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Volumn 288, Issue 34, 2013, Pages 24503-24517

C-Abl-dependent molecular circuitry involving Smad5 and phosphatidylinositol 3-kinase regulates bone morphogenetic protein-2-induced osteogenesis

Author keywords

[No Author keywords available]

Indexed keywords

AKT PHOSPHORYLATION; ALKALINE PHOSPHATASE; CHRONIC MYELOID LEUKEMIAS; DOMINANT-NEGATIVE MUTANTS; OSTEOBLAST DIFFERENTIATION; OSTEOCLAST DIFFERENTIATION; PHARMACOLOGICAL INHIBITORS; PHOSPHATIDYLINOSITOL 3-KINASE;

EID: 84883163204     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.455733     Document Type: Article
Times cited : (30)

References (78)
  • 1
    • 81255142013 scopus 로고    scopus 로고
    • Bone development: Overview of bone cells and signaling
    • Teti, A. (2011) Bone development: overview of bone cells and signaling. Curr. Osteoporos. Rep. 9, 264-273
    • (2011) Curr. Osteoporos. Rep. , vol.9 , pp. 264-273
    • Teti, A.1
  • 2
    • 0036061947 scopus 로고    scopus 로고
    • Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2, and BMP-2 signaling
    • Marie, P. J., Debiais, F., and Haÿ, E. (2002) Regulation of human cranial osteoblast phenotype by FGF-2, FGFR-2, and BMP-2 signaling. Histol. Histopathol. 17, 877-885
    • (2002) Histol. Histopathol. , vol.17 , pp. 877-885
    • Marie, P.J.1    Debiais, F.2    Haÿ, E.3
  • 3
    • 0034600953 scopus 로고    scopus 로고
    • BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II
    • Kirsch, T., Nickel, J., and Sebald, W. (2000) BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II. EMBO J. 19, 3314-3324
    • (2000) EMBO J. , vol.19 , pp. 3314-3324
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 4
    • 33646749327 scopus 로고    scopus 로고
    • Structure of the ternary signaling complex of a TGF-β superfamily member
    • Allendorph, G. P., Vale, W. W., and Choe, S. (2006) Structure of the ternary signaling complex of a TGF-β superfamily member. Proc. Natl. Acad. Sci. U.S.A. 103, 7643-7648
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 7643-7648
    • Allendorph, G.P.1    Vale, W.W.2    Choe, S.3
  • 5
    • 0034043106 scopus 로고    scopus 로고
    • Crystal structure of the BMP-2-BRIA ectodomain complex
    • Kirsch, T., Sebald, W., and Dreyer, M. K. (2000) Crystal structure of the BMP-2-BRIA ectodomain complex. Nat. Struct. Biol. 7, 492-496
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 492-496
    • Kirsch, T.1    Sebald, W.2    Dreyer, M.K.3
  • 6
    • 0033975972 scopus 로고    scopus 로고
    • Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2
    • Kirsch, T., Nickel, J., and Sebald, W. (2000) Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2. FEBS Lett. 468, 215-219
    • (2000) FEBS Lett. , vol.468 , pp. 215-219
    • Kirsch, T.1    Nickel, J.2    Sebald, W.3
  • 7
    • 21644447416 scopus 로고    scopus 로고
    • Bone morphogenetic protein (BMP) type II receptor deletion reveals BMP ligandspecific gain of signaling in pulmonary artery smooth muscle cells
    • Yu, P. B., Beppu, H., Kawai, N., Li, E., and Bloch, K. D. (2005) Bone morphogenetic protein (BMP) type II receptor deletion reveals BMP ligandspecific gain of signaling in pulmonary artery smooth muscle cells. J. Biol. Chem. 280, 24443-24450
    • (2005) J. Biol. Chem. , vol.280 , pp. 24443-24450
    • Yu, P.B.1    Beppu, H.2    Kawai, N.3    Li, E.4    Bloch, K.D.5
  • 9
    • 13444291335 scopus 로고    scopus 로고
    • BMP signaling in skeletal development
