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Volumn 4, Issue 3, 2009, Pages

Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN RECEPTOR 2; ACTIVIN RECEPTOR 2B; GLUCOSE; INSULIN; MYOSTATIN; UNCLASSIFIED DRUG; PROTEIN KINASE B;

EID: 63349107479     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0004937     Document Type: Article
Times cited : (313)

References (49)
  • 1
    • 8444243360 scopus 로고    scopus 로고
    • Regulation of muscle mass by myostatin
    • Lee SJ (2004) Regulation of muscle mass by myostatin. Annu Rev Cell Dev Biol 20: 61-86.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 61-86
    • Lee, S.J.1
  • 2
    • 13444293017 scopus 로고    scopus 로고
    • The function of Myostatin and strategies of Myostatin blockade-new hope for therapies aimed at promoting growth of skeletal muscle
    • Patel K, Amthor H (2005) The function of Myostatin and strategies of Myostatin blockade-new hope for therapies aimed at promoting growth of skeletal muscle. Neuromuscul Disord 15: 117-126.
    • (2005) Neuromuscul Disord , vol.15 , pp. 117-126
    • Patel, K.1    Amthor, H.2
  • 3
    • 34848912839 scopus 로고    scopus 로고
    • Sprinting without myostatin: A genetic determinant of athletic prowess
    • Lee SJ (2007) Sprinting without myostatin: a genetic determinant of athletic prowess. Trends Genet 23: 475-477.
    • (2007) Trends Genet , vol.23 , pp. 475-477
    • Lee, S.J.1
  • 5
    • 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
  • 7
    • 29144466479 scopus 로고    scopus 로고
    • Regulation of muscle growth by multiple ligands signaling through activin type II receptors
    • Lee SJ, Reed LA, Davies MV, Girgenrath S, Goad ME, et al. (2005) Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Proc Natl Acad Sci U S A 102: 18117-18122.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 18117-18122
    • Lee, S.J.1    Reed, L.A.2    Davies, M.V.3    Girgenrath, S.4    Goad, M.E.5
  • 8
    • 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 LA (2005) Loss of myostatin expression alters fiber-type distribution and expression of myosin heavy chain isoforms in slow- and fast-type skeletal muscle. Muscle Nerve 31: 34-40.
    • (2005) Muscle Nerve , vol.31 , pp. 34-40
    • Girgenrath, S.1    Song, K.2    Whittemore, L.A.3
  • 9
  • 10
    • 0033120212 scopus 로고    scopus 로고
    • A novel BMP expressed in developing mouse limb, spinal cord, and tail bud is a potent mesoderm inducer in Xenopus embryos
    • Gamer LW, Wolfman NM, Celeste AJ, Hattersley G, Hewick R, et al. (1999) A novel BMP expressed in developing mouse limb, spinal cord, and tail bud is a potent mesoderm inducer in Xenopus embryos. Dev Biol 208: 222-232.
    • (1999) Dev Biol , vol.208 , pp. 222-232
    • Gamer, L.W.1    Wolfman, N.M.2    Celeste, A.J.3    Hattersley, G.4    Hewick, R.5
  • 12
    • 43749111385 scopus 로고    scopus 로고
    • Identification of a novel pool of extracellular pro-myostatin in skeletal muscle
    • Anderson SB, Goldberg AL, Whitman M (2008) Identification of a novel pool of extracellular pro-myostatin in skeletal muscle. J Biol Chem 283: 7027-7035.
    • (2008) J Biol Chem , vol.283 , pp. 7027-7035
    • Anderson, S.B.1    Goldberg, A.L.2    Whitman, M.3
  • 13
    • 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, et al. (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
  • 15
    • 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
  • 16
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-b superfamily member
    • McPherron AC, Lawler AM, Lee SJ (1997) Regulation of skeletal muscle mass in mice by a new TGF-b 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
  • 18
    • 0036200822 scopus 로고    scopus 로고
    • Suppression of body fat accumulation in myostatin-deficient mice
    • McPherron AC, Lee SJ (2002) Suppression of body fat accumulation in myostatin-deficient mice. J Clin Invest 109: 595-601.
    • (2002) J Clin Invest , vol.109 , pp. 595-601
    • McPherron, A.C.1    Lee, S.J.2
  • 19
    • 33646352965 scopus 로고    scopus 로고
    • Resistance to body fat gain in 'double-muscled' mice fed a high-fat diet
    • Hamrick MW, Pennington C, Webb CN, Isales CM (2006) Resistance to body fat gain in 'double-muscled' mice fed a high-fat diet. Int J Obes (Lond) 30: 868-870.
