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Volumn 25, Issue 9, 2011, Pages 1636-1649

IGF-I stimulates cooperative interaction between the IGF-I receptor and CSK homologous kinase that regulates SHPS-1 phosphorylation in vascular smooth muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEOME; SOMATOMEDIN C; SOMATOMEDIN C RECEPTOR;

EID: 80052280239     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2011-0035     Document Type: Article
Times cited : (15)

References (44)
  • 1
    • 0029392515 scopus 로고
    • The insulinlike growth factor system in vascular smooth muscle: Interaction with insulin and growth factors
    • Arnqvist HJ, Bornfeldt KE, Chen Y, Lindström T 1995 The insulinlike growth factor system in vascular smooth muscle: interaction with insulin and growth factors. Metabolism 44:58-66.
    • (1995) Metabolism , vol.44 , pp. 58-66
    • Arnqvist, H.J.1    Bornfeldt, K.E.2    Chen, Y.3    Lindström, T.4
  • 3
    • 77952379818 scopus 로고    scopus 로고
    • Insulin-like growth factor-I-stimulated insulin receptor substrate-1 negatively regulates Src homology 2 domain-containing protein-tyrosine phosphatase substrate-1 function in vascular smooth muscle cells
    • Radhakrishnan Y, Busby Jr WH, Shen X, Maile LA, Clemmons DR 2010 Insulin-like growth factor-I-stimulated insulin receptor substrate-1 negatively regulates Src homology 2 domain-containing protein-tyrosine phosphatase substrate-1 function in vascular smooth muscle cells. J Biol Chem 285:15682-15695.
    • (2010) J Biol Chem , vol.285 , pp. 15682-15695
    • Radhakrishnan, Y.1    Busby, W.H.2    Shen, X.3    Maile, L.A.4    Clemmons, D.R.5
  • 4
    • 70349162087 scopus 로고    scopus 로고
    • ClemmonsDR2009 Identification of novel SHPS-1-associated proteins and their roles in regulation of insulin-like growth factor-dependent responses in vascular smooth muscle cells
    • Shen X, Xi G, Radhakrishnan Y, ClemmonsDR2009 Identification of novel SHPS-1-associated proteins and their roles in regulation of insulin-like growth factor-dependent responses in vascular smooth muscle cells. Mol Cell Proteomics 8:1539-1551
    • Mol Cell Proteomics , vol.8 , pp. 1539-1551
    • Shen, X.1    Xi, G.2    Radhakrishnan, Y.3
  • 5
    • 21844459734 scopus 로고    scopus 로고
    • Role of SHPS-1 in the regulation of insulin-like growth factor I-stimulated Shc and mitogen-activated protein kinase activation in vascular smooth muscle cells
    • Ling Y, Maile LA, Lieskovska J, Badley-Clarke J, Clemmons DR 2005 Role of SHPS-1 in the regulation of insulin-like growth factor I-stimulated Shc and mitogen-activated protein kinase activation in vascular smooth muscle cells. Mol Biol Cell 16:3353-3364.
    • (2005) Mol Biol Cell , vol.16 , pp. 3353-3364
    • Ling, Y.1    Maile, L.A.2    Lieskovska, J.3    Badley-Clarke, J.4    Clemmons, D.R.5
  • 6
    • 43049104174 scopus 로고    scopus 로고
    • Glucose regulation of integrin-associated protein cleavage controls the response of vascular smooth muscle cells to insulin-like growth factor-I
    • Maile LA, Capps BE, Miller EC, Allen LB, Veluvolu U, Aday AW, Clemmons DR 2008 Glucose regulation of integrin-associated protein cleavage controls the response of vascular smooth muscle cells to insulin-like growth factor-I. Mol Endocrinol 22:1226-1237.
    • (2008) Mol Endocrinol , vol.22 , pp. 1226-1237
    • Maile, L.A.1    Capps, B.E.2    Miller, E.C.3    Allen, L.B.4    Veluvolu, U.5    Aday, A.W.6    Clemmons, D.R.7
  • 7
    • 34249794018 scopus 로고    scopus 로고
    • Hyperglycemia alters the responsiveness of smooth muscle cells to insulinlike growth factor-I
    • Maile LA, Capps BE, Ling Y, Xi G, Clemmons DR 2007 Hyperglycemia alters the responsiveness of smooth muscle cells to insulinlike growth factor-I. Endocrinology 148:2435-2443.