    • Wan, M., and Cao, X. (2005) BMP signaling in skeletal development. Biochem. Biophys. Res. Commun. 328, 651-657
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 651-657
    • Wan, M.1    Cao, X.2
  • 10
    • 0038682002 scopus 로고    scopus 로고
    • Mechanisms of TGF-β signaling from cell membrane to the nucleus
    • Shi, Y., and Massagué, J. (2003) Mechanisms of TGF-β signaling from cell membrane to the nucleus. Cell 113, 685-700
    • (2003) Cell , vol.113 , pp. 685-700
    • Shi, Y.1    Massagué, J.2
  • 11
    • 75649127963 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptors and signal transduction
    • Miyazono, K., Kamiya, Y., and Morikawa, M. (2010) Bone morphogenetic protein receptors and signal transduction. J. Biochem. 147, 35-51
    • (2010) J. Biochem. , vol.147 , pp. 35-51
    • Miyazono, K.1    Kamiya, Y.2    Morikawa, M.3
  • 12
    • 0346996450 scopus 로고    scopus 로고
    • Signal transduction of bone morphogenetic protein receptors
    • Nohe, A., Keating, E., Knaus, P., and Petersen, N. O. (2004) Signal transduction of bone morphogenetic protein receptors. Cell. Signal. 16, 291-299
    • (2004) Cell. Signal. , vol.16 , pp. 291-299
    • Nohe, A.1    Keating, E.2    Knaus, P.3    Petersen, N.O.4
  • 13
    • 0033178337 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase functionally contributes to chondrogenesis induced by growth/differentiation factor-5 in ATDC5 cells
    • Nakamura, K., Shirai, T., Morishita, S., Uchida, S., Saeki-Miura, K., and Makishima, F. (1999) p38 mitogen-activated protein kinase functionally contributes to chondrogenesis induced by growth/differentiation factor-5 in ATDC5 cells. Exp. Cell Res. 250, 351-363
    • (1999) Exp. Cell Res. , vol.250 , pp. 351-363
    • Nakamura, K.1    Shirai, T.2    Morishita, S.3    Uchida, S.4    Saeki-Miura, K.5    Makishima, F.6
  • 16
    • 33646713486 scopus 로고    scopus 로고
    • The TGF-β-activated kinase TAK1 regulates vascular development in vivo
    • Jadrich, J. L., O'Connor, M. B., and Coucouvanis, E. (2006) The TGF-β-activated kinase TAK1 regulates vascular development in vivo. Development 133, 1529-1541
    • (2006) Development , vol.133 , pp. 1529-1541
    • Jadrich, J.L.1    O'Connor, M.B.2    Coucouvanis, E.3
  • 19
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr-Abl tyrosine kinases
    • Hantschel, O., and Superti-Furga, G. (2004) Regulation of the c-Abl and Bcr-Abl tyrosine kinases. Nat. Rev. Mol. Cell Biol. 5, 33-44
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 20
    • 78650517027 scopus 로고    scopus 로고
    • The Cain and Abl of epithelial-mesenchymal transition and transforming growth factor-α in mammary epithelial cells
    • Allington, T. M., and Schiemann, W. P. (2011) The Cain and Abl of epithelial-mesenchymal transition and transforming growth factor-α in mammary epithelial cells. Cells Tissues Organs 193, 98-113
    • (2011) Cells Tissues Organs , vol.193 , pp. 98-113
    • Allington, T.M.1    Schiemann, W.P.2
  • 21
    • 15244339164 scopus 로고    scopus 로고
    • Imatinib mesylate inhibits the profibrogenic activity of TGF-β and prevents bleomycin-mediated lung fibrosis
    • Daniels, C. E., Wilkes, M. C., Edens, M., Kottom, T. J., Murphy, S. J., Limper, A. H., and Leof, E. B. (2004) Imatinib mesylate inhibits the profibrogenic activity of TGF-β and prevents bleomycin-mediated lung fibrosis. J. Clin. Invest. 114, 1308-1316
    • (2004) J. Clin. Invest. , vol.114 , pp. 1308-1316
