메뉴 건너뛰기




Volumn 33, Issue 11, 2012, Pages 902-907

The expression and potential functions of placental myostatin

Author keywords

GDF 8; Myostatin; Placenta

Indexed keywords

CYTOKERATIN 7; CYTOKINE ANTIBODY; CYTOKINE RECEPTOR; FOLLISTATIN; FOLLISTATIN LIKE 3 PROTEIN; FOLLISTATIN RELATED PROTEIN; GLUCOSE; INTERLEUKIN 1BETA; INTERLEUKIN 6; MYOSTATIN; MYOSTATIN ANTIBODY; MYOSTATIN RECEPTOR; PROTEIN PRECURSOR; RECOMBINANT MYOSTATIN; RECOMBINANT PROTEIN; SMAD PROTEIN; SMALL INTERFERING RNA; SOTATERCEPT; STAMULUMAB; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84868102517     PISSN: 01434004     EISSN: 15323102     Source Type: Journal    
DOI: 10.1016/j.placenta.2012.06.021     Document Type: Article
Times cited : (18)

References (78)
  • 1
    • 7044233074 scopus 로고    scopus 로고
    • Growth and function of the normal human placenta
    • DOI 10.1016/j.thromres.2004.06.038, PII S0049384804003421, SPEC. ISS.
    • N.M. Gude, C.T. Roberts, B. Kalionis, and R.G. King Growth and function of the normal human placenta Thromb Res 114 5-6 2004 397 407 (Pubitemid 39422572)
    • (2004) Thrombosis Research , vol.114 , Issue.5-6 , pp. 397-407
    • Gude, N.M.1    Roberts, C.T.2    Kalionis, B.3    King, R.G.4
  • 2
    • 12744254780 scopus 로고    scopus 로고
    • Developmental biology of the placenta and the origins of placental insufficiency
    • V. Chaddha, S. Viero, B. Huppertz, and J. Kingdom Developmental biology of the placenta and the origins of placental insufficiency Semin Fetal Neonatal Med 9 5 2004 357 369
    • (2004) Semin Fetal Neonatal Med , vol.9 , Issue.5 , pp. 357-369
    • Chaddha, V.1    Viero, S.2    Huppertz, B.3    Kingdom, J.4
  • 3
    • 33645306841 scopus 로고    scopus 로고
    • Placental adaptive responses and fetal programming
    • L. Myatt Placental adaptive responses and fetal programming J Physiol 572 Pt 1 2006 25 30
    • (2006) J Physiol , vol.572 , Issue.PART 1 , pp. 25-30
    • Myatt, L.1
  • 5
    • 34748883081 scopus 로고    scopus 로고
    • A maternal 'junk food' diet in pregnancy and lactation promotes an exacerbated taste for 'junk food' and a greater propensity for obesity in rat offspring
    • DOI 10.1017/S0007114507812037, PII S0007114507812037
    • S.A. Bayol, S.J. Farrington, and N.C. Stickland A maternal 'junk food' diet in pregnancy and lactation promotes an exacerbated taste for 'junk food' and a greater propensity for obesity in rat offspring Br J Nutr 98 4 2007 843 851 (Pubitemid 47487954)
    • (2007) British Journal of Nutrition , vol.98 , Issue.4 , pp. 843-851
    • Bayol, S.A.1    Farrington, S.J.2    Stickland, N.C.3
  • 6
    • 46449087037 scopus 로고    scopus 로고
    • Effect of in utero and early-life conditions on adult health and disease
    • 6
    • P.D. Gluckman, M.A. Hanson, C. Cooper, and K.L. Thornburg Effect of in utero and early-life conditions on adult health and disease N Engl J Med 359 1 2008 61 73 +6
    • (2008) N Engl J Med , vol.359 , Issue.1 , pp. 61-73
    • Gluckman, P.D.1    Hanson, M.A.2    Cooper, C.3    Thornburg, K.L.4
  • 8
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • A.C. McPherron, A.M. Lawler, and S.J. Lee Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member Nature 387 6628 1997 83 90 (Pubitemid 27202654)
    • (1997) Nature , vol.387 , Issue.6628 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.-J.3
  • 9
    • 8444243360 scopus 로고    scopus 로고
    • Regulation of muscle mass by myostatin
