메뉴 건너뛰기




Volumn 311, Issue 1, 2005, Pages 167-176

Insulin-like growth factor binding protein (IGFBP)-3 and IGFBP-5 mediate TGF-β- and myostatin-induced suppression of proliferation in porcine embryonic myogenic cell cultures

Author keywords

IGFBP 3; IGFBP 5; Muscle; Myostatin; Proliferation; Smad; TGF

Indexed keywords

DNA; MYOSTATIN; SMAD2 PROTEIN; SOMATOMEDIN BINDING PROTEIN 3; SOMATOMEDIN BINDING PROTEIN 5; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA1;

EID: 27344457469     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2005.09.003     Document Type: Article
Times cited : (27)

References (51)
  • 1
    • 8444243360 scopus 로고    scopus 로고
    • Regulation of muscle mass by myostatin
    • S.J. Lee Regulation of muscle mass by myostatin Annu. Rev. Cell Dev. Biol. 20 2004 61 86
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 61-86
    • Lee, S.J.1
  • 2
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • A.C. McPherron, A.M. Lawler, and S.J. Lee Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member Nature 387 1997 83 90
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 4
    • 0030818314 scopus 로고    scopus 로고
    • Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle
    • R. Kambadur, M. Sharma, T.P. Smith, and J.J. Bass Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle Genome Res. 7 1997 910 916
    • (1997) Genome Res. , vol.7 , pp. 910-916
    • Kambadur, R.1    Sharma, M.2    Smith, T.P.3    Bass, J.J.4
  • 5
    • 0032871622 scopus 로고    scopus 로고
    • Myostatin and the control of skeletal muscle mass
    • S.J. Lee, and A.C. McPherron Myostatin and the control of skeletal muscle mass Curr. Opin. Genet. Dev. 9 1999 604 607
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 604-607
    • Lee, S.J.1    McPherron, A.C.2
  • 7
    • 0034704106 scopus 로고    scopus 로고
    • Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation
    • M. Thomas, B. Langley, C. Berry, M. Sharma, S. Kirk, J. Bass, and R. Kambadur Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation J. Biol. Chem. 275 2000 40235 40243
    • (2000) J. Biol. Chem. , vol.275 , pp. 40235-40243
    • Thomas, M.1    Langley, B.2    Berry, C.3    Sharma, M.4    Kirk, S.5    Bass, J.6    Kambadur, R.7
  • 8
    • 0037147210 scopus 로고    scopus 로고
    • Myostatin inhibits myoblast differentiation by down-regulating MyoD expression
    • B. Langley, M. Thomas, A. Bishop, M. Sharma, S. Gilmour, and R. Kambadur Myostatin inhibits myoblast differentiation by down-regulating MyoD expression J. Biol. Chem. 277 2002 49831 49840
    • (2002) J. Biol. Chem. , vol.277 , pp. 49831-49840
    • Langley, B.1    Thomas, M.2    Bishop, A.3    Sharma, M.4    Gilmour, S.5    Kambadur, R.6
  • 9
    • 0035890328 scopus 로고    scopus 로고
    • TGF-beta inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3
    • D. Liu, B.L. Black, and R. Derynck TGF-beta inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3 Genes Dev. 15 2001 2950 2966
    • (2001) Genes Dev. , vol.15 , pp. 2950-2966
    • Liu, D.1    Black, B.L.2    Derynck, R.3
  • 10
    • 2342514242 scopus 로고    scopus 로고
    • TGF-beta-activated Smad3 represses MEF2-dependent transcription in myogenic differentiation
    • D. Liu, J.S. Kang, and R. Derynck TGF-beta-activated Smad3 represses MEF2-dependent transcription in myogenic differentiation EMBO J. 23 2004 1557 1566
    • (2004) EMBO J. , vol.23 , pp. 1557-1566
    • Liu, D.1    Kang, J.S.2    Derynck, R.3
  • 11
    • 0242285718 scopus 로고    scopus 로고
    • Role of insulin-like growth factor binding protein (IGFBP)-3 in TGF-beta- and GDF-8 (myostatin)-induced suppression of proliferation in porcine embryonic myogenic cell cultures
