메뉴 건너뛰기




Volumn 20, Issue 4, 2014, Pages 398-407

An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia

(21)  Dussiot, Michael a,b,c,d,e   Maciel, Thiago T a,b,c,d,e   Fricot, Aurélie a,b,c,d,e   Chartier, Céline a,b,c,d,e   Negre, Olivier f,g   Veiga, Joel d   Grapton, Damien a,b,c,d,e   Paubelle, Etienne a,b,c,d,e   Payen, Emmanuel f,g   Beuzard, Yves f,g   Leboulch, Philippe f,g   Ribeil, Jean Antoine a,b,c,d,h   Arlet, Jean Benoit a,b,c,d   Coté, Francine a,b,c,d   Courtois, Geneviève a,b,c,d   Ginzburg, Yelena Z i   Daniel, Thomas O j   Chopra, Rajesh j   Sung, Victoria k   Hermine, Olivier a,b,c,d,h   more..

a INSERM   (France)
c CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN RECEPTOR 2; CYTOKINE; FAS LIGAND; GROWTH DIFFERENTIATION FACTOR; GROWTH DIFFERENTIATION FACTOR 11; GROWTH FACTOR; HEMOGLOBIN ALPHA CHAIN; LIGAND; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84898049056     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.3468     Document Type: Article
Times cited : (243)

References (42)
  • 2
    • 64049099283 scopus 로고    scopus 로고
    • Chaperoning erythropoiesis
    • Weiss, M.J. & dos Santos, C.O. Chaperoning erythropoiesis. Blood 113, 2136-2144 (2009).
    • (2009) Blood , vol.113 , pp. 2136-2144
    • Weiss, M.J.1    Dos Santos, C.O.2
  • 3
    • 0037071860 scopus 로고    scopus 로고
    • An abundant erythroid protein that stabilizes free α-haemoglobin
    • Kihm, A.J. et al. An abundant erythroid protein that stabilizes free α-haemoglobin. Nature 417, 758-763 (2002).
    • (2002) Nature , vol.417 , pp. 758-763
    • Kihm, A.J.1
  • 4
    • 84876568733 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in β-thalassemia
    • Ribeil, J.A. et al. Ineffective erythropoiesis in β-thalassemia. ScientificWorldJournal 2013, 1-11 (2013).
    • (2013) ScientificWorldJournal , vol.2013 , pp. 1-11
    • Ribeil, J.A.1
  • 5
    • 0025239986 scopus 로고
    • The role of membrane skeletal-associated α-globin in the pathophysiology of β-thalassemia
    • Sorensen, S., Rubin, E., Polster, H., Mohandas, N. & Schrier, S. The role of membrane skeletal-associated α-globin in the pathophysiology of β-thalassemia. Blood 75, 1333-1336 (1990).
    • (1990) Blood , vol.75 , pp. 1333-1336
    • Sorensen, S.1    Rubin, E.2    Polster, H.3    Mohandas, N.4    Schrier, S.5
  • 6
    • 80054838641 scopus 로고    scopus 로고
    • β-thalassemia: A model for elucidating the dynamic regulation of ineffective erythropoiesis and iron metabolism
    • Ginzburg, Y. & Rivella, S. β-thalassemia: a model for elucidating the dynamic regulation of ineffective erythropoiesis and iron metabolism. Blood 118, 4321-4330 (2011).
    • (2011) Blood , vol.118 , pp. 4321-4330
    • Ginzburg, Y.1    Rivella, S.2
  • 7
    • 0033824309 scopus 로고    scopus 로고
    • Transforming growth factor inhibits erythropoiesis by blocking proliferation and accelerating differentiation of erythroid progenitors
    • Zermati, Y. et al. Transforming growth factor inhibits erythropoiesis by blocking proliferation and accelerating differentiation of erythroid progenitors. Exp. Hematol. 28, 885-894 (2000).
    • (2000) Exp. Hematol. , vol.28 , pp. 885-894
    • Zermati, Y.1
  • 8
    • 0037871588 scopus 로고    scopus 로고
    • Cytokines and BMP-4 promote hematopoietic differentiation of human embryonic stem cells
    • Chadwick, K. et al. Cytokines and BMP-4 promote hematopoietic differentiation of human embryonic stem cells. Blood 102, 906-915 (2003).
    • (2003) Blood , vol.102 , pp. 906-915
    • Chadwick, K.1
  • 9
    • 36849074704 scopus 로고    scopus 로고
    • An intronic sequence mutated in flexed-tail mice regulates splicing of Smad5
    • Hegde, S. et al. An intronic sequence mutated in flexed-tail mice regulates splicing of Smad5. Mamm. Genome 18, 852-860 (2007).