    • (2007) Endocrinology , vol.148 , pp. 2435-2443
    • Maile, L.A.1    Capps, B.E.2    Ling, Y.3    Xi, G.4    Clemmons, D.R.5
  • 8
    • 47749131217 scopus 로고    scopus 로고
    • Insulin-like growth factor-I stimulates Shc-dependent phosphatidylinositol 3-kinase activation via Grb2-associated p85 in vascular smooth muscle cells
    • Radhakrishnan Y, Maile LA, Ling Y, Graves LM, Clemmons DR 2008 Insulin-like growth factor-I stimulates Shc-dependent phosphatidylinositol 3-kinase activation via Grb2-associated p85 in vascular smooth muscle cells. J Biol Chem 283:16320-16331.
    • (2008) J Biol Chem , vol.283 , pp. 16320-16331
    • Radhakrishnan, Y.1    Maile, L.A.2    Ling, Y.3    Graves, L.M.4    Clemmons, D.R.5
  • 9
    • 0034464025 scopus 로고    scopus 로고
    • Functional trans-inactivation of insulin receptor kinase by growth-inhibitory angiotensin II AT2 receptor
    • Elbaz N, Bedecs K, Masson M, Sutren M, Strosberg AD, Nahmias C 2000 Functional trans-inactivation of insulin receptor kinase by growth-inhibitory angiotensin II AT2 receptor. Mol Endocrinol 14: 795-804.
    • (2000) Mol Endocrinol , vol.14 , pp. 795-804
    • Elbaz, N.1    Bedecs, K.2    Masson, M.3    Sutren, M.4    Strosberg, A.D.5    Nahmias, C.6
  • 10
    • 0030893120 scopus 로고    scopus 로고
    • A family of proteins that inhibit signalling through tyrosine kinase receptors
    • Kharitonenkov A, Chen Z, Sures I, Wang H, Schilling J, Ullrich A 1997 A family of proteins that inhibit signalling through tyrosine kinase receptors. Nature 386:181-186.
    • (1997) Nature , vol.386 , pp. 181-186
    • Kharitonenkov, A.1    Chen, Z.2    Sures, I.3    Wang, H.4    Schilling, J.5    Ullrich, A.6
  • 11
    • 0029860950 scopus 로고    scopus 로고
    • A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion
    • Fujioka Y, Matozaki T, Noguchi T, Iwamatsu A, Yamao T, Takahashi N, Tsuda M, Takada T, Kasuga M 1996 A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion. Mol Cell Biol 16:6887-6899.
    • (1996) Mol Cell Biol , vol.16 , pp. 6887-6899
    • Fujioka, Y.1    Matozaki, T.2    Noguchi, T.3    Iwamatsu, A.4    Yamao, T.5    Takahashi, N.6    Tsuda, M.7    Takada, T.8    Kasuga, M.9
  • 12
    • 0032549527 scopus 로고    scopus 로고
    • Growth hormone regulation of SIRP and SHP-2 tyrosyl phosphorylation and association
    • Stofega MR, Wang H, Ullrich A, Carter-Su C 1998 Growth hormone regulation of SIRP and SHP-2 tyrosyl phosphorylation and association. J Biol Chem 273:7112-7117.
    • (1998) J Biol Chem , vol.273 , pp. 7112-7117
    • Stofega, M.R.1    Wang, H.2    Ullrich, A.3    Carter-Su, C.4
  • 13
    • 41149180888 scopus 로고    scopus 로고
    • Csk-homologous kinase interacts with SHPS-1 and enhances neurite outgrowth of PC12 cells
    • Mitsuhashi H, Futai E, Sasagawa N, Hayashi Y, Nishino I, Ishiura S 2008 Csk-homologous kinase interacts with SHPS-1 and enhances neurite outgrowth of PC12 cells. J Neurochem 105:101-112.
    • (2008) J Neurochem , vol.105 , pp. 101-112
    • Mitsuhashi, H.1    Futai, E.2    Sasagawa, N.3    Hayashi, Y.4    Nishino, I.5    Ishiura, S.6
  • 16
    • 0027965251 scopus 로고
    • Identification and characterization of Batk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk
    • Kuo SS, Moran P, Gripp J, Armanini M, Phillips HS, Goddard A, Caras IW 1994 Identification and characterization of Batk, a predominantly brain-specific non-receptor protein tyrosine kinase related to Csk. J Neurosci Res 38:705-715.
