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Volumn 95, Issue 11, 2000, Pages 3371-3379

Smad7 selectively interferes with different pathways of activin signaling and inhibits erythroid leukemia cell differentiation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVIN; ACTIVIN RECEPTOR; PROTEIN SERINE THREONINE KINASE; RNA; TRANSFORMING GROWTH FACTOR BETA;

EID: 0034210252     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.11.3371     Document Type: Article
Times cited : (23)

References (92)
  • 1
    • 0028170237 scopus 로고
    • TGF-β related genes in development
    • Wall NA, Hogan BL. TGF-β related genes in development. Curr Opin Genet Dev. 1994;4:517-522.
    • (1994) Curr Opin Genet Dev. , vol.4 , pp. 517-522
    • Wall, N.A.1    Hogan, B.L.2
  • 3
    • 0028893294 scopus 로고
    • Genetic screens to identify elements of the decapenlaplegic signaling pathway in Drosophila
    • Raftery LA, Twombly V, Wharton K, Gelbart WM. Genetic screens to identify elements of the decapenlaplegic signaling pathway in Drosophila. Genetics. 1995;139:241-254.
    • (1995) Genetics , vol.139 , pp. 241-254
    • Raftery, L.A.1    Twombly, V.2    Wharton, K.3    Gelbart, W.M.4
  • 4
    • 0028940853 scopus 로고
    • Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster
    • Sekelsky JJ, Newfeld SJ, Raftery LA, Chartoff EH, Gelbart WM. Genetic characterization and cloning of mothers against dpp, a gene required for decapentaplegic function in Drosophila melanogaster. Genetics. 1995;139:1347-1358.
    • (1995) Genetics , vol.139 , pp. 1347-1358
    • Sekelsky, J.J.1    Newfeld, S.J.2    Raftery, L.A.3    Chartoff, E.H.4    Gelbart, W.M.5
  • 5
    • 0031438047 scopus 로고    scopus 로고
    • TGF-β signalling from cell membrane to nucleus through SMAD proteins
    • Heldin CH, Miyazono K, ten Dijke P. TGF-β signalling from cell membrane to nucleus through SMAD proteins. Nature. 1997;390:465-471.
    • (1997) Nature , vol.390 , pp. 465-471
    • Heldin, C.H.1    Miyazono, K.2    Ten Dijke, P.3
  • 6
    • 0031685620 scopus 로고    scopus 로고
    • TGF-β signal transduction
    • Massagué J. TGF-β signal transduction. Annu Rev Biochem. 1998;67:753-791.
    • (1998) Annu Rev Biochem. , vol.67 , pp. 753-791
    • Massagué, J.1
  • 7
    • 0030013242 scopus 로고    scopus 로고
    • Serine phosphorylation, chromosomal localization, and transforming growth factor-β signal transduction by human bsp-1
    • Lechleider RJ, de Caestecker MP, Dehejia A, Polymeropoulos MH, Roberts AB. Serine phosphorylation, chromosomal localization, and transforming growth factor-β signal transduction by human bsp-1. J Biol Chem. 1996;271:17,617-17,620.
    • (1996) J Biol Chem. , vol.271 , pp. 17617-17620
    • Lechleider, R.J.1    De Caestecker, M.P.2    Dehejia, A.3    Polymeropoulos, M.H.4    Roberts, A.B.5
  • 8
    • 0029833909 scopus 로고    scopus 로고
    • Mammalian dwarfins are phosphorylated in response to transforming growth factor β and are implicated in control of cell growth
    • Yingling JM, Das P, Savage C, Zhang M, Padgett RW, Wang XF. Mammalian dwarfins are phosphorylated in response to transforming growth factor β and are implicated in control of cell growth. Proc Natl Acad Sci U S A. 1996;93:8940-8944.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8940-8944
    • Yingling, J.M.1    Das, P.2    Savage, C.3    Zhang, M.4    Padgett, R.W.5    Wang, X.F.6
  • 9
    • 0029940972 scopus 로고    scopus 로고
    • Xenopus mad proteins transduce distinct subsets of signals for the TGF-β superfamily
    • Graff JM, Bansal A, Melton DA. Xenopus Mad proteins transduce distinct subsets of signals for the TGF-β superfamily. Cell. 1996;85:479-487.
    • (1996) Cell , vol.85 , pp. 479-487
    • Graff, J.M.1    Bansal, A.2    Melton, D.A.3
  • 10
    • 0029829230 scopus 로고    scopus 로고
    • A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway
    • Baker JC, Harland RM. A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway. Genes Dev. 1996;10:1880-1889.
    • (1996) Genes Dev. , vol.10 , pp. 1880-1889
    • Baker, J.C.1    Harland, R.M.2
  • 11
    • 0029834231 scopus 로고    scopus 로고
    • Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor
    • Thomsen GH. Xenopus mothers against decapentaplegic is an embryonic ventralizing agent that acts downstream of the BMP-2/4 receptor. Development. 1996;122:2359-2366.
