메뉴 건너뛰기




Volumn 9, Issue 11, 2010, Pages 2482-2496

Dynamics of the skeletal muscle secretome during myoblast differentiation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYTOKINE; GROWTH FACTOR; HYDROXYPROLINE; MESSENGER RNA; METALLOPROTEINASE; SEMAPHORIN; SOMATOMEDIN BINDING PROTEIN 1; SOMATOMEDIN BINDING PROTEIN 2; TRANSFORMING GROWTH FACTOR BETA1; TRANSFORMING GROWTH FACTOR BETA2; TRANSFORMING GROWTH FACTOR BETA3;

EID: 78149306422     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.002113     Document Type: Article
Times cited : (246)

References (78)
  • 1
    • 71249157791 scopus 로고    scopus 로고
    • The diseasome of physical inactivity - and the role of myokines in muscle-fat cross talk
    • Pedersen, B. K. (2009) The diseasome of physical inactivity - and the role of myokines in muscle-fat cross talk. J. Physiol. 587, 5559-5568
    • (2009) J. Physiol. , vol.587 , pp. 5559-5568
    • Pedersen, B.K.1
  • 2
    • 0034668926 scopus 로고    scopus 로고
    • Production of interleukin-6 in contracting human skeletal muscles can account for the exercise-induced increase in plasma interleukin-6
    • Steensberg, A., van Hall, G., Osada, T., Sacchetti, M., Saltin, B., and Klarlund Pedersen, B. (2000) Production of interleukin-6 in contracting human skeletal muscles can account for the exercise-induced increase in plasma interleukin-6. J. Physiol. 529, 237-242
    • (2000) J. Physiol. , vol.529 , pp. 237-242
    • Steensberg, A.1    Van Hall, G.2    Osada, T.3    Sacchetti, M.4    Saltin, B.5    Klarlund Pedersen, B.6
  • 3
    • 55949119252 scopus 로고    scopus 로고
    • Muscle as an endocrine organ: Focus on muscle-derived interleukin-6
    • Pedersen, B. K., and Febbraio, M. A. (2008) Muscle as an endocrine organ: focus on muscle-derived interleukin-6. Physiol. Rev. 88, 1379-1406
    • (2008) Physiol. Rev. , vol.88 , pp. 1379-1406
    • Pedersen, B.K.1    Febbraio, M.A.2
  • 5
    • 58549110244 scopus 로고    scopus 로고
    • Adipokines, myokines and cardiovascular disease
    • Walsh, K. (2009) Adipokines, myokines and cardiovascular disease. Circ. J. 73, 13-18
    • (2009) Circ. J. , vol.73 , pp. 13-18
    • Walsh, K.1
  • 6
    • 33847396262 scopus 로고    scopus 로고
    • Identification of secreted proteins during skeletal muscle development
    • Chan, X. C., McDermott, J. C., and Siu, K. W. (2007) Identification of secreted proteins during skeletal muscle development. J. Proteome Res. 6, 698-710
    • (2007) J. Proteome Res. , vol.6 , pp. 698-710
    • Chan, X.C.1    McDermott, J.C.2    Siu, K.W.3
  • 7
    • 63249100559 scopus 로고    scopus 로고
    • Increased secretion and expression of myostatin in skeletal muscle from extremely obese women
    • Hittel, D. S., Berggren, J. R., Shearer, J., Boyle, K., and Houmard, J. A. (2009) Increased secretion and expression of myostatin in skeletal muscle from extremely obese women. Diabetes 58, 30-38
    • (2009) Diabetes , vol.58 , pp. 30-38
    • Hittel, D.S.1    Berggren, J.R.2    Shearer, J.3    Boyle, K.4    Houmard, J.A.5
  • 9
    • 70349321247 scopus 로고    scopus 로고
    • Receptor tyrosine kinase signaling: A view from quantitative proteomics
    • Dengjel, J., Kratchmarova, I., and Blagoev, B. (2009) Receptor tyrosine kinase signaling: a view from quantitative proteomics. Mol. Biosyst. 5, 1112-1121
    • (2009) Mol. Biosyst. , vol.5 , pp. 1112-1121
    • Dengjel, J.1    Kratchmarova, I.2    Blagoev, B.3
  • 10
    • 20344363684 scopus 로고    scopus 로고
    • Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation
    • Kratchmarova, I., Blagoev, B., Haack-Sorensen, M., Kassem, M., and Mann, M. (2005) Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation. Science 308, 1472-1477
    • (2005) Science , vol.308 , pp. 1472-1477
    • Kratchmarova, I.1    Blagoev, B.2    Haack-Sorensen, M.3    Kassem, M.4    Mann, M.5
  • 12
    • 67449107495 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) and quantitative comparison of the membrane proteomes of self-renewing and differentiating human embryonic stem cells
    • Prokhorova, T. A., Rigbolt, K. T., Johansen, P. T., Henningsen, J., Kratchmarova, I., Kassem, M., and Blagoev, B. (2009) Stable isotope labeling by amino acids in cell culture (SILAC) and quantitative comparison of the membrane proteomes of self-renewing and differentiating human embryonic stem cells. Mol. Cell. Proteomics 8, 959-970
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 959-970
    • Prokhorova, T.A.1    Rigbolt, K.T.2    Johansen, P.T.3    Henningsen, J.4    Kratchmarova, I.5    Kassem, M.6    Blagoev, B.7
  • 13
    • 33750336592 scopus 로고    scopus 로고
    • Quantitative proteomics to study mitogen-activated protein kinases
    • DOI 10.1016/j.ymeth.2006.08.001, PII S1046202306001691
    • Blagoev, B., and Mann, M. (2006) Quantitative proteomics to study mitogen-activated protein kinases. Methods 40, 243-250 (Pubitemid 44635297)
    • (2006) Methods , vol.40 , Issue.3 , pp. 243-250
    • Blagoev, B.1    Mann, M.2
  • 14
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 15
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • Rappsilber, J., Mann, M., and Ishihama, Y. (2007) Protocol for micropurification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat. Protoc. 2, 1896-1906
    • (2007) Nat. Protoc. , vol.2 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 17
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox, J., Matic, I., Hilger, M., Nagaraj, N., Selbach, M., Olsen, J. V., and Mann, M. (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4, 698-705
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 19
    • 61349177268 scopus 로고    scopus 로고
    • Mfuzz: A software package for soft clustering of microarray data
    • Kumar, L., and Futschik, M. E. (2007) Mfuzz: a software package for soft clustering of microarray data. Bioinformation 2, 5-7
    • (2007) Bioinformation , vol.2 , pp. 5-7
    • Kumar, L.1    Futschik, M.E.2
  • 20
    • 35748932852 scopus 로고    scopus 로고
    • R Development Core Team R Foundation for Statistical Computing, Vienna, Austria
    • R Development Core Team (2007) R: a Language and Environment for Statistical Computing, R Foundation for Statistical Computing, Vienna, Austria
    • (2007) R: A Language and Environment for Statistical Computing
  • 21
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 23
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 24
    • 0347989458 scopus 로고    scopus 로고
    • Cellular and molecular regulation of muscle regeneration
    • Chargé, S. B., and Rudnicki, M. A. (2004) Cellular and molecular regulation of muscle regeneration. Physiol. Rev. 84, 209-238
    • (2004) Physiol. Rev. , vol.84 , pp. 209-238
    • Chargé, S.B.1    Rudnicki, M.A.2
  • 25
    • 84934434314 scopus 로고    scopus 로고
    • Molecular control of mammalian myoblast fusion
    • Jansen, K. M., and Pavlath, G. K. (2008) Molecular control of mammalian myoblast fusion. Methods Mol. Biol. 475, 115-133
    • (2008) Methods Mol. Biol. , vol.475 , pp. 115-133
