메뉴 건너뛰기




Volumn 23, Issue 3, 2015, Pages 434-444

Development of novel activin-targeted therapeutics

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN A; ACTIVIN A PRODOMAIN IMMUNOGLOBULIN FC FRAGMENT FUSION PROTEIN; ACTIVIN B PRODOMAIN IMMUNOGLOBULIN FC FRAGMENT FUSION PROTEIN; ACTIVIN RECEPTOR; ACTIVIN RECEPTOR 2A; ACTIVIN RECEPTOR 2B; ALANINE; CYTOKINE; CYTOKINE RECEPTOR ANTAGONIST; GROWTH DIFFERENTIATION FACTOR 11; HISTIDINE; LYSINE; MYELOPID; MYOSTATIN; PARVOVIRUS VECTOR; TRANSFORMING GROWTH FACTOR BETA; TYROSINE; UNCLASSIFIED DRUG; ACTIVIN; BONE MORPHOGENETIC PROTEIN; GDF11 PROTEIN, HUMAN; GROWTH DIFFERENTIATION FACTOR; HYBRID PROTEIN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; MSTN PROTEIN, HUMAN;

EID: 84924028266     PISSN: 15250016     EISSN: 15250024     Source Type: Journal    
DOI: 10.1038/mt.2014.221     Document Type: Article
Times cited : (42)

References (43)
  • 2
    • 33646811178 scopus 로고    scopus 로고
    • Activin-A binds follistatin and type II receptors through overlapping binding sites: Generation of mutants with isolated binding activities
    • Harrison, CA, Chan, KL and Robertson, DM (2006). Activin-A binds follistatin and type II receptors through overlapping binding sites: generation of mutants with isolated binding activities. Endocrinology 147: 2744-2753.
    • (2006) Endocrinology , vol.147 , pp. 2744-2753
    • Harrison, C.A.1    Chan, K.L.2    Robertson, D.M.3
  • 3
    • 27644494876 scopus 로고    scopus 로고
    • Smad transcription factors
    • Massagué, J, Seoane, J and Wotton, D (2005). Smad transcription factors. Genes Dev 19: 2783-2810.
    • (2005) Genes Dev , vol.19 , pp. 2783-2810
    • Massagué, J.1    Seoane, J.2    Wotton, D.3
  • 4
    • 77956029835 scopus 로고    scopus 로고
    • Administration of a soluble activin type IIB receptor promotes skeletal muscle growth independent of fiber type
    • Cadena, SM, Tomkinson, KN, Monnell, TE, Spaits, MS, Kumar, R, Underwood, KW et al. (2010). Administration of a soluble activin type IIB receptor promotes skeletal muscle growth independent of fiber type. J Appl Physiol 109: 635-642.
    • (2010) J Appl Physiol , vol.109 , pp. 635-642
    • Cadena, S.M.1    Tomkinson, K.N.2    Monnell, T.E.3    Spaits, M.S.4    Kumar, R.5    Underwood, K.W.6
  • 5
    • 77957727888 scopus 로고    scopus 로고
    • Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo
    • Chantry, AD, Heath, D, Mulivor, AW, Pearsall, S, Baud'huin, M, Coulton, L et al. (2010). Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction in vivo. J Bone Miner Res 25: 2633-2646.
    • (2010) J Bone Miner Res , vol.25 , pp. 2633-2646
    • Chantry, A.D.1    Heath, D.2    Mulivor, A.W.3    Pearsall, S.4    Baud'Huin, M.5    Coulton, L.6
  • 6
    • 77950533566 scopus 로고    scopus 로고
    • A soluble activin receptor Type IIA fusion protein (ACE-011) increases bone mass via a dual anabolic-antiresorptive effect in Cynomolgus monkeys
    • Lotinun, S, Pearsall, RS, Davies, MV, Marvell, TH, Monnell, TE, Ucran, J et al. (2010). A soluble activin receptor Type IIA fusion protein (ACE-011) increases bone mass via a dual anabolic-antiresorptive effect in Cynomolgus monkeys. Bone 46: 1082-1088.
    • (2010) Bone , vol.46 , pp. 1082-1088
    • Lotinun, S.1    Pearsall, R.S.2    Davies, M.V.3    Marvell, T.H.4    Monnell, T.E.5    Ucran, J.6
  • 7
    • 84861722759 scopus 로고    scopus 로고
    • Activin receptor signaling: A potential therapeutic target for osteoporosis
    • Lotinun, S, Pearsall, RS, Horne, WC and Baron, R (2012). Activin receptor signaling: a potential therapeutic target for osteoporosis. Curr Mol Pharmacol 5: 195-204.