    • (1996) Development. , vol.122 , pp. 2359-2366
    • Thomsen, G.H.1
  • 12
    • 0030593038 scopus 로고    scopus 로고
    • DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1
    • Hahn SA, Schutte M, Hoque AT, et al. DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1. Science. 1996;271:350-353.
    • (1996) Science , vol.271 , pp. 350-353
    • Hahn, S.A.1    Schutte, M.2    Hoque, A.T.3
  • 13
    • 0032521421 scopus 로고    scopus 로고
    • The Smad5 gene is involved in the intracellular signaling pathways that mediate the inhibitory effects of transforming growth factor-β on human hematopoiesis
    • Bruno E, Horrigan SK, Van Den Berg D, et al. The Smad5 gene is involved in the intracellular signaling pathways that mediate the inhibitory effects of transforming growth factor-β on human hematopoiesis. Blood. 1998;91:1917-1923.
    • (1998) Blood , vol.91 , pp. 1917-1923
    • Bruno, E.1    Horrigan, S.K.2    Van Den Berg, D.3
  • 14
    • 0030765945 scopus 로고    scopus 로고
    • Smad6 inhibits signalling by the TGF-β superfamily
    • Imamura T, Takase M, Nishihara A, et al. Smad6 inhibits signalling by the TGF-β superfamily. Nature. 1997;389:622-626.
    • (1997) Nature , vol.389 , pp. 622-626
    • Imamura, T.1    Takase, M.2    Nishihara, A.3
  • 15
    • 0031964859 scopus 로고    scopus 로고
    • Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor
    • Hata A, Lagna G, Massagué J, Hemmati-Brivanlou A. Smad6 inhibits BMP/Smad1 signaling by specifically competing with the Smad4 tumor suppressor. Genes Dev. 1998;12:186-197.
    • (1998) Genes Dev. , vol.12 , pp. 186-197
    • Hata, A.1    Lagna, G.2    Massagué, J.3    Hemmati-Brivanlou, A.4
  • 16
    • 0031587828 scopus 로고    scopus 로고
    • The MAD-related protein Smad7 associates with the TGF-β receptor and functions as an antagonist of TGF-β signaling
    • Hayashi H, Abdollah S, Qiu Y, et al. The MAD-related protein Smad7 associates with the TGF-β receptor and functions as an antagonist of TGF-β signaling. Cell. 1997;89:1165-1173.
    • (1997) Cell , vol.89 , pp. 1165-1173
    • Hayashi, H.1    Abdollah, S.2    Qiu, Y.3
  • 17
    • 0030611757 scopus 로고    scopus 로고
    • Identification of Smad7, a TGF-β-inducible antagonist of TGF-β signalling
    • Nakao A, Afrakhte M, Morén A, et al. Identification of Smad7, a TGF-β-inducible antagonist of TGF-β signalling. Nature. 1997;389:631-635.
    • (1997) Nature , vol.389 , pp. 631-635
    • Nakao, A.1    Afrakhte, M.2    Morén, A.3
  • 18
    • 0031939483 scopus 로고    scopus 로고
    • Xenopus Smad8 acts downstream of BMP-4 to modulate its activity during vertebrate embryonic patterning
    • Nakayama T, Snyder MA, Grewal SS, Tsuneizumi K, Tabata T, Christian JL. Xenopus Smad8 acts downstream of BMP-4 to modulate its activity during vertebrate embryonic patterning. Development. 1998;125:857-867.
    • (1998) Development , vol.125 , pp. 857-867
    • Nakayama, T.1    Snyder, M.A.2    Grewal, S.S.3    Tsuneizumi, K.4    Tabata, T.5    Christian, J.L.6
  • 19
    • 0032101098 scopus 로고    scopus 로고
    • Xenopus Smad7 inhibits both the activin and BMP pathways and acts as a neural inducer
    • Casellas R, Brivanlou AH. Xenopus Smad7 inhibits both the activin and BMP pathways and acts as a neural inducer. Dev Biol. 1998;198:1-12.
    • (1998) Dev Biol. , vol.198 , pp. 1-12
    • Casellas, R.1    Brivanlou, A.H.2
  • 20
    • 0032529532 scopus 로고    scopus 로고
    • Smad7 inhibits mesoderm formation and promotes neural cell fate in Xenopus embryos
    • Bhushan A, Chen Y, Vale W. Smad7 inhibits mesoderm formation and promotes neural cell fate in Xenopus embryos. Dev Biol. 1998;200:260-268.
    • (1998) Dev Biol. , vol.200 , pp. 260-268
    • Bhushan, A.1    Chen, Y.2    Vale, W.3
  • 21
    • 0022907945 scopus 로고
    • Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid
    • Vale W, Rivier J, Vaughan J, et al. Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid. Nature. 1986; 321:776-779.
    • (1986) Nature , vol.321 , pp. 776-779
    • Vale, W.1    Rivier, J.2    Vaughan, J.3
  • 22
    • 0022470831 scopus 로고
    • Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin
    • Ling N, Ying SY, Ueno N, et al. Pituitary FSH is released by a heterodimer of the β-subunits from the two forms of inhibin. Nature. 1986;321:779-782.