    • (2007) Mamm. Genome , vol.18 , pp. 852-860
    • Hegde, S.1
  • 10
    • 79955020013 scopus 로고    scopus 로고
    • Stress erythropoiesis: New signals and new stress progenitor cells
    • Paulson, R.F., Shi, L. & Wu, D.C. Stress erythropoiesis: new signals and new stress progenitor cells. Curr. Opin. Hematol. 18, 139-145 (2011).
    • (2011) Curr. Opin. Hematol. , vol.18 , pp. 139-145
    • Paulson, R.F.1    Shi, L.2    Wu, D.C.3
  • 11
    • 34948904750 scopus 로고    scopus 로고
    • High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
    • Tanno, T. et al. High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin. Nat. Med. 13, 1096-1101 (2007).
    • (2007) Nat. Med. , vol.13 , pp. 1096-1101
    • Tanno, T.1
  • 12
    • 0010259884 scopus 로고
    • Selective and indirect modulation of human multipotential and erythroid hematopoietic progenitor cell proliferation by recombinant human activin and inhibin
    • Broxmeyer, H.E. et al. Selective and indirect modulation of human multipotential and erythroid hematopoietic progenitor cell proliferation by recombinant human activin and inhibin. Proc. Natl. Acad. Sci. USA 85, 9052-9056 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9052-9056
    • Broxmeyer, H.E.1
  • 13
    • 0025936920 scopus 로고
    • Effects of erythroid differentiation factor (EDF) on proliferation and differentiation of human hematopoietic progenitors
    • Nakao, K., Kosaka, M. & Saito, S. Effects of erythroid differentiation factor (EDF) on proliferation and differentiation of human hematopoietic progenitors. Exp. Hematol. 19, 1090-1095 (1991).
    • (1991) Exp. Hematol. , vol.19 , pp. 1090-1095
    • Nakao, K.1    Kosaka, M.2    Saito, S.3
  • 14
    • 0027216054 scopus 로고
    • Activin A suppresses proliferation of interleukin-3-responsive granulocyte-macrophage colony-forming progenitors and stimulates proliferation and differentiation of interleukin-3-responsive erythroid burst-forming progenitors in the peripheral blood
    • Mizuguchi, T., Kosaka, M. & Saito, S. Activin A suppresses proliferation of interleukin-3-responsive granulocyte-macrophage colony-forming progenitors and stimulates proliferation and differentiation of interleukin-3-responsive erythroid burst-forming progenitors in the peripheral blood. Blood 81, 2891-2897 (1993).
    • (1993) Blood , vol.81 , pp. 2891-2897
    • Mizuguchi, T.1    Kosaka, M.2    Saito, S.3
  • 15
    • 0032567665 scopus 로고    scopus 로고
    • Activin A: A commitment factor in erythroid differentiation
    • Shiozaki, M., Kosaka, M. & Eto, Y. Activin A: a commitment factor in erythroid differentiation. Biochem. Biophys. Res. Commun. 242, 631-635 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 631-635
    • Shiozaki, M.1    Kosaka, M.2    Eto, Y.3
  • 16
    • 0023598057 scopus 로고
    • Importance of FSH-releasing protein and inhibin in erythrodifferentiation
    • Yu, J. et al. Importance of FSH-releasing protein and inhibin in erythrodifferentiation. Nature 330, 765-767 (1987).
    • (1987) Nature , vol.330 , pp. 765-767
    • Yu, J.1
  • 17
    • 65549147617 scopus 로고    scopus 로고
    • Single-dose, randomized, double-blind, placebo-controlled study of ACE-011 (ActRIIA-IgG1) in postmenopausal women
    • Ruckle, J. et al. Single-dose, randomized, double-blind, placebo-controlled study of ACE-011 (ActRIIA-IgG1) in postmenopausal women. J. Bone Miner. Res. 24, 744-752 (2009).
    • (2009) J. Bone Miner. Res. , vol.24 , pp. 744-752
    • Ruckle, J.1
  • 18
    • 0020564074 scopus 로고
    • A mouse model for β-thalassemia
    • Skow, L.C. et al. A mouse model for β-thalassemia. Cell 34, 1043-1052 (1983).
    • (1983) Cell , vol.34 , pp. 1043-1052
    • Skow, L.C.1
  • 19
    • 77955870192 scopus 로고    scopus 로고
    • Iron metabolism and ineffective erythropoiesis in β-thalassemia mouse models
    • Ramos, P. et al. Iron metabolism and ineffective erythropoiesis in β-thalassemia mouse models. Ann. NY Acad. Sci. 1202, 24-30 (2010).