    • E. Kamanga-Sollo, M.S. Pampusch, M.E. White, and W.R. Dayton Role of insulin-like growth factor binding protein (IGFBP)-3 in TGF-beta- and GDF-8 (myostatin)-induced suppression of proliferation in porcine embryonic myogenic cell cultures J. Cell. Physiol. 197 2003 225 231
    • (2003) J. Cell. Physiol. , vol.197 , pp. 225-231
    • Kamanga-Sollo, E.1    Pampusch, M.S.2    White, M.E.3    Dayton, W.R.4
  • 12
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • R. Derynck, and Y.E. Zhang Smad-dependent and Smad-independent pathways in TGF-beta family signalling Nature 425 2003 577 584
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 13
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • S.J. Lee, and A.C. McPherron Regulation of myostatin activity and muscle growth Proc. Natl. Acad. Sci. U. S. A. 98 2001 9306 9311
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 14
    • 0033889365 scopus 로고    scopus 로고
    • Antiproliferative and pro-apoptotic activities of insulin-like growth factor-binding protein-3
    • R.C. Baxter, A.J. Butt, L.J. Schedlich, and J.L. Martin Antiproliferative and pro-apoptotic activities of insulin-like growth factor-binding protein-3 Growth Horm. IGF Res. 10 Suppl. A 2000 S10 S11
    • (2000) Growth Horm. IGF Res. , vol.10 , Issue.SUPPL. A
    • Baxter, R.C.1    Butt, A.J.2    Schedlich, L.J.3    Martin, J.L.4
  • 15
    • 0033920612 scopus 로고    scopus 로고
    • Insulin-like growth factor (IGF)-binding proteins: Interactions with IGFs and intrinsic bioactivities
    • R.C. Baxter Insulin-like growth factor (IGF)-binding proteins: interactions with IGFs and intrinsic bioactivities Am. J. Physiol. Endocrinol. Metab. 278 2000 E967 E976
    • (2000) Am. J. Physiol. Endocrinol. Metab. , vol.278
    • Baxter, R.C.1
  • 17
    • 0033304507 scopus 로고    scopus 로고
    • The insulin-like growth factor-binding protein (IGFBP) superfamily
    • V. Hwa, Y. Oh, and R.G. Rosenfeld The insulin-like growth factor-binding protein (IGFBP) superfamily Endocr. Rev. 20 1999 761 787
    • (1999) Endocr. Rev. , vol.20 , pp. 761-787
    • Hwa, V.1    Oh, Y.2    Rosenfeld, R.G.3
  • 18
    • 0035513075 scopus 로고    scopus 로고
    • Effects of growth factors on insulin-like growth factor binding protein (IGFBP) secretion by primary porcine satellite cell cultures
    • Z. Yi, M.R. Hathaway, W.R. Dayton, and M.E. White Effects of growth factors on insulin-like growth factor binding protein (IGFBP) secretion by primary porcine satellite cell cultures J. Anim. Sci. 79 2001 2820 2826
    • (2001) J. Anim. Sci. , vol.79 , pp. 2820-2826
    • Yi, Z.1    Hathaway, M.R.2    Dayton, W.R.3    White, M.E.4
  • 19
    • 0032949745 scopus 로고    scopus 로고
    • Decreased steady-state insulin-like growth factor binding protein-3 (IGFBP-3) mRNA level is associated with differentiation of cultured porcine myogenic cells
    • B.J. Johnson, M.E. White, M.R. Hathaway, and W.R. Dayton Decreased steady-state insulin-like growth factor binding protein-3 (IGFBP-3) mRNA level is associated with differentiation of cultured porcine myogenic cells J. Cell. Physiol. 179 1999 237 243
    • (1999) J. Cell. Physiol. , vol.179 , pp. 237-243
    • Johnson, B.J.1    White, M.E.2    Hathaway, M.R.3    Dayton, W.R.4
  • 20
    • 0030183613 scopus 로고    scopus 로고
    • Cultured porcine myogenic cells produce insulin-like growth factor binding protein-3 (IGFBP-3) and transforming growth factor beta-1 stimulates IGFBP-3 production
    • J.R. Hembree, M.S. Pampusch, F. Yang, J.L. Causey, M.R. Hathaway, and W.R. Dayton Cultured porcine myogenic cells produce insulin-like growth factor binding protein-3 (IGFBP-3) and transforming growth factor beta-1 stimulates IGFBP-3 production J. Anim. Sci. 74 1996 1530 1540