    • (1986) Nature , vol.321 , pp. 779-782
    • Ling, N.1    Ying, S.Y.2    Ueno, N.3
  • 23
    • 0000775642 scopus 로고
    • The inhibin/activin family of hormones and growth factors
    • Sporn MB, Roberts AB, eds. Berlin, Germany: Springer-Verlag
    • Vale W, Hsueh A, River C, Yu J. The inhibin/activin family of hormones and growth factors. In: Sporn MB, Roberts AB, eds. Peptide Growth Factors and their Receptors. Part II. Berlin, Germany: Springer-Verlag; 1990:211-248.
    • (1990) Peptide Growth Factors and their Receptors. , Issue.PART II , pp. 211-248
    • Vale, W.1    Hsueh, A.2    River, C.3    Yu, J.4
  • 25
    • 0027380203 scopus 로고
    • Mesoderm-inducing factors in early vertebrate development
    • Smith JC. Mesoderm-inducing factors in early vertebrate development. EMBO J. 1993;12:4463-4470.
    • (1993) EMBO J. , vol.12 , pp. 4463-4470
    • Smith, J.C.1
  • 27
    • 0023106040 scopus 로고
    • Purification and characterization of erythroid differentiation factor (EDF) isolated from human leukemia cell line THP-1
    • Eto Y, Tsuji T, Takezawa M, Takano S, Yokogawa Y, Shibai H. Purification and characterization of erythroid differentiation factor (EDF) isolated from human leukemia cell line THP-1. Biochem Biophys Res Commun. 1987;142:1095-1103.
    • (1987) Biochem Biophys Res Commun. , vol.142 , pp. 1095-1103
    • Eto, Y.1    Tsuji, T.2    Takezawa, M.3    Takano, S.4    Yokogawa, Y.5    Shibai, H.6
  • 28
    • 0023598057 scopus 로고
    • Importance of FSH-releasing protein and inhibin in erythrodifferentiation
    • Yu J, Shao LE, Lemas V, et al. Importance of FSH-releasing protein and inhibin in erythrodifferentiation. Nature. 1987;330:765-767.
    • (1987) Nature , vol.330 , pp. 765-767
    • Yu, J.1    Shao, L.E.2    Lemas, V.3
  • 30
    • 0031018483 scopus 로고    scopus 로고
    • Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation
    • Lebrun JJ, Vale WW. Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation. Mol Cell Biol. 1997;17:1682-1691.
    • (1997) Mol Cell Biol. , vol.17 , pp. 1682-1691
    • Lebrun, J.J.1    Vale, W.W.2
  • 31
    • 0027525105 scopus 로고
    • Identification of human activin and TGF-β type I receptors that form heteromeric kinase complexes with type II receptors
    • Attisano L, Cárcamo J, Ventura F, Weis FM, Massagué J, Wrana JL. Identification of human activin and TGF-β type I receptors that form heteromeric kinase complexes with type II receptors. Cell. 1993;75:671-680.
    • (1993) Cell , vol.75 , pp. 671-680
    • Attisano, L.1    Cárcamo, J.2    Ventura, F.3    Weis, F.M.4    Massagué, J.5    Wrana, J.L.6
  • 32
    • 0027483939 scopus 로고
    • Cloning and characterization of a transmembrane serine kinase that acts as an activin type I receptor
    • Tsuchida K, Mathews LS, Vale WW. Cloning and characterization of a transmembrane serine kinase that acts as an activin type I receptor. Proc Natl Acad Sci U S A. 1993;90:11,242-11,246.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11242-11246
    • Tsuchida, K.1    Mathews, L.S.2    Vale, W.W.3
  • 33
    • 0028359376 scopus 로고
    • Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor β and activin
    • Cárcamo J, Weis FM, Ventura F, et al. Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor β and activin. Mol Cell Biol. 1994;14:3810-3821.
    • (1994) Mol Cell Biol. , vol.14 , pp. 3810-3821
    • Cárcamo, J.1    Weis, F.M.2    Ventura, F.3
  • 34
    • 0027739933 scopus 로고
    • Determination of type I and specificity by the type II receptors for TGF-β or activin
    • Ebner R, Chen RH, Lawler S, Zioncheck T, Derynck R. Determination of type I and specificity by the type II receptors for TGF-β or activin. Science. 1993;262:900-902.
    • (1993) Science. , vol.262 , pp. 900-902
    • Ebner, R.1    Chen, R.H.2    Lawler, S.3    Zioncheck, T.4    Derynck, R.5
  • 35
    • 0027328191 scopus 로고
    • Activin receptor-like kinases: A novel subclass of cell surface receptors with predicted serine/threonine kinase activity
    • ten Dijke P, Ichijo H, Franzén P, et al. Activin receptor-like kinases: a novel subclass of cell surface receptors with predicted serine/threonine kinase activity. Oncogene. 1993;8:2879-2887.