    • (2012) Curr Mol Pharmacol , vol.5 , pp. 195-204
    • Lotinun, S.1    Pearsall, R.S.2    Horne, W.C.3    Baron, R.4
  • 9
    • 84898042418 scopus 로고    scopus 로고
    • Transforming growth factor-β superfamily ligand trap ACE-536 corrects anemia by promoting late-stage erythropoiesis
    • Suragani, RN, Cadena, SM, Cawley, SM, Sako, D, Mitchell, D, Li, R et al. (2014). Transforming growth factor-β superfamily ligand trap ACE-536 corrects anemia by promoting late-stage erythropoiesis. Nat Med 20: 408-414.
    • (2014) Nat Med , vol.20 , pp. 408-414
    • Suragani, R.N.1    Cadena, S.M.2    Cawley, S.M.3    Sako, D.4    Mitchell, D.5    Li, R.6
  • 10
    • 84898049056 scopus 로고    scopus 로고
    • An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia
    • Dussiot, M, Maciel, TT, Fricot, A, Chartier, C, Negre, O, Veiga, J et al. (2014). An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia. Nat Med 20: 398-407.
    • (2014) Nat Med , vol.20 , pp. 398-407
    • Dussiot, M.1    Maciel, T.T.2    Fricot, A.3    Chartier, C.4    Negre, O.5    Veiga, J.6
  • 11
    • 79952764909 scopus 로고    scopus 로고
    • Targeting the activin type IIB receptor to improve muscle mass and function in the mdx mouse model of Duchenne muscular dystrophy
    • Pistilli, EE, Bogdanovich, S, Goncalves, MD, Ahima, RS, Lachey, J, Seehra, J et al. (2011). Targeting the activin type IIB receptor to improve muscle mass and function in the mdx mouse model of Duchenne muscular dystrophy. Am J Pathol 178: 1287-1297.
    • (2011) Am J Pathol , vol.178 , pp. 1287-1297
    • Pistilli, E.E.1    Bogdanovich, S.2    Goncalves, M.D.3    Ahima, R.S.4    Lachey, J.5    Seehra, J.6
  • 12
    • 77955642517 scopus 로고    scopus 로고
    • Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival
    • Zhou, X, Wang, JL, Lu, J, Song, Y, Kwak, KS, Jiao, Q et al. (2010). Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival. Cell 142: 531-543.
    • (2010) Cell , vol.142 , pp. 531-543
    • Zhou, X.1    Wang, J.L.2    Lu, J.3    Song, Y.4    Kwak, K.S.5    Jiao, Q.6
  • 13
    • 84892954839 scopus 로고    scopus 로고
    • An antibody blocking activin type II receptors induces strong skeletal muscle hypertrophy and protects from atrophy
    • Lach-Trifilieff, E, Minetti, GC, Sheppard, K, Ibebunjo, C, Feige, JN, Hartmann, S et al. (2014). An antibody blocking activin type II receptors induces strong skeletal muscle hypertrophy and protects from atrophy. Mol Cell Biol 34: 606-618.
    • (2014) Mol Cell Biol , vol.34 , pp. 606-618
    • Lach-Trifilieff, E.1    Minetti, G.C.2    Sheppard, K.3    Ibebunjo, C.4    Feige, J.N.5    Hartmann, S.6
  • 14
    • 84863992227 scopus 로고    scopus 로고
    • Blockade of the activin receptor IIb activates functional brown adipogenesis and thermogenesis by inducing mitochondrial oxidative metabolism
    • Fournier, B, Murray, B, Gutzwiller, S, Marcaletti, S, Marcellin, D, Bergling, S et al. (2012). Blockade of the activin receptor IIb activates functional brown adipogenesis and thermogenesis by inducing mitochondrial oxidative metabolism. Mol Cell Biol 32: 2871-2879.
    • (2012) Mol Cell Biol , vol.32 , pp. 2871-2879
    • Fournier, B.1    Murray, B.2    Gutzwiller, S.3    Marcaletti, S.4    Marcellin, D.5    Bergling, S.6
  • 15
    • 0025373853 scopus 로고
    • Requirement for activin A and transforming growth factor-beta 1 pro-regions in homodimer assembly
    • Gray, AM and Mason, AJ (1990). Requirement for activin A and transforming growth factor-beta 1 pro-regions in homodimer assembly. Science 247: 1328-1330.