    • Daniels, C.E.1    Wilkes, M.C.2    Edens, M.3    Kottom, T.J.4    Murphy, S.J.5    Limper, A.H.6    Leof, E.B.7
  • 22
    • 74049137551 scopus 로고    scopus 로고
    • Noncanonical TGF-β pathways, mTORC1 and Abl, in renal interstitial fibrogenesis
    • Wang, S., Wilkes, M. C., Leof, E. B., and Hirschberg, R. (2010) Noncanonical TGF-β pathways, mTORC1 and Abl, in renal interstitial fibrogenesis. Am. J. Physiol. Renal Physiol. 298, F142-F149
    • (2010) Am. J. Physiol. Renal Physiol. , vol.298
    • Wang, S.1    Wilkes, M.C.2    Leof, E.B.3    Hirschberg, R.4
  • 23
    • 27344444026 scopus 로고    scopus 로고
    • Bcr-Abl activates the AKT/Fox O3 signalling pathway to restrict transforming growth factor-β-mediated cytostatic signals
    • Atfi, A., Abécassis, L., and Bourgeade, M. F. (2005) Bcr-Abl activates the AKT/Fox O3 signalling pathway to restrict transforming growth factor-β-mediated cytostatic signals. EMBO Rep. 6, 985-991
    • (2005) EMBO Rep. , vol.6 , pp. 985-991
    • Atfi, A.1    Abécassis, L.2    Bourgeade, M.F.3
  • 25
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz, V. L., Crawford, C. E., Jackson, P. K., Bronson, R. T., and Mulligan, R. C. (1991) Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell 65, 1153-1163
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 26
    • 68049099370 scopus 로고    scopus 로고
    • Abl knockout differentially affects p130 Crk-associated substrate, vinculin, and paxillin in blood vessels of mice
    • Chen, S., Wang, R., Li, Q. F., and Tang, D. D. (2009) Abl knockout differentially affects p130 Crk-associated substrate, vinculin, and paxillin in blood vessels of mice. Am. J. Physiol. Heart Circ. Physiol. 297, H533-H539
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Chen, S.1    Wang, R.2    Li, Q.F.3    Tang, D.D.4
  • 27
    • 75749113347 scopus 로고    scopus 로고
    • C-Abl tyrosine kinase regulates cardiac growth and development
    • Qiu, Z., Cang, Y., and Goff, S. P. (2010) c-Abl tyrosine kinase regulates cardiac growth and development. Proc. Natl. Acad. Sci. U.S.A. 107, 1136-1141
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1136-1141
    • Qiu, Z.1    Cang, Y.2    Goff, S.P.3
  • 28
    • 0024353722 scopus 로고
    • The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization
    • Van Etten, R. A., Jackson, P., and Baltimore, D. (1989) The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization. Cell 58, 669-678
    • (1989) Cell , vol.58 , pp. 669-678
    • Van Etten, R.A.1    Jackson, P.2    Baltimore, D.3
  • 30
    • 0029879676 scopus 로고    scopus 로고
    • The cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products
    • Wen, S. T., Jackson, P. K., and Van Etten, R. A. (1996) The cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products. EMBO J. 15, 1583-1595
    • (1996) EMBO J. , vol.15 , pp. 1583-1595
    • Wen, S.T.1    Jackson, P.K.2    Van Etten, R.A.3
  • 31
    • 77956920417 scopus 로고    scopus 로고
    • ABL tyrosine kinases: Evolution of function, regulation, and specificity
    • re6
    • Colicelli, J. (2010) ABL tyrosine kinases: evolution of function, regulation, and specificity. Sci. Signal. 3, re6
    • (2010) Sci. Signal. , pp. 3
    • Colicelli, J.1
  • 34
    • 84866167173 scopus 로고    scopus 로고
    • Imatinib mesylate causes growth deceleration in pediatric patients with chronic myelogenous leukemia
    • Rastogi, M. V., Stork, L., Druker, B., Blasdel, C., Nguyen, T., and Boston, B. A. (2012) Imatinib mesylate causes growth deceleration in pediatric patients with chronic myelogenous leukemia. Pediatr. Blood Cancer 59, 840-845