    • (1993) Oncogene , vol.8 , pp. 2879-2887
    • Ten Dijke, P.1    Ichijo, H.2    Franzén, P.3
  • 36
    • 0028295762 scopus 로고
    • Characterization of type I receptors for transforming growth factor-β and activin
    • ten Dijke P, Yamashita H, Ichijo H, et al. Characterization of type I receptors for transforming growth factor-β and activin. Science. 1994;264: 101-104.
    • (1994) Science , vol.264 , pp. 101-104
    • Ten Dijke, P.1    Yamashita, H.2    Ichijo, H.3
  • 37
    • 0025905181 scopus 로고
    • Expression cloning of an activin receptor, a predicted transmembrane serine kinase
    • Mathews LS, Vale WW. Expression cloning of an activin receptor, a predicted transmembrane serine kinase. Cell. 1991;65:973-982.
    • (1991) Cell , vol.65 , pp. 973-982
    • Mathews, L.S.1    Vale, W.W.2
  • 38
    • 0026527384 scopus 로고
    • Novel activin receptors: Distinct genes and alternative mRNA splicing generate a repertoire of serine/threonine kinase receptors
    • Attisano L, Wrana JL, Cheifetz S, Massagué J. Novel activin receptors: distinct genes and alternative mRNA splicing generate a repertoire of serine/threonine kinase receptors. Cell. 1992;68: 97-108.
    • (1992) Cell , vol.68 , pp. 97-108
    • Attisano, L.1    Wrana, J.L.2    Cheifetz, S.3    Massagué, J.4
  • 39
    • 0026529503 scopus 로고
    • Cloning of a second type of activin receptor and functional characterization in Xenopus embryos
    • Mathews LS, Vale WW, Kintner CR. Cloning of a second type of activin receptor and functional characterization in Xenopus embryos. Science. 1992;255:1702-1705.
    • (1992) Science , vol.255 , pp. 1702-1705
    • Mathews, L.S.1    Vale, W.W.2    Kintner, C.R.3
  • 40
    • 0029003377 scopus 로고
    • Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects
    • Yamashita H, ten Dijke P, Huylebroeck D, et al. Osteogenic protein-1 binds to activin type II receptors and induces certain activin-like effects. J Cell Biol. 1995;130:217-226.
    • (1995) J Cell Biol. , vol.130 , pp. 217-226
    • Yamashita, H.1    Ten Dijke, P.2    Huylebroeck, D.3
  • 41
    • 0030785446 scopus 로고    scopus 로고
    • The ALK-2 and ALK-4 activin receptors transduce distinct mesoderm-inducing signals during early xenopus development but do not co-operate to establish thresholds
    • Armes NA, Smith JC. The ALK-2 and ALK-4 activin receptors transduce distinct mesoderm-inducing signals during early Xenopus development but do not co-operate to establish thresholds. Development. 1997;124:3797-3804.
    • (1997) Development , vol.124 , pp. 3797-3804
    • Armes, N.A.1    Smith, J.C.2
  • 42
    • 0016166975 scopus 로고
    • Epithelial cell cultures from normal glandular tissue of mice
    • Owens RB, Smith HS, Hackett AJ. Epithelial cell cultures from normal glandular tissue of mice. J Natl Cancer Inst. 1974;53:261-269.
    • (1974) J Natl Cancer Inst. , vol.53 , pp. 261-269
    • Owens, R.B.1    Smith, H.S.2    Hackett, A.J.3
  • 43
    • 0024003645 scopus 로고
    • B cell ontogeny in murine embryo studied by a culture system with the monolayer of a stromal cell clone, ST2: B cell progenitor develops first in the embryonal body rather than in the yolk sac
    • Ogawa M, Nishikawa S, Ikuta K, et al. B cell ontogeny in murine embryo studied by a culture system with the monolayer of a stromal cell clone, ST2: B cell progenitor develops first in the embryonal body rather than in the yolk sac. EMBO J. 1988;7:1337-1343.
    • (1988) EMBO J. , vol.7 , pp. 1337-1343
    • Ogawa, M.1    Nishikawa, S.2    Ikuta, K.3
  • 44
    • 0027219671 scopus 로고
    • Cloning of a type I TGF-β receptor and its effect on TGF-β binding to the type II receptor
    • Ebner R, Chen RH, Shum L, et al. Cloning of a type I TGF-β receptor and its effect on TGF-β binding to the type II receptor. Science. 1993;260: 1344-1348.
    • (1993) Science , vol.260 , pp. 1344-1348
    • Ebner, R.1    Chen, R.H.2    Shum, L.3
  • 45
    • 0029087923 scopus 로고
    • Expression of type I and type IB receptors for activin in midgestation mouse embryos suggests distinct functions in organogeresis
    • Verschueren K, Dewulf N, Goumans MJ, et al. Expression of type I and type IB receptors for activin in midgestation mouse embryos suggests distinct functions in organogeresis. Mech Dev. 1995;52:109-123.
    • (1995) Mech Dev. , vol.52 , pp. 109-123
    • Verschueren, K.1    Dewulf, N.2    Goumans, M.J.3
  • 46
    • 0028787249 scopus 로고
    • The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki K, Sagata N. The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J. 1995;14:5048-5059.