    • (2006) Int J Obes (Lond) , vol.30 , pp. 868-870
    • Hamrick, M.W.1    Pennington, C.2    Webb, C.N.3    Isales, C.M.4
  • 20
    • 25844484021 scopus 로고    scopus 로고
    • Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance
    • Zhao B, Wall RJ, Yang J (2005) Transgenic expression of myostatin propeptide prevents diet-induced obesity and insulin resistance. Biochem Biophys Res Commun 337: 248-255.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 248-255
    • Zhao, B.1    Wall, R.J.2    Yang, J.3
  • 21
    • 23044501742 scopus 로고    scopus 로고
    • Myostatin inhibits myogenesis and promotes adipogenesis in C3H 10T(1/2) mesenchymal multipotent cells
    • Artaza JN, Bhasin S, Magee TR, Reisz-Porszasz S, Shen R, et al. (2005) Myostatin inhibits myogenesis and promotes adipogenesis in C3H 10T(1/2) mesenchymal multipotent cells. Endocrinology 146: 3547-3557.
    • (2005) Endocrinology , vol.146 , pp. 3547-3557
    • Artaza, J.N.1    Bhasin, S.2    Magee, T.R.3    Reisz-Porszasz, S.4    Shen, R.5
  • 22
    • 33750345334 scopus 로고    scopus 로고
    • Myostatin modulates adipogenesis to generate adipocytes with favorable metabolic effects
    • Feldman BJ, Streeper RS, Farese RV Jr, Yamamoto KR (2006) Myostatin modulates adipogenesis to generate adipocytes with favorable metabolic effects. Proc Natl Acad Sci U S A 103: 15675-15680.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15675-15680
    • Feldman, B.J.1    Streeper, R.S.2    Farese Jr, R.V.3    Yamamoto, K.R.4
  • 23
  • 24
    • 0037165983 scopus 로고    scopus 로고
    • Induction of cachexia in mice by systemically administered myostatin
    • Zimmers TA, Davies MV, Koniaris LG, Haynes P, Esquela AF, et al. (2002) Induction of cachexia in mice by systemically administered myostatin. Science 296: 1486-1488.
    • (2002) Science , vol.296 , pp. 1486-1488
    • Zimmers, T.A.1    Davies, M.V.2    Koniaris, L.G.3    Haynes, P.4    Esquela, A.F.5
  • 25
    • 45549109223 scopus 로고    scopus 로고
    • Myostatin, activin receptor IIb, and follistatin-like-3 gene expression are altered in adipose tissue and skeletal muscle of obese mice
    • Allen DL, Cleary AS, Speaker KJ, Lindsay SF, Uyenishi J, et al. (2008) Myostatin, activin receptor IIb, and follistatin-like-3 gene expression are altered in adipose tissue and skeletal muscle of obese mice. Am J Physiol Endocrinol Metab 294: E918-927.
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Allen, D.L.1    Cleary, A.S.2    Speaker, K.J.3    Lindsay, S.F.4    Uyenishi, J.5
  • 26
    • 38049186807 scopus 로고    scopus 로고
    • Administration of myostatin does not alter fat mass in adult mice
    • Stolz LE, Li D, Qadri A, Jalenak M, Klaman LD, et al. (2008) Administration of myostatin does not alter fat mass in adult mice. Diabetes Obes Metab 10: 135-142.
    • (2008) Diabetes Obes Metab , vol.10 , pp. 135-142
    • Stolz, L.E.1    Li, D.2    Qadri, A.3    Jalenak, M.4    Klaman, L.D.5
  • 27
    • 33846633796 scopus 로고    scopus 로고
    • FSTL3 deletion reveals roles for TGF-b family ligands in glucose and fat homeostasis in adults
    • Mukherjee A, Sidis Y, Mahan A, Raher MJ, Xia Y, et al. (2007) FSTL3 deletion reveals roles for TGF-b family ligands in glucose and fat homeostasis in adults. Proc Natl Acad Sci U S A 104: 1348-1353.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1348-1353
    • Mukherjee, A.1    Sidis, Y.2    Mahan, A.3    Raher, M.J.4    Xia, Y.5
  • 28
    • 6344256238 scopus 로고    scopus 로고
    • Conditional activation of Akt in adult skeletal muscle induces rapid hypertrophy
    • Lai KM, Gonzalez M, Poueymirou WT, Kline WO, Na E, et al. (2004) Conditional activation of Akt in adult skeletal muscle induces rapid hypertrophy. Mol Cell Biol 24: 9295-9304.