    • (2012) Pediatr. Blood Cancer , vol.59 , pp. 840-845
    • Rastogi, M.V.1    Stork, L.2    Druker, B.3    Blasdel, C.4    Nguyen, T.5    Boston, B.A.6
  • 35
    • 70350332198 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt signal relay cooperates with Smad in bone morphogenetic protein-2-induced colony stimulating factor-1 (CSF-1) expression and osteoclast differentiation
    • Mandal, C. C., Ghosh Choudhury, G., and Ghosh-Choudhury, N. (2009) Phosphatidylinositol 3-kinase/Akt signal relay cooperates with Smad in bone morphogenetic protein-2-induced colony stimulating factor-1 (CSF-1) expression and osteoclast differentiation. Endocrinology 150, 4989-4998
    • (2009) Endocrinology , vol.150 , pp. 4989-4998
    • Mandal, C.C.1    Ghosh Choudhury, G.2    Ghosh-Choudhury, N.3
  • 37
    • 0037031854 scopus 로고    scopus 로고
    • Requirement of BMP-2-induced phosphatidylinositol 3-kinase and Akt serine/threonine kinase in osteoblast differentiation and Smad-dependent BMP-2 gene transcription
    • Ghosh-Choudhury, N., Abboud, S. L., Nishimura, R., Celeste, A., Mahimainathan, L., and Choudhury, G. G. (2002) Requirement of BMP-2-induced phosphatidylinositol 3-kinase and Akt serine/threonine kinase in osteoblast differentiation and Smad-dependent BMP-2 gene transcription. J. Biol. Chem. 277, 33361-33368
    • (2002) J. Biol. Chem. , vol.277 , pp. 33361-33368
    • Ghosh-Choudhury, N.1    Abboud, S.L.2    Nishimura, R.3    Celeste, A.4    Mahimainathan, L.5    Choudhury, G.G.6
  • 38
    • 0028233970 scopus 로고
    • The nuclear tyrosine kinase c-Abl negatively regulates cell growth
    • Sawyers, C. L., McLaughlin, J., Goga, A., Havlik, M., and Witte, O. (1994) The nuclear tyrosine kinase c-Abl negatively regulates cell growth. Cell 77, 121-131
    • (1994) Cell , vol.77 , pp. 121-131
    • Sawyers, C.L.1    McLaughlin, J.2    Goga, A.3    Havlik, M.4    Witte, O.5
  • 39
    • 33745975802 scopus 로고    scopus 로고
    • Concerted action of Smad and CREB-binding protein regulates bone morphogenetic protein-2-stimulated osteoblastic colony-stimulating factor-1 expression
    • Ghosh-Choudhury, N., Singha, P. K., Woodruff, K., St Clair, P., Bsoul, S., Werner, S. L., and Choudhury, G. G. (2006) Concerted action of Smad and CREB-binding protein regulates bone morphogenetic protein-2-stimulated osteoblastic colony-stimulating factor-1 expression. J. Biol. Chem. 281, 20160-20170
    • (2006) J. Biol. Chem. , vol.281 , pp. 20160-20170
    • Ghosh-Choudhury, N.1    Singha, P.K.2    Woodruff, K.3    St Clair, P.4    Bsoul, S.5    Werner, S.L.6    Choudhury, G.G.7
  • 40
    • 78649324674 scopus 로고    scopus 로고
    • Integration of phosphatidylinositol 3-kinase, Akt kinase, and Smad signaling pathway in BMP-2-induced osterix expression
    • Mandal, C. C., Drissi, H., Choudhury, G. G., and Ghosh-Choudhury, N. (2010) Integration of phosphatidylinositol 3-kinase, Akt kinase, and Smad signaling pathway in BMP-2-induced osterix expression. Calcif. Tissue Int. 87, 533-540
    • (2010) Calcif. Tissue Int. , vol.87 , pp. 533-540
    • Mandal, C.C.1    Drissi, H.2    Choudhury, G.G.3    Ghosh-Choudhury, N.4
  • 41
    • 0032514135 scopus 로고    scopus 로고
    • Differential roles for bone morphogenetic protein (BMP) receptor type IB and IA in differentiation and specification of mesenchymal precursor cells to osteoblast and adipocyte lineages
