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Volumn 28, Issue 2, 2014, Pages 375-386

Modulators of erythropoiesis: Emerging therapies for hemoglobinopathies and disorders of red cell production

Author keywords

ACE 011; ACE 536; Hemoglobinopathies; JAK2; LY 2157299; Steady state; Stress and ineffective erythropoiesis; Transforming growth factor

Indexed keywords

ACTIVIN A; ANTIANEMIC AGENT; BONE MORPHOGENETIC PROTEIN 2; BONE MORPHOGENETIC PROTEIN 4; FOLLITROPIN; GALUNISERTIB; INHIBIN A; JANUS KINASE 2; JANUS KINASE 2 INHIBITOR; LUSPATERCEPT; SOTATERCEPT; STAT5 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; ACE-011; ACTIVIN RECEPTOR 2; HYBRID PROTEIN; RAP-536;

EID: 84896718827     PISSN: 08898588     EISSN: 15581977     Source Type: Journal    
DOI: 10.1016/j.hoc.2013.12.001     Document Type: Review
Times cited : (22)

References (82)
  • 1
    • 33646782974 scopus 로고    scopus 로고
    • Erythroblastic islands: specialized microenvironmental niches for erythropoiesis
    • Chasis J.A. Erythroblastic islands: specialized microenvironmental niches for erythropoiesis. Curr Opin Hematol 2006, 13:137-141.
    • (2006) Curr Opin Hematol , vol.13 , pp. 137-141
    • Chasis, J.A.1
  • 2
    • 50949089311 scopus 로고    scopus 로고
    • Erythroblastic islands: niches for erythropoiesis
    • Chasis J.A., Mohandas N. Erythroblastic islands: niches for erythropoiesis. Blood 2008, 112:470-478.
    • (2008) Blood , vol.112 , pp. 470-478
    • Chasis, J.A.1    Mohandas, N.2
  • 3
    • 84878439561 scopus 로고    scopus 로고
    • Macrophages support pathological erythropoiesis in polycythemia vera and beta-thalassemia
    • Ramos P., Casu C., Gardenghi S., et al. Macrophages support pathological erythropoiesis in polycythemia vera and beta-thalassemia. Nat Med 2013, 19:437-445.
    • (2013) Nat Med , vol.19 , pp. 437-445
    • Ramos, P.1    Casu, C.2    Gardenghi, S.3
  • 4
    • 0021978919 scopus 로고
    • Isolation and characterization of genomic and cDNA clones of human erythropoietin
    • Jacobs K., Shoemaker C., Rudersdorf R., et al. Isolation and characterization of genomic and cDNA clones of human erythropoietin. Nature 1985, 313:806-810.
    • (1985) Nature , vol.313 , pp. 806-810
    • Jacobs, K.1    Shoemaker, C.2    Rudersdorf, R.3
  • 5
    • 0242611254 scopus 로고
    • Cloning and expression of the human erythropoietin gene
    • Lin F.K., Suggs S., Lin C.H., et al. Cloning and expression of the human erythropoietin gene. Proc Natl Acad Sci USA 1985, 82:7580-7584.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7580-7584
    • Lin, F.K.1    Suggs, S.2    Lin, C.H.3
  • 7
    • 0024373139 scopus 로고
    • Cloning of cDNA for the major DNA-binding protein of the erythroid lineage through expression in mammalian cells
    • Tsai S.F., Martin D.I., Zon L.I., et al. Cloning of cDNA for the major DNA-binding protein of the erythroid lineage through expression in mammalian cells. Nature 1989, 339:446-451.
    • (1989) Nature , vol.339 , pp. 446-451
    • Tsai, S.F.1    Martin, D.I.2    Zon, L.I.3
  • 8
    • 0024563574 scopus 로고
    • Expression cloning of the murine erythropoietin receptor
    • D'Andrea A.D., Lodish H.F., Wong G.G. Expression cloning of the murine erythropoietin receptor. Cell 1989, 57:277-285.
    • (1989) Cell , vol.57 , pp. 277-285
    • D'Andrea, A.D.1    Lodish, H.F.2    Wong, G.G.3
  • 9
    • 0025029837 scopus 로고
    • Erythropoietin receptor: cloning strategy and structural features
    • D'Andrea A., Fasman G., Wong G., et al. Erythropoietin receptor: cloning strategy and structural features. Int J Cell Cloning 1990, 8(Suppl 1):173-180.
    • (1990) Int J Cell Cloning , vol.8 , Issue.SUPPL 1 , pp. 173-180
    • D'Andrea, A.1    Fasman, G.2    Wong, G.3
  • 10
    • 0027327484 scopus 로고
    • JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
    • Witthuhn B.A., Quelle F.W., Silvennoinen O., et al. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell 1993, 74:227-236.