    • Jansen, K.M.1    Pavlath, G.K.2
  • 26
    • 24344491888 scopus 로고    scopus 로고
    • MyoD and the transcriptional control of myogenesis
    • Berkes, C. A., and Tapscott, S. J. (2005) MyoD and the transcriptional control of myogenesis. Semin. Cell Dev. Biol. 16, 585-595
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 585-595
    • Berkes, C.A.1    Tapscott, S.J.2
  • 27
    • 21644434750 scopus 로고    scopus 로고
    • The circuitry of a master switch: Myod and the regulation of skeletal muscle gene transcription
    • Tapscott, S. J. (2005) The circuitry of a master switch: Myod and the regulation of skeletal muscle gene transcription. Development 132, 2685-2695
    • (2005) Development , vol.132 , pp. 2685-2695
    • Tapscott, S.J.1
  • 28
    • 0034918907 scopus 로고    scopus 로고
    • Myogenic satellite cells: Physiology to molecular biology
    • Hawke, T. J., and Garry, D. J. (2001) Myogenic satellite cells: physiology to molecular biology. J. Appl. Physiol. 91, 534-551
    • (2001) J. Appl. Physiol. , vol.91 , pp. 534-551
    • Hawke, T.J.1    Garry, D.J.2
  • 29
    • 41549084155 scopus 로고    scopus 로고
    • Kollias, H. D., and McDermott, J. C. (2008) Transforming growth factor-beta 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
  • 30
    • 47549090432 scopus 로고    scopus 로고
    • TGFbeta in cancer
    • Massagué, J. (2008) TGFbeta in cancer. Cell 134, 215-230
    • (2008) Cell , vol.134 , pp. 215-230
    • Massagué, J.1
  • 31
    • 0025859372 scopus 로고
    • Secretion and transcriptional regulation of transforming growth factor-beta 3 during myogenesis
    • Lafyatis, R., Lechleider, R., Roberts, A. B., and Sporn, M. B. (1991) Secretion and transcriptional regulation of transforming growth factor-beta 3 during myogenesis. Mol. Cell. Biol. 11, 3795-3803
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3795-3803
    • Lafyatis, R.1    Lechleider, R.2    Roberts, A.B.3    Sporn, M.B.4
  • 32
    • 0038622952 scopus 로고    scopus 로고
    • Characterization of proliferating human skeletal muscle-derived cells in vitro: Differential modulation of myoblast markers by TGF-beta2
    • Stewart, J. D., Masi, T. L., Cumming, A. E., Molnar, G. M., Wentworth, B. M., Sampath, K., McPherson, J. M., and Yaeger, P. C. (2003) Characterization of proliferating human skeletal muscle-derived cells in vitro: differential modulation of myoblast markers by TGF-beta2. J. Cell. Physiol. 196, 70-78
    • (2003) J. Cell. Physiol. , vol.196 , pp. 70-78
    • Stewart, J.D.1    Masi, T.L.2    Cumming, A.E.3    Molnar, G.M.4    Wentworth, B.M.5    Sampath, K.6    McPherson, J.M.7    Yaeger, P.C.8
  • 33
    • 58149494139 scopus 로고    scopus 로고
    • TGF-beta's delay skeletal muscle progenitor cell differentiation in an isoform-independent manner
    • Schabort, E. J., van der Merwe, M., Loos, B., Moore, F. P., and Niesler, C. U. (2009) TGF-beta's delay skeletal muscle progenitor cell differentiation in an isoform-independent manner. Exp. Cell Res. 315, 373-384
    • (2009) Exp. Cell Res. , vol.315 , pp. 373-384
    • Schabort, E.J.1    Van Der Merwe, M.2    Loos, B.3    Moore, F.P.4    Niesler, C.U.5
  • 34
    • 0026625171 scopus 로고
    • Transforming growth factor beta induces myoblast differentiation in the presence of mitogens
    • Zentella, A., and Massagué, J. (1992) Transforming growth factor beta induces myoblast differentiation in the presence of mitogens. Proc. Natl. Acad. Sci. U.S.A. 89, 5176-5180