    • (1996) J. Anim. Sci. , vol.74 , pp. 1530-1540
    • Hembree, J.R.1    Pampusch, M.S.2    Yang, F.3    Causey, J.L.4    Hathaway, M.R.5    Dayton, W.R.6
  • 21
    • 0037291587 scopus 로고    scopus 로고
    • Effect of recombinant porcine IGF-binding protein-3 on proliferation of embryonic porcine myogenic cell cultures in the presence and absence of IGF-I
    • M.S. Pampusch, E. Kamanga-Sollo, M.E. White, M.R. Hathaway, and W.R. Dayton Effect of recombinant porcine IGF-binding protein-3 on proliferation of embryonic porcine myogenic cell cultures in the presence and absence of IGF-I J. Endocrinol. 176 2003 227 235
    • (2003) J. Endocrinol. , vol.176 , pp. 227-235
    • Pampusch, M.S.1    Kamanga-Sollo, E.2    White, M.E.3    Hathaway, M.R.4    Dayton, W.R.5
  • 22
    • 0031713316 scopus 로고    scopus 로고
    • Modulation of insulin-like growth factor actions in L6A1 myoblasts by insulin-like growth factor binding protein (IGFBP)-4 and IGFBP-5: A dual role for IGFBP-5
    • D.Z. Ewton, S.A. Coolican, S. Mohan, S.D. Chernausek, and J.R. Florini Modulation of insulin-like growth factor actions in L6A1 myoblasts by insulin-like growth factor binding protein (IGFBP)-4 and IGFBP-5: a dual role for IGFBP-5 J. Cell. Physiol. 177 1998 47 57
    • (1998) J. Cell. Physiol. , vol.177 , pp. 47-57
    • Ewton, D.Z.1    Coolican, S.A.2    Mohan, S.3    Chernausek, S.D.4    Florini, J.R.5
  • 23
    • 17844379761 scopus 로고    scopus 로고
    • Production of recombinant porcine IGF-binding protein-5 (IGFBP-5) and its effect on proliferation of porcine embryonic myoblast cultures (PEMC) in the presence and absence of IGF-I and Long-R3-IGF-I
    • M.S. Pampusch, E. Kamanga-Sollo, K.J. Loseth, M.R. Hathaway, W.R. Dayton, and M.E. White Production of recombinant porcine IGF-binding protein-5 (IGFBP-5) and its effect on proliferation of porcine embryonic myoblast cultures (PEMC) in the presence and absence of IGF-I and Long-R3-IGF-I J. Endocrinol. 185 2005 197 206
    • (2005) J. Endocrinol. , vol.185 , pp. 197-206
    • Pampusch, M.S.1    Kamanga-Sollo, E.2    Loseth, K.J.3    Hathaway, M.R.4    Dayton, W.R.5    White, M.E.6
  • 24
    • 0032897868 scopus 로고    scopus 로고
    • Effect of insulin-like growth factor (IGF)-I and des (1-3) IGF-I on the level of IGF binding protein-3 and IGF binding protein-3 mRNA in cultured porcine embryonic muscle cells
    • F. Yang, B.J. Johnson, M.E. White, M.R. Hathaway, and W.R. Dayton Effect of insulin-like growth factor (IGF)-I and Des (1-3) IGF-I on the level of IGF binding protein-3 and IGF binding protein-3 mRNA in cultured porcine embryonic muscle cells J. Cell. Physiol. 178 1999 227 234
    • (1999) J. Cell. Physiol. , vol.178 , pp. 227-234
    • Yang, F.1    Johnson, B.J.2    White, M.E.3    Hathaway, M.R.4    Dayton, W.R.5
  • 25
    • 0026210081 scopus 로고
    • Isolation and culture of porcine myogenic cells and the effect of insulin, IGF-1 and sera on protein turnover in porcine myotube cultures
    • J.R. Hembree, M.R. Hathaway, and W.R. Dayton Isolation and culture of porcine myogenic cells and the effect of insulin, IGF-1 and sera on protein turnover in porcine myotube cultures J. Anim. Sci. 69 1991 3241 3250
    • (1991) J. Anim. Sci. , vol.69 , pp. 3241-3250
    • Hembree, J.R.1    Hathaway, M.R.2    Dayton, W.R.3
  • 26
    • 0025298892 scopus 로고
    • Effect of transforming growth factor beta on proliferation of L6 and embryonic porcine myogenic cells
    • M.S. Pampusch, J.R. Hembree, M.R. Hathaway, and W.R. Dayton Effect of transforming growth factor beta on proliferation of L6 and embryonic porcine myogenic cells J. Cell. Physiol. 143 1990 524 528