    • (1990) Science , vol.247 , pp. 1328-1330
    • Gray, A.M.1    Mason, A.J.2
  • 16
    • 80052874703 scopus 로고    scopus 로고
    • Prodomains regulate the synthesis, extracellular localisation and activity of TGF-β superfamily ligands
    • Harrison, CA, Al-Musawi, SL and Walton, KL (2011). Prodomains regulate the synthesis, extracellular localisation and activity of TGF-β superfamily ligands. Growth Factors 29: 174-186.
    • (2011) Growth Factors , vol.29 , pp. 174-186
    • Harrison, C.A.1    Al-Musawi, S.L.2    Walton, K.L.3
  • 17
    • 77952784624 scopus 로고    scopus 로고
    • Two distinct regions of latency-associated peptide coordinate stability of the latent transforming growth factor-beta1 complex
    • Walton, KL, Makanji, Y, Chen, J, Wilce, MC, Chan, KL, Robertson, DM et al. (2010). Two distinct regions of latency-associated peptide coordinate stability of the latent transforming growth factor-beta1 complex. J Biol Chem 285: 17029-17037.
    • (2010) J Biol Chem , vol.285 , pp. 17029-17037
    • Walton, K.L.1    Makanji, Y.2    Chen, J.3    Wilce, M.C.4    Chan, K.L.5    Robertson, D.M.6
  • 18
    • 0037439630 scopus 로고    scopus 로고
    • Making sense of latent TGFbeta activation
    • Annes, JP, Munger, JS and Rifkin, DB (2003). Making sense of latent TGFbeta activation. J Cell Sci 116(Pt 2): 217-224.
    • (2003) J Cell Sci , vol.116 , Issue.2 , pp. 217-224
    • Annes, J.P.1    Munger, J.S.2    Rifkin, D.B.3
  • 19
    • 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 and 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
  • 21
    • 79959250326 scopus 로고    scopus 로고
    • Latent TGF-β structure and activation
    • Shi, M, Zhu, J, Wang, R, Chen, X, Mi, L, Walz, T et al. (2011). Latent TGF-β structure and activation. Nature 474: 343-349.
    • (2011) Nature , vol.474 , pp. 343-349
    • Shi, M.1    Zhu, J.2    Wang, R.3    Chen, X.4    Mi, L.5    Walz, T.6
  • 22
    • 0029897379 scopus 로고    scopus 로고
    • The recombinant proregion of transforming growth factor beta1 (latency-associated peptide) inhibits active transforming growth factor beta1 in transgenic mice
    • Böttinger, EP, Factor, VM, Tsang, ML, Weatherbee, JA, Kopp, JB, Qian, SW et al. (1996). The recombinant proregion of transforming growth factor beta1 (latency-associated peptide) inhibits active transforming growth factor beta1 in transgenic mice. Proc Natl Acad Sci USA 93: 5877-5882.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5877-5882
    • Böttinger, E.P.1    Factor, V.M.2    Tsang, M.L.3    Weatherbee, J.A.4    Kopp, J.B.5    Qian, S.W.6
  • 23
    • 67649668906 scopus 로고    scopus 로고
    • Molecular, cellular and physiological investigation of myostatin propeptide-mediated muscle growth in adult mice
    • Matsakas, A, Foster, K, Otto, A, Macharia, R, Elashry, MI, Feist, S et al. (2009). Molecular, cellular and physiological investigation of myostatin propeptide-mediated muscle growth in adult mice. Neuromuscul Disord 19: 489-499.
    • (2009) Neuromuscul Disord , vol.19 , pp. 489-499
    • Matsakas, A.1    Foster, K.2    Otto, A.3    Macharia, R.4    Elashry, M.I.5    Feist, S.6
  • 24
    • 41149152962 scopus 로고    scopus 로고
    • Myostatin propeptide gene delivery by adeno-associated virus serotype 8 vectors enhances muscle growth and ameliorates dystrophic phenotypes in mdx mice
    • Qiao, C, Li, J, Jiang, J, Zhu, X, Wang, B, Li, J et al. (2008). Myostatin propeptide gene delivery by adeno-associated virus serotype 8 vectors enhances muscle growth and ameliorates dystrophic phenotypes in mdx mice. Hum Gene Ther 19: 241-254.