    • (1994) J Neurosci Res , vol.38 , pp. 705-715
    • Kuo, S.S.1    Moran, P.2    Gripp, J.3    Armanini, M.4    Phillips, H.S.5    Goddard, A.6    Caras, I.W.7
  • 19
    • 0028347585 scopus 로고
    • Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase)
    • Sakano S, Iwama A, Inazawa J, Ariyama T, Ohno M, Suda T 1994 Molecular cloning of a novel non-receptor tyrosine kinase, HYL (hematopoietic consensus tyrosine-lacking kinase). Oncogene 9:1155-1161.
    • (1994) Oncogene , vol.9 , pp. 1155-1161
    • Sakano, S.1    Iwama, A.2    Inazawa, J.3    Ariyama, T.4    Ohno, M.5    Suda, T.6
  • 20
    • 0037184030 scopus 로고    scopus 로고
    • Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer
    • Kim S, Zagozdzon R, Meisler A, Baleja JD, Fu Y, Avraham S, Avraham H 2002 Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer. J Biol Chem 277:36465-36470.
    • (2002) J Biol Chem , vol.277 , pp. 36465-36470
    • Kim, S.1    Zagozdzon, R.2    Meisler, A.3    Baleja, J.D.4    Fu, Y.5    Avraham, S.6    Avraham, H.7
  • 21
    • 0031438179 scopus 로고    scopus 로고
    • Csk and BatK show opposite temporal expression in the rat CNS: Consistent with its late expression in development, BatK induces differentiation of PC12 cells
    • Kuo SS, Armanini MP, Phillips HS, Caras IW 1997 Csk and BatK show opposite temporal expression in the rat CNS: consistent with its late expression in development, BatK induces differentiation of PC12 cells. Eur J Neurosci 9:2383-2393.
    • (1997) Eur J Neurosci , vol.9 , pp. 2383-2393
    • Kuo, S.S.1    Armanini, M.P.2    Phillips, H.S.3    Caras, I.W.4
  • 22
    • 0033591229 scopus 로고    scopus 로고
    • The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells
    • Yamashita H, Avraham S, Jiang S, Dikic I, Avraham H 1999 The Csk homologous kinase associates with TrkA receptors and is involved in neurite outgrowth of PC12 cells. J Biol Chem 274:15059-15065.
    • (1999) J Biol Chem , vol.274 , pp. 15059-15065
    • Yamashita, H.1    Avraham, S.2    Jiang, S.3    Dikic, I.4    Avraham, H.5
  • 23
    • 0031048834 scopus 로고    scopus 로고
    • Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes
    • Price DJ, Rivnay B, Fu Y, Jiang S, Avraham S, Avraham H 1997 Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. J Biol Chem 272:5915-5920.
    • (1997) J Biol Chem , vol.272 , pp. 5915-5920
    • Price, D.J.1    Rivnay, B.2    Fu, Y.3    Jiang, S.4    Avraham, S.5    Avraham, H.6
  • 24
    • 58149340146 scopus 로고    scopus 로고
    • Integrin-associated protein association with SRC homology 2 domain containing tyrosine phosphatase substrate 1 regulates IGF-I signaling in vivo
    • Maile LA, Capps BE, Miller EC, Aday AW, Clemmons DR 2008 Integrin-associated protein association with SRC homology 2 domain containing tyrosine phosphatase substrate 1 regulates IGF-I signaling in vivo. Diabetes 57:2637-2643.
    • (2008) Diabetes , vol.57 , pp. 2637-2643
    • Maile, L.A.1    Capps, B.E.2    Miller, E.C.3    Aday, A.W.4    Clemmons, D.R.5
  • 25
    • 33748751592 scopus 로고    scopus 로고
    • The role of Src kinase in insulin-like growth factor-dependent mitogenic signaling in vascular smooth muscle cells
    • Lieskovska J, Ling Y, Badley-Clarke J, Clemmons DR 2006 The role of Src kinase in insulin-like growth factor-dependent mitogenic signaling in vascular smooth muscle cells. J Biol Chem 281:25041-25053.
