메뉴 건너뛰기




Volumn 426, Issue 1, 2012, Pages 83-88

Myostatin facilitates slow and inhibits fast myosin heavy chain expression during myogenic differentiation

Author keywords

ActRIIB; EDL; Mstn; Myh; Myofiber; Myosin heavy chain; Myostatin (Mstn); Satellite cells; SOL; TGF

Indexed keywords

ACTIVIN RECEPTOR; MYOSIN HEAVY CHAIN; MYOSTATIN;

EID: 84866335275     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.08.040     Document Type: Article
Times cited : (53)

References (38)
  • 1
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member
    • McPherron A.C., Lawler A.M., Lee S.J. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 1997, 387:83-90.
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 2
    • 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 J.J., Qiu Y., Hewick R.M., Wolfman N.M. 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. 2003, 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
  • 3
    • 0037174939 scopus 로고    scopus 로고
    • The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum
    • Hill J.J., Davies M.V., Pearson A.A., Wang J.H., Hewick R.M., Wolfman N.M., Qiu Y. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J. Biol. Chem. 2002, 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
  • 5
    • 0031685620 scopus 로고    scopus 로고
    • TGF-beta signal transduction
    • Massague J. TGF-beta signal transduction. Annu. Rev. Biochem. 1998, 67:753-791.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 753-791
    • Massague, J.1
  • 6
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling from cell membrane to the nucleus
    • Shi Y., Massague J. Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell 2003, 113:685-700.
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massague, J.2
  • 7
    • 41549084155 scopus 로고    scopus 로고
    • Transforming growth factor-beta and myostatin signaling in skeletal muscle
    • Kollias H.D., McDermott J.C. Transforming growth factor-beta and myostatin signaling in skeletal muscle. J. Appl. Physiol. 2008, 104:579-587.
    • (2008) J. Appl. Physiol. , vol.104 , pp. 579-587
    • Kollias, H.D.1    McDermott, J.C.2
  • 8
    • 8444243360 scopus 로고    scopus 로고
    • Regulation of muscle mass by myostatin
    • Lee S.J. Regulation of muscle mass by myostatin. Annu. Rev. Cell Dev. Biol. 2004, 20:61-86.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 61-86
    • Lee, S.J.1
  • 9
    • 80054760368 scopus 로고    scopus 로고
    • Fiber Types in Mammalian Skeletal Muscles
    • Schiaffino S., Reggiani C. Fiber Types in Mammalian Skeletal Muscles. Physiol. Rev. 2011, 91:1447-1531.
    • (2011) Physiol. Rev. , vol.91 , pp. 1447-1531
    • Schiaffino, S.1    Reggiani, C.2
  • 11
    • 78651353542 scopus 로고    scopus 로고
    • Posttranscriptional mechanisms involving microRNA-27a and b contribute to fast-specific and glucocorticoid-mediated myostatin expression in skeletal muscle
    • Allen D.L., Loh A.S. Posttranscriptional mechanisms involving microRNA-27a and b contribute to fast-specific and glucocorticoid-mediated myostatin expression in skeletal muscle. Am. J. Physiol. Cell Physiol. 2011, 300:C124-137.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300
    • Allen, D.L.1    Loh, A.S.2
  • 12
    • 84995103242 scopus 로고
    • Muscle fibre type and size, and muscle capillary density in young double-muscled blue Belgian cattle
    • Stavaux D., Art T., McEntee K., Reznick M., Lekeux P. Muscle fibre type and size, and muscle capillary density in young double-muscled blue Belgian cattle. Zentralbl. Veterinarmed. A 1994, 41:229-236.
    • (1994) Zentralbl. Veterinarmed. A , vol.41 , pp. 229-236
    • Stavaux, D.1    Art, T.2    McEntee, K.3    Reznick, M.4    Lekeux, P.5
  • 13
    • 11144247719 scopus 로고    scopus 로고
    • Loss of myostatin expression alters fiber-type distribution and expression of myosin heavy chain isoforms in slow- and fast-type skeletal muscle
    • Girgenrath S., Song K., Whittemore L.A. Loss of myostatin expression alters fiber-type distribution and expression of myosin heavy chain isoforms in slow- and fast-type skeletal muscle. Muscle Nerve 2005, 31:34-40.
    • (2005) Muscle Nerve , vol.31 , pp. 34-40
    • Girgenrath, S.1    Song, K.2    Whittemore, L.A.3
  • 14
    • 0141768237 scopus 로고    scopus 로고
    • Myostatin negatively regulates satellite cell activation and self-renewal