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5176-5180
    • Zentella, A.1    Massagué, J.2
  • 35
    • 0032514696 scopus 로고    scopus 로고
    • Inhibition of myogenesis by transforming growth factor beta is density-dependent and related to the translocation of transcription factor MEF2 to the cytoplasm
    • De Angelis, L., Borghi, S., Melchionna, R., Berghella, L., Baccarani-Contri, M., Parise, F., Ferrari, S., and Cossu, G. (1998) Inhibition of myogenesis by transforming growth factor beta is density-dependent and related to the translocation of transcription factor MEF2 to the cytoplasm. Proc. Natl. Acad. Sci. U.S.A. 95, 12358-12363
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12358-12363
    • De Angelis, L.1    Borghi, S.2    Melchionna, R.3    Berghella, L.4    Baccarani-Contri, M.5    Parise, F.6    Ferrari, S.7    Cossu, G.8
  • 37
    • 0031032250 scopus 로고    scopus 로고
    • Cellular localisation of transforming growth factor-beta 2 and -beta 3 (TGF-beta2, TGF-beta3) in damaged and regenerating skeletal muscles
    • McLennan, I. S., and Koishi, K. (1997) Cellular localisation of transforming growth factor-beta 2 and -beta 3 (TGF-beta2, TGF-beta3) in damaged and regenerating skeletal muscles. Dev. Dyn. 208, 278-289
    • (1997) Dev. Dyn. , vol.208 , pp. 278-289
    • McLennan, I.S.1    Koishi, K.2
  • 38
    • 31144456086 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 upregulates myostatin expression in mouse C2C12 myoblasts
    • Budasz-Swiderska, M., Jank, M., and Motyl, T. (2005) Transforming growth factor-beta1 upregulates myostatin expression in mouse C2C12 myoblasts. J. Physiol. Pharmacol. 56, Suppl. 3, 195-214
    • (2005) J. Physiol. Pharmacol. , vol.56 , Issue.SUPPL. 3 , pp. 195-214
    • Budasz-Swiderska, M.1    Jank, M.2    Motyl, T.3
  • 39
    • 33846888550 scopus 로고    scopus 로고
    • Transforming growth factor-beta following skeletal muscle strain injury in rats
    • Smith, C. A., Stauber, F., Waters, C., Alway, S. E., and Stauber, W. T. (2007) Transforming growth factor-beta following skeletal muscle strain injury in rats. J. Appl. Physiol. 102, 755-761
    • (2007) J. Appl. Physiol. , vol.102 , pp. 755-761
    • Smith, C.A.1    Stauber, F.2    Waters, C.3    Alway, S.E.4    Stauber, W.T.5
  • 40
    • 33747015300 scopus 로고    scopus 로고
    • Extracellular proteoglycans modify TGF-beta bio-availability attenuating its signaling during skeletal muscle differentiation
    • Droguett, R., Cabello-Verrugio, C., Riquelme, C., and Brandan, E. (2006) Extracellular 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
    • Droguett, R.1    Cabello-Verrugio, C.2    Riquelme, C.3    Brandan, E.4
  • 41
    • 56949083199 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy
    • Brandan, E., Cabello-Verrugio, C., and Vial, C. (2008) Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy. Matrix Biol. 27, 700-708
    • (2008) Matrix Biol. , vol.27 , pp. 700-708
    • Brandan, E.1    Cabello-Verrugio, C.2    Vial, C.3
  • 42
    • 15844399441 scopus 로고    scopus 로고
    • Insulin-like growth factor-II is an autocrine survival factor for differentiating myoblasts
    • Stewart, C. E., and Rotwein, P. (1996) Insulin-like growth factor-II is an autocrine survival factor for differentiating myoblasts. J. Biol. Chem. 271, 11330-11338
    • (1996) J. Biol. Chem. , vol.271 , pp. 11330-11338
    • Stewart, C.E.1    Rotwein, P.2
  • 43
    • 24744449943 scopus 로고    scopus 로고
    • IGF-1, inflammation and stem cells: Interactions during muscle regeneration