    • Chen, D., Ji, X., Harris, M. A., Feng, J. Q., Karsenty, G., Celeste, A. J., Rosen, V., Mundy, G. R., and Harris, S. E. (1998) Differential roles for bone morphogenetic protein (BMP) receptor type IB and IA in differentiation and specification of mesenchymal precursor cells to osteoblast and adipocyte lineages. J. Cell Biol. 142, 295-305
    • (1998) J. Cell Biol. , vol.142 , pp. 295-305
    • Chen, D.1    Ji, X.2    Harris, M.A.3    Feng, J.Q.4    Karsenty, G.5    Celeste, A.J.6    Rosen, V.7    Mundy, G.R.8    Harris, S.E.9
  • 46
    • 33947508765 scopus 로고    scopus 로고
    • Statin-induced Ras activation integrates the phosphatidylinositol 3-kinase signal to Akt and MAPK for bone morphogenetic protein-2 expression in osteoblast differentiation
    • Ghosh-Choudhury, N., Mandal, C. C., and Choudhury, G. G. (2007) Statin-induced Ras activation integrates the phosphatidylinositol 3-kinase signal to Akt and MAPK for bone morphogenetic protein-2 expression in osteoblast differentiation. J. Biol. Chem. 282, 4983-4993
    • (2007) J. Biol. Chem. , vol.282 , pp. 4983-4993
    • Ghosh-Choudhury, N.1    Mandal, C.C.2    Choudhury, G.G.3
  • 47
    • 0031550534 scopus 로고    scopus 로고
    • Clonal osteoblastic cell lines from p53 null mouse calvariae are immortalized and dependent on bone morphogenetic protein 2 for mature osteoblastic phenotype
    • Ghosh-Choudhury, N., Harris, M. A., Wozney, J., Mundy, G. R., and Harris, S. E. (1997) Clonal osteoblastic cell lines from p53 null mouse calvariae are immortalized and dependent on bone morphogenetic protein 2 for mature osteoblastic phenotype. Biochem. Biophys. Res. Commun. 231, 196-202
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 196-202
    • Ghosh-Choudhury, N.1    Harris, M.A.2    Wozney, J.3    Mundy, G.R.4    Harris, S.E.5
  • 48
    • 79953217743 scopus 로고    scopus 로고
    • Simvastatin prevents skeletal metastasis of breast cancer by an antagonistic interplay between p53 and CD44
    • Mandal, C. C., Ghosh-Choudhury, N., Yoneda, T., and Choudhury, G. G. (2011) Simvastatin prevents skeletal metastasis of breast cancer by an antagonistic interplay between p53 and CD44. J. Biol. Chem. 286, 11314-11327
    • (2011) J. Biol. Chem. , vol.286 , pp. 11314-11327
    • Mandal, C.C.1    Ghosh-Choudhury, N.2    Yoneda, T.3    Choudhury, G.G.4
  • 49
    • 0038159330 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates bone morphogenetic protein-2 (BMP-2)-induced myocyte enhancer factor 2A-dependent transcription of BMP-2 gene in cardiomyocyte precursor cells
    • Ghosh-Choudhury, N., Abboud, S. L., Mahimainathan, L., Chandrasekar, B., and Choudhury, G. G. (2003) Phosphatidylinositol 3-kinase regulates bone morphogenetic protein-2 (BMP-2)-induced myocyte enhancer factor 2A-dependent transcription of BMP-2 gene in cardiomyocyte precursor cells. J. Biol. Chem. 278, 21998-22005
    • (2003) J. Biol. Chem. , vol.278 , pp. 21998-22005
    • Ghosh-Choudhury, N.1    Abboud, S.L.2    Mahimainathan, L.3    Chandrasekar, B.4    Choudhury, G.G.5
  • 50
    • 0343200750 scopus 로고    scopus 로고
    • Association and direct activation of signal transducer and activator of transcription 1α by platelet-derived growth factor receptor
    • Choudhury, G. G., Ghosh-Choudhury, N., and Abboud, H. E. (1998) Association and direct activation of signal transducer and activator of transcription 1α by platelet-derived growth factor receptor. J. Clin. Invest. 101, 2751-2760
    • (1998) J. Clin. Invest. , vol.101 , pp. 2751-2760