    • (1990) J. Cell. Physiol. , vol.143 , pp. 524-528
    • Pampusch, M.S.1    Hembree, J.R.2    Hathaway, M.R.3    Dayton, W.R.4
  • 27
    • 3442895006 scopus 로고    scopus 로고
    • Effect of recombinant porcine IGFBP-3 on IGF-I and Long-R3-IGF-I- stimulated proliferation and differentiation of L6 myogenic cells
    • G. Xi, E. Kamanga-Sollo, M.S. Pampusch, M.E. White, M.R. Hathaway, and W.R. Dayton Effect of recombinant porcine IGFBP-3 on IGF-I and Long-R3-IGF-I-stimulated proliferation and differentiation of L6 myogenic cells J. Cell. Physiol. 200 2004 387 394
    • (2004) J. Cell. Physiol. , vol.200 , pp. 387-394
    • Xi, G.1    Kamanga-Sollo, E.2    Pampusch, M.S.3    White, M.E.4    Hathaway, M.R.5    Dayton, W.R.6
  • 28
    • 0032949745 scopus 로고    scopus 로고
    • Decreased steady-state insulin-like growth factor binding protein-3 (IGFBP-3) mRNA level is associated with differentiation of cultured porcine myogenic cells
    • B.J. Johnson, M.E. White, M.R. Hathaway, and W.R. Dayton Decreased steady-state insulin-like growth factor binding protein-3 (IGFBP-3) mRNA level is associated with differentiation of cultured porcine myogenic cells J. Cell. Physiol. 179 1999 237 243
    • (1999) J. Cell. Physiol. , vol.179 , pp. 237-243
    • Johnson, B.J.1    White, M.E.2    Hathaway, M.R.3    Dayton, W.R.4
  • 29
    • 0037042216 scopus 로고    scopus 로고
    • Isolation and characterization of circulating fragments of the insulin-like growth factor binding protein-3
    • B. Kubler, C. Draeger, H. John, U. Andag, J.G. Scharf, W.G. Forssmann, T. Braulke, and L. Standker Isolation and characterization of circulating fragments of the insulin-like growth factor binding protein-3 FEBS Lett. 518 2002 124 128
    • (2002) FEBS Lett. , vol.518 , pp. 124-128
    • Kubler, B.1    Draeger, C.2    John, H.3    Andag, U.4    Scharf, J.G.5    Forssmann, W.G.6    Braulke, T.7    Standker, L.8
  • 30
    • 0036510391 scopus 로고    scopus 로고
    • Signaling through the Smad pathway by insulin-like growth factor-binding protein-3 in breast cancer cells. Relationship to transforming growth factor-beta 1 signaling
    • S. Fanayan, S.M. Firth, and R.C. Baxter Signaling through the Smad pathway by insulin-like growth factor-binding protein-3 in breast cancer cells. Relationship to transforming growth factor-beta 1 signaling J. Biol. Chem. 277 2002 7255 7261
    • (2002) J. Biol. Chem. , vol.277 , pp. 7255-7261
    • Fanayan, S.1    Firth, S.M.2    Baxter, R.C.3
  • 31
    • 0036714333 scopus 로고    scopus 로고
    • Smad signalling network
    • A. Moustakas Smad signalling network J. Cell Sci. 115 2002 3355 3356
    • (2002) J. Cell Sci. , vol.115 , pp. 3355-3356
    • Moustakas, A.1
  • 32
    • 0037423374 scopus 로고    scopus 로고
    • Elucidation of Smad requirement in transforming growth factor-beta type I receptor-induced responses
    • S. Itoh, M. Thorikay, M. Kowanetz, A. Moustakas, F. Itoh, C.H. Heldin, and P. Ten Dijke Elucidation of Smad requirement in transforming growth factor-beta type I receptor-induced responses J. Biol. Chem. 278 2003 3751 3761
    • (2003) J. Biol. Chem. , vol.278 , pp. 3751-3761
    • Itoh, S.1    Thorikay, M.2    Kowanetz, M.3    Moustakas, A.4    Itoh, F.5    Heldin, C.H.6    Ten Dijke, P.7
  • 33
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-beta signals
    • J. Massague How cells read TGF-beta signals Nat. Rev. Mol. Cell Biol. 1 2000 169 178
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massague, J.1
  • 34
    • 0024357562 scopus 로고
    • The ski oncogene induces muscle differentiation in quail embryo cells