    • S.J. Lee Regulation of muscle mass by myostatin Annu Rev Cell Dev Biol 20 2004 61 86
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 61-86
    • Lee, S.J.1
  • 10
    • 34249733201 scopus 로고    scopus 로고
    • A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs
    • D.S. Mosher, P. Quignon, C.D. Bustamante, N.B. Sutter, C.S. Mellersh, and H.G. Parker A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs PLoS Genet 3 5 2007 e79
    • (2007) PLoS Genet , vol.3 , Issue.5 , pp. 79
    • Mosher, D.S.1    Quignon, P.2    Bustamante, C.D.3    Sutter, N.B.4    Mellersh, C.S.5    Parker, H.G.6
  • 14
    • 13844282120 scopus 로고    scopus 로고
    • Myostatin and its implications on animal breeding: A review
    • DOI 10.1111/j.1365-2052.2004.01229.x
    • R.H. Bellinge, D.A. Liberles, S.P. Iaschi, P.A. O'Brien, and G.K. Tay Myostatin and its implications on animal breeding: a review Anim Genet 36 1 2005 1 6 (Pubitemid 40252767)
    • (2005) Animal Genetics , vol.36 , Issue.1 , pp. 1-6
    • Bellinge, R.H.S.1    Liberles, D.A.2    Iaschi, S.P.A.3    O'Brien, P.A.4    Tay, G.K.5
  • 15
    • 38349145459 scopus 로고    scopus 로고
    • Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways
    • S.J. Lee Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways PLoS ONE 2 8 2007 e789
    • (2007) PLoS ONE , vol.2 , Issue.8 , pp. 789
    • Lee, S.J.1
  • 18
    • 49449119079 scopus 로고    scopus 로고
    • Clinical, agricultural, and evolutionary biology of myostatin: A comparative review
    • B.D. Rodgers, and D.K. Garikipati Clinical, agricultural, and evolutionary biology of myostatin: a comparative review Endocr Rev 29 5 2008 513 534
    • (2008) Endocr Rev , vol.29 , Issue.5 , pp. 513-534
    • Rodgers, B.D.1    Garikipati, D.K.2
  • 19
    • 0033006969 scopus 로고    scopus 로고
    • Myostatin, a transforming growth factor-β superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct
    • DOI 10.1002/(SICI)1097-4652(199907)180:1<1::AID-JCP1>3.0.CO;2-V
    • M. Sharma, R. Kambadur, K.G. Matthews, W.G. Somers, G.P. Devlin, and J.V. Conaglen Myostatin, a transforming growth factor-beta superfamily member, is expressed in heart muscle and is upregulated in cardiomyocytes after infarct J Cell Physiol 180 1 1999 1 9 (Pubitemid 29249707)
    • (1999) Journal of Cellular Physiology , vol.180 , Issue.1 , pp. 1-9
    • Sharma, M.1    Kambadur, R.2    Matthews, K.G.3    Somers, W.G.4    Devlin, G.P.5    Conaglen, J.V.6    Fowke, P.J.7    Bass, J.J.8
  • 20
    • 0035793972 scopus 로고    scopus 로고
    • Differential skeletal muscle expression of myostatin across teleost species, and the isolation of multiple myostatin isoforms
    • DOI 10.1016/S0014-5793(01)02196-2, PII S0014579301021962
    • S.B. Roberts, and F.W. Goetz Differential skeletal muscle expression of myostatin across teleost species, and the isolation of multiple myostatin isoforms FEBS Letters 491 3 2001 212 216 (Pubitemid 32193798)
    • (2001) FEBS Letters , vol.491 , Issue.3 , pp. 212-216
    • Roberts, S.B.1    Goetz, F.W.2
  • 21
    • 0242495018 scopus 로고    scopus 로고
    • Myostatin protein and RNA transcript levels in adult and developing brook trout
    • DOI 10.1016/j.mce.2003.09.002
    • S.B. Roberts, and F.W. Goetz Myostatin protein and RNA transcript levels in adult and developing brook trout Mol Cell Endocrinol 210 1-2 2003 9 20 (Pubitemid 37386313)
    • (2003) Molecular and Cellular Endocrinology , vol.210 , Issue.1-2 , pp. 9-20