    • Choudhury, G.G.1    Ghosh-Choudhury, N.2    Abboud, H.E.3
  • 51
    • 55049083860 scopus 로고    scopus 로고
    • A crucial role in cell spreading for the interaction of Abl PXXP motifs with Crk and Nck adaptors
    • Antoku, S., Saksela, K., Rivera, G. M., and Mayer, B. J. (2008) A crucial role in cell spreading for the interaction of Abl PXXP motifs with Crk and Nck adaptors. J. Cell Sci. 121, 3071-3082
    • (2008) J. Cell Sci. , vol.121 , pp. 3071-3082
    • Antoku, S.1    Saksela, K.2    Rivera, G.M.3    Mayer, B.J.4
  • 52
    • 0034634597 scopus 로고    scopus 로고
    • C-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines
    • Brasher, B. B., and Van Etten, R. A. (2000) c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines. J. Biol. Chem. 275, 35631-35637
    • (2000) J. Biol. Chem. , vol.275 , pp. 35631-35637
    • Brasher, B.B.1    Van Etten, R.A.2
  • 53
    • 0037508877 scopus 로고    scopus 로고
    • Two distinct phosphorylation pathways have additive effects on Abl family kinase activation
    • Tanis, K. Q., Veach, D., Duewel, H. S., Bornmann, W. G., and Koleske, A. J. (2003) Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol. Cell. Biol. 23, 3884-3896
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3884-3896
    • Tanis, K.Q.1    Veach, D.2    Duewel, H.S.3    Bornmann, W.G.4    Koleske, A.J.5
  • 54
    • 0026721147 scopus 로고
    • The bone morphogenetic protein family and osteogenesis
    • Wozney, J. M. (1992) The bone morphogenetic protein family and osteogenesis. Mol. Reprod. Dev. 32, 160-167
    • (1992) Mol. Reprod. Dev. , vol.32 , pp. 160-167
    • Wozney, J.M.1
  • 56
    • 0028341364 scopus 로고
    • Effects of transforming growth factorβ on bone nodule formation and expression of bone morphogenetic protein 2, osteocalcin, osteopontin, alkaline phosphatase, and type i collagen mRNA in long-term cultures of fetal rat calvarial osteoblasts
    • Harris, S. E., Bonewald, L. F., Harris, M. A., Sabatini, M., Dallas, S., Feng, J. Q., Ghosh-Choudhury, N., Wozney, J., and Mundy, G. R. (1994) Effects of transforming growth factorβ on bone nodule formation and expression of bone morphogenetic protein 2, osteocalcin, osteopontin, alkaline phosphatase, and type I collagen mRNA in long-term cultures of fetal rat calvarial osteoblasts. J. Bone Miner. Res. 9, 855-863
    • (1994) J. Bone Miner. Res. , vol.9 , pp. 855-863
    • Harris, S.E.1    Bonewald, L.F.2    Harris, M.A.3    Sabatini, M.4    Dallas, S.5    Feng, J.Q.6    Ghosh-Choudhury, N.7    Wozney, J.8    Mundy, G.R.9
  • 57
    • 0037059614 scopus 로고    scopus 로고
    • The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation
    • Nakashima, K., Zhou, X., Kunkel, G., Zhang, Z., Deng, J. M., Behringer, R. R., and de Crombrugghe, B. (2002) The novel zinc finger-containing transcription factor osterix is required for osteoblast differentiation and bone formation. Cell 108, 17-29
    • (2002) Cell , vol.108 , pp. 17-29
    • Nakashima, K.1    Zhou, X.2    Kunkel, G.3    Zhang, Z.4    Deng, J.M.5    Behringer, R.R.6    De Crombrugghe, B.7
  • 58
    • 0345447504 scopus 로고    scopus 로고
    • Prevalence and correlates of overweight and obesity among older adults: Findings from the Canadian National Population Health Survey
    • Kaplan, M. S., Huguet, N., Newsom, J. T., McFarland, B. H., and Lindsay, J. (2003) Prevalence and correlates of overweight and obesity among older adults: findings from the Canadian National Population Health Survey. J. Gerontol. A Biol. Sci. Med. Sci. 58, 1018-1030