    • McCroskery S., Thomas M., Maxwell L., Sharma M., Kambadur R. Myostatin negatively regulates satellite cell activation and self-renewal. J. Cell Biol. 2003, 162:1135-1147.
    • (2003) J. Cell Biol. , vol.162 , pp. 1135-1147
    • McCroskery, S.1    Thomas, M.2    Maxwell, L.3    Sharma, M.4    Kambadur, R.5
  • 17
    • 67650071006 scopus 로고    scopus 로고
    • Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin
    • Gilson H., Schakman O., Kalista S., Lause P., Tsuchida K., Thissen J.P. Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. Am. J. Physiol. Endocrinol. Metab. 2009, 297:E157-E164.
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.297
    • Gilson, H.1    Schakman, O.2    Kalista, S.3    Lause, P.4    Tsuchida, K.5    Thissen, J.P.6
  • 18
    • 77749292129 scopus 로고    scopus 로고
    • High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo
    • Yamada M., Tatsumi R., Yamanouchi K., Hosoyama T., Shiratsuchi S., Sato A., Mizunoya W., Ikeuchi Y., Furuse M., Allen R.E. High concentrations of HGF inhibit skeletal muscle satellite cell proliferation in vitro by inducing expression of myostatin: a possible mechanism for reestablishing satellite cell quiescence in vivo. Am. J. Physiol. Cell Physiol. 2010, 298:C465-C476.
    • (2010) Am. J. Physiol. Cell Physiol. , vol.298
    • Yamada, M.1    Tatsumi, R.2    Yamanouchi, K.3    Hosoyama, T.4    Shiratsuchi, S.5    Sato, A.6    Mizunoya, W.7    Ikeuchi, Y.8    Furuse, M.9    Allen, R.E.10
  • 19
    • 84862834932 scopus 로고    scopus 로고
    • MicroRNA-27a promotes myoblast proliferation by targeting myostatin
    • Huang Z., Chen X., Yu B., He J., Chen D. MicroRNA-27a promotes myoblast proliferation by targeting myostatin. Biochem. Biophys. Res. Commun. 2012, 423:265-269.
    • (2012) Biochem. Biophys. Res. Commun. , vol.423 , pp. 265-269
    • Huang, Z.1    Chen, X.2    Yu, B.3    He, J.4    Chen, D.5
  • 20
    • 84860523933 scopus 로고    scopus 로고
    • Myostatin stimulates myosatellite cell differentiation in a novel model system: evidence for gene subfunctionalization
    • Garikipati D.K., Rodgers B.D. Myostatin stimulates myosatellite cell differentiation in a novel model system: evidence for gene subfunctionalization. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2012, 302:R1059-1066.
    • (2012) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.302
    • Garikipati, D.K.1    Rodgers, B.D.2
  • 22
    • 78149345366 scopus 로고    scopus 로고
    • Myostatin genotype regulates muscle-specific miRNA expression in mouse pectoralis muscle
    • Rachagani S., Cheng Y., Reecy J.M. Myostatin genotype regulates muscle-specific miRNA expression in mouse pectoralis muscle. BMC Res. Notes 2010, 3:297.
    • (2010) BMC Res. Notes , vol.3 , pp. 297
    • Rachagani, S.1    Cheng, Y.2    Reecy, J.M.3
  • 24
    • 33745576161 scopus 로고    scopus 로고
    • Production of a monoclonal anti-myostatin antibody and the effects of in ovo administration of the antibody on posthatch broiler growth and muscle mass
    • Kim Y.S., Bobbili N.K., Paek K.S., Jin H.J. Production of a monoclonal anti-myostatin antibody and the effects of in ovo administration of the antibody on posthatch broiler growth and muscle mass. Poult. Sci. 2006, 85:1062-1071.
    • (2006) Poult. Sci. , vol.85 , pp. 1062-1071
    • Kim, Y.S.1    Bobbili, N.K.2    Paek, K.S.3    Jin, H.J.4
  • 25
    • 83655201207 scopus 로고    scopus 로고
    • Production of bioactive extracellular domain of pig and chicken activin type IIB receptors in Pichiapastoris
    • Kim Y.S., Kim K.H., Kim C.J. Production of bioactive extracellular domain of pig and chicken activin type IIB receptors in Pichiapastoris. Process Biochem. 2012, 47:139-146.
    • (2012) Process Biochem. , vol.47 , pp. 139-146
    • Kim, Y.S.1    Kim, K.H.2    Kim, C.J.3
  • 27
    • 0022480289 scopus 로고
    • Effects of age on enzyme-histochemical fiber spectra and contractile properties of fast-twitch and slow-twitch skeletal-muscles in the rat
    • Larsson L., Edstrom L. Effects of age on enzyme-histochemical fiber spectra and contractile properties of fast-twitch and slow-twitch skeletal-muscles in the rat. J. Neurol. Sci. 1986, 76:69-89.
    • (1986) J. Neurol. Sci. , vol.76 , pp. 69-89
    • Larsson, L.1    Edstrom, L.2
  • 28
    • 13844280354 scopus 로고    scopus 로고
    • 'Fast' and 'slow' muscle fibres in hindlimb muscles of adult rats regenerate from intrinsically different satellite cells