    • (2004) Mol Cell Biol , vol.24 , pp. 9295-9304
    • Lai, K.M.1    Gonzalez, M.2    Poueymirou, W.T.3    Kline, W.O.4    Na, E.5
  • 29
    • 38649091396 scopus 로고    scopus 로고
    • Fast/ Glycolytic muscle fiber growth reduces fat mass and improves metabolic parameters in obese mice
    • Izumiya Y, Hopkins T, Morris C, Sato K, Zeng L, et al. (2008) Fast/ Glycolytic muscle fiber growth reduces fat mass and improves metabolic parameters in obese mice. Cell Metab 7: 159-172.
    • (2008) Cell Metab , vol.7 , pp. 159-172
    • Izumiya, Y.1    Hopkins, T.2    Morris, C.3    Sato, K.4    Zeng, L.5
  • 30
    • 0035136062 scopus 로고    scopus 로고
    • Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
    • Musaro A, McCullagh K, Paul A, Houghton L, Dobrowolny G, et al. (2001) Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nat Genet 27: 195-200.
    • (2001) Nat Genet , vol.27 , pp. 195-200
    • Musaro, A.1    McCullagh, K.2    Paul, A.3    Houghton, L.4    Dobrowolny, G.5
  • 31
    • 0025182773 scopus 로고
    • ski can cause selective growth of skeletal muscle in transgenic mice
    • Sutrave P, Kelly AM, Hughes SH (1990) ski can cause selective growth of skeletal muscle in transgenic mice. Genes Dev 4: 1462-1472.
    • (1990) Genes Dev , vol.4 , pp. 1462-1472
    • Sutrave, P.1    Kelly, A.M.2    Hughes, S.H.3
  • 33
    • 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 U S A 98: 9306-9311.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 34
    • 33746199834 scopus 로고    scopus 로고
    • Myostatin regulates cardiomyocyte growth through modulation of Akt signaling
    • Morissette MR, Cook SA, Foo S, McKoy G, Ashida N, et al. (2006) Myostatin regulates cardiomyocyte growth through modulation of Akt signaling. Circ Res 99: 15-24.
    • (2006) Circ Res , vol.99 , pp. 15-24
    • Morissette, M.R.1    Cook, S.A.2    Foo, S.3    McKoy, G.4    Ashida, N.5
  • 35
    • 33749254273 scopus 로고    scopus 로고
    • Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-kappaB-independent, FoxO1-dependent mechanism
    • McFarlane C, Plummer E, Thomas M, Hennebry A, Ashby M, et al. (2006) Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-kappaB-independent, FoxO1-dependent mechanism. J Cell Physiol 209: 501-514.
    • (2006) J Cell Physiol , vol.209 , pp. 501-514
    • McFarlane, C.1    Plummer, E.2    Thomas, M.3    Hennebry, A.4    Ashby, M.5
  • 36
    • 33947538814 scopus 로고    scopus 로고
    • Myostatin induces cyclin D1 degradation to cause cell cycle arrest through a phosphatidylinositol 3-kinase/AKT/GSK-3β pathway and is antagonized by insulin-like growth factor 1
    • Yang W, Zhang Y, Li Y, Wu Z, Zhu D (2007) Myostatin induces cyclin D1 degradation to cause cell cycle arrest through a phosphatidylinositol 3-kinase/AKT/GSK-3β pathway and is antagonized by insulin-like growth factor 1. J Biol Chem 282: 3799-3808.
    • (2007) J Biol Chem , vol.282 , pp. 3799-3808
    • Yang, W.1    Zhang, Y.2    Li, Y.3    Wu, Z.4    Zhu, D.5
  • 38
    • 0036402110 scopus 로고    scopus 로고
    • Metabolic lessons from genetically lean mice
    • Reitman ML (2002) Metabolic lessons from genetically lean mice. Annu Rev Nutr 22: 459-482.
    • (2002) Annu Rev Nutr , vol.22 , pp. 459-482
    • Reitman, M.L.1
  • 39
    • 33748476501 scopus 로고    scopus 로고
    • Contractile properties of EDL and soleus muscles of myostatin-deficient mice
    • Mendias CL, Marcin JE, Calerdon DR, Faulkner JA (2006) Contractile properties of EDL and soleus muscles of myostatin-deficient mice. J Appl Physiol 101: 898-905.
