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Volumn 14, Issue 9, 2003, Pages 3519-3528

The association between integrin-associated protein and SHPS-1 regulates insulin-like growth factor-I receptor signaling in vascular smooth muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

CD47 ANTIGEN; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MONOCLONAL ANTIBODY; PLATELET DERIVED GROWTH FACTOR; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE SUBSTRATE 1; SOMATOMEDIN C; SOMATOMEDIN C RECEPTOR; UNCLASSIFIED DRUG;

EID: 0141521689     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-04-0239     Document Type: Article
Times cited : (44)

References (38)
  • 2
    • 0034177519 scopus 로고    scopus 로고
    • SHPS-1 induces aggregation of Ba/F3 pro-B cells via an interaction with CD47
    • Babic, I., Schallhorn, A., Lindberg, F.P., and Jirik, F.R. (2000). SHPS-1 induces aggregation of Ba/F3 pro-B cells via an interaction with CD47. J. Immunol. 164, 3652-3658.
    • (2000) J. Immunol. , vol.164 , pp. 3652-3658
    • Babic, I.1    Schallhorn, A.2    Lindberg, F.P.3    Jirik, F.R.4
  • 3
    • 0025666501 scopus 로고
    • Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins
    • Brown, E., Hooper, L., Ho, T., and Gresham, H. (1990). Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins. J. Cell Biol. 111, 2785-2794.
    • (1990) J. Cell Biol. , vol.111 , pp. 2785-2794
    • Brown, E.1    Hooper, L.2    Ho, T.3    Gresham, H.4
  • 4
    • 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., and 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
  • 5
    • 0029125685 scopus 로고
    • Insulin-like growth factor (IGF)-binding proteins inhibit the smooth muscle cell migration responses to IGF-I and IGF-II
    • Gockerman, A., Prevette, T., Jones, J.I., and Clemmons, D.R. (1995). Insulin-like growth factor (IGF)-binding proteins inhibit the smooth muscle cell migration responses to IGF-I and IGF-II. Endocrinology 136, 4168-4173.
    • (1995) Endocrinology , vol.136 , pp. 4168-4173
    • Gockerman, A.1    Prevette, T.2    Jones, J.I.3    Clemmons, D.R.4
  • 6
    • 0030734794 scopus 로고    scopus 로고
    • Protease-resistant form of insulin-like growth factor-binding protein 5 is an inhibitor of insulin-like growth factor-I actions on porcine smooth muscle cells in culture
    • Imai, Y., Busby, W.H., Jr., Smith, C.E., Clarke, J.B., Garmong, A.J., Horwitz, G.D., Rees, C., and Clemmons, D.R. (1997). Protease-resistant form of insulin-like growth factor-binding protein 5 is an inhibitor of insulin-like growth factor-I actions on porcine smooth muscle cells in culture. J. Clin. Investig. 100, 2596-2605.
    • (1997) J. Clin. Investig. , vol.100 , pp. 2596-2605
    • Imai, Y.1    Busby W.H., Jr.2    Smith, C.E.3    Clarke, J.B.4    Garmong, A.J.5    Horwitz, G.D.6    Rees, C.7    Clemmons, D.R.8
  • 7
    • 0033304619 scopus 로고    scopus 로고
    • Roles of phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways in stimulation of vascular smooth muscle cell migration and deoxyribonucleic acid synthesis by insulin-like growth factor-I
    • Imai, Y., and Clemmons, D.R. (1999). Roles of phosphatidylinositol 3-kinase and mitogen-activated protein kinase pathways in stimulation of vascular smooth muscle cell migration and deoxyribonucleic acid synthesis by insulin-like growth factor-I. Endocrinology 140, 4228-42235.
    • (1999) Endocrinology , vol.140 , pp. 4228-42235
    • Imai, Y.1    Clemmons, D.R.2
  • 8
    • 0033534716 scopus 로고    scopus 로고
    • Integrin-associated protein is a ligand for the P84 neural adhesion molecule
    • Jiang, P., Lagenaur, C.F., and Narayanan, V. (1999). Integrin-associated protein is a ligand for the P84 neural adhesion molecule. J. Biol. Chem. 274, 559-562.
    • (1999) J. Biol. Chem. , vol.274 , pp. 559-562
    • Jiang, P.1    Lagenaur, C.F.2    Narayanan, V.3
  • 9
    • 0029867915 scopus 로고    scopus 로고
    • Ligand occupancy of the alpha-V-beta3 integrin is necessary for smooth muscle cells to migrate in response to insulin-like growth factor
    • Jones, J.I., Prevette, T., Gockerman, A., and Clemmons, D.R. (1996). Ligand occupancy of the alpha-V-beta3 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
  • 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., and 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
    • 0031692910 scopus 로고    scopus 로고
    • Density- and proliferation status- dependent expression of T-cadherin, a novel lipoprotein-binding glycoprotein: A function in negative regulation of smooth muscle cell growth?
    • Kuzmenko, Y., Kern, F., Bochkov, V., Tkachuk, V., and Resink, T. (1998). Density- and proliferation status- dependent expression of T-cadherin, a novel lipoprotein-binding glycoprotein: a function in negative regulation of smooth muscle cell growth? FEBS Lett. 434, 183-187.
    • (1998) FEBS Lett. , vol.434 , pp. 183-187
    • Kuzmenko, Y.1    Kern, F.2    Bochkov, V.3    Tkachuk, V.4    Resink, T.5
  • 12
    • 0036826862 scopus 로고    scopus 로고
    • The alphaVbeta3 integrin regulates insulin-like growth factor I (IGF-I) receptor phosphorylation by altering the rate of recruitment of the Src-homology 2-containing phosphotyrosine phosphatase-2 to the activated IGF-I receptor