    • (1993) Cell , vol.74 , pp. 227-236
    • Witthuhn, B.A.1    Quelle, F.W.2    Silvennoinen, O.3
  • 11
    • 0027179365 scopus 로고
    • Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase
    • Argetsinger L.S., Campbell G.S., Yang X., et al. Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell 1993, 74:237-244.
    • (1993) Cell , vol.74 , pp. 237-244
    • Argetsinger, L.S.1    Campbell, G.S.2    Yang, X.3
  • 12
    • 18244432009 scopus 로고    scopus 로고
    • Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis
    • Neubauer H., Cumano A., Muller M., et al. Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 1998, 93:397-409.
    • (1998) Cell , vol.93 , pp. 397-409
    • Neubauer, H.1    Cumano, A.2    Muller, M.3
  • 13
    • 0033604519 scopus 로고    scopus 로고
    • Signal transduction in the erythropoietin receptor system
    • Wojchowski D.M., Gregory R.C., Miller C.P., et al. Signal transduction in the erythropoietin receptor system. Exp Cell Res 1999, 253:143-156.
    • (1999) Exp Cell Res , vol.253 , pp. 143-156
    • Wojchowski, D.M.1    Gregory, R.C.2    Miller, C.P.3
  • 15
    • 84865768673 scopus 로고    scopus 로고
    • Stat5 signaling specifies basal versus stress erythropoietic responses through distinct binary and graded dynamic modalities
    • Porpiglia E., Hidalgo D., Koulnis M., et al. Stat5 signaling specifies basal versus stress erythropoietic responses through distinct binary and graded dynamic modalities. PLoS Biol 2012, 10:e1001383.
    • (2012) PLoS Biol , vol.10
    • Porpiglia, E.1    Hidalgo, D.2    Koulnis, M.3
  • 16
    • 50949133924 scopus 로고    scopus 로고
    • Decreased differentiation of erythroid cells exacerbates ineffective erythropoiesis in beta-thalassemia
    • Libani I.V., Guy E.C., Melchiori L., et al. Decreased differentiation of erythroid cells exacerbates ineffective erythropoiesis in beta-thalassemia. Blood 2008, 112:875-885.
    • (2008) Blood , vol.112 , pp. 875-885
    • Libani, I.V.1    Guy, E.C.2    Melchiori, L.3
  • 17
    • 84878444005 scopus 로고    scopus 로고
    • CD169(+) macrophages provide a niche promoting erythropoiesis under homeostasis and stress
    • Chow A., Huggins M., Ahmed J., et al. CD169(+) macrophages provide a niche promoting erythropoiesis under homeostasis and stress. Nat Med 2013, 19:429-436.
    • (2013) Nat Med , vol.19 , pp. 429-436
    • Chow, A.1    Huggins, M.2    Ahmed, J.3
  • 18
    • 0034012330 scopus 로고    scopus 로고
    • Regulation of the Jak2 tyrosine kinase by its pseudokinase domain
    • Saharinen P., Takaluoma K., Silvennoinen O. Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol Cell Biol 2000, 20:3387-3395.
    • (2000) Mol Cell Biol , vol.20 , pp. 3387-3395
    • Saharinen, P.1    Takaluoma, K.2    Silvennoinen, O.3
  • 19
    • 20144363192 scopus 로고    scopus 로고
    • Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders
    • Baxter E.J., Scott L.M., Campbell P.J., et al. Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders. Lancet 2005, 365:1054-1061.
    • (2005) Lancet , vol.365 , pp. 1054-1061
    • Baxter, E.J.1    Scott, L.M.2    Campbell, P.J.3
  • 20
    • 17844383458 scopus 로고    scopus 로고
    • Aunique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera
    • James C., Ugo V., Le Couedic J.P., et al. Aunique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 2005, 434:1144-1148.
    • (2005) Nature , vol.434 , pp. 1144-1148
    • James, C.1    Ugo, V.2    Le Couedic, J.P.3
  • 21
    • 17644424955 scopus 로고    scopus 로고
    • Again-of-function mutation of JAK2 in myeloproliferative disorders
    • Kralovics R., Passamonti F., Buser A.S., et al. Again-of-function mutation of JAK2 in myeloproliferative disorders. NEngl J Med 2005, 352:1779-1790.
    • (2005) NEngl J Med , vol.352 , pp. 1779-1790
    • Kralovics, R.1    Passamonti, F.2    Buser, A.S.3
  • 22
    • 20244369569 scopus 로고    scopus 로고
    • Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis
    • Levine R.L., Wadleigh M., Cools J., et al. Activating mutation in the tyrosine kinase JAK2 in polycythemia vera, essential thrombocythemia, and myeloid metaplasia with myelofibrosis. Cancer Cell 2005, 7:387-397.
