메뉴 건너뛰기




Volumn 514, Issue 7521, 2014, Pages 242-246

HSP70 sequestration by free α-globin promotes ineffective erythropoiesis in β-thalassaemia

(24)  Arlet, Jean Benoît a,b,c,d   Ribeil, Jean Antoine a,c,d,e   Guillem, Flavia a,c,d   Negre, Olivier f   Hazoume, Adonis g,h   Marcion, Guillaume g,h   Beuzard, Yves f   Dussiot, Michaël a,c,d,i   Moura, Ivan Cruz a,c,d,i,j   Demarest, Samuel a   De Beauchêne, Isaure Chauvot a,k   Belaid Choucair, Zakia a,c,d   Sevin, Margaux g,h   Maciel, Thiago Trovati a,c,d,i,j   Auclair, Christian a,k   Leboulch, Philippe f,l   Chretien, Stany f   Tchertanov, Luba a,k   Baudin Creuza, Véronique g   Seigneuric, Renaud h   more..

a CNRS   (France)
g INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; GATA1 PROTEIN, HUMAN; HEAT SHOCK PROTEIN 70; HEMOGLOBIN ALPHA CHAIN; TRANSCRIPTION FACTOR GATA 1;

EID: 84908377214     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13614     Document Type: Article
Times cited : (112)

