor β-like signaling pathway to block adipogenesis
    • Rebbapragada A, Benchabane H, Wrana JL, Celeste AJ, Attisano L 2003 Myostatin signals through a transforming growth factor β-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
  • 19
    • 1642473157 scopus 로고    scopus 로고
    • The transforming growth factor-β superfamily of receptors
    • de Caestecker M 2004 The transforming growth factor-β superfamily of receptors. Cytokine Growth Factor Rev 15:1-11
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 1-11
    • de Caestecker, M.1
  • 21
    • 0033852903 scopus 로고    scopus 로고
    • Regulation of activin's access to the cell: Why is mother nature such a control freak?
    • Phillips DJ 2000 Regulation of activin's access to the cell: why is mother nature such a control freak? Bioessays 22:689-696
    • (2000) Bioessays , vol.22 , pp. 689-696
    • Phillips, D.J.1
  • 22
    • 0031911356 scopus 로고    scopus 로고
    • SMADs: Mediators and regulators of TGF-β signaling
    • Kretzschmar M, Massague J 1998 SMADs: mediators and regulators of TGF-β signaling. Curr Opin Genet Dev 8:103-111
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 103-111
    • Kretzschmar, M.1    Massague, J.2
  • 23
    • 0032101178 scopus 로고    scopus 로고
    • Direct binding of Smad3 and Smad4 to critical TGF β-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene
    • Dennler S, Itoh S, Vivien D, ten Dijke P, Huet S, Gauthier JM 1998 Direct binding of Smad3 and Smad4 to critical TGF β-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene. EMBO J 17:3091-3100
    • (1998) EMBO J , vol.17 , pp. 3091-3100
    • Dennler, S.1    Itoh, S.2    Vivien, D.3    ten Dijke, P.4    Huet, S.5    Gauthier, J.M.6
  • 24
    • 0037085441 scopus 로고    scopus 로고
    • Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter
    • Korchynskyi O, ten Dijke P 2002 Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter. J Biol Chem 277:4883-4891
    • (2002) J Biol Chem , vol.277 , pp. 4883-4891
    • Korchynskyi, O.1    ten Dijke, P.2
  • 25
    • 0038636430 scopus 로고    scopus 로고
    • Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin
    • Joulia D, Bernardi H, Garandel V, Rabenoelina F, Vernus B, Cabello G 2003 Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin. Exp Cell Res 286:263-275
    • (2003) Exp Cell Res , vol.286 , pp. 263-275
    • Joulia, D.1    Bernardi, H.2    Garandel, V.3    Rabenoelina, F.4    Vernus, B.5    Cabello, G.6
  • 26
    • 0037147210 scopus 로고    scopus 로고
    • Myostatin inhibits myoblast differentiation by down-regulating MyoD expression
    • Langley B, Thomas M, Bishop A, Sharma M, Gilmour S, Kambadur R 2002 Myostatin inhibits myoblast differentiation by down-regulating MyoD expression. J Biol Chem 277:49831-49840
    • (2002) J Biol Chem , vol.277 , pp. 49831-49840
    • Langley, B.1    Thomas, M.2    Bishop, A.3    Sharma, M.4    Gilmour, S.5    Kambadur, R.6
  • 28
    • 0034704106 scopus 로고    scopus 로고
    • Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation
    • Thomas M, Langley B, Berry C, Sharma M, Kirk S, Bass J, Kambadur R 2000 Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation. J Biol Chem 275:40235-40243
    • (2000) J Biol Chem , vol.275 , pp. 40235-40243
    • Thomas, M.1    Langley, B.2    Berry, C.3    Sharma, M.4    Kirk, S.5    Bass, J.6    Kambadur, R.7
  • 30
    • 85130085953 scopus 로고    scopus 로고
    • Cheng H, Jiang W, Phillips FM, Haydon RC, Peng Y, Zhou L, Luu HH, An N, Breyer B, Vanichakarn P, Szatkowski JP, Park JY, He TC 2003 Osteogenic activity of the fourteen types of human bone morphogenetic proteins (BMPs). J Bone Joint Surg Am [Erratum (2004) 86-A:141] 85-A:1544-1552