    • (2005) Cancer Cell , vol.7 , pp. 387-397
    • Levine, R.L.1    Wadleigh, M.2    Cools, J.3
  • 23
    • 20744460045 scopus 로고    scopus 로고
    • Identification of an acquired JAK2 mutation in polycythemia vera
    • Zhao R., Xing S., Li Z., et al. Identification of an acquired JAK2 mutation in polycythemia vera. JBiol Chem 2005, 280:22788-22792.
    • (2005) JBiol Chem , vol.280 , pp. 22788-22792
    • Zhao, R.1    Xing, S.2    Li, Z.3
  • 25
    • 84874959297 scopus 로고    scopus 로고
    • Polycythemia vera: current pharmacotherapy and future directions
    • Hensley B., Geyer H., Mesa R. Polycythemia vera: current pharmacotherapy and future directions. Expert Opin Pharmacother 2013, 14:609-617.
    • (2013) Expert Opin Pharmacother , vol.14 , pp. 609-617
    • Hensley, B.1    Geyer, H.2    Mesa, R.3
  • 26
    • 84878169183 scopus 로고    scopus 로고
    • Polycythemia vera and essential thrombocythemia: 2013 update on diagnosis, risk-stratification, and management
    • Tefferi A. Polycythemia vera and essential thrombocythemia: 2013 update on diagnosis, risk-stratification, and management. Am J Hematol 2013, 88:507-516.
    • (2013) Am J Hematol , vol.88 , pp. 507-516
    • Tefferi, A.1
  • 27
    • 80054838641 scopus 로고    scopus 로고
    • Beta-thalassemia: a model for elucidating the dynamic regulation of ineffective erythropoiesis and iron metabolism
    • Ginzburg Y., Rivella S. Beta-thalassemia: a model for elucidating the dynamic regulation of ineffective erythropoiesis and iron metabolism. Blood 2011, 118:4321-4330.
    • (2011) Blood , vol.118 , pp. 4321-4330
    • Ginzburg, Y.1    Rivella, S.2
  • 28
    • 84861357425 scopus 로고    scopus 로고
    • The role of ineffective erythropoiesis in non-transfusion-dependent thalassemia
    • Rivella S. The role of ineffective erythropoiesis in non-transfusion-dependent thalassemia. Blood Rev 2012, 26(Suppl 1):S12-S15.
    • (2012) Blood Rev , vol.26 , Issue.SUPPL 1
    • Rivella, S.1
  • 30
    • 67749103803 scopus 로고    scopus 로고
    • Ineffective erythropoiesis and thalassemias
    • Rivella S. Ineffective erythropoiesis and thalassemias. Curr Opin Hematol 2009, 16:187-194.
    • (2009) Curr Opin Hematol , vol.16 , pp. 187-194
    • Rivella, S.1
  • 31
    • 77953372767 scopus 로고    scopus 로고
    • Future alternative therapies for beta-thalassemia
    • Rivella S., Rachmilewitz E. Future alternative therapies for beta-thalassemia. Expert Rev Hematol 2009, 2:685.
    • (2009) Expert Rev Hematol , vol.2 , pp. 685
    • Rivella, S.1    Rachmilewitz, E.2
  • 32
    • 77954568361 scopus 로고    scopus 로고
    • Beta-thalassemia: HiJAKing ineffective erythropoiesis and iron overload
    • Melchiori L., Gardenghi S., Rivella S. Beta-thalassemia: HiJAKing ineffective erythropoiesis and iron overload. Adv Hematol 2010, 2010:938640.
    • (2010) Adv Hematol , vol.2010 , pp. 938640
    • Melchiori, L.1    Gardenghi, S.2    Rivella, S.3
  • 33
    • 78249289938 scopus 로고    scopus 로고
    • Anemia, ineffective erythropoiesis, and hepcidin: interacting factors in abnormal iron metabolism leading to iron overload in beta-thalassemia
    • Gardenghi S., Grady R.W., Rivella S. Anemia, ineffective erythropoiesis, and hepcidin: interacting factors in abnormal iron metabolism leading to iron overload in beta-thalassemia. Hematol Oncol Clin North Am 2010, 24:1089-1107.
    • (2010) Hematol Oncol Clin North Am , vol.24 , pp. 1089-1107
    • Gardenghi, S.1    Grady, R.W.2    Rivella, S.3
  • 34
    • 80052874703 scopus 로고    scopus 로고
    • Prodomains regulate the synthesis, extracellular localisation and activity of TGF-beta superfamily ligands
    • Harrison C.A., Al-Musawi S.L., Walton K.L. Prodomains regulate the synthesis, extracellular localisation and activity of TGF-beta superfamily ligands. Growth Factors 2011, 29:174-186.