    • (1995) EMBO J. , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 47
    • 0029022221 scopus 로고
    • GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex
    • Wieser R, Wrana JL, Massagué J. GS domain mutations that constitutively activate TβR-I, the downstream signaling component in the TGF-β receptor complex. EMBO J. 1995;14:2199-2208.
    • (1995) EMBO J. , vol.14 , pp. 2199-2208
    • Wieser, R.1    Wrana, J.L.2    Massagué, J.3
  • 48
    • 0025117392 scopus 로고
    • Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome
    • Daley GQ, Van Etten RA, Baltimore D. Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science. 1990;247:824-830.
    • (1990) Science , vol.247 , pp. 824-830
    • Daley, G.Q.1    Van Etten, R.A.2    Baltimore, D.3
  • 50
    • 0027236954 scopus 로고
    • Production of high-titer helper-free retroviruses by transient transfection
    • Pear WS, Nolan GP, Scott ML, Baltimore D. Production of high-titer helper-free retroviruses by transient transfection. Proc Natl Acad Sci U S A. 1993;90:8392-8396.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 8392-8396
    • Pear, W.S.1    Nolan, G.P.2    Scott, M.L.3    Baltimore, D.4
  • 51
    • 0018220351 scopus 로고
    • The sequence of the chromosomal mouse β-globin major gene: Homologies in capping, splicing and poly(a) sites
    • Konkel DA, Tilghman SM, Leder P. The sequence of the chromosomal mouse β-globin major gene: homologies in capping, splicing and poly(a) sites. Cell. 1978;15:1125-1132.
    • (1978) Cell , vol.15 , pp. 1125-1132
    • Konkel, D.A.1    Tilghman, S.M.2    Leder, P.3
  • 52
    • 0023037890 scopus 로고
    • The antiproliferative effect of type β transforming growth factor occurs at a level distal from receptors for growth-activating factors
    • Like B, Massagué J. The antiproliferative effect of type β transforming growth factor occurs at a level distal from receptors for growth-activating factors. J Biol Chem. 1986;261:13,426-13,429.
    • (1986) J Biol Chem. , vol.261 , pp. 13426-13429
    • Like, B.1    Massagué, J.2
  • 53
    • 0026636152 scopus 로고
    • Immunomodulatory effects of transforming growth factor-β on T lymphocytes. Induction of CD8 expression in the CTLL-2 cell line and in normal thymocytes
    • Inge TH, McCoy KM, Susskind BM, Barrett SK, Zhao G, Bear HD. Immunomodulatory effects of transforming growth factor-β on T lymphocytes. Induction of CD8 expression in the CTLL-2 cell line and in normal thymocytes. J Immunol. 1992; 148:3847-3856.
    • (1992) J Immunol. , vol.148 , pp. 3847-3856
    • Inge, T.H.1    McCoy, K.M.2    Susskind, B.M.3    Barrett, S.K.4    Zhao, G.5    Bear, H.D.6
  • 54
    • 0028818438 scopus 로고
    • The plasmacytoma growth inhibitor restrictin-P is an antagonist of interleukin 6 and interleukin 11: Identification as a stroma-derived activin A
    • Brosh N, Sternberg D, Honigwachs-Sha'anani J, et al. The plasmacytoma growth inhibitor restrictin-P is an antagonist of interleukin 6 and interleukin 11: identification as a stroma-derived activin A. J Biol Chem. 1995;270:29,594-29,600.
    • (1995) J Biol Chem. , vol.270 , pp. 29594-29600
    • Brosh, N.1    Sternberg, D.2    Honigwachs-Sha'anani, J.3
  • 56
    • 0028934824 scopus 로고
    • Distribution and characterization of specific cellular binding proteins for bone morphogenetic protein-2
    • Iwasaki S, Tsuruoka N, Hattori A, Sato M, Tsujimoto M, Kohno M. Distribution and characterization of specific cellular binding proteins for bone morphogenetic protein-2. J Biol Chem. 1995;270: 5476-5482.
    • (1995) J Biol Chem. , vol.270 , pp. 5476-5482
    • Iwasaki, S.1    Tsuruoka, N.2    Hattori, A.3    Sato, M.4    Tsujimoto, M.5    Kohno, M.6
  • 57
    • 0025923249 scopus 로고
    • Inhibition by vitamin d3 of erythroid differentiation of human leukemia line cells induced by transforming growth factor β or erythroid differentiation factor (activin A)
    • Okabe-Kado J, Honma Y, Hozumi M. Inhibition by vitamin D3 of erythroid differentiation of human leukemia line cells induced by transforming growth factor β or erythroid differentiation factor (activin A). Leuk Res. 1991;15:721-726.