    • Cheng H, Jiang W, Phillips FM, Haydon RC, Peng Y, Zhou L, Luu HH, An N, Breyer B, Vanichakarn P, Szatkowski JP, Park JY, He TC 2003 Osteogenic activity of the fourteen types of human bone morphogenetic proteins (BMPs). J Bone Joint Surg Am [Erratum (2004) 86-A:141] 85-A:1544-1552
  • 32
    • 0025857671 scopus 로고
    • Recombinant human bone morphogenetic protein-2 stimulates osteoblastic maturation and inhibits myogenic differentiation in vitro
    • Yamaguchi A, Katagiri T, Ikeda T, Wozney JM, Rosen V, Wang EA, Kahn AJ, Suda T, Yoshiki S 1991 Recombinant human bone morphogenetic protein-2 stimulates osteoblastic maturation and inhibits myogenic differentiation in vitro. J Cell Biol 113:681-687
    • (1991) J Cell Biol , vol.113 , pp. 681-687
    • Yamaguchi, A.1    Katagiri, T.2    Ikeda, T.3    Wozney, J.M.4    Rosen, V.5    Wang, E.A.6    Kahn, A.J.7    Suda, T.8    Yoshiki, S.9
  • 34
    • 0031080176 scopus 로고    scopus 로고
    • Bone morphogenetic protein-2 inhibits terminal differentiation of myogenic cells by suppressing the transcriptional activity of MyoD and myogenin
    • Katagiri T, Akiyama S, Namiki M, Komaki M, Yamaguchi A, Rosen V, Wozney JM, Fujisawa-Sehara A, Suda T 1997 Bone morphogenetic protein-2 inhibits terminal differentiation of myogenic cells by suppressing the transcriptional activity of MyoD and myogenin. Exp Cell Res 230:342-351
    • (1997) Exp Cell Res , vol.230 , pp. 342-351
    • Katagiri, T.1    Akiyama, S.2    Namiki, M.3    Komaki, M.4    Yamaguchi, A.5    Rosen, V.6    Wozney, J.M.7    Fujisawa-Sehara, A.8    Suda, T.9
  • 36
    • 0027738464 scopus 로고
    • The MyoD family and myogenesis: Redundancy, networks, and thresholds
    • Weintraub H 1993 The MyoD family and myogenesis: redundancy, networks, and thresholds. Cell 75:1241-1244
    • (1993) Cell , vol.75 , pp. 1241-1244
    • Weintraub, H.1
  • 38
    • 0029364173 scopus 로고
    • Determination versus differentiation and the MyoD family of transcription factors
    • Megeney LA, Rudnicki MA 1995 Determination versus differentiation and the MyoD family of transcription factors. Biochem Cell Biol 73:723-732
    • (1995) Biochem Cell Biol , vol.73 , pp. 723-732
    • Megeney, L.A.1    Rudnicki, M.A.2
  • 39
    • 33947538814 scopus 로고    scopus 로고
    • Yang W, Zhang Y, Li Y, Wu Z, Zhu D, McFarlane C, Plummer E, Thomas M, Hennebry A, Ashby M, Ling N, Smith H, Sharma M, Kambadur R, Morissette MR, Cook SA, Foo S, McKoy G, Ashida N, Novikov M, Scherrer-Crosbie M, Li L, Matsui T, Brooks G, Rosenzweig A, Zhao B, Wall RJ, Yang J, Guttridge DC 2007 Myostatin induces cyclin D1 degradation to cause cell cycle arrest through a phosphatidylinositol 3-kinase/AKT/GSK-3 β pathway and is antagonized by insulin-like growth factor 1. J Biol Chem 282:3799-3808
    • Yang W, Zhang Y, Li Y, Wu Z, Zhu D, McFarlane C, Plummer E, Thomas M, Hennebry A, Ashby M, Ling N, Smith H, Sharma M, Kambadur R, Morissette MR, Cook SA, Foo S, McKoy G, Ashida N, Novikov M, Scherrer-Crosbie M, Li L, Matsui T, Brooks G, Rosenzweig A, Zhao B, Wall RJ, Yang J, Guttridge DC 2007 Myostatin induces cyclin D1 degradation to cause cell cycle arrest through a phosphatidylinositol 3-kinase/AKT/GSK-3 β pathway and is antagonized by insulin-like growth factor 1. J Biol Chem 282:3799-3808
  • 43
  • 44
    • 0032980052 scopus 로고    scopus 로고
    • Heart specific expression of mouse BMP-10 a novel member of the TGF-β superfamily