    • (2011) Growth Factors , vol.29 , pp. 174-186
    • Harrison, C.A.1    Al-Musawi, S.L.2    Walton, K.L.3
  • 35
    • 84866985855 scopus 로고    scopus 로고
    • Targeting the TGFbeta signalling pathway in disease
    • Akhurst R.J., Hata A. Targeting the TGFbeta signalling pathway in disease. Nat Rev Drug Discov 2012, 11:790-811.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 790-811
    • Akhurst, R.J.1    Hata, A.2
  • 37
    • 79957839527 scopus 로고    scopus 로고
    • Activin signaling as an emerging target for therapeutic interventions
    • Tsuchida K., Nakatani M., Hitachi K., et al. Activin signaling as an emerging target for therapeutic interventions. Cell Commun Signal 2009, 7:15.
    • (2009) Cell Commun Signal , vol.7 , pp. 15
    • Tsuchida, K.1    Nakatani, M.2    Hitachi, K.3
  • 38
    • 70349307046 scopus 로고    scopus 로고
    • Inhibin B is a more potent suppressor of rat follicle-stimulating hormone release than inhibin a invitro and invivo
    • Makanji Y., Temple-Smith P.D., Walton K.L., et al. Inhibin B is a more potent suppressor of rat follicle-stimulating hormone release than inhibin a invitro and invivo. Endocrinology 2009, 150:4784-4793.
    • (2009) Endocrinology , vol.150 , pp. 4784-4793
    • Makanji, Y.1    Temple-Smith, P.D.2    Walton, K.L.3
  • 39
    • 79951906630 scopus 로고    scopus 로고
    • The synthesis and secretion of inhibins
    • Walton K.L., Makanji Y., Robertson D.M., et al. The synthesis and secretion of inhibins. Vitam Horm 2011, 85:149-184.
    • (2011) Vitam Horm , vol.85 , pp. 149-184
    • Walton, K.L.1    Makanji, Y.2    Robertson, D.M.3
  • 40
    • 84861681431 scopus 로고    scopus 로고
    • New insights into the mechanisms of activin action and inhibition
    • Walton K.L., Makanji Y., Harrison C.A. New insights into the mechanisms of activin action and inhibition. Mol Cell Endocrinol 2012, 359:2-12.
    • (2012) Mol Cell Endocrinol , vol.359 , pp. 2-12
    • Walton, K.L.1    Makanji, Y.2    Harrison, C.A.3
  • 41
    • 0028918915 scopus 로고
    • Multiple defects and perinatal death in mice deficient in follistatin
    • Matzuk M.M., Lu N., Vogel H., et al. Multiple defects and perinatal death in mice deficient in follistatin. Nature 1995, 374:360-363.
    • (1995) Nature , vol.374 , pp. 360-363
    • Matzuk, M.M.1    Lu, N.2    Vogel, H.3
  • 42
    • 84870997478 scopus 로고    scopus 로고
    • Activin receptor antagonists for cancer-related anemia and bone disease
    • Fields S.Z., Parshad S., Anne M., et al. Activin receptor antagonists for cancer-related anemia and bone disease. Expert Opin Investig Drugs 2013, 22:87-101.
    • (2013) Expert Opin Investig Drugs , vol.22 , pp. 87-101
    • Fields, S.Z.1    Parshad, S.2    Anne, M.3
  • 43
    • 0026767087 scopus 로고
    • Myelodysplastic syndromes (refractory anemia). A perspective of the biologic, clinical, and therapeutic issues
    • Besa E.C. Myelodysplastic syndromes (refractory anemia). A perspective of the biologic, clinical, and therapeutic issues. Med Clin North Am 1992, 76:599-617.
    • (1992) Med Clin North Am , vol.76 , pp. 599-617
    • Besa, E.C.1
  • 44
    • 84920248056 scopus 로고
    • Ineffective erythropoiesis
    • Ineffective erythropoiesis. Lancet 1973, 301:1164-1165.
    • (1973) Lancet , vol.301 , pp. 1164-1165
  • 45
    • 0034669951 scopus 로고    scopus 로고
    • The importance of erythroid expansion in determining the extent of apoptosis in erythroid precursors in patients with beta-thalassemia major
    • Centis F., Tabellini L., Lucarelli G., et al. The importance of erythroid expansion in determining the extent of apoptosis in erythroid precursors in patients with beta-thalassemia major. Blood 2000, 96:3624-3629.