    • Mourkioti, F., and Rosenthal, N. (2005) IGF-1, inflammation and stem cells: interactions during muscle regeneration. Trends Immunol. 26, 535-542
    • (2005) Trends Immunol. , vol.26 , pp. 535-542
    • Mourkioti, F.1    Rosenthal, N.2
  • 44
    • 61649096363 scopus 로고    scopus 로고
    • Insulin-like growth factor I (IGF-I) is a more potent regulator of gene expression than insulin in primary human myoblasts and myotubes
    • Palsgaard, J., Brown, A. E., Jensen, M., Borup, R., Walker, M., and De Meyts, P. (2009) Insulin-like growth factor I (IGF-I) is a more potent regulator of gene expression than insulin in primary human myoblasts and myotubes. Growth Horm. IGF Res. 19, 168-178
    • (2009) Growth Horm. IGF Res. , vol.19 , pp. 168-178
    • Palsgaard, J.1    Brown, A.E.2    Jensen, M.3    Borup, R.4    Walker, M.5    De Meyts, P.6
  • 46
    • 20744455262 scopus 로고    scopus 로고
    • IGF-binding proteins - The pieces are falling into place
    • Bach, L. A., Headey, S. J., and Norton, R. S. (2005) IGF-binding proteins-the pieces are falling into place. Trends Endocrinol. Metab. 16, 228-234
    • (2005) Trends Endocrinol. Metab. , vol.16 , pp. 228-234
    • Bach, L.A.1    Headey, S.J.2    Norton, R.S.3
  • 47
    • 18144407972 scopus 로고    scopus 로고
    • Roles of insulin-like growth factor (IGF) binding proteins in regulating IGF actions
    • Duan, C., and Xu, Q. (2005) Roles of insulin-like growth factor (IGF) binding proteins in regulating IGF actions. Gen. Comp. Endocrinol. 142, 44-52
    • (2005) Gen. Comp. Endocrinol. , vol.142 , pp. 44-52
    • Duan, C.1    Xu, Q.2
  • 48
    • 27844611241 scopus 로고    scopus 로고
    • Pregnancy-associated plasma protein-A regulates myoblast proliferation and differentiation through an insulin-like growth factor-dependent mechanism
    • Kumar, A., Mohan, S., Newton, J., Rehage, M., Tran, K., Baylink, D. J., and Qin, X. (2005) Pregnancy-associated plasma protein-A regulates myoblast proliferation and differentiation through an insulin-like growth factor-dependent mechanism. J. Biol. Chem. 280, 37782-37789
    • (2005) J. Biol. Chem. , vol.280 , pp. 37782-37789
    • Kumar, A.1    Mohan, S.2    Newton, J.3    Rehage, M.4    Tran, K.5    Baylink, D.J.6    Qin, X.7
  • 49
    • 0027518204 scopus 로고
    • A highly conserved insulin-like growth factor-binding protein (IGFBP-5) is expressed during myoblast differentiation
    • James, P. L., Jones, S. B., Busby, W. H., Jr., Clemmons, D. R., and Rotwein, P. (1993) A highly conserved insulin-like growth factor-binding protein (IGFBP-5) is expressed during myoblast differentiation. J. Biol. Chem. 268, 22305-22312
    • (1993) J. Biol. Chem. , vol.268 , pp. 22305-22312
    • James, P.L.1    Jones, S.B.2    Busby Jr., W.H.3    Clemmons, D.R.4    Rotwein, P.5
  • 51
    • 38049021087 scopus 로고    scopus 로고
    • Insulin-like growth factor (IGF) binding protein-5 blocks skeletal muscle differentiation by inhibiting IGF actions
    • Mukherjee, A., Wilson, E. M., and Rotwein, P. (2008) Insulin-like growth factor (IGF) binding protein-5 blocks skeletal muscle differentiation by inhibiting IGF actions. Mol. Endocrinol. 22, 206-215
    • (2008) Mol. Endocrinol. , vol.22 , pp. 206-215
    • Mukherjee, A.1    Wilson, E.M.2    Rotwein, P.3
  • 52
    • 51649125241 scopus 로고    scopus 로고
    • IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop
    • Ren, H., Yin, P., and Duan, C. (2008) IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop. J. Cell Biol. 182, 979-991