    • (2003) J. Gerontol. A Biol. Sci. Med. Sci. , vol.58 , pp. 1018-1030
    • Kaplan, M.S.1    Huguet, N.2    Newsom, J.T.3    McFarland, B.H.4    Lindsay, J.5
  • 59
    • 0034455103 scopus 로고    scopus 로고
    • Birth and death of bone cells: Basic teoporosis
    • Manolagas, S. C. (2000) Birth and death of bone cells: basic teoporosis. Endocr. Rev. 21, 115-137
    • (2000) Endocr. Rev. , vol.21 , pp. 115-137
    • Manolagas, S.C.1
  • 60
    • 63049090100 scopus 로고    scopus 로고
    • Metastasis: From dissemination to organ-specific colonization
    • Nguyen, D. X., Bos, P. D., and Massagué, J. (2009) Metastasis: from dissemination to organ-specific colonization. Nat. Rev. Cancer 9, 274-284
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 274-284
    • Nguyen, D.X.1    Bos, P.D.2    Massagué, J.3
  • 61
    • 79751499788 scopus 로고    scopus 로고
    • Disorders of bone remodeling
    • Feng, X., and McDonald, J. M. (2011) Disorders of bone remodeling. Annu. Rev. Pathol. 6, 121-145
    • (2011) Annu. Rev. Pathol. , vol.6 , pp. 121-145
    • Feng, X.1    McDonald, J.M.2
  • 63
    • 0025085822 scopus 로고
    • Relationship of cell growth to the regulation of tissue-specific gene expression during osteoblast differentiation
    • Stein, G. S., Lian, J. B., and Owen, T. A. (1990) Relationship of cell growth to the regulation of tissue-specific gene expression during osteoblast differentiation. FASEB J. 4, 3111-3123
    • (1990) FASEB J. , vol.4 , pp. 3111-3123
    • Stein, G.S.1    Lian, J.B.2    Owen, T.A.3
  • 64
    • 15044338824 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase in disease: Timing, location, and scaffolding
    • Wymann, M. P., and Marone, R. (2005) Phosphoinositide 3-kinase in disease: timing, location, and scaffolding. Curr. Opin. Cell Biol. 17, 141-149
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 141-149
    • Wymann, M.P.1    Marone, R.2
  • 65
    • 34347395580 scopus 로고    scopus 로고
    • PI3 kinases in cancer: From oncogene artifact to leading cancer target
    • pe52
    • Zhao, J. J., and Roberts, T. M. (2006) PI3 kinases in cancer: from oncogene artifact to leading cancer target. Sci. STKE 2006, pe52
    • (2006) Sci. STKE 2006
    • Zhao, J.J.1    Roberts, T.M.2
  • 66
    • 0025967280 scopus 로고
    • Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants
    • Varticovski, L., Daley, G. Q., Jackson, P., Baltimore, D., and Cantley, L. C. (1991) Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants. Mol. Cell. Biol. 11, 1107-1113
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1107-1113
    • Varticovski, L.1    Daley, G.Q.2    Jackson, P.3    Baltimore, D.4    Cantley, L.C.5
  • 68
    • 1542314233 scopus 로고    scopus 로고
    • Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor
    • Plattner, R., Koleske, A. J., Kazlauskas, A., and Pendergast, A. M. (2004) Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor. Mol. Cell. Biol. 24, 2573-2583
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2573-2583
    • Plattner, R.1    Koleske, A.J.2    Kazlauskas, A.3    Pendergast, A.M.4
  • 69
    • 33645314375 scopus 로고    scopus 로고
    • Phosphoinositide, phosphopeptide, and pyridone interactions of the Abl SH2 domain
    • Tokonzaba, E., Capelluto, D. G., Kutateladze, T. G., and Overduin, M. (2006) Phosphoinositide, phosphopeptide, and pyridone interactions of the Abl SH2 domain. Chem. Biol. Drug Des. 67, 230-237