    • (2000) Blood , vol.96 , pp. 3624-3629
    • Centis, F.1    Tabellini, L.2    Lucarelli, G.3
  • 46
    • 84896729941 scopus 로고    scopus 로고
    • The thalassemias
    • Elsevier, Philadelphia, L. Goldman, A.I. Shafer (Eds.)
    • Cappellini M.D. The thalassemias. Goldman's Cecil medicine 2011, 1060-1066. Elsevier, Philadelphia. L. Goldman, A.I. Shafer (Eds.).
    • (2011) Goldman's Cecil medicine , pp. 1060-1066
    • Cappellini, M.D.1
  • 47
    • 84879346295 scopus 로고    scopus 로고
    • Sickle cell disease and other hemoglobinopathies
    • Elsevier, Philadelphia, L. Goldman, A.I. Shafer (Eds.)
    • Steinberg M.H. Sickle cell disease and other hemoglobinopathies. Goldman's Cecil medicine 2011, 1066-1075. Elsevier, Philadelphia. L. Goldman, A.I. Shafer (Eds.).
    • (2011) Goldman's Cecil medicine , pp. 1066-1075
    • Steinberg, M.H.1
  • 48
    • 84861813324 scopus 로고    scopus 로고
    • Do not super-excess me!
    • Rivella S. Do not super-excess me!. Blood 2012, 119:5064-5065.
    • (2012) Blood , vol.119 , pp. 5064-5065
    • Rivella, S.1
  • 49
    • 0000928772 scopus 로고
    • Abnormal ("ringed") sideroblasts in various hematologic and non-hematologic disorders
    • Bowman W.D. Abnormal ("ringed") sideroblasts in various hematologic and non-hematologic disorders. Blood 1961, 18:662-671.
    • (1961) Blood , vol.18 , pp. 662-671
    • Bowman, W.D.1
  • 50
    • 77954611973 scopus 로고    scopus 로고
    • Iron loading and overloading due to ineffective erythropoiesis
    • Tanno T., Miller J.L. Iron loading and overloading due to ineffective erythropoiesis. Adv Hematol 2010, 2010:358283.
    • (2010) Adv Hematol , vol.2010 , pp. 358283
    • Tanno, T.1    Miller, J.L.2
  • 51
    • 27744469194 scopus 로고    scopus 로고
    • Evidence for ineffective erythropoiesis in severe sickle cell disease
    • Wu C.J., Krishnamurti L., Kutok J.L., et al. Evidence for ineffective erythropoiesis in severe sickle cell disease. Blood 2005, 106:3639-3645.
    • (2005) Blood , vol.106 , pp. 3639-3645
    • Wu, C.J.1    Krishnamurti, L.2    Kutok, J.L.3
  • 52
    • 65449117261 scopus 로고    scopus 로고
    • Recombinant human erythropoiesis-stimulating agents and mortality in patients with cancer: a meta-analysis of randomised trials
    • Bohlius J., Schmidlin K., Brillant C., et al. Recombinant human erythropoiesis-stimulating agents and mortality in patients with cancer: a meta-analysis of randomised trials. Lancet 2009, 373:1532-1542.
    • (2009) Lancet , vol.373 , pp. 1532-1542
    • Bohlius, J.1    Schmidlin, K.2    Brillant, C.3
  • 53
    • 80053204645 scopus 로고    scopus 로고
    • Hematopoietic growth factors in myelodysplastic syndromes
    • Steensma D.P. Hematopoietic growth factors in myelodysplastic syndromes. Semin Oncol 2011, 38:635-647.
    • (2011) Semin Oncol , vol.38 , pp. 635-647
    • Steensma, D.P.1
  • 54
    • 33947370286 scopus 로고    scopus 로고
    • Inhibin A is an endocrine stimulator of bone mass and strength
    • Perrien D.S., Akel N.S., Edwards P.K., et al. Inhibin A is an endocrine stimulator of bone mass and strength. Endocrinology 2007, 148:1654-1665.
    • (2007) Endocrinology , vol.148 , pp. 1654-1665
    • Perrien, D.S.1    Akel, N.S.2    Edwards, P.K.3
  • 55
    • 0036144102 scopus 로고    scopus 로고
    • Inhibin suppresses and activin stimulates osteoblastogenesis and osteoclastogenesis in murine bone marrow cultures
    • Gaddy-Kurten D., Coker J.K., Abe E., et al. Inhibin suppresses and activin stimulates osteoblastogenesis and osteoclastogenesis in murine bone marrow cultures. Endocrinology 2002, 143:74-83.