    • (2008) Hum Gene Ther , vol.19 , pp. 241-254
    • Qiao, C.1    Li, J.2    Jiang, J.3    Zhu, X.4    Wang, B.5    Li, J.6
  • 28
    • 34548388339 scopus 로고    scopus 로고
    • Prevention of cachexia-like syndrome development and reduction of tumor progression in inhibin-deficient mice following administration of a chimeric activin receptor type II-murine Fc protein
    • Li, Q, Kumar, R, Underwood, K, O'Connor, AE, Loveland, KL, Seehra, JS et al. (2007). Prevention of cachexia-like syndrome development and reduction of tumor progression in inhibin-deficient mice following administration of a chimeric activin receptor type II-murine Fc protein. Mol Hum Reprod 13: 675-683.
    • (2007) Mol Hum Reprod , vol.13 , pp. 675-683
    • Li, Q.1    Kumar, R.2    Underwood, K.3    O'Connor, A.E.4    Loveland, K.L.5    Seehra, J.S.6
  • 29
    • 36049023174 scopus 로고    scopus 로고
    • Activin A is a critical component of the inflammatory response, and its binding protein, follistatin, reduces mortality in endotoxemia
    • Jones, KL, Mansell, A, Patella, S, Scott, BJ, Hedger, MP, de Kretser, DM et al. (2007). Activin A is a critical component of the inflammatory response, and its binding protein, follistatin, reduces mortality in endotoxemia. Proc Natl Acad Sci USA 104: 16239-16244.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16239-16244
    • Jones, K.L.1    Mansell, A.2    Patella, S.3    Scott, B.J.4    Hedger, M.P.5    De Kretser, D.M.6
  • 30
    • 0033214191 scopus 로고    scopus 로고
    • Overexpression of activin A in the skin of transgenic mice reveals new activities of activin in epidermal morphogenesis, dermal fibrosis and wound repair
    • Munz, B, Smola, H, Engelhardt, F, Bleuel, K, Brauchle, M, Lein, I et al. (1999). Overexpression of activin A in the skin of transgenic mice reveals new activities of activin in epidermal morphogenesis, dermal fibrosis and wound repair. EMBO J 18: 5205-5215.
    • (1999) EMBO J , vol.18 , pp. 5205-5215
    • Munz, B.1    Smola, H.2    Engelhardt, F.3    Bleuel, K.4    Brauchle, M.5    Lein, I.6
  • 31
    • 0008478647 scopus 로고
    • Chemical and biological characterization of the inhibin family of protein hormones
    • Vale, W, Rivier, C, Hsueh, A, Campen, C, Meunier, H, Bicsak, T et al. (1988). Chemical and biological characterization of the inhibin family of protein hormones. Recent Prog Horm Res 44: 1-34.
    • (1988) Recent Prog Horm Res , vol.44 , pp. 1-34
    • Vale, W.1    Rivier, C.2    Hsueh, A.3    Campen, C.4    Meunier, H.5    Bicsak, T.6
  • 32
    • 67650717476 scopus 로고    scopus 로고
    • The biology of activin: Recent advances in structure, regulation and function
    • Xia, Y and Schneyer, AL (2009). The biology of activin: recent advances in structure, regulation and function. J Endocrinol 202: 1-12.
    • (2009) J Endocrinol , vol.202 , pp. 1-12
    • Xia, Y.1    Schneyer, A.L.2
  • 33
    • 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 and 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
  • 34
    • 84924049938 scopus 로고    scopus 로고
    • Balancing Efficacy versus safety: Learnings from development of myostatin inhibitiors
    • Morris, C (2013). Balancing Efficacy versus safety: learnings from development of myostatin inhibitiors. DACC News 29: 8.
    • (2013) DACC News , vol.29 , pp. 8
    • Morris, C.1
  • 35
    • 84872691147 scopus 로고    scopus 로고
    • Species differences in the expression and activity of bone morphogenetic protein 15
    • Al-Musawi, SL, Walton, KL, Heath, D, Simpson, CM and Harrison, CA (2013). Species differences in the expression and activity of bone morphogenetic protein 15. Endocrinology 154: 888-899.