    • (2006) Chem. Biol. Drug Des. , vol.67 , pp. 230-237
    • Tokonzaba, E.1    Capelluto, D.G.2    Kutateladze, T.G.3    Overduin, M.4
  • 70
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman, M., Downes, C. P., Keeler, M., Keller, T., and Cantley, L. (1988) Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332, 644-646
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Cantley, L.5
  • 71
    • 0025611910 scopus 로고
    • Phosphoinositide kinases
    • Carpenter, C. L., and Cantley, L. C. (1990) Phosphoinositide kinases. Biochemistry 29, 11147-11156
    • (1990) Biochemistry , vol.29 , pp. 11147-11156
    • Carpenter, C.L.1    Cantley, L.C.2
  • 72
    • 0029669975 scopus 로고    scopus 로고
    • The proto-oncogene product p120CBL and the adaptor proteins CRKL and c-CRK link c-ABL, p190BCR/ABL and p210BCR/ABL to the phosphatidylinositol- 3′ kinase pathway
    • Sattler, M., Salgia, R., Okuda, K., Uemura, N., Durstin, M. A., Pisick, E., Xu, G., Li, J. L., Prasad, K. V., and Griffin, J. D. (1996) The proto-oncogene product p120CBL and the adaptor proteins CRKL and c-CRK link c-ABL, p190BCR/ABL and p210BCR/ABL to the phosphatidylinositol-3′ kinase pathway. Oncogene 12, 839-846
    • (1996) Oncogene , vol.12 , pp. 839-846
    • Sattler, M.1    Salgia, R.2    Okuda, K.3    Uemura, N.4    Durstin, M.A.5    Pisick, E.6    Xu, G.7    Li, J.L.8    Prasad, K.V.9    Griffin, J.D.10
  • 73
    • 0029815798 scopus 로고    scopus 로고
    • PI 3-kinase activation in BCR/abl-transformed hematopoietic cells does not require interaction of p85 SH2 domains with p210 BCR/abl
    • Jain, S. K., Susa, M., Keeler, M. L., Carlesso, N., Druker, B., and Varticovski, L. (1996) PI 3-kinase activation in BCR/abl-transformed hematopoietic cells does not require interaction of p85 SH2 domains with p210 BCR/abl. Blood 88, 1542-1550
    • (1996) Blood , vol.88 , pp. 1542-1550
    • Jain, S.K.1    Susa, M.2    Keeler, M.L.3    Carlesso, N.4    Druker, B.5    Varticovski, L.6
  • 74
    • 26244439049 scopus 로고    scopus 로고
    • Intrinsic regulation of the interactions between the SH3 domain of p85 subunit of phosphatidylinositol-3 kinase and the protein network of BCR/ABL oncogenic tyrosine kinase
    • Ren, S. Y., Xue, F., Feng, J., and Skorski, T. (2005) Intrinsic regulation of the interactions between the SH3 domain of p85 subunit of phosphatidylinositol-3 kinase and the protein network of BCR/ABL oncogenic tyrosine kinase. Exp. Hematol. 33, 1222-1228
    • (2005) Exp. Hematol. , vol.33 , pp. 1222-1228
    • Ren, S.Y.1    Xue, F.2    Feng, J.3    Skorski, T.4
  • 75
    • 33745958768 scopus 로고    scopus 로고
    • Dose-dependent Smad1, Smad5, and Smad8 signaling in the early mouse embryo
    • Arnold, S. J., Maretto, S., Islam, A., Bikoff, E. K., and Robertson, E. J. (2006) Dose-dependent Smad1, Smad5, and Smad8 signaling in the early mouse embryo. Dev. Biol. 296, 104-118
    • (2006) Dev. Biol. , vol.296 , pp. 104-118
    • Arnold, S.J.1    Maretto, S.2    Islam, A.3    Bikoff, E.K.4    Robertson, E.J.5
  • 77
    • 0032428684 scopus 로고    scopus 로고
    • SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor
    • Tsukazaki, T., Chiang, T. A., Davison, A. F., Attisano, L., and Wrana, J. L. (1998) SARA, a FYVE domain protein that recruits Smad2 to the TGFβ receptor. Cell 95, 779-791
    • (1998) Cell , vol.95 , pp. 779-791
    • Tsukazaki, T.1    Chiang, T.A.2    Davison, A.F.3    Attisano, L.4    Wrana, J.L.5


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