    • (2002) Endocrinology , vol.143 , pp. 74-83
    • Gaddy-Kurten, D.1    Coker, J.K.2    Abe, E.3
  • 56
  • 57
    • 33748954261 scopus 로고    scopus 로고
    • Activin A circulating levels in patients with bone metastasis from breast or prostate cancer
    • Leto G., Incorvaia L., Badalamenti G., et al. Activin A circulating levels in patients with bone metastasis from breast or prostate cancer. Clin Exp Metastasis 2006, 23:117-122.
    • (2006) Clin Exp Metastasis , vol.23 , pp. 117-122
    • Leto, G.1    Incorvaia, L.2    Badalamenti, G.3
  • 58
    • 84867135322 scopus 로고    scopus 로고
    • Circulating activin-A is elevated in patients with advanced multiple myeloma and correlates with extensive bone involvement and inferior survival; no alterations post-lenalidomide and dexamethasone therapy
    • Terpos E., Kastritis E., Christoulas D., et al. Circulating activin-A is elevated in patients with advanced multiple myeloma and correlates with extensive bone involvement and inferior survival; no alterations post-lenalidomide and dexamethasone therapy. Ann Oncol 2012, 23:2681-2686.
    • (2012) Ann Oncol , vol.23 , pp. 2681-2686
    • Terpos, E.1    Kastritis, E.2    Christoulas, D.3
  • 59
    • 77950438331 scopus 로고    scopus 로고
    • Activin A promotes multiple myeloma-induced osteolysis and is a promising target for myeloma bone disease
    • Vallet S., Mukherjee S., Vaghela N., et al. Activin A promotes multiple myeloma-induced osteolysis and is a promising target for myeloma bone disease. Proc Natl Acad Sci USA 2010, 107:5124-5129.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5124-5129
    • Vallet, S.1    Mukherjee, S.2    Vaghela, N.3
  • 60
    • 0026621796 scopus 로고
    • Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in mice
    • Matzuk M.M., Finegold M.J., Su J.G., et al. Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in mice. Nature 1992, 360:313-319.
    • (1992) Nature , vol.360 , pp. 313-319
    • Matzuk, M.M.1    Finegold, M.J.2    Su, J.G.3
  • 61
    • 0034457003 scopus 로고    scopus 로고
    • Follistatin is a modulator of gonadal tumor progression and the activin-induced wasting syndrome in inhibin-deficient mice
    • Cipriano S.C., Chen L., Kumar T.R., et al. Follistatin is a modulator of gonadal tumor progression and the activin-induced wasting syndrome in inhibin-deficient mice. Endocrinology 2000, 141:2319-2327.
    • (2000) Endocrinology , vol.141 , pp. 2319-2327
    • Cipriano, S.C.1    Chen, L.2    Kumar, T.R.3
  • 62
    • 0142244909 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of follistatin enlarges intact liver of adult rats
    • Takabe K., Wang L., Leal A.M., et al. Adenovirus-mediated overexpression of follistatin enlarges intact liver of adult rats. Hepatology 2003, 38:1107-1115.
    • (2003) Hepatology , vol.38 , pp. 1107-1115
    • Takabe, K.1    Wang, L.2    Leal, A.M.3
  • 63
    • 0037440420 scopus 로고    scopus 로고
    • Regulation of human erythropoiesis by activin A, BMP2, and BMP4, members of the TGFbeta family
    • Maguer-Satta V., Bartholin L., Jeanpierre S., et al. Regulation of human erythropoiesis by activin A, BMP2, and BMP4, members of the TGFbeta family. Exp Cell Res 2003, 282:110-120.
    • (2003) Exp Cell Res , vol.282 , pp. 110-120
    • Maguer-Satta, V.1    Bartholin, L.2    Jeanpierre, S.3
  • 64
    • 1342309778 scopus 로고    scopus 로고
    • FLRG, member of the follistatin family, a new player in hematopoiesis
    • Maguer-Satta V., Rimokh R. FLRG, member of the follistatin family, a new player in hematopoiesis. Mol Cell Endocrinol 2004, 225:109-118.
    • (2004) Mol Cell Endocrinol , vol.225 , pp. 109-118
    • Maguer-Satta, V.1    Rimokh, R.2
  • 65
    • 0028970392 scopus 로고
    • Evidence for involvement of activin A and bone morphogenetic protein 4 in mammalian mesoderm and hematopoietic development
    • Johansson B.M., Wiles M.V. Evidence for involvement of activin A and bone morphogenetic protein 4 in mammalian mesoderm and hematopoietic development. Mol Cell Biol 1995, 15:141-151.