    • (2006) J Appl Physiol , vol.101 , pp. 898-905
    • Mendias, C.L.1    Marcin, J.E.2    Calerdon, D.R.3    Faulkner, J.A.4
  • 40
    • 34047108726 scopus 로고    scopus 로고
    • Mitochondrial oxidative function and type 2 diabetes
    • Rabol R, Boushel R, Dela F (2006) Mitochondrial oxidative function and type 2 diabetes. Appl Physiol Nutr Metab 31: 675-683.
    • (2006) Appl Physiol Nutr Metab , vol.31 , pp. 675-683
    • Rabol, R.1    Boushel, R.2    Dela, F.3
  • 41
    • 34548757192 scopus 로고    scopus 로고
    • Effects of aerobic training, resistance training, or both on glycemic control in type 2 diabetes: A randomized trial
    • Sigal RJ, Kenny GP, Boule NG, Wells GA, Prud'homme D, et al. (2007) Effects of aerobic training, resistance training, or both on glycemic control in type 2 diabetes: a randomized trial. Ann Intern Med 147: 357-369.
    • (2007) Ann Intern Med , vol.147 , pp. 357-369
    • Sigal, R.J.1    Kenny, G.P.2    Boule, N.G.3    Wells, G.A.4    Prud'homme, D.5
  • 42
    • 33746447698 scopus 로고    scopus 로고
    • Physical activity/exercise and type 2 diabetes: A consensus statement from the American Diabetes Association
    • Sigal RJ, Kenny GP, Wasserman DH, Castaneda-Sceppa C, White RD (2006) Physical activity/exercise and type 2 diabetes: a consensus statement from the American Diabetes Association. Diabetes Care 29: 1433-1438.
    • (2006) Diabetes Care , vol.29 , pp. 1433-1438
    • Sigal, R.J.1    Kenny, G.P.2    Wasserman, D.H.3    Castaneda-Sceppa, C.4    White, R.D.5
  • 43
    • 33846471910 scopus 로고    scopus 로고
    • The adaptations to strength training : Morphological and neurological contributions to increased strength
    • Folland JP, Williams AG (2007) The adaptations to strength training : morphological and neurological contributions to increased strength. Sports Med 37: 145-168.
    • (2007) Sports Med , vol.37 , pp. 145-168
    • Folland, J.P.1    Williams, A.G.2
  • 44
    • 40349085764 scopus 로고    scopus 로고
    • Myostatin promotes the terminal differentiation of embryonic muscle progenitors
    • Manceau M, Gros J, Savage K, Thome V, McPherron A, et al. (2008) Myostatin promotes the terminal differentiation of embryonic muscle progenitors. Genes Dev 22: 668-681.
    • (2008) Genes Dev , vol.22 , pp. 668-681
    • Manceau, M.1    Gros, J.2    Savage, K.3    Thome, V.4    McPherron, A.5
  • 45
    • 23844556589 scopus 로고    scopus 로고
    • Leptin improves insulin resistance and hyperglycemia in a mouse model of type 2 diabetes
    • Toyoshima Y, Gavrilova O, Yakar S, Jou W, Pack S, et al. (2005) Leptin improves insulin resistance and hyperglycemia in a mouse model of type 2 diabetes. Endocrinology 146: 4024-4035.
    • (2005) Endocrinology , vol.146 , pp. 4024-4035
    • Toyoshima, Y.1    Gavrilova, O.2    Yakar, S.3    Jou, W.4    Pack, S.5
  • 46
    • 0034018370 scopus 로고    scopus 로고
    • Paternal versus maternal transmission of a stimulatory G-protein a subunit knockout produces opposite effects on energy metabolism
    • Yu S, Gavrilova O, Chen H, Lee R, Liu J, et al. (2000) Paternal versus maternal transmission of a stimulatory G-protein a subunit knockout produces opposite effects on energy metabolism. J Clin Invest 105: 615-623.
    • (2000) J Clin Invest , vol.105 , pp. 615-623
    • Yu, S.1    Gavrilova, O.2    Chen, H.3    Lee, R.4    Liu, J.5
  • 47
    • 33750488455 scopus 로고    scopus 로고
    • Beneficial metabolic effects of M3 muscarinic acetylcholine receptor deficiency
    • Gautam D, Gavrilova O, Jeon J, Pack S, Jou W, et al. (2006) Beneficial metabolic effects of M3 muscarinic acetylcholine receptor deficiency. Cell Metab 4: 363-375.
    • (2006) Cell Metab , vol.4 , pp. 363-375
    • Gautam, D.1    Gavrilova, O.2    Jeon, J.3    Pack, S.4    Jou, W.5


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