    • (2008) J. Cell Biol. , vol.182 , pp. 979-991
    • Ren, H.1    Yin, P.2    Duan, C.3
  • 53
    • 52649157711 scopus 로고    scopus 로고
    • Combined use of RNAi and quantitative proteomics to study gene function in Drosophila
    • Bonaldi, T., Straub, T., Cox, J., Kumar, C., Becker, P. B., and Mann, M. (2008) Combined use of RNAi and quantitative proteomics to study gene function in Drosophila. Mol. Cell 31, 762-772
    • (2008) Mol. Cell , vol.31 , pp. 762-772
    • Bonaldi, T.1    Straub, T.2    Cox, J.3    Kumar, C.4    Becker, P.B.5    Mann, M.6
  • 54
  • 55
    • 0025993772 scopus 로고
    • "Spontaneous" differentiation of skeletal myoblasts is dependent upon autocrine secretion of insulin-like growth factor-II
    • Florini, J. R., Magri, K. A., Ewton, D. Z., James, P. L., Grindstaff, K., and Rotwein, P. S. (1991) "Spontaneous" differentiation of skeletal myoblasts is dependent upon autocrine secretion of insulin-like growth factor-II. J. Biol. Chem. 266, 15917-15923
    • (1991) J. Biol. Chem. , vol.266 , pp. 15917-15923
    • Florini, J.R.1    Magri, K.A.2    Ewton, D.Z.3    James, P.L.4    Grindstaff, K.5    Rotwein, P.S.6
  • 56
    • 0348108124 scopus 로고    scopus 로고
    • Role of semaphorins in the adult nervous system
    • de Wit, J., and Verhaagen, J. (2003) Role of semaphorins in the adult nervous system. Prog. Neurobiol. 71, 249-267
    • (2003) Prog. Neurobiol. , vol.71 , pp. 249-267
    • De Wit, J.1    Verhaagen, J.2
  • 61
    • 68849090941 scopus 로고    scopus 로고
    • A new role for satellite cells: Control of reinnervation after muscle injury by semaphorin 3A. Focus on "Possible implication of satellite cells in regenerative motoneuritogenesis: HGF upregulates neural chemorepellent Sema3A during myogenic differentiation"
    • McLoon, L. K. (2009) A new role for satellite cells: control of reinnervation after muscle injury by semaphorin 3A. Focus on "Possible implication of satellite cells in regenerative motoneuritogenesis: HGF upregulates neural chemorepellent Sema3A during myogenic differentiation". Am. J. Physiol. Cell Physiol. 297, C227-C230
    • (2009) Am. J. Physiol. Cell Physiol. , vol.297
    • McLoon, L.K.1
  • 62
    • 41549099965 scopus 로고    scopus 로고
    • Semaphorin signaling: Progress made and promises ahead
    • Zhou, Y., Gunput, R. A., and Pasterkamp, R. J. (2008) Semaphorin signaling: progress made and promises ahead. Trends Biochem. Sci. 33, 161-170
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 161-170
    • Zhou, Y.1    Gunput, R.A.2    Pasterkamp, R.J.3
  • 63
    • 38349097288 scopus 로고    scopus 로고
    • Semaphorin 6C expression in innervated and denervated skeletal muscle
    • Svensson, A., Libelius, R., and Tågerud, S. (2008) Semaphorin 6C expression in innervated and denervated skeletal muscle. J. Mol. Histol. 39, 5-13
    • (2008) J. Mol. Histol. , vol.39 , pp. 5-13
    • Svensson, A.1    Libelius, R.2    Tågerud, S.3
  • 64
    • 0030722135 scopus 로고    scopus 로고
    • The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing
    • Adams, R. H., Lohrum, M., Klostermann, A., Betz, H., and Püschel, A. W. (1997) The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing. EMBO J. 16, 6077-6086
    • (1997) EMBO J. , vol.16 , pp. 6077-6086
    • Adams, R.H.1    Lohrum, M.2    Klostermann, A.3    Betz, H.4    Püschel, A.W.5
  • 66
    • 34547665538 scopus 로고    scopus 로고