    • (1995) Mol Cell Biol , vol.15 , pp. 141-151
    • Johansson, B.M.1    Wiles, M.V.2
  • 66
    • 0035880235 scopus 로고    scopus 로고
    • Bone morphogenetic protein 4 induces efficient hematopoietic differentiation of rhesus monkey embryonic stem cells invitro
    • Li F., Lu S., Vida L., et al. Bone morphogenetic protein 4 induces efficient hematopoietic differentiation of rhesus monkey embryonic stem cells invitro. Blood 2001, 98:335-342.
    • (2001) Blood , vol.98 , pp. 335-342
    • Li, F.1    Lu, S.2    Vida, L.3
  • 67
    • 0024847874 scopus 로고
    • Invivo treatment with erythroid differentiation factor (EDF/activin A) increases erythroid precursors (CFU-E and BFU-E) in mice
    • Shiozaki M., Sakai R., Tabuchi M., et al. Invivo treatment with erythroid differentiation factor (EDF/activin A) increases erythroid precursors (CFU-E and BFU-E) in mice. Biochem Biophys Res Commun 1989, 165:1155-1161.
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 1155-1161
    • Shiozaki, M.1    Sakai, R.2    Tabuchi, M.3
  • 68
    • 0036304178 scopus 로고    scopus 로고
    • Inhibition of Smad5 in human hematopoietic progenitors blocks erythroid differentiation induced by BMP4
    • Fuchs O., Simakova O., Klener P., et al. Inhibition of Smad5 in human hematopoietic progenitors blocks erythroid differentiation induced by BMP4. Blood Cells Mol Dis 2002, 28:221-233.
    • (2002) Blood Cells Mol Dis , vol.28 , pp. 221-233
    • Fuchs, O.1    Simakova, O.2    Klener, P.3
  • 69
    • 34248335074 scopus 로고    scopus 로고
    • BMP4, SCF, and hypoxia cooperatively regulate the expansion of murine stress erythroid progenitors
    • Perry J.M., Harandi O.F., Paulson R.F. BMP4, SCF, and hypoxia cooperatively regulate the expansion of murine stress erythroid progenitors. Blood 2007, 109:4494-4502.
    • (2007) Blood , vol.109 , pp. 4494-4502
    • Perry, J.M.1    Harandi, O.F.2    Paulson, R.F.3
  • 70
    • 59649088676 scopus 로고    scopus 로고
    • Maintenance of the BMP4-dependent stress erythropoiesis pathway in the murine spleen requires hedgehog signaling
    • Perry J.M., Harandi O.F., Porayette P., et al. Maintenance of the BMP4-dependent stress erythropoiesis pathway in the murine spleen requires hedgehog signaling. Blood 2009, 113:911-918.
    • (2009) Blood , vol.113 , pp. 911-918
    • Perry, J.M.1    Harandi, O.F.2    Porayette, P.3
  • 71
    • 50449091974 scopus 로고    scopus 로고
    • Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin
    • Schneyer A.L., Sidis Y., Gulati A., et al. Differential antagonism of activin, myostatin and growth and differentiation factor 11 by wild-type and mutant follistatin. Endocrinology 2008, 149:4589-4595.
    • (2008) Endocrinology , vol.149 , pp. 4589-4595
    • Schneyer, A.L.1    Sidis, Y.2    Gulati, A.3
  • 72
    • 0035099687 scopus 로고    scopus 로고
    • Expression of FLRG, a novel activin A ligand, is regulated by TGF-beta and during hematopoiesis [corrected]
    • Maguer-Satta V., Bartholin L., Jeanpierre S., et al. Expression of FLRG, a novel activin A ligand, is regulated by TGF-beta and during hematopoiesis [corrected]. Exp Hematol 2001, 29:301-308.
    • (2001) Exp Hematol , vol.29 , pp. 301-308
    • Maguer-Satta, V.1    Bartholin, L.2    Jeanpierre, S.3
  • 73
    • 0030765945 scopus 로고    scopus 로고
    • Smad6 inhibits signalling by the TGF-beta superfamily
    • Imamura T., Takase M., Nishihara A., et al. Smad6 inhibits signalling by the TGF-beta superfamily. Nature 1997, 389:622-626.
    • (1997) Nature , vol.389 , pp. 622-626
    • Imamura, T.1    Takase, M.2    Nishihara, A.3
  • 74
    • 79551518231 scopus 로고    scopus 로고
    • Reduced SMAD7 leads to overactivation of TGF-beta signaling in MDS that can be reversed by a specific inhibitor of TGF-beta receptor I kinase
    • Zhou L., McMahon C., Bhagat T., et al. Reduced SMAD7 leads to overactivation of TGF-beta signaling in MDS that can be reversed by a specific inhibitor of TGF-beta receptor I kinase. Cancer Res 2011, 71:955-963.