References (31)
  • 1
    • 78249279351 scopus 로고    scopus 로고
    • Protein quality control during erythropoiesis and hemoglobin synthesis
    • Khandros, E. & Weiss, M. J. Protein quality control during erythropoiesis and hemoglobin synthesis. Hematol. Oncol. Clin. North Am. 24, 1071-1088 (2010).
    • (2010) Hematol. Oncol. Clin. North Am. , vol.24 , pp. 1071-1088
    • Khandros, E.1    Weiss, M.J.2
  • 2
    • 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
  • 3
    • 0027181636 scopus 로고
    • Accelerated programmed cell death (apoptosis) in erythroid precursors of patients with severe β-thalassemia (Cooley's anemia)
    • Yuan, J. et al. Accelerated programmed cell death (apoptosis) in erythroid precursors of patients with severe β-thalassemia (Cooley's anemia). Blood 82, 374-377 (1993).
    • (1993) Blood , vol.82 , pp. 374-377
    • Yuan, J.1
  • 4
    • 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
  • 5
    • 0034669951 scopus 로고    scopus 로고
    • The importance of erythroid expansion in determining the extent of apoptosis in erythroid precursors in patients with β-thalassemia major
    • Centis, F. et al. The importance of erythroid expansion in determining the extent of apoptosis in erythroid precursors in patients with β-thalassemia major. Blood 96, 3624-3629 (2000).
    • (2000) Blood , vol.96 , pp. 3624-3629
    • Centis, F.1
  • 6
    • 84876568733 scopus 로고    scopus 로고
    • Ineffective erythropoiesis in β-thalassemia
    • Ribeil, J. A. et al. Ineffective erythropoiesis in β-thalassemia. ScientificWorldJournal 2013, 394295 (2013).
    • (2013) ScientificWorldJournal , vol.2013 , pp. 394295
    • Ribeil, J.A.1
  • 7
    • 0035862331 scopus 로고    scopus 로고
    • Caspase activation is required for terminal erythroid differentiation
    • Zermati, Y. et al. Caspase activation is required for terminal erythroid differentiation. J. Exp. Med. 193, 247-254 (2001).
    • (2001) J. Exp. Med. , vol.193 , pp. 247-254
    • Zermati, Y.1
  • 8
    • 33846087085 scopus 로고    scopus 로고
    • Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1
    • Ribeil, J.-A. et al. Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445, 102-105 (2007).
    • (2007) Nature , vol.445 , pp. 102-105
    • Ribeil, J.-A.1
  • 9
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A. & Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332 (2011).
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 10
    • 84879142151 scopus 로고    scopus 로고
    • Isolation and functional characterization of human erythroblasts at distinct stages: Implications for understanding of normal and disordered erythropoiesis in vivo
    • Hu, J. et al. Isolation and functional characterization of human erythroblasts at distinct stages: implications for understanding of normal and disordered erythropoiesis in vivo. Blood 121, 3246-3253 (2013).
    • (2013) Blood , vol.121 , pp. 3246-3253
    • Hu, J.1
  • 11
    • 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
  • 12
    • 84856920241 scopus 로고    scopus 로고
    • Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes
    • Frisan, E. et al. Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes. Blood 119, 1532-1542 (2012).
    • (2012) Blood , vol.119 , pp. 1532-1542
    • Frisan, E.1
  • 13
    • 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
  • 14
    • 0023275919 scopus 로고
    • Fetal hemoglobin-containing cells have the same mean corpuscular hemoglobin as cells without fetal hemoglobin: A reciprocal relationship between gamma- and beta-globin gene expression in normal subjects and in those with high fetal hemoglobin production
    • Dover, G. J. & Boyer, S. H. Fetal hemoglobin-containing cells have the same mean corpuscular hemoglobin as cells without fetal hemoglobin: a reciprocal relationship between gamma- and beta-globin gene expression in normal subjects and in those with high fetal hemoglobin production. Blood 69, 1109-1113 (1987).
    • (1987) Blood , vol.69 , pp. 1109-1113
    • Dover, G.J.1    Boyer, S.H.2
  • 15
    • 67650088333 scopus 로고    scopus 로고
    • Role of STAT3 and GATA-1 interactions in gamma-globin gene expression
    • Yao, X. et al. Role of STAT3 and GATA-1 interactions in gamma-globin gene expression. Exp. Hematol. 37, 889-900 (2009).
    • (2009) Exp. Hematol. , vol.37 , pp. 889-900
    • Yao, X.1
  • 16
    • 80052429874 scopus 로고    scopus 로고
    • The distinctive roles of erythroid specific activator GATA-1 and NF-E2 in transcription of the human fetal γ-globin genes
    • Woon Kim, Y., Kim, S., Geun Kim, C. & Kim, A. The distinctive roles of erythroid specific activator GATA-1 and NF-E2 in transcription of the human fetal γ-globin genes. Nucleic Acids Res. 39, 6944-6955 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6944-6955
    • Woon Kim, Y.1    Kim, S.2    Geun Kim, C.3    Kim, A.4
  • 17
    • 79953076380 scopus 로고    scopus 로고