    • C. Colmenares, and E. Stavnezer The ski oncogene induces muscle differentiation in quail embryo cells Cell 59 1989 293 303
    • (1989) Cell , vol.59 , pp. 293-303
    • Colmenares, C.1    Stavnezer, E.2
  • 35
    • 0842281496 scopus 로고    scopus 로고
    • Ski and SnoN: Negative regulators of TGF-beta signaling
    • K. Luo Ski and SnoN: negative regulators of TGF-beta signaling Curr. Opin. Genet. Dev. 14 2004 65 70
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 65-70
    • Luo, K.1
  • 37
    • 9644281085 scopus 로고    scopus 로고
    • Regulation of GDF-8 signaling by the p38 MAPK
    • B. Philip, Z. Lu, and Y. Gao Regulation of GDF-8 signaling by the p38 MAPK Cell Signalling 17 2005 365 375
    • (2005) Cell Signalling , vol.17 , pp. 365-375
    • Philip, B.1    Lu, Z.2    Gao, Y.3
  • 38
    • 1542305591 scopus 로고    scopus 로고
    • Differential effect of transforming growth factor beta (TGF-beta) on the genes encoding hyaluronan synthases and utilization of the p38 MAPK pathway in TGF-beta-induced hyaluronan synthase 1 activation
    • K.M. Stuhlmeier, and C. Pollaschek Differential effect of transforming growth factor beta (TGF-beta) on the genes encoding hyaluronan synthases and utilization of the p38 MAPK pathway in TGF-beta-induced hyaluronan synthase 1 activation J. Biol. Chem. 279 2004 8753 8760
    • (2004) J. Biol. Chem. , vol.279 , pp. 8753-8760
    • Stuhlmeier, K.M.1    Pollaschek, C.2
  • 39
    • 12544257249 scopus 로고    scopus 로고
    • Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-beta-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo
    • A.K. Kamaraju, and A.B. Roberts Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-beta-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo J. Biol. Chem. 280 2005 1024 1036
    • (2005) J. Biol. Chem. , vol.280 , pp. 1024-1036
    • Kamaraju, A.K.1    Roberts, A.B.2
  • 40
    • 0036888335 scopus 로고    scopus 로고
    • Integration of the TGF-beta pathway into the cellular signalling network
    • M. Lutz, and P. Knaus Integration of the TGF-beta pathway into the cellular signalling network Cell Signalling 14 2002 977 988
    • (2002) Cell Signalling , vol.14 , pp. 977-988
    • Lutz, M.1    Knaus, P.2
  • 41
    • 0037013742 scopus 로고    scopus 로고
    • Mechanisms of TGF-beta signaling in regulation of cell growth and differentiation
    • A. Moustakas, K. Pardali, A. Gaal, and C.H. Heldin Mechanisms of TGF-beta signaling in regulation of cell growth and differentiation Immunol. Lett. 82 2002 85 91
    • (2002) Immunol. Lett. , vol.82 , pp. 85-91
    • Moustakas, A.1    Pardali, K.2    Gaal, A.3    Heldin, C.H.4
  • 42
    • 0038636430 scopus 로고    scopus 로고
    • Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin
    • D. Joulia, H. Bernardi, V. Garandel, F. Rabenoelina, B. Vernus, and G. Cabello Mechanisms involved in the inhibition of myoblast proliferation and differentiation by myostatin Exp. Cell Res. 286 2003 263 275
    • (2003) Exp. Cell Res. , vol.286 , pp. 263-275
    • Joulia, D.1    Bernardi, H.2    Garandel, V.3    Rabenoelina, F.4    Vernus, B.5    Cabello, G.6
  • 43
    • 0141768237 scopus 로고    scopus 로고
    • Myostatin negatively regulates satellite cell activation and self-renewal
    • S. McCroskery, M. Thomas, L. Maxwell, M. Sharma, and R. Kambadur Myostatin negatively regulates satellite cell activation and self-renewal J. Cell Biol. 162 2003 1135 1147
    • (2003) J. Cell Biol. , vol.162 , pp. 1135-1147
    • McCroskery, S.1    Thomas, M.2    Maxwell, L.3    Sharma, M.4    Kambadur, R.5
  • 45
    • 0028822797 scopus 로고