    • Kalhovde J.M., Jerkovic R., Sefland I., Cordonnier C., Calabria E., Schiaffino S., Lomo T. 'Fast' and 'slow' muscle fibres in hindlimb muscles of adult rats regenerate from intrinsically different satellite cells. J. Physiol. Lond. 2005, 562:847-857.
    • (2005) J. Physiol. Lond. , vol.562 , pp. 847-857
    • Kalhovde, J.M.1    Jerkovic, R.2    Sefland, I.3    Cordonnier, C.4    Calabria, E.5    Schiaffino, S.6    Lomo, T.7
  • 29
    • 43749121617 scopus 로고    scopus 로고
    • Slow- and fast-twitch rat hind limb skeletal muscle phenotypes 8 months after spinal cord transection and olfactory ensheathing glia transplantation
    • Negredo P., Rivero J.L.L., Gonzalez B., Ramon-Cueto A., Manso R. Slow- and fast-twitch rat hind limb skeletal muscle phenotypes 8 months after spinal cord transection and olfactory ensheathing glia transplantation. J. Physiol. Lond. 2008, 586:2593-2610.
    • (2008) J. Physiol. Lond. , vol.586 , pp. 2593-2610
    • Negredo, P.1    Rivero, J.L.L.2    Gonzalez, B.3    Ramon-Cueto, A.4    Manso, R.5
  • 31
    • 83055184196 scopus 로고    scopus 로고
    • Intramuscular adipose is derived from a non-Pax3 lineage and required for efficient regeneration of skeletal muscles
    • Liu W.Y., Liu Y.Q., Lai X.S., Kuang S.H. Intramuscular adipose is derived from a non-Pax3 lineage and required for efficient regeneration of skeletal muscles. Dev. Biol. 2012, 361:27-38.
    • (2012) Dev. Biol. , vol.361 , pp. 27-38
    • Liu, W.Y.1    Liu, Y.Q.2    Lai, X.S.3    Kuang, S.H.4
  • 32
    • 0032832616 scopus 로고    scopus 로고
    • Skeletal muscle myostatin mRNA expression is fiber-type specific and increases dining hindlimb unloading
    • Carlson C.J., Booth F.W., Gordon S.E. Skeletal muscle myostatin mRNA expression is fiber-type specific and increases dining hindlimb unloading. Am. J. Physiol. Regul. Integr. Comp. Physiol. 1999, 277:R601-R606.
    • (1999) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.277
    • Carlson, C.J.1    Booth, F.W.2    Gordon, S.E.3
  • 33
    • 0025826301 scopus 로고
    • Functionally complex muscles of the cat hindlimb. V. The roles of histochemical fiber-type regionalization and mechanical heterogeneity in differential muscle activation
    • Chanaud C.M., Pratt C.A., Loeb G.E. Functionally complex muscles of the cat hindlimb. V. The roles of histochemical fiber-type regionalization and mechanical heterogeneity in differential muscle activation. Exp. Brain Res. 1991, 85:300-313.
    • (1991) Exp. Brain Res. , vol.85 , pp. 300-313
    • Chanaud, C.M.1    Pratt, C.A.2    Loeb, G.E.3
  • 34
    • 0037063727 scopus 로고    scopus 로고
    • Recovery of type I fiber regionalization in gastrocnemius medialis of the rat after reinnervation along original and foreign paths, with and without muscle rotation
    • Wang L.C., Kernell D. Recovery of type I fiber regionalization in gastrocnemius medialis of the rat after reinnervation along original and foreign paths, with and without muscle rotation. Neuroscience 2002, 114:629-640.
    • (2002) Neuroscience , vol.114 , pp. 629-640
    • Wang, L.C.1    Kernell, D.2
  • 35
    • 80054950719 scopus 로고    scopus 로고
    • Elevated levels of active matrix metalloproteinase-9 cause hypertrophy in skeletal muscle of normal and dystrophin-deficient mdx mice
    • Dahiya S., Bhatnagar S., Hindi S.M., Jiang C., Paul P.K., Kuang S., Kumar A. Elevated levels of active matrix metalloproteinase-9 cause hypertrophy in skeletal muscle of normal and dystrophin-deficient mdx mice. Hum. Mol. Genet. 2011, 20:4345-4359.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4345-4359
    • Dahiya, S.1    Bhatnagar, S.2    Hindi, S.M.3    Jiang, C.4    Paul, P.K.5    Kuang, S.6    Kumar, A.7
  • 36
  • 37
    • 0022490182 scopus 로고
    • Effect of exercise on the motor unit
    • Edstrom L., Grimby L. Effect of exercise on the motor unit. Muscle Nerve 1986, 9:104-126.
    • (1986) Muscle Nerve , vol.9 , pp. 104-126
    • Edstrom, L.1    Grimby, L.2
  • 38
    • 77955088234 scopus 로고    scopus 로고
    • The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers
    • Hwang Y.H., Kim G.D., Jeong J.Y., Hur S.J., Joo S.T. The relationship between muscle fiber characteristics and meat quality traits of highly marbled Hanwoo (Korean native cattle) steers. Meat Sci. 2010, 86:456-461.
    • (2010) Meat Sci. , vol.86 , pp. 456-461
    • Hwang, Y.H.1    Kim, G.D.2    Jeong, J.Y.3    Hur, S.J.4    Joo, S.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.