    • Neuhaus H, Rosen V, Thies RS 1999 Heart specific expression of mouse BMP-10 a novel member of the TGF-β superfamily. Mech Dev 80:181-184
    • (1999) Mech Dev , vol.80 , pp. 181-184
    • Neuhaus, H.1    Rosen, V.2    Thies, R.S.3
  • 45
    • 0022977185 scopus 로고
    • Regulation of myogenic differentiation by type β transforming growth factor
    • Olson EN, Sternberg E, Hu JS, Spizz G, Wilcox C 1986 Regulation of myogenic differentiation by type β transforming growth factor. J Cell Biol 103:1799-1805
    • (1986) J Cell Biol , vol.103 , pp. 1799-1805
    • Olson, E.N.1    Sternberg, E.2    Hu, J.S.3    Spizz, G.4    Wilcox, C.5
  • 46
    • 0011899697 scopus 로고
    • Type β transforming growth factor is an inhibitor of myogenic differentiation
    • Massague J, Cheifetz S, Endo T, Nadal-Ginard B 1986 Type β 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
  • 47
    • 1242293760 scopus 로고    scopus 로고
    • Transforming growth factorbeta1 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 factorbeta1 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
  • 49
    • 33847369980 scopus 로고    scopus 로고
    • Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells
    • David L, Mallet C, Mazerbourg S, Feige JJ, Bailly S 2007 Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells. Blood 109:1953-1961
    • (2007) Blood , vol.109 , pp. 1953-1961
    • David, L.1    Mallet, C.2    Mazerbourg, S.3    Feige, J.J.4    Bailly, S.5
  • 50
    • 41549084155 scopus 로고    scopus 로고
    • Transforming growth factor-β and myostatin signaling in skeletal muscle
    • Kollias HD, McDermott JC 2008 Transforming growth factor-β and myostatin signaling in skeletal muscle. J Appl Physiol 104:579-587
    • (2008) J Appl Physiol , vol.104 , pp. 579-587
    • Kollias, H.D.1    McDermott, J.C.2
  • 52
    • 21744434744 scopus 로고    scopus 로고
    • GDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cells
    • Ge G, Hopkins DR, Ho WB, Greenspan DS 2005 GDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cells. Mol Cell Biol 25:5846-5858
    • (2005) Mol Cell Biol , vol.25 , pp. 5846-5858
    • Ge, G.1    Hopkins, D.R.2    Ho, W.B.3    Greenspan, D.S.4
  • 53
    • 0035862774 scopus 로고    scopus 로고
    • Gdf11 is a negative regulator of chondrogenesis and myogenesis in the developing chick limb
    • Gamer LW, Cox KA, Small C, Rosen V 2001 Gdf11 is a negative regulator of chondrogenesis and myogenesis in the developing chick limb. Dev Biol 229:407-420
    • (2001) Dev Biol , vol.229 , pp. 407-420
    • Gamer, L.W.1    Cox, K.A.2    Small, C.3    Rosen, V.4
  • 55
    • 0031570780 scopus 로고    scopus 로고
    • Opposing effects of activin A and follistatin on developing skeletal muscle cells
    • Link BA, Nishi R 1997 Opposing effects of activin A and follistatin on developing skeletal muscle cells. Exp Cell Res 233:350-362
    • (1997) Exp Cell Res , vol.233 , pp. 350-362
    • Link, B.A.1    Nishi, R.2
  • 57
    • 0025741546 scopus 로고
    • Follistatin binds to both activin and inhibin through the common subunit
    • Shimonaka M, Inouye S, Shimasaki S, Ling N 1991 Follistatin binds to both activin and inhibin through the common subunit. Endocrinology 128:3313-3315
    • (1991) Endocrinology , vol.128 , pp. 3313-3315
    • Shimonaka, M.1    Inouye, S.2    Shimasaki, S.3    Ling, N.4
  • 62
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M 1996 Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem 68:850-858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4


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