    • Roberts, S.B.1    Goetz, F.W.2
  • 22
    • 33748707456 scopus 로고    scopus 로고
    • Myostatin expression in ventricular myocardium in a rat model of volume-overload heart failure
    • DOI 10.1111/j.1365-2362.2006.01718.x
    • K.G. Shyu, M.J. Lu, B.W. Wang, H.Y. Sun, and H. Chang Myostatin expression in ventricular myocardium in a rat model of volume-overload heart failure Eur J Clin Invest 36 10 2006 713 719 (Pubitemid 44393930)
    • (2006) European Journal of Clinical Investigation , vol.36 , Issue.10 , pp. 713-719
    • Shyu, K.G.1    Lu, M.J.2    Wang, B.W.3    Sun, H.Y.4    Chang, H.5
  • 23
    • 36649001772 scopus 로고    scopus 로고
    • Developmental changes in extracellular matrix messenger RNAs in the mouse placenta during the second half of pregnancy: Possible factors involved in the regulation of placental extracellular matrix expression
    • DOI 10.1095/biolreprod.107.061382
    • K.Y. Arai, and T. Nishiyama Developmental changes in extracellular matrix messenger RNAs in the mouse placenta during the second half of pregnancy: possible factors involved in the regulation of placental extracellular matrix expression Biol Reprod 77 6 2007 923 933 (Pubitemid 350197969)
    • (2007) Biology of Reproduction , vol.77 , Issue.6 , pp. 923-933
    • Arai, K.Y.1    Nishiyama, T.2
  • 25
    • 56449103953 scopus 로고    scopus 로고
    • Mammary gland differentiation inversely correlates with GDF-8 expression
    • R. Manickam, R.N. Pena, and C.B.A. Whitelaw Mammary gland differentiation inversely correlates with GDF-8 expression Mol Reprod Dev 75 12 2008 1783 1788
    • (2008) Mol Reprod Dev , vol.75 , Issue.12 , pp. 1783-1788
    • Manickam, R.1    Pena, R.N.2    Whitelaw, C.B.A.3
  • 26
    • 44449125724 scopus 로고    scopus 로고
    • A distinct cohort of the TGFβ superfamily members expressed in human endometrium regulate decidualization
    • DOI 10.1093/humrep/den110
    • C.J. Stoikos, C.A. Harrison, L.A. Salamonsen, and E. Dimitriadis A distinct cohort of the TGFbeta superfamily members expressed in human endometrium regulate decidualization Hum Reprod 23 6 2008 1447 1456 (Pubitemid 351770587)
    • (2008) Human Reproduction , vol.23 , Issue.6 , pp. 1447-1456
    • Stoikos, C.J.1    Harrison, C.A.2    Salamonsen, L.A.3    Dimitriadis, E.4
  • 27
    • 76649138257 scopus 로고    scopus 로고
    • Genetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure
    • J. Heineke, M. Auger-Messier, J. Xu, M. Sargent, A. York, and S. Welle Genetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure Circulation 121 3 2010 419 425
    • (2010) Circulation , vol.121 , Issue.3 , pp. 419-425
    • Heineke, J.1    Auger-Messier, M.2    Xu, J.3    Sargent, M.4    York, A.5    Welle, S.6
  • 28
    • 44049094434 scopus 로고    scopus 로고
    • The effects of myostatin on adipogenic differentiation of human bone marrow-derived mesenchymal stem cells are mediated through cross-communication between Smad3 and Wnt/beta-catenin signaling pathways
    • W. Guo, J. Flanagan, R. Jasuja, J. Kirkland, L. Jiang, and S. Bhasin The effects of myostatin on adipogenic differentiation of human bone marrow-derived mesenchymal stem cells are mediated through cross-communication between Smad3 and Wnt/beta-catenin signaling pathways J Biol Chem 283 14 2008 9136 9145
    • (2008) J Biol Chem , vol.283 , Issue.14 , pp. 9136-9145
    • Guo, W.1    Flanagan, J.2    Jasuja, R.3    Kirkland, J.4    Jiang, L.5    Bhasin, S.6
  • 31
  • 33