    • (2006) J Biol Chem , vol.281 , pp. 25041-25053
    • Lieskovska, J.1    Ling, Y.2    Badley-Clarke, J.3    Clemmons, D.R.4
  • 27
    • 51849180729 scopus 로고
    • Insulin and IGF-I stimulate phosphorylation of their respective receptors in intact neuronal and glial cells in primary culture
    • Shemer J, Adamo M, Raizada MK, Heffez D, Zick Y, LeRoith D 1989 Insulin and IGF-I stimulate phosphorylation of their respective receptors in intact neuronal and glial cells in primary culture. J Mol Neurosci 1:3-8.
    • (1989) J Mol Neurosci , vol.1 , pp. 3-8
    • Shemer, J.1    Adamo, M.2    Raizada, M.K.3    Heffez, D.4    Zick, Y.5    Leroith, D.6
  • 28
    • 0037088639 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor I receptor dephosphorylation by SHPS-1 and the tyrosine phosphatase SHP-2
    • Maile LA, Clemmons DR 2002 Regulation of insulin-like growth factor I receptor dephosphorylation by SHPS-1 and the tyrosine phosphatase SHP-2. J Biol Chem 277:8955-8960.
    • (2002) J Biol Chem , vol.277 , pp. 8955-8960
    • Maile, L.A.1    Clemmons, D.R.2
  • 29
    • 0141521689 scopus 로고    scopus 로고
    • The association between integrin-associated protein and SHPS-1 regulates insulinlike growth factor-I receptor signaling in vascular smooth muscle cells
    • Maile LA, Badley-Clarke J, Clemmons DR 2003 The association between integrin-associated protein and SHPS-1 regulates insulinlike growth factor-I receptor signaling in vascular smooth muscle cells. Mol Biol Cell 14:3519-3528.
    • (2003) Mol Biol Cell , vol.14 , pp. 3519-3528
    • Maile, L.A.1    Badley-Clarke, J.2    Clemmons, D.R.3
  • 30
    • 70449677662 scopus 로고    scopus 로고
    • Human aortic smooth muscle cells are insulin resistant at the receptor level but sensitive to IGF1 and IGF2
    • Chisalita SI, Johansson GS, Liefvendahl E, Bäck K, Arnqvist HJ 2009 Human aortic smooth muscle cells are insulin resistant at the receptor level but sensitive to IGF1 and IGF2. J Mol Endocrinol 43:231-239.
    • (2009) J Mol Endocrinol , vol.43 , pp. 231-239
    • Chisalita, S.I.1    Johansson, G.S.2    Liefvendahl, E.3    Bäck, K.4    Arnqvist, H.J.5
  • 31
    • 21844465391 scopus 로고    scopus 로고
    • Functional diversity of Csk, Chk, and Src SH2 domains due to a single residue variation
    • Ayrapetov MK, Nam NH, Ye G, Kumar A, Parang K, Sun G 2005 Functional diversity of Csk, Chk, and Src SH2 domains due to a single residue variation. J Biol Chem 280:25780-25787.
    • (2005) J Biol Chem , vol.280 , pp. 25780-25787
    • Ayrapetov, M.K.1    Nam, N.H.2    Ye, G.3    Kumar, A.4    Parang, K.5    Sun, G.6
  • 32
    • 0038695015 scopus 로고    scopus 로고
    • Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK
    • Mikkola ET, Bergman M 2003 Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK. FEBS Lett 544:11-14.
    • (2003) FEBS Lett , vol.544 , pp. 11-14
    • Mikkola, E.T.1    Bergman, M.2
  • 34
    • 34047227257 scopus 로고    scopus 로고
    • Control of apoptosis in human multiple myeloma by insulin-like growth factor I (IGF-I)
    • Jernberg-Wiklund H, Nilsson K 2007 Control of apoptosis in human multiple myeloma by insulin-like growth factor I (IGF-I). Adv Cancer Res 97:139-165.
    • (2007) Adv Cancer Res , vol.97 , pp. 139-165
    • Jernberg-Wiklund, H.1    Nilsson, K.2
  • 35
    • 70449435684 scopus 로고    scopus 로고
    • The tyrosine kinase Csk dimerizes through its SH3 domain
    • Levinson NM, Visperas PR, Kuriyan J 2009 The tyrosine kinase Csk dimerizes through its SH3 domain. PLoS One 4:e7683
    • (2009) PLoS One , vol.4
    • Levinson, N.M.1    Visperas, P.R.2    Kuriyan, J.3
  • 36
    • 32144460477 scopus 로고    scopus 로고
    • C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) endogenous negative regulators of Src-family protein kinases
    • Chong YP, Mulhern TD, Cheng HC 2005 C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) endogenous negative regulators of Src-family protein kinases. Growth Factors 23:233-244.