    • (2013) Endocrinology , vol.154 , pp. 888-899
    • Al-Musawi, S.L.1    Walton, K.L.2    Heath, D.3    Simpson, C.M.4    Harrison, C.A.5
  • 36
    • 84857412359 scopus 로고    scopus 로고
    • Activation of latent human GDF9 by a single residue change (Gly 391 Arg) in the mature domain
    • Simpson, CM, Stanton, PG, Walton, KL, Chan, KL, Ritter, LJ, Gilchrist, RB et al. (2012). Activation of latent human GDF9 by a single residue change (Gly 391 Arg) in the mature domain. Endocrinology 153: 1301-1310.
    • (2012) Endocrinology , vol.153 , pp. 1301-1310
    • Simpson, C.M.1    Stanton, P.G.2    Walton, K.L.3    Chan, K.L.4    Ritter, L.J.5    Gilchrist, R.B.6
  • 37
    • 66149084397 scopus 로고    scopus 로고
    • A common biosynthetic pathway governs the dimerization and secretion of inhibin and related transforming growth factor beta (TGFbeta) ligands
    • Walton, KL, Makanji, Y, Wilce, MC, Chan, KL, Robertson, DM and Harrison, CA (2009). A common biosynthetic pathway governs the dimerization and secretion of inhibin and related transforming growth factor beta (TGFbeta) ligands. J Biol Chem 284: 9311-9320.
    • (2009) J Biol Chem , vol.284 , pp. 9311-9320
    • Walton, K.L.1    Makanji, Y.2    Wilce, M.C.3    Chan, K.L.4    Robertson, D.M.5    Harrison, C.A.6
  • 38
    • 84886735949 scopus 로고    scopus 로고
    • Serum activin A and B levels predict outcome in patients with acute respiratory failure: A prospective cohort study
    • de Kretser, DM, Bensley, JG, Pettilä, V, Linko, R, Hedger, MP, Hayward, S et al. (2013). Serum activin A and B levels predict outcome in patients with acute respiratory failure: a prospective cohort study. Crit Care 17: R263.
    • (2013) Crit Care , vol.17 , pp. R263
    • De Kretser, D.M.1    Bensley, J.G.2    Pettilä, V.3    Linko, R.4    Hedger, M.P.5    Hayward, S.6
  • 39
    • 38349145459 scopus 로고    scopus 로고
    • Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways
    • Lee, SJ (2007). Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways. PLoS ONE 2: e789.
    • (2007) PLoS One , vol.2 , pp. e789
    • Lee, S.J.1
  • 40
    • 34249807636 scopus 로고    scopus 로고
    • Inhibin A and B in vitro bioactivities are modified by their degree of glycosylation and their affinities to betaglycan
    • Makanji, Y, Harrison, CA, Stanton, PG, Krishna, R and Robertson, DM (2007). Inhibin A and B in vitro bioactivities are modified by their degree of glycosylation and their affinities to betaglycan. Endocrinology 148: 2309-2316.
    • (2007) Endocrinology , vol.148 , pp. 2309-2316
    • Makanji, Y.1    Harrison, C.A.2    Stanton, P.G.3    Krishna, R.4    Robertson, D.M.5
  • 41
    • 4644252083 scopus 로고    scopus 로고
    • Efficient transduction of skeletal muscle using vectors based on adeno-associated virus serotype 6
    • Blankinship, MJ, Gregorevic, P, Allen, JM, Harper, SQ, Harper, H, Halbert, CL et al. (2004). Efficient transduction of skeletal muscle using vectors based on adeno-associated virus serotype 6. Mol Ther 10: 671-678.
    • (2004) Mol Ther , vol.10 , pp. 671-678
    • Blankinship, M.J.1    Gregorevic, P.2    Allen, J.M.3    Harper, S.Q.4    Harper, H.5    Halbert, C.L.6
  • 43
    • 79954623314 scopus 로고    scopus 로고
    • TGF-beta regulates miR-206 and miR-29 to control myogenic differentiation through regulation of HDAC4
    • Winbanks, CE, Wang, B, Beyer, C, Koh, P, White, L, Kantharidis, P et al. (2011). TGF-beta regulates miR-206 and miR-29 to control myogenic differentiation through regulation of HDAC4. J Biol Chem 286: 13805-13814.
    • (2011) J Biol Chem , vol.286 , pp. 13805-13814
    • Winbanks, C.E.1    Wang, B.2    Beyer, C.3    Koh, P.4    White, L.5    Kantharidis, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.