    • (2010) Ann. NY Acad. Sci. , vol.1202 , pp. 24-30
    • Ramos, P.1
  • 20
    • 33745634866 scopus 로고    scopus 로고
    • Suppression of Fas-FasL coexpression by erythropoietin mediates erythroblast expansion during the erythropoietic stress response in vivo
    • Liu, Y. et al. Suppression of Fas-FasL coexpression by erythropoietin mediates erythroblast expansion during the erythropoietic stress response in vivo. Blood 108, 123-133 (2006).
    • (2006) Blood , vol.108 , pp. 123-133
    • Liu, Y.1
  • 21
    • 0034538786 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in β-thalassemia major is due to apoptosis at the polychromatophilic normoblast stage
    • Mathias, L.A. et al. Ineffective erythropoiesis in β-thalassemia major is due to apoptosis at the polychromatophilic normoblast stage. Exp. Hematol. 28, 1343-1353 (2000).
    • (2000) Exp. Hematol. , vol.28 , pp. 1343-1353
    • Mathias, L.A.1
  • 22
    • 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. 26 (suppl. 1), S12-S15 (2012).
    • (2012) Blood Rev. , vol.26 , Issue.SUPPL. 1
    • Rivella, S.1
  • 23
    • 77951494122 scopus 로고    scopus 로고
    • Growth differentiation factor 15 in erythroid health and disease
    • Tanno, T., Noel, P. & Miller, J.L. Growth differentiation factor 15 in erythroid health and disease. Curr. Opin. Hematol. 17, 184-190 (2010).
    • (2010) Curr. Opin. Hematol. , vol.17 , pp. 184-190
    • Tanno, T.1    Noel, P.2    Miller, J.L.3
  • 24
    • 84876817355 scopus 로고    scopus 로고
    • Beyond TGFβ: Roles of other TGFβ superfamily members in cancer
    • Wakefield, L.M. & Hill, C.S. Beyond TGFβ: roles of other TGFβ superfamily members in cancer. Nat. Rev. Cancer 13, 328-341 (2013).
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 328-341
    • Wakefield, L.M.1    Hill, C.S.2
  • 25
    • 0342684469 scopus 로고    scopus 로고
    • The dorsalizing and neural inducing gene follistatin is an antagonist of BMP-4
    • Fainsod, A. et al. The dorsalizing and neural inducing gene follistatin is an antagonist of BMP-4. Mech. Dev. 63, 39-50 (1997).
    • (1997) Mech. Dev. , vol.63 , pp. 39-50
    • Fainsod, A.1
  • 26
    • 0029616567 scopus 로고
    • Competition between noggin and bone morphogenetic protein 4 activities may regulate dorsalization during Xenopus development
    • Re'em-Kalma, Y., Lamb, T. & Frank, D. Competition between noggin and bone morphogenetic protein 4 activities may regulate dorsalization during Xenopus development. Proc. Natl. Acad. Sci. USA 92, 12141-12145 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12141-12145
    • Re'em-Kalma, Y.1    Lamb, T.2    Frank, D.3
  • 27
    • 81255135833 scopus 로고    scopus 로고
    • Polymeric IgA1 controls erythroblast proliferation and accelerates erythropoiesis recovery in anemia
    • Coulon, S. et al. Polymeric IgA1 controls erythroblast proliferation and accelerates erythropoiesis recovery in anemia. Nat. Med. 17, 1456-1465 (2011).
    • (2011) Nat. Med. , vol.17 , pp. 1456-1465
    • Coulon, S.1
  • 28
    • 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. et al. Stromal cell-mediated inhibition of erythropoiesis can be attenuated by sotatercept (ACE-011), an activin receptor type II ligand trap. Exp. Hematol. 41, 155-166 (2013).
    • (2013) Exp. Hematol. , vol.41 , pp. 155-166
    • Iancu-Rubin, C.1
  • 29
    • 34447121854 scopus 로고    scopus 로고
    • An erythroid chaperone that facilitates folding of α-globin subunits for hemoglobin synthesis
    • Yu, X. et al. An erythroid chaperone that facilitates folding of α-globin subunits for hemoglobin synthesis. J. Clin. Invest. 117, 1856-1865 (2007).
    • (2007) J. Clin. Invest. , vol.117 , pp. 1856-1865
    • Yu, X.1
  • 30
    • 34547699517 scopus 로고    scopus 로고
    • Foxo3 is required for the regulation of oxidative stress in erythropoiesis
    • Marinkovic, D. et al. Foxo3 is required for the regulation of oxidative stress in erythropoiesis. J. Clin. Invest. 117, 2133-2144 (2007).
    • (2007) J. Clin. Invest. , vol.117 , pp. 2133-2144
    • Marinkovic, D.1
  • 31
    • 84861886359 scopus 로고    scopus 로고
    • Heme-regulated eIF2α kinase activated Atf4 signaling pathway in oxidative stress and erythropoiesis
    • Suragani, R.N. et al. Heme-regulated eIF2α kinase activated Atf4 signaling pathway in oxidative stress and erythropoiesis. Blood 119, 5276-5284 (2012).