    • (1991) Leuk Res. , vol.15 , pp. 721-726
    • Okabe-Kado, J.1    Honma, Y.2    Hozumi, M.3
  • 58
    • 0026496172 scopus 로고
    • TGF-β signals through a heteromeric protein kinase receptor complex
    • Wrana JL, Attisano L, Cárcamo J, et al. TGF-β signals through a heteromeric protein kinase receptor complex. Cell. 1992;71:1003-1014.
    • (1992) Cell , vol.71 , pp. 1003-1014
    • Wrana, J.L.1    Attisano, L.2    Cárcamo, J.3
  • 60
    • 0030920284 scopus 로고    scopus 로고
    • Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells
    • Martens JW, de Winter JP, Timmerman MA, et al. Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells. Endocrinology. 1997;138:2928-2936.
    • (1997) Endocrinology , vol.138 , pp. 2928-2936
    • Martens, J.W.1    De Winter, J.P.2    Timmerman, M.A.3
  • 61
    • 0027332995 scopus 로고
    • Cloning of a TGF-β type I receptor that forms a heteromeric complex with the TGF-β type II receptor
    • Franzén P, ten Dijke P, Ichijo H, et al. Cloning of a TGF-β type I receptor that forms a heteromeric complex with the TGF-β type II receptor. Cell. 1993;75:681-692.
    • (1993) Cell , vol.75 , pp. 681-692
    • Franzén, P.1    Ten Dijke, P.2    Ichijo, H.3
  • 62
    • 17544376741 scopus 로고    scopus 로고
    • Ligand-independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors
    • Feng XH, Derynck R. Ligand-independent activation of transforming growth factor (TGF) β signaling pathways by heteromeric cytoplasmic domains of TGF-β receptors. J Biol Chem. 1996; 271:13,123-13,129.
    • (1996) J Biol Chem. , vol.271 , pp. 13123-13129
    • Feng, X.H.1    Derynck, R.2
  • 63
    • 0000116653 scopus 로고
    • The transforming growth factor-βs
    • Sporn MB, Roberts AB, eds. Berlin, Germany: Springer-Verlag
    • Roberts AB, Sporn MB. The transforming growth factor-βs. In: Sporn MB, Roberts AB, eds. Peptide Growth Factors and their Receptors. Part I. Berlin, Germany: Springer-Verlag; 1990:419-472.
    • (1990) Peptide Growth Factors and their Receptors , Issue.PART I , pp. 419-472
    • Roberts, A.B.1    Sporn, M.B.2
  • 64
    • 0029737070 scopus 로고    scopus 로고
    • Bone morphogenetic proteins: Multifunctional regulators of vertebrate development
    • Hogan BL. Bone morphogenetic proteins: multifunctional regulators of vertebrate development. Genes Dev. 1996;10:1580-1594.
    • (1996) Genes Dev. , vol.10 , pp. 1580-1594
    • Hogan, B.L.1
  • 65
    • 0032544594 scopus 로고    scopus 로고
    • Smad7 is an activin-inducible inhibitor of activin-induced growth arrest and apoptosis in mouse B cells
    • Ishisaki A, Yamato K, Nakao A, et al. Smad7 is an activin-inducible inhibitor of activin-induced growth arrest and apoptosis in mouse B cells. J Biol Chem. 1998;273:24,293-24,296.
    • (1998) J Biol Chem. , vol.273 , pp. 24293-24296
    • Ishisaki, A.1    Yamato, K.2    Nakao, A.3
  • 66
    • 0033531948 scopus 로고    scopus 로고
    • Differential inhibition of Smad6 and Smad7 on bone morphogenetic protein- and activin-mediated growth arrest and apoptosis in B cells
    • Ishisaki A, Yamato K, Hashimoto S, et.al. Differential inhibition of Smad6 and Smad7 on bone morphogenetic protein- and activin-mediated growth arrest and apoptosis in B cells. J Biol Chem. 1999;274:13,637-13,642.
    • (1999) J Biol Chem. , vol.274 , pp. 13637-13642
    • Ishisaki, A.1    Yamato, K.2    Hashimoto, S.3
  • 67
    • 0010259884 scopus 로고
    • Selective and indirect modulation of human multipotential and erythroid hematopoietic progenitor cell proliferation by recombinant human activin and inhibin
    • Broxmeyer HE, Lu L, Cooper S, Schwall RH, Mason AJ, Nikolics K. Selective and indirect modulation of human multipotential and erythroid hematopoietic progenitor cell proliferation by recombinant human activin and inhibin. Proc Natl Acad Sci U S A. 1988;85:9052-9056.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 9052-9056
    • Broxmeyer, H.E.1    Lu, L.2    Cooper, S.3    Schwall, R.H.4    Mason, A.J.5    Nikolics, K.6
  • 68
    • 0026565263 scopus 로고
    • Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis
    • Shiozaki M, Sakai R, Tabuchi M, et al. Evidence for the participation of endogenous activin A/erythroid differentiation factor in the regulation of erythropoiesis. Proc Natl Acad Sci U S A. 1992; 89:1553-1556.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 1553-1556
    • Shiozaki, M.1    Sakai, R.2    Tabuchi, M.3
  • 69
    • 0027216054 scopus 로고
    • Activin A suppresses proliferation of interleukin-3-responsive granulocyte-macrophage colony-forming progenitors and stimulates proliferation and differentiation of interteukin-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 interteukin-3-responsive erythroid burst-forming progenitors in the peripheral blood. Blood. 1993;81:2891-2897.