    • (2011) Cancer Res , vol.71 , pp. 955-963
    • Zhou, L.1    McMahon, C.2    Bhagat, T.3
  • 75
    • 77956682613 scopus 로고    scopus 로고
    • Regulation of TGF-beta signalling by protein phosphatases
    • Liu T., Feng X.H. Regulation of TGF-beta signalling by protein phosphatases. Biochem J 2010, 430:191-198.
    • (2010) Biochem J , vol.430 , pp. 191-198
    • Liu, T.1    Feng, X.H.2
  • 76
    • 84896713290 scopus 로고    scopus 로고
    • RAP-011, a soluble activin receptor type IIa murine IgG-Fc fusion protein, prevents chemotherapy induced anemia
    • Available at:
    • Aaron W., Mulivor D.B., Kumar R., et al. RAP-011, a soluble activin receptor type IIa murine IgG-Fc fusion protein, prevents chemotherapy induced anemia. Blood 2009, Available at:. http://https://ash.confex.com/ash/2009/webprogram/Paper23536.html.
    • (2009) Blood
    • Aaron, W.1    Mulivor, D.B.2    Kumar, R.3
  • 77
    • 77957727888 scopus 로고    scopus 로고
    • Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction invivo
    • Chantry A.D., Heath D., Mulivor A.W., et al. Inhibiting activin-A signaling stimulates bone formation and prevents cancer-induced bone destruction invivo. JBone Miner Res 2010, 25:2633-2646.
    • (2010) JBone Miner Res , vol.25 , pp. 2633-2646
    • Chantry, A.D.1    Heath, D.2    Mulivor, A.W.3
  • 78
    • 71649091151 scopus 로고    scopus 로고
    • ACE-011, a soluble activin receptor type IIaIgG-Fc fusion protein, increases hemoglobin and hematocrit levels in postmenopausal healthy women
    • Available at:
    • Kim K.T., Borgstein N.G., Yang Y., et al. ACE-011, a soluble activin receptor type IIaIgG-Fc fusion protein, increases hemoglobin and hematocrit levels in postmenopausal healthy women. Blood 2008, Available at:. https://ash.confex.com/ash/2008/webprogram/Paper13363.html.
    • (2008) Blood
    • Kim, K.T.1    Borgstein, N.G.2    Yang, Y.3
  • 79
    • 65549147617 scopus 로고    scopus 로고
    • Single-dose, randomized, double-blind, placebo-controlled study of ACE-011 (ActRIIA-IgG1) in postmenopausal women
    • Ruckle J., Jacobs M., Kramer W., et al. Single-dose, randomized, double-blind, placebo-controlled study of ACE-011 (ActRIIA-IgG1) in postmenopausal women. JBone Miner Res 2009, 24:744-752.
    • (2009) JBone Miner Res , vol.24 , pp. 744-752
    • Ruckle, J.1    Jacobs, M.2    Kramer, W.3
  • 80
    • 84873505981 scopus 로고    scopus 로고
    • Stromal cell-mediated inhibition of erythropoiesis can be attenuated by sotatercept (ACE-011), an activin receptor type II ligand trap
    • Iancu-Rubin C., Mosoyan G., Wang J., et al. Stromal cell-mediated inhibition of erythropoiesis can be attenuated by sotatercept (ACE-011), an activin receptor type II ligand trap. Exp Hematol 2013, 41:155-166.e17.
    • (2013) Exp Hematol , vol.41
    • Iancu-Rubin, C.1    Mosoyan, G.2    Wang, J.3
  • 81
    • 84896729181 scopus 로고    scopus 로고
    • RAP-536 promotes terminal erythroid differentiation and reduces anemia in a murine model of myelodysplastic syndromes
    • 54th ASH Annual Meeting and Exposition. Atlanta, GA. December
    • Rajasekhar NV, Suragani RL, Sako D, etal. RAP-536 promotes terminal erythroid differentiation and reduces anemia in a murine model of myelodysplastic syndromes. In 54th ASH Annual Meeting and Exposition. Atlanta, GA. December 8-11, 2012.
    • (2012) , pp. 8-11
    • Rajasekhar, N.V.1    Suragani, R.L.2    Sako, D.3
  • 82
    • 22044450619 scopus 로고    scopus 로고
    • NUP98-HOXD13 transgenic mice develop a highly penetrant, severe myelodysplastic syndrome that progresses to acute leukemia
    • Lin Y.W., Slape C., Zhang Z., et al. NUP98-HOXD13 transgenic mice develop a highly penetrant, severe myelodysplastic syndrome that progresses to acute leukemia. Blood 2005, 106:287-295.
    • (2005) Blood , vol.106 , pp. 287-295
    • Lin, Y.W.1    Slape, C.2    Zhang, Z.3


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