    • 0034704106 scopus 로고    scopus 로고
    • Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation
    • DOI 10.1074/jbc.M004356200
    • M. Thomas, B. Langley, C. Berry, M. Sharma, S. Kirk, and J. Bass Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation J Biol Chem 275 51 2000 40235 40243 (Pubitemid 32064654)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40235-40243
    • Thomas, M.1    Langley, B.2    Berry, C.3    Sharma, M.4    Kirk, S.5    Bass, J.6    Kambadur, R.7
  • 34
    • 79955667805 scopus 로고    scopus 로고
    • Pharmacological inhibition of myostatin suppresses systemic inflammation and muscle atrophy in mice with chronic kidney disease
    • L. Zhang, V. Rajan, E. Lin, Z. Hu, H.Q. Han, and X. Zhou Pharmacological inhibition of myostatin suppresses systemic inflammation and muscle atrophy in mice with chronic kidney disease Faseb J 25 5 2011 1653 1663
    • (2011) Faseb J , vol.25 , Issue.5 , pp. 1653-1663
    • Zhang, L.1    Rajan, V.2    Lin, E.3    Hu, Z.4    Han, H.Q.5    Zhou, X.6
  • 35
    • 65549149871 scopus 로고    scopus 로고
    • Loss-of-function mutation in myostatin reduces tumor necrosis factor alpha production and protects liver against obesity-induced insulin resistance
    • J.J. Wilkes, D.J. Lloyd, and N. Gekakis Loss-of-function mutation in myostatin reduces tumor necrosis factor alpha production and protects liver against obesity-induced insulin resistance Diabetes 58 5 2009 1133 1143
    • (2009) Diabetes , vol.58 , Issue.5 , pp. 1133-1143
    • Wilkes, J.J.1    Lloyd, D.J.2    Gekakis, N.3
  • 36
    • 78751574354 scopus 로고    scopus 로고
    • Glutamine prevents myostatin hyperexpression and protein hypercatabolism induced in C2C12 myotubes by tumor necrosis factor-alpha
    • A. Bonetto, F. Penna, V.G. Minero, P. Reffo, D. Costamagna, and G. Bonelli Glutamine prevents myostatin hyperexpression and protein hypercatabolism induced in C2C12 myotubes by tumor necrosis factor-alpha Amino Acids 40 2 2011 585 594
    • (2011) Amino Acids , vol.40 , Issue.2 , pp. 585-594
    • Bonetto, A.1    Penna, F.2    Minero, V.G.3    Reffo, P.4    Costamagna, D.5    Bonelli, G.6
  • 37
    • 71949125322 scopus 로고    scopus 로고
    • Growth-differentiation factor-8 (GDF-8) in the uterus: Its identification and functional significance in the golden hamster
    • C.L. Wong, Y.Y. Huang, W.K. Ho, H.K. Poon, P.L. Cheung, and O. Wai Sum Growth-differentiation factor-8 (GDF-8) in the uterus: its identification and functional significance in the golden hamster Reprod Biol Endocrinol 7 2009 134
    • (2009) Reprod Biol Endocrinol , vol.7 , pp. 134
    • Wong, C.L.1    Huang, Y.Y.2    Ho, W.K.3    Poon, H.K.4    Cheung, P.L.5    Wai Sum, O.6
  • 38
    • 33745854176 scopus 로고    scopus 로고
    • Myostatin regulation of muscle development: Molecular basis, natural mutations, physiopathological aspects
    • D. Joulia-Ekaza, and G. Cabello Myostatin regulation of muscle development: molecular basis, natural mutations, physiopathological aspects Exp Cell Res 312 13 2006 2401 2414
    • (2006) Exp Cell Res , vol.312 , Issue.13 , pp. 2401-2414
    • Joulia-Ekaza, D.1    Cabello, G.2
  • 39
    • 14644435182 scopus 로고    scopus 로고
    • The growth factor myostatin, a key regulator in skeletal muscle growth and homeostasis
    • DOI 10.1055/s-2004-830451
    • A. Matsakas, and P. Diel The growth factor myostatin, a key regulator in skeletal muscle growth and homeostasis Int J Sports Med 26 2 2005 83 89 (Pubitemid 40321569)