    • (1993) Blood , vol.81 , pp. 2891-2897
    • Mizuguchi, T.1    Kosaka, M.2    Saito, S.3
  • 70
    • 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. 1991;19:1090-1095.
    • (1991) Exp Hematol. , vol.19 , pp. 1090-1095
    • Nakao, K.1    Kosaka, M.2    Saito, S.3
  • 71
    • 0026595714 scopus 로고
    • Effect of activin A on globin gene expression in purified human erythroid progenitors
    • Shao L, Frigon NL Jr, Young AL, et al. Effect of activin A on globin gene expression in purified human erythroid progenitors. Blood. 1992;79: 773-781.
    • (1992) Blood , vol.79 , pp. 773-781
    • Shao, L.1    Frigon N.L., Jr.2    Young, A.L.3
  • 72
    • 0017173818 scopus 로고
    • Isolation and characterization of high and low differentiation-inducible Friend leukemia lines
    • Ikawa Y, Aida M, Inoue Y. Isolation and characterization of high and low differentiation-inducible Friend leukemia lines. Gann. 1976;67:767-770.
    • (1976) Gann. , vol.67 , pp. 767-770
    • Ikawa, Y.1    Aida, M.2    Inoue, Y.3
  • 73
    • 0016640079 scopus 로고
    • Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome
    • Lozzio CB, Lozzio BB. Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome. Blood. 1975;45:321-334.
    • (1975) Blood , vol.45 , pp. 321-334
    • Lozzio, C.B.1    Lozzio, B.B.2
  • 74
    • 0020321974 scopus 로고
    • HEL cells: A new human erythroleukemia cell line with spontaneous and induced globin expression
    • Martin P, Papayannopoulou T. HEL cells: a new human erythroleukemia cell line with spontaneous and induced globin expression. Science. 1982;216:1233-1235.
    • (1982) Science , vol.216 , pp. 1233-1235
    • Martin, P.1    Papayannopoulou, T.2
  • 75
    • 12644260471 scopus 로고    scopus 로고
    • Vascular MADs: Two newel MAD-related genes selectively inducible by flow in human vascular endothelium
    • Topper JN, Cai J, Qiu Y, et al. Vascular MADs: two newel MAD-related genes selectively inducible by flow in human vascular endothelium. Proc Natl Acad Sci U S A. 1997;94:9314-9319.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 9314-9319
    • Topper, J.N.1    Cai, J.2    Qiu, Y.3
  • 76
    • 0026445528 scopus 로고
    • Transforming growth factor-β: Recent progress and new challenges
    • Sporn MB, Roberts AB. Transforming growth factor-β: recent progress and new challenges. J Cell Biol. 1992;119:1017-1021.
    • (1992) J Cell Biol. , vol.119 , pp. 1017-1021
    • Sporn, M.B.1    Roberts, A.B.2
  • 77
    • 16044369574 scopus 로고    scopus 로고
    • Madr2 maps to 18q21 and encodes a TGF-β-regulated Mad-related protein that is functionally mutated in colorectal carcinoma
    • Eppert K, Scherer SW, Ozcelik H. et al. Madr2 maps to 18q21 and encodes a TGF-β-regulated Mad-related protein that is functionally mutated in colorectal carcinoma. Cell. 1996;86:543-552.
    • (1996) Cell , vol.86 , pp. 543-552
    • Eppert, K.1    Scherer, S.W.2    Ozcelik, H.3
  • 79
    • 0030825516 scopus 로고    scopus 로고
    • Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4
    • Hata A, Lo RS, Wotton D, Lagna G, Massagué J. Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4. Nature. 1997;388:82-87.
    • (1997) Nature , vol.388 , pp. 82-87
    • Hata, A.1    Lo, R.S.2    Wotton, D.3    Lagna, G.4    Massagué, J.5
  • 80
    • 0025942785 scopus 로고
    • Expression of a Xenopus homolog of Brachyury (T) is an immediate-early response to mesoderm induction
    • Smith JC, Price BMJ, Green JBA, Weigel D, Herrmann BG. Expression of a Xenopus homolog of Brachyury (T) is an immediate-early response to mesoderm induction. Cell. 1991;67:79-87.
    • (1991) Cell , vol.67 , pp. 79-87
    • Smith, J.C.1    Price, B.M.J.2    Green, J.B.A.3    Weigel, D.4    Herrmann, B.G.5
  • 81
    • 0025166072 scopus 로고
    • Graded changes in dose of a Xenopus activin A homologue elicit stepwise transitions in embryonic cell fate
    • Green JB, Smith JC. Graded changes in dose of a Xenopus activin A homologue elicit stepwise transitions in embryonic cell fate. Nature. 1990; 347:391-394.