    • Functional interaction between matrix metalloproteinase-3 and semaphorin-3C during cortical axonal growth and guidance
    • Gonthier, B., Nasarre, C., Roth, L., Perraut, M., Thomasset, N., Roussel, G., Aunis, D., and Bagnard, D. (2007) Functional interaction between matrix metalloproteinase-3 and semaphorin-3C during cortical axonal growth and guidance. Cereb. Cortex 17, 1712-1721
    • (2007) Cereb. Cortex , vol.17 , pp. 1712-1721
    • Gonthier, B.1    Nasarre, C.2    Roth, L.3    Perraut, M.4    Thomasset, N.5    Roussel, G.6    Aunis, D.7    Bagnard, D.8
  • 70
    • 0035313110 scopus 로고    scopus 로고
    • Biological activity of soluble CD100. I. The extracellular region of CD100 is released from the surface of T lymphocytes by regulated proteolysis
    • Elhabazi, A., Delaire, S., Bensussan, A., Boumsell, L., and Bismuth, G. (2001) Biological activity of soluble CD100. I. The extracellular region of CD100 is released from the surface of T lymphocytes by regulated proteolysis. J. Immunol. 166, 4341-4347
    • (2001) J. Immunol. , vol.166 , pp. 4341-4347
    • Elhabazi, A.1    Delaire, S.2    Bensussan, A.3    Boumsell, L.4    Bismuth, G.5
  • 71
    • 34250307200 scopus 로고    scopus 로고
    • MT1-MMP controls tumor-induced angiogenesis through the release of semaphorin 4D
    • DOI 10.1074/jbc.M609570200
    • Basile, J. R., Holmbeck, K., Bugge, T. H., and Gutkind, J. S. (2007) MT1-MMP controls tumor-induced angiogenesis through the release of semaphorin 4D. J. Biol. Chem. 282, 6899-6905 (Pubitemid 47100895)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6899-6905
    • Basile, J.R.1    Holmbeck, K.2    Bugge, T.H.3    Gutkind, J.S.4
  • 72
    • 34247341829 scopus 로고    scopus 로고
    • Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome
    • Dean, R. A., and Overall, C. M. (2007) Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome. Mol. Cell. Proteomics 6, 611-623
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 611-623
    • Dean, R.A.1    Overall, C.M.2
  • 73
    • 22244440847 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression
    • Kaelin, W. G. (2005) Proline hydroxylation and gene expression. Annu. Rev. Biochem. 74, 115-128
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 115-128
    • Kaelin, W.G.1
  • 74
    • 53849096006 scopus 로고    scopus 로고
    • The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens
    • Krane, S. M. (2008) The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens. Amino Acids 35, 703-710
    • (2008) Amino Acids , vol.35 , pp. 703-710
    • Krane, S.M.1
  • 76
    • 0034881956 scopus 로고    scopus 로고
    • You are what you secrete
    • Saltiel, A. R. (2001) You are what you secrete. Nat. Med. 7, 887-888
    • (2001) Nat. Med. , vol.7 , pp. 887-888
    • Saltiel, A.R.1
  • 77
    • 70350159156 scopus 로고    scopus 로고
    • Edward F. Adolph distinguished lecture: Muscle as an endocrine organ: IL-6 and other myokines
    • Pedersen, B. K. (2009) Edward F. Adolph distinguished lecture: muscle as an endocrine organ: IL-6 and other myokines. J. Appl. Physiol. 107, 1006-1014
    • (2009) J. Appl. Physiol. , vol.107 , pp. 1006-1014
    • Pedersen, B.K.1
  • 78
    • 77953916879 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y., and Hochberg, Y. (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. Journal of the Royal Statistical Society 57, 125-133
    • (1995) Journal of the Royal Statistical Society , vol.57 , pp. 125-133
    • Benjamini, Y.1    Hochberg, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.