    • (2005) International Journal of Sports Medicine , vol.26 , Issue.2 , pp. 83-89
    • Matsakas, A.1    Diel, P.2
  • 40
    • 34248324912 scopus 로고    scopus 로고
    • The myostatin gene: physiology and pharmacological relevance
    • DOI 10.1016/j.coph.2006.11.011, PII S1471489207000501, Respiratory/Musculoskeletal
    • D. Joulia-Ekaza, and G. Cabello The myostatin gene: physiology and pharmacological relevance Curr Opin Pharmacol 7 3 2007 310 315 (Pubitemid 46738500)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.3 , pp. 310-315
    • Joulia-Ekaza, D.1    Cabello, G.2
  • 43
    • 45749153791 scopus 로고    scopus 로고
    • Genetic analysis of the role of proteolysis in the activation of latent myostatin
    • S.J. Lee Genetic analysis of the role of proteolysis in the activation of latent myostatin PLoS ONE 3 2 2008 e1628
    • (2008) PLoS ONE , vol.3 , Issue.2 , pp. 1628
    • Lee, S.J.1
  • 44
    • 77956314874 scopus 로고    scopus 로고
    • Myostatin activation in patients with advanced heart failure and after mechanical unloading
    • I. George, L.T. Bish, G. Kamalakkannan, C.M. Petrilli, M.C. Oz, and Y. Naka Myostatin activation in patients with advanced heart failure and after mechanical unloading Eur J Heart Fail 12 5 2010 444 453
    • (2010) Eur J Heart Fail , vol.12 , Issue.5 , pp. 444-453
    • George, I.1    Bish, L.T.2    Kamalakkannan, G.3    Petrilli, C.M.4    Oz, M.C.5    Naka, Y.6
  • 45
    • 0037174939 scopus 로고    scopus 로고
    • The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum
    • DOI 10.1074/jbc.M206379200
    • J.J. Hill, M.V. Davies, A.A. Pearson, J.H. Wang, R.M. Hewick, and N.M. Wolfman The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum J Biol Chemistry 277 43 2002 40735 40741 (Pubitemid 35215657)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , 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
  • 46
    • 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
    • DOI 10.1016/j.nmd.2004.10.018, PII S0960896604003098
    • K. Patel, and H. Amthor The function of Myostatin and strategies of Myostatin blockade-new hope for therapies aimed at promoting growth of skeletal muscle Neuromuscular Disord 15 2 2005 117 126 (Pubitemid 40202738)
    • (2005) Neuromuscular Disorders , vol.15 , Issue.2 , pp. 117-126
    • Patel, K.1    Amthor, H.2
  • 48
    • 68049117225 scopus 로고    scopus 로고
    • Genetic disruption of myostatin reduces the development of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice
    • P. Tu, S. Bhasin, P.W. Hruz, K.L. Herbst, L.W. Castellani, and N. Hua Genetic disruption of myostatin reduces the development of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice Diabetes 58 8 2009 1739 1748
    • (2009) Diabetes , vol.58 , Issue.8 , pp. 1739-1748
    • Tu, P.1    Bhasin, S.2    Hruz, P.W.3    Herbst, K.L.4    Castellani, L.W.5    Hua, N.6
  • 49
    • 63349107479 scopus 로고    scopus 로고
    • Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity
    • T. Guo, W. Jou, T. Chanturiya, J. Portas, O. Gavrilova, and A.C. McPherron Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity PLoS ONE 4 3 2009
    • (2009) PLoS ONE , vol.4 , Issue.3
    • Guo, T.1    Jou, W.2    Chanturiya, T.3    Portas, J.4    Gavrilova, O.5    McPherron, A.C.6
  • 50
    • 33646352965 scopus 로고    scopus 로고
    • Resistance to body fat gain in 'double-muscled' mice fed a high-fat diet