    • (2005) Growth Factors , vol.23 , pp. 233-244
    • Chong, Y.P.1    Mulhern, T.D.2    Cheng, H.C.3
  • 39
    • 32144437781 scopus 로고    scopus 로고
    • Csk homologous kinase (CHK), unlike Csk, enhances MAPK activation via Ras-mediated signaling in a Src-independent manner
    • Zagozdzon R, Kaminski R, Fu Y, Fu W, Bougeret C, Avraham HK 2006 Csk homologous kinase (CHK), unlike Csk, enhances MAPK activation via Ras-mediated signaling in a Src-independent manner. Cell Signal 18:871-881
    • (2006) Cell Signal , vol.18 , pp. 871-881
    • Zagozdzon, R.1    Kaminski, R.2    Fu, Y.3    Fu, W.4    Bougeret, C.5    Avraham, H.K.6
  • 40
    • 1842834301 scopus 로고    scopus 로고
    • Overexpression of the Csk homologous kinase facilitates phosphorylation of Akt/PKB in MCF-7 cells
    • Zagozdzon R, Bougeret C, Fu Y, Avraham HK 2002 Overexpression of the Csk homologous kinase facilitates phosphorylation of Akt/PKB in MCF-7 cells. Int J Oncol 21:1347-1352.
    • (2002) Int J Oncol , vol.21 , pp. 1347-1352
    • Zagozdzon, R.1    Bougeret, C.2    Fu, Y.3    Avraham, H.K.4
  • 41
    • 0028893184 scopus 로고    scopus 로고
    • LeRoithD1995 Mutation of a conserved amino acid residue (tryptophan 1173) in the tyrosine kinase domain of the IGF-I receptor abolishes autophosphorylation but does not eliminate biologic function
    • Blakesley VA, Kato H, Roberts Jr CT, LeRoithD1995 Mutation of a conserved amino acid residue (tryptophan 1173) in the tyrosine kinase domain of the IGF-I receptor abolishes autophosphorylation but does not eliminate biologic function. J Biol Chem 270:2764-2769.
    • J Biol Chem , vol.270 , pp. 2764-2769
    • Blakesley, V.A.1    Kato, H.2    Roberts, C.T.3
  • 42
    • 0036121371 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts
    • Buckley DA, Cheng A, Kiely PA, Tremblay ML, O'Connor R 2002 Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts. Mol Cell Biol 22:1998-2010.
    • (2002) Mol Cell Biol , vol.22 , pp. 1998-2010
    • Buckley, D.A.1    Cheng, A.2    Kiely, P.A.3    Tremblay, M.L.4    O'Connor, R.5
  • 43
    • 0034455127 scopus 로고    scopus 로고
    • Thrombospondin and osteopontin bind to insulin-like growth factor (IGF)-binding protein-5 leading to an alteration in IGF-I-stimulated cell growth
    • Nam TJ, Busby Jr WH, Rees C, Clemmons DR 2000 Thrombospondin and osteopontin bind to insulin-like growth factor (IGF)-binding protein-5 leading to an alteration in IGF-I-stimulated cell growth. Endocrinology 141:1100-1106.
    • (2000) Endocrinology , vol.141 , pp. 1100-1106
    • Nam, T.J.1    Busby, W.H.2    Rees, C.3    Clemmons, D.R.4
  • 44
    • 0029867915 scopus 로고    scopus 로고
    • Ligand occupancy of the α-V-β3 integrin is necessary for smooth muscle cells to migrate in response to insulin-like growth factor
    • Jones JI, Prevette T, Gockerman A, Clemmons DR 1996 Ligand occupancy of the α-V-β3 integrin is necessary for smooth muscle cells to migrate in response to insulin-like growth factor. Proc Natl Acad Sci USA 93:2482-2487
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2482-2487
    • Jones, J.I.1    Prevette, T.2    Gockerman, A.3    Clemmons, D.R.4


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