    • (1990) Nature , vol.347 , pp. 391-394
    • Green, J.B.1    Smith, J.C.2
  • 82
    • 0028122987 scopus 로고
    • Activin signalling and response to a morphogen gradient
    • Gurdon JB, Harger P, Mitchell A, Lemaire P. Activin signalling and response to a morphogen gradient. Nature. 1994;371:487-492.
    • (1994) Nature , vol.371 , pp. 487-492
    • Gurdon, J.B.1    Harger, P.2    Mitchell, A.3    Lemaire, P.4
  • 83
    • 0028224649 scopus 로고
    • Hormonal regulation of embryogenesis: The formation of mesoderm in Xenopus laevis
    • Klein PS, Melton DA. Hormonal regulation of embryogenesis: the formation of mesoderm in Xenopus laevis. Endocr Rev. 1994;15:326-341.
    • (1994) Endocr Rev. , vol.15 , pp. 326-341
    • Klein, P.S.1    Melton, D.A.2
  • 84
    • 0028807860 scopus 로고
    • Inactivation of activin-dependent transcription by kinase-deficient activin receptors
    • Tsuchida K, Vaughan JM, Wiater E, Gaddy-Kurten D, Vale WW. Inactivation of activin-dependent transcription by kinase-deficient activin receptors. Endocrinology. 1995;136:5493-5503.
    • (1995) Endocrinology , vol.136 , pp. 5493-5503
    • Tsuchida, K.1    Vaughan, J.M.2    Wiater, E.3    Gaddy-Kurten, D.4    Vale, W.W.5
  • 85
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signaling
    • Macias-Silva M, Abdollah S, Hoodless PA, Pirone R, Attisano L, Wrana JL. MADR2 is a substrate of the TGF-β receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell. 1996;87:1215-1224.
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macias-Silva, M.1    Abdollah, S.2    Hoodless, P.A.3    Pirone, R.4    Attisano, L.5    Wrana, J.L.6
  • 86
    • 0029786212 scopus 로고    scopus 로고
    • Receptor-associated Mad homologues synergize as effectors of the TGF-β response
    • Zhang Y, Feng XH, Wu RY, Derynck R. Receptor-associated Mad homologues synergize as effectors of the TGF-β response. Nature. 1996;383: 168-172.
    • (1996) Nature , vol.383 , pp. 168-172
    • Zhang, Y.1    Feng, X.H.2    Wu, R.Y.3    Derynck, R.4
  • 87
    • 0029802485 scopus 로고    scopus 로고
    • A transcriptional partner for MAD proteins in TGF-β signalling
    • Chen X, Rubock MJ, Whitman M. A transcriptional partner for MAD proteins in TGF-β signalling. Nature. 1996;383:691-696.
    • (1996) Nature , vol.383 , pp. 691-696
    • Chen, X.1    Rubock, M.J.2    Whitman, M.3
  • 88
    • 0029806078 scopus 로고    scopus 로고
    • Regulation of transforming growth factor β- and activin-induced transcription by mammalian Mad proteins
    • Chen Y, Lebrun JJ, Vale W. Regulation of transforming growth factor β- and activin-induced transcription by mammalian Mad proteins. Proc Natl Acad Sci U S A. 1996;93:12,992-12.997.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 12992-12997
    • Chen, Y.1    Lebrun, J.J.2    Vale, W.3
  • 89
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • Lagna G, Hata A, Hemmati-Brivanlou A, Massagué J. Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. Nature. 1996;383:832-836.
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    Hemmati-Brivanlou, A.3    Massagué, J.4
  • 90
    • 0032110463 scopus 로고    scopus 로고
    • Smad2 and Smad3 positively and negatively regulate TGF β-dependent transcription through the forkhead DNA-binding protein FAST2
    • Labbé E, Silvestri C, Hoodless PA, Wrana JL, Attisano L. Smad2 and Smad3 positively and negatively regulate TGF β-dependent transcription through the forkhead DNA-binding protein FAST2. Mol Cell. 1998;2:109-120.
    • (1998) Mol Cell. , vol.2 , pp. 109-120
    • Labbé, E.1    Silvestri, C.2    Hoodless, P.A.3    Wrana, J.L.4    Attisano, L.5
  • 91
    • 0030911104 scopus 로고    scopus 로고
    • The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase
    • Kretzschmar M, Liu F, Hata A, Doody J, Massagué J. The TGF-β family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase. Genes Dev. 1997; 11:984-995.
    • (1997) Genes Dev. , vol.11 , pp. 984-995
    • Kretzschmar, M.1    Liu, F.2    Hata, A.3    Doody, J.4    Massagué, J.5
  • 92
    • 0030667930 scopus 로고    scopus 로고
    • Smad8 mediates the signaling of the ALK-2 receptor serine kinase
    • Chen Y, Bhushan A, Vale W. Smad8 mediates the signaling of the ALK-2 receptor serine kinase. Proc Natl Acad Sci U S A. 1997;94:12,938-12,943.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12938-12943
    • Chen, Y.1    Bhushan, A.2    Vale, W.3


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