    • M.W. Hamrick, C. Pennington, C.N. Webb, and C.M. Isales Resistance to body fat gain in 'double-muscled' mice fed a high-fat diet Int J Obes 30 5 2006 868 870
    • (2006) Int J Obes , vol.30 , Issue.5 , pp. 868-870
    • Hamrick, M.W.1    Pennington, C.2    Webb, C.N.3    Isales, C.M.4
  • 52
    • 62849108016 scopus 로고    scopus 로고
    • Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease
    • L.R. Rodino-Klapac, A.M. Haidet, J. Kota, C. Handy, B.K. Kaspar, and J.R. Mendell Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease Muscle Nerve 39 3 2009 283 296
    • (2009) Muscle Nerve , vol.39 , Issue.3 , pp. 283-296
    • Rodino-Klapac, L.R.1    Haidet, A.M.2    Kota, J.3    Handy, C.4    Kaspar, B.K.5    Mendell, J.R.6
  • 53
    • 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
    • DOI 10.1002/mus.20175
    • S. Girgenrath, K. Song, and L.A. Whittemore 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 1 2005 34 40 (Pubitemid 40053924)
    • (2005) Muscle and Nerve , vol.31 , Issue.1 , pp. 34-40
    • Girgenrath, S.1    Song, K.2    Whittemore, L.-A.3
  • 56
    • 84868123175 scopus 로고    scopus 로고
    • Myostatin (GDF-8) as a therapeutic target for the prevention of osteoporotic fractures
    • M.W. Hamrick Myostatin (GDF-8) as a therapeutic target for the prevention of osteoporotic fractures IBMS BoneKEy 7 1 2010 8 17
    • (2010) IBMS BoneKEy , vol.7 , Issue.1 , pp. 8-17
    • Hamrick, M.W.1
  • 57
    • 51849146897 scopus 로고    scopus 로고
    • Global burden of obesity in 2005 and projections to 2030
    • T. Kelly, W. Yang, C.S. Chen, K. Reynolds, and J. He Global burden of obesity in 2005 and projections to 2030 Int J Obes (Lond) 32 9 2008 1431 1437
    • (2008) Int J Obes (Lond) , vol.32 , Issue.9 , pp. 1431-1437
    • Kelly, T.1    Yang, W.2    Chen, C.S.3    Reynolds, K.4    He, J.5
  • 59
    • 63249100559 scopus 로고    scopus 로고
    • Increased secretion and expression of myostatin in skeletal muscle from extremely obese women
    • D.S. Hittel, J.R. Berggren, J. Shearer, K. Boyle, and J.A. Houmard Increased secretion and expression of myostatin in skeletal muscle from extremely obese women Diabetes 58 1 2009 30 38
    • (2009) Diabetes , vol.58 , Issue.1 , pp. 30-38
    • Hittel, D.S.1    Berggren, J.R.2    Shearer, J.3    Boyle, K.4    Houmard, J.A.5
  • 60
    • 68949122307 scopus 로고    scopus 로고
    • Gene expression in skeletal muscle biopsies from people with type 2 diabetes and relatives: Differential regulation of insulin signaling pathways
    • J. Palsgaard, C. Brons, M. Friedrichsen, H. Dominguez, M. Jensen, and H. Storgaard Gene expression in skeletal muscle biopsies from people with type 2 diabetes and relatives: differential regulation of insulin signaling pathways PLoS ONE 4 8 2009 e6575
    • (2009) PLoS ONE , vol.4 , Issue.8 , pp. 6575
    • Palsgaard, J.1    Brons, C.2    Friedrichsen, M.3    Dominguez, H.4    Jensen, M.5    Storgaard, H.6
  • 62
    • 84864599052 scopus 로고    scopus 로고
    • Alterations of maternal serum and placental follistatin-like 3 and myostatin in pre-eclampsia
    • J. Guo, T. Tian, D. Lu, G. Xia, H. Wang, and M. Dong Alterations of maternal serum and placental follistatin-like 3 and myostatin in pre-eclampsia J Obstet Gynaecol Res 2012
    • (2012) J Obstet Gynaecol Res
    • Guo, J.1    Tian, T.2    Lu, D.3    Xia, G.4    Wang, H.5    Dong, M.6
  • 65
    • 78650519656 scopus 로고    scopus 로고
    • Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli
    • M. Hayot, J. Rodriguez, B. Vernus, G. Carnac, E. Jean, and D. Allen Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli Mol Cell Endocrinol 332 1-2 2011 38 47
    • (2011) Mol Cell Endocrinol , vol.332 , Issue.12 , pp. 38-47
    • Hayot, M.1    Rodriguez, J.2    Vernus, B.3    Carnac, G.4    Jean, E.5    Allen, D.6
  • 66
    • 37649009046 scopus 로고    scopus 로고
    • Hypoxia enhances the expression of follistatin-like 3 in term human trophoblasts
    • T. Biron-Shental, W.T. Schaiff, E. Rimon, T.L. Shim, D.M. Nelson, and Y. Sadovsky Hypoxia enhances the expression of follistatin-like 3 in term human trophoblasts Placenta 29 1 2008 51 57
    • (2008) Placenta , vol.29 , Issue.1 , pp. 51-57
    • Biron-Shental, T.1    Schaiff, W.T.2    Rimon, E.3    Shim, T.L.4    Nelson, D.M.5    Sadovsky, Y.6
  • 67
    • 84856213419 scopus 로고    scopus 로고
    • Decreased maternal and placental concentrations of follistatin-like 3 in gestational diabetes
    • D. Hu, T. Tian, J. Guo, H. Wang, D. Chen, and M. Dong Decreased maternal and placental concentrations of follistatin-like 3 in gestational diabetes Clinica Chimica Acta 413 5-6 2012 533 536
    • (2012) Clinica Chimica Acta , vol.413 , Issue.56 , pp. 533-536
    • Hu, D.1    Tian, T.2    Guo, J.3    Wang, H.4    Chen, D.5    Dong, M.6
  • 68
    • 77649255917 scopus 로고    scopus 로고
    • First-trimester follistatin-like-3 levels in pregnancies complicated by subsequent gestational diabetes mellitus
    • R. Thadhani, C.E. Powe, M.L. Tjoa, E. Khankin, J. Ye, and J. Ecker First-trimester follistatin-like-3 levels in pregnancies complicated by subsequent gestational diabetes mellitus Diabetes Care 33 3 2010 664 669
    • (2010) Diabetes Care , vol.33 , Issue.3 , pp. 664-669
    • Thadhani, R.1    Powe, C.E.2    Tjoa, M.L.3    Khankin, E.4    Ye, J.5    Ecker, J.6
  • 69
    • 0036896631 scopus 로고    scopus 로고
    • Regulation of placental nutrient transport and implications for fetal growth
    • A.W. Bell, and R.A. Ehrhardt Regulation of placental nutrient transport and implications for fetal growth Nutr Res Rev 15 2 2002 211 230 (Pubitemid 35423604)
    • (2002) Nutrition Research Reviews , vol.15 , Issue.2 , pp. 211-230
    • Bell, A.W.1    Ehrhardt, R.A.2
  • 70
    • 78149282298 scopus 로고    scopus 로고
    • Myostatin regulates glucose metabolism via the AMP-activated protein kinase pathway in skeletal muscle cells
    • Y. Chen, J. Ye, L. Cao, Y. Zhang, W. Xia, and D. Zhu Myostatin regulates glucose metabolism via the AMP-activated protein kinase pathway in skeletal muscle cells Int J Biochem Cell Biol 42 12 2010 2072 2081
    • (2010) Int J Biochem Cell Biol , vol.42 , Issue.12 , pp. 2072-2081
    • Chen, Y.1    Ye, J.2    Cao, L.3    Zhang, Y.4    Xia, W.5    Zhu, D.6
  • 71
    • 63849192339 scopus 로고    scopus 로고
    • Human leucocyte antigen (HLA) expression of primary trophoblast cells and placental cell lines, determined using single antigen beads to characterize allotype specificities of anti-HLA antibodies
    • R. Apps, S.P. Murphy, R. Fernando, L. Gardner, T. Ahad, and A. Moffett Human leucocyte antigen (HLA) expression of primary trophoblast cells and placental cell lines, determined using single antigen beads to characterize allotype specificities of anti-HLA antibodies Immunology 127 1 2009 26 39
    • (2009) Immunology , vol.127 , Issue.1 , pp. 26-39
    • Apps, R.1    Murphy, S.P.2    Fernando, R.3    Gardner, L.4    Ahad, T.5    Moffett, A.6