    • (2012) Blood , vol.119 , pp. 5276-5284
    • Suragani, R.N.1
  • 32
    • 0013974622 scopus 로고
    • Thalassemia: The consequences of unbalanced hemoglobin synthesis
    • Nathan, D.G. & Gunn, R.B. Thalassemia: the consequences of unbalanced hemoglobin synthesis. Am. J. Med. 41, 815-830 (1966).
    • (1966) Am. J. Med. , vol.41 , pp. 815-830
    • Nathan, D.G.1    Gunn, R.B.2
  • 33
    • 0036180342 scopus 로고    scopus 로고
    • Pathophysiology of thalassemia
    • Schrier, S.L. Pathophysiology of thalassemia. Curr. Opin. Hematol. 9, 123-126 (2002).
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 123-126
    • Schrier, S.L.1
  • 34
    • 85047690518 scopus 로고    scopus 로고
    • Loss of α-hemoglobin-stabilizing protein impairs erythropoiesis and exacerbates β-thalassemia
    • Kong, Y. et al. Loss of α-hemoglobin-stabilizing protein impairs erythropoiesis and exacerbates β-thalassemia. J. Clin. Invest. 114, 1457-1466 (2004).
    • (2004) J. Clin. Invest. , vol.114 , pp. 1457-1466
    • Kong, Y.1
  • 35
    • 33745511278 scopus 로고    scopus 로고
    • A road map toward defining the role of Smad signaling in hematopoietic stem cells
    • Utsugisawa, T. et al. A road map toward defining the role of Smad signaling in hematopoietic stem cells. Stem Cells 24, 1128-1136 (2006).
    • (2006) Stem Cells , vol.24 , pp. 1128-1136
    • Utsugisawa, T.1
  • 36
    • 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 109, 4494-4502 (2007).
    • (2007) Blood , vol.109 , pp. 4494-4502
    • Perry, J.M.1    Harandi, O.F.2    Paulson, R.F.3
  • 37
    • 34247129126 scopus 로고    scopus 로고
    • Molecular insights into stress erythropoiesis
    • Socolovsky, M. Molecular insights into stress erythropoiesis. Curr. Opin. Hematol. 14, 215-224 (2007).
    • (2007) Curr. Opin. Hematol. , vol.14 , pp. 215-224
    • Socolovsky, M.1
  • 38
    • 0033619265 scopus 로고    scopus 로고
    • Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1
    • De Maria, R. et al. Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1. Nature 401, 489-493 (1999).
    • (1999) Nature , vol.401 , pp. 489-493
    • De Maria, R.1
  • 39
    • 0034099058 scopus 로고    scopus 로고
    • Dyserythropoiesis associated with a Fas-deficient condition in childhood
    • Bader-Meunier, B. et al. Dyserythropoiesis associated with a Fas-deficient condition in childhood. Br. J. Haematol. 108, 300-304 (2000).
    • (2000) Br. J. Haematol. , vol.108 , pp. 300-304
    • Bader-Meunier, B.1
  • 40
    • 0037033433 scopus 로고    scopus 로고
    • Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: Selective regulation of mitogen-activated protein kinase activation and Fas ligand expression
    • Devadas, S., Zaritskaya, L., Rhee, S.G., Oberley, L. & Williams, M.S. Discrete generation of superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and Fas ligand expression. J. Exp. Med. 195, 59-70 (2002).
    • (2002) J. Exp. Med. , vol.195 , pp. 59-70
    • Devadas, S.1    Zaritskaya, L.2    Rhee, S.G.3    Oberley, L.4    Williams, M.S.5
  • 41
    • 0035377208 scopus 로고    scopus 로고
    • Establishment of normal, terminally differentiating mouse erythroid progenitors: Molecular characterization by cDNA arrays
    • Dolznig, H. et al. Establishment of normal, terminally differentiating mouse erythroid progenitors: molecular characterization by cDNA arrays. FASEB J. 15, 1442-1444 (2001).
    • (2001) FASEB J. , vol.15 , pp. 1442-1444
    • Dolznig, H.1
  • 42
    • 84861816666 scopus 로고    scopus 로고
    • Integrated protein quality-control pathways regulate free α-globin in murine β-thalassemia
    • Khandros, E., Thom, C.S., D'Souza, J. & Weiss, M.J. Integrated protein quality-control pathways regulate free α-globin in murine β-thalassemia. Blood 119, 5265-5275 (2012).
    • (2012) Blood , vol.119 , pp. 5265-5275
    • Khandros, E.1    Thom, C.S.2    D'souza, J.3    Weiss, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.