    • Heparin modulates the binding of insulin-like growth factor (IGF) binding protein-5 to a membrane protein in osteoblastic cells
    • D.L. Andress Heparin modulates the binding of insulin-like growth factor (IGF) binding protein-5 to a membrane protein in osteoblastic cells J. Biol. Chem. 270 1995 28289 28296
    • (1995) J. Biol. Chem. , vol.270 , pp. 28289-28296
    • Andress, D.L.1
  • 46
    • 0031958404 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein-5 (IGFBP-5) stimulates phosphorylation of the IGFBP-5 receptor
    • D.L. Andress Insulin-like growth factor-binding protein-5 (IGFBP-5) stimulates phosphorylation of the IGFBP-5 receptor Am. J. Physiol. 274 1998 E744 E750
    • (1998) Am. J. Physiol. , vol.274
    • Andress, D.L.1
  • 47
    • 0037036404 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein-5 (IGFBP-5) stimulates growth and IGF-I secretion in human intestinal smooth muscle by Ras-dependent activation of p38 MAP kinase and Erk1/2 pathways
    • J.F. Kuemmerle, and H. Zhou Insulin-like growth factor-binding protein-5 (IGFBP-5) stimulates growth and IGF-I secretion in human intestinal smooth muscle by Ras-dependent activation of p38 MAP kinase and Erk1/2 pathways J. Biol. Chem. 277 2002 20563 20571
    • (2002) J. Biol. Chem. , vol.277 , pp. 20563-20571
    • Kuemmerle, J.F.1    Zhou, H.2
  • 48
    • 0037474298 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein-3 potentiates epidermal growth factor action in MCF-10A mammary epithelial cells. Involvement of p44/42 and p38 mitogen-activated protein kinases
    • J.L. Martin, S.M. Weenink, and R.C. Baxter Insulin-like growth factor-binding protein-3 potentiates epidermal growth factor action in MCF-10A mammary epithelial cells. Involvement of p44/42 and p38 mitogen-activated protein kinases J. Biol. Chem. 278 2003 2969 2976
    • (2003) J. Biol. Chem. , vol.278 , pp. 2969-2976
    • Martin, J.L.1    Weenink, S.M.2    Baxter, R.C.3
  • 49
    • 0034604529 scopus 로고    scopus 로고
    • Nuclear import of insulin-like growth factor-binding protein-3 and -5 is mediated by the importin beta subunit
    • L.J. Schedlich, S.L. Le Page, S.M. Firth, L.J. Briggs, D.A. Jans, and R.C. Baxter Nuclear import of insulin-like growth factor-binding protein-3 and -5 is mediated by the importin beta subunit J. Biol. Chem. 275 2000 23462 23470
    • (2000) J. Biol. Chem. , vol.275 , pp. 23462-23470
    • Schedlich, L.J.1    Le Page, S.L.2    Firth, S.M.3    Briggs, L.J.4    Jans, D.A.5    Baxter, R.C.6
  • 50
    • 0034721879 scopus 로고    scopus 로고
    • Direct functional interactions between insulin-like growth factor-binding protein-3 and retinoid X receptor-alpha regulate transcriptional signaling and apoptosis
    • B. Liu, H.Y. Lee, S.A. Weinzimer, D.R. Powell, J.L. Clifford, J.M. Kurie, and P. Cohen Direct functional interactions between insulin-like growth factor-binding protein-3 and retinoid X receptor-alpha regulate transcriptional signaling and apoptosis J. Biol. Chem. 275 2000 33607 33613
    • (2000) J. Biol. Chem. , vol.275 , pp. 33607-33613
    • Liu, B.1    Lee, H.Y.2    Weinzimer, S.A.3    Powell, D.R.4    Clifford, J.L.5    Kurie, J.M.6    Cohen, P.7
  • 51
    • 0037023685 scopus 로고    scopus 로고
    • Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2)
    • Y.G. Amaar, G.R. Thompson, T.A. Linkhart, S.T. Chen, D.J. Baylink, and S. Mohan Insulin-like growth factor-binding protein 5 (IGFBP-5) interacts with a four and a half LIM protein 2 (FHL2) J. Biol. Chem. 277 2002 12053 12060
    • (2002) J. Biol. Chem. , vol.277 , pp. 12053-12060
    • Amaar, Y.G.1    Thompson, G.R.2    Linkhart, T.A.3    Chen, S.T.4    Baylink, D.J.5    Mohan, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.