  • 72
    • 4444244818 scopus 로고    scopus 로고
    • Differential display RT-PCR analysis of human choriocarcinoma cell lines and normal term trophoblast cells: Identification of new genes expressed in placenta
    • DOI 10.1016/j.placenta.2003.10.020, PII S0143400404000451
    • J. Garcia, and J.L. Castrillo Differential display RT-PCR analysis of human choriocarcinoma cell lines and normal term trophoblast cells: identification of new genes expressed in placenta Placenta 25 8-9 2004 684 693 (Pubitemid 39185945)
    • (2004) Placenta , vol.25 , Issue.8-9 , pp. 684-693
    • Garcia, J.1    Castrillo, J.L.2
  • 73
    • 79957477728 scopus 로고    scopus 로고
    • Wide-ranging DNA methylation differences of primary trophoblast cell populations and derived cell lines: Implications and opportunities for understanding trophoblast function
    • B. Novakovic, L. Gordon, N.C. Wong, A. Moffett, U. Manuelpillai, and J.M. Craig Wide-ranging DNA methylation differences of primary trophoblast cell populations and derived cell lines: implications and opportunities for understanding trophoblast function Mol Hum Reprod 17 6 2011 344 353
    • (2011) Mol Hum Reprod , vol.17 , Issue.6 , pp. 344-353
    • Novakovic, B.1    Gordon, L.2    Wong, N.C.3    Moffett, A.4    Manuelpillai, U.5    Craig, J.M.6
  • 74
    • 0032763349 scopus 로고    scopus 로고
    • Differential gene expression pattern between normal human trophoblast and choriocarcinoma cell lines: Downregulation of heat shock protein-27 in choriocarcinoma in vitro and in vivo
    • G.L. Vegh, V. Fulop, Y. Liu, S.W. Ng, Z.S. Tuncer, and D.R. Genest Differential gene expression pattern between normal human trophoblast and choriocarcinoma cell lines: downregulation of heat shock protein-27 in choriocarcinoma in vitro and in vivo Gynecol Oncology 75 3 1999 391 396
    • (1999) Gynecol Oncology , vol.75 , Issue.3 , pp. 391-396
    • Vegh, G.L.1    Fulop, V.2    Liu, Y.3    Ng, S.W.4    Tuncer, Z.S.5    Genest, D.R.6
  • 75
    • 0035829844 scopus 로고    scopus 로고
    • Implantation and the survival of early pregnancy
    • E.R. Norwitz, D.J. Schust, and S.J. Fisher Implantation and the survival of early pregnancy N Engl J Med 345 19 2001 1400 1408
    • (2001) N Engl J Med , vol.345 , Issue.19 , pp. 1400-1408
    • Norwitz, E.R.1    Schust, D.J.2    Fisher, S.J.3
  • 76
    • 0036549808 scopus 로고    scopus 로고
    • Cytokines of the placenta and extra-placental membranes: Biosynthesis, secretion and roles in establishment of pregnancy in women
    • DOI 10.1053/plac.2001.0781
    • J.M. Bowen, L. Chamley, M.D. Mitchell, and J.A. Keelan Cytokines of the placenta and extra-placental membranes: biosynthesis, secretion and roles in establishment of pregnancy in women Placenta 23 4 2002 239 256 (Pubitemid 41348517)
    • (2002) Placenta , vol.23 , Issue.4 , pp. 239-256
    • Bowen, J.M.1    Chamley, L.2    Mitchell, M.D.3    Keelan, J.A.4
  • 77
    • 70349225807 scopus 로고    scopus 로고
    • BMP-11 and myostatin support undifferentiated growth of human embryonic stem cells in feeder-free cultures
    • N.R. Hannan, P. Jamshidi, M.F. Pera, and E.J. Wolvetang BMP-11 and myostatin support undifferentiated growth of human embryonic stem cells in feeder-free cultures Cloning Stem Cells 11 3 2009 427 435
    • (2009) Cloning Stem Cells , vol.11 , Issue.3 , pp. 427-435
    • Hannan, N.R.1    Jamshidi, P.2    Pera, M.F.3    Wolvetang, E.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.