    • Recombinant erythroid Kruppel-like factor fused to GATA1 up-regulates δ- and γ-globin expression in erythroid cells
    • Zhu, J. et al. Recombinant erythroid Kruppel-like factor fused to GATA1 up-regulates δ- and γ-globin expression in erythroid cells. Blood 117, 3045-3052 (2011).
    • (2011) Blood , vol.117 , pp. 3045-3052
    • Zhu, J.1
  • 19
    • 50949133924 scopus 로고    scopus 로고
    • Decreased differentiation of erythroid cells exacerbates ineffective erythropoiesis in beta-thalassemia
    • Libani, I. V. et al. Decreased differentiation of erythroid cells exacerbates ineffective erythropoiesis in beta-thalassemia. Blood 112, 875-885 (2008).
    • (2008) Blood , vol.112 , pp. 875-885
    • Libani, I.V.1
  • 20
    • 84878439561 scopus 로고    scopus 로고
    • Macrophages support pathological erythropoiesis in polycythemia vera and β-thalassemia
    • Ramos, P. et al. Macrophages support pathological erythropoiesis in polycythemia vera and β-thalassemia. Nature Med. 19, 437-445 (2013).
    • (2013) Nature Med. , vol.19 , pp. 437-445
    • Ramos, P.1
  • 21
    • 84898049056 scopus 로고    scopus 로고
    • An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia
    • Dussiot, M. et al. An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia. Nature Med. 20, 398-407 (2014).
    • (2014) Nature Med. , vol.20 , pp. 398-407
    • Dussiot, M.1
  • 22
    • 84902668877 scopus 로고    scopus 로고
    • Modified activin receptor IIB ligand trap mitigates ineffective erythropoiesis and disease complications in murine β-thalassemia
    • 19 June
    • Suragani, R. N. V. S. et al. Modified activin receptor IIB ligand trap mitigates ineffective erythropoiesis and disease complications in murine β-thalassemia. Blood http://dx.doi.org/10.1182/blood-2013-06-511238 (19 June 2014).
    • (2014) Blood
    • Suragani, R.N.V.S.1
  • 23
    • 36348943529 scopus 로고    scopus 로고
    • K-CL co-transport plays an important role in normal and beta thalassemic erythropoiesis
    • De Franceschi, L. et al. K-CL co-transport plays an important role in normal and beta thalassemic erythropoiesis. Haematologica 92, 1319-1326 (2007).
    • (2007) Haematologica , vol.92 , pp. 1319-1326
    • De Franceschi, L.1
  • 24
    • 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
  • 25
    • 79952624787 scopus 로고    scopus 로고
    • Caspase-activated ROCK-1 allows erythroblast terminal maturation independently of cytokine-induced Rho signaling
    • Gabet, A.-S. et al. Caspase-activated ROCK-1 allows erythroblast terminal maturation independently of cytokine-induced Rho signaling. Cell Death Differ. 18, 678-689 (2011).
    • (2011) Cell Death Differ. , vol.18 , pp. 678-689
    • Gabet, A.-S.1
  • 26
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S. & Cordelières, F. P. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224, 213-232 (2006).
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 27
    • 33947386148 scopus 로고    scopus 로고
    • Sensitive protein detection via triple-binder proximity ligation assays
    • Schallmeiner, E. et al. Sensitive protein detection via triple-binder proximity ligation assays. Nature Methods 4, 135-137 (2007).
    • (2007) Nature Methods , vol.4 , pp. 135-137
    • Schallmeiner, E.1
  • 28
    • 84885334945 scopus 로고    scopus 로고
    • Dynamics of α-Hb chain binding to its chaperone AHSP depends on heme coordination and redox state
    • Kiger, L. et al. Dynamics of α-Hb chain binding to its chaperone AHSP depends on heme coordination and redox state. Biochim. Biophys. Acta 1840, 277-287 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 277-287
    • Kiger, L.1
  • 29
    • 0017206985 scopus 로고
    • Separation of human hemoglobins by DEAE-cellulose chromatography using glycine-KCN-NaC1 developers
    • Abraham, E. C., Reese, A., Stallings, M. & Huisman, T. H. Separation of human hemoglobins by DEAE-cellulose chromatography using glycine-KCN-NaC1 developers. Hemoglobin 1, 27-44 (1976).
    • (1976) Hemoglobin , vol.1 , pp. 27-44
    • Abraham, E.C.1    Reese, A.2    Stallings, M.3    Huisman, T.H.4
  • 30
    • 0001720527 scopus 로고
    • A new method for the preparation of alpha and beta subunits of human hemoglobin
    • Bucci, E. & Fronticelli, C. A new method for the preparation of alpha and beta subunits of human hemoglobin. J. Biol. Chem. 240, 551-552 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 551-552
    • Bucci, E.1    Fronticelli, C.2
  • 31
    • 84938024925 scopus 로고
    • Protein coagulation andits reversal: The preparation of insoluble globin, soluble globin and heme
    • Anson, M. L. & Mirsky, A. E. Protein coagulation andits reversal: the preparation of insoluble globin, soluble globin and heme. J. Gen. Physiol. 13, 469-476 (1930).
    • (1930) J. Gen. Physiol. , vol.13 , pp. 469-476
    • Anson, M.L.1    Mirsky, A.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.