    • Maile, L.A., and Clemmons, D.R. (2002a). The alphaVbeta3 integrin regulates insulin-like growth factor I (IGF-I) receptor phosphorylation by altering the rate of recruitment of the Src-homology 2-containing phosphotyrosine phosphatase-2 to the activated IGF-I receptor. Endocr. J. 143, 4259-4264.
    • (2002) Endocr. J. , vol.143 , pp. 4259-4264
    • Maile, L.A.1    Clemmons, D.R.2
  • 13
    • 0037088639 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor I receptor dephosphorylation by SHPS-1 and the tyrosine phosphatase SHP-2
    • Maile, L.A., and Clemmons, D.R. (2002b). 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
  • 14
    • 0037127193 scopus 로고    scopus 로고
    • Insulin-like growth factor I increases alphaVbeta 3 affinity by increasing the amount of integrin-associated protein that is associated with non-raft domains of the cellular membrane
    • Maile, L.A., Imai, Y., Clarke, J,B., and Clemmons, D.R. (2002). Insulin-like growth factor I increases alphaVbeta 3 affinity by increasing the amount of integrin-associated protein that is associated with non-raft domains of the cellular membrane. J. Biol. Chem. 277, 1800-1805.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1800-1805
    • Maile, L.A.1    Imai, Y.2    Clarke, J.B.3    Clemmons, D.R.4
  • 15
    • 0039441744 scopus 로고    scopus 로고
    • Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase regulation of cell motility
    • Manes, S., Mira, E., Gomez-Mouton, C., Zhao, Z.J., Lacalle, R.A., and Martinez, A.C. (1999). Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase regulation of cell motility. Mol. Cell. Biol. 4, 3125-3135.
    • (1999) Mol. Cell. Biol. , vol.4 , pp. 3125-3135
    • Manes, S.1    Mira, E.2    Gomez-Mouton, C.3    Zhao, Z.J.4    Lacalle, R.A.5    Martinez, A.C.6
  • 16
    • 0035955627 scopus 로고    scopus 로고
    • IGF-I receptor induced cell-cell adhesion of MCF-7 breast cancer cells requires the expression of ZO-1
    • Mauro, L., Bartucci, M., Morelli, C., Ando', S., and Surmacz, E. (2001). IGF-I receptor induced cell-cell adhesion of MCF-7 breast cancer cells requires the expression of ZO-1. J. Biol. Chem. 276, 39892-39897.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39892-39897
    • Mauro, L.1    Bartucci, M.2    Morelli, C.3    Ando', S.4    Surmacz, E.5
  • 17
    • 0037292936 scopus 로고    scopus 로고
    • Role of the IGF-I receptor in the regulation of cell-cell adhesion: Implications in cancer development and progression
    • Mauro, L., Salerno, M., Morelli, C., Boterberg, T., Bracke, M., and Surmacz, E. (2003). Role of the IGF-I receptor in the regulation of cell-cell adhesion: implications in cancer development and progression. J. Cell Physiol. 194, 108-116.
    • (2003) J. Cell Physiol. , vol.194 , pp. 108-116
    • Mauro, L.1    Salerno, M.2    Morelli, C.3    Boterberg, T.4    Bracke, M.5    Surmacz, E.6
  • 18
    • 0028136280 scopus 로고
    • Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin
    • Milarski, K.L., and Saltiel, A.R. (1994). Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin. J. Biol. Chem. 269, 21239-21243.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21239-21243
    • Milarski, K.L.1    Saltiel, A.R.2
  • 19
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., Teramoto, H., Gutkind, J.S., and Yamada, K.M. (1996). Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135, 1633-1642.
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 20
    • 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, T., Busby, W.H., Jr., Rees, C., and Clemmons, D.R. (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.1    Busby W.H., Jr.2    Rees, C.3    Clemmons, D.R.4
  • 21
    • 0029973602 scopus 로고    scopus 로고
    • Characterization of a 115-kDa protein that binds to SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in Chinese hamster ovary cells
    • Noguchi, T., Matozaki, T., Fujioka, Y., Yamao, T., Tsuda, M., Takada, T., and Kasuga, M. (1996). Characterization of a 115-kDa protein that binds to SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in Chinese hamster ovary cells. J. Biol. Chem. 271, 27652-27658.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27652-27658
    • Noguchi, T.1    Matozaki, T.2    Fujioka, Y.3    Yamao, T.4    Tsuda, M.5    Takada, T.6    Kasuga, M.7
  • 22
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation
    • Noguchi, T., Matozaki, T., Horita, K., Fujioka, Y., and Kasuga, M. (1994). Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated Ras activation. Mol. Cell. Biol. 14, 6674-6682.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 25
    • 0035860685 scopus 로고    scopus 로고
    • Normal ligand binding and signaling by CD47 (integrin associated protein) requires a long range disulphide bond between the extracellular and membrane-spanning domains
    • Rebres, R.A., Vaz, L.E., Green, J.M., and Brown, E.J. (2001). Normal ligand binding and signaling by CD47 (integrin associated protein) requires a long range disulphide bond between the extracellular and membrane-spanning domains. J. Biol. Chem. 276, 34607-34616.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34607-34616
    • Rebres, R.A.1    Vaz, L.E.2    Green, J.M.3    Brown, E.J.4
  • 26
    • 0026705149 scopus 로고
    • Expression of the 50-kDa integrin-associated protein on myeloid cells and erythrocytes
    • Rosales, C., Gresham, H.D., and Brown, E.J. (1992). Expression of the 50-kDa integrin-associated protein on myeloid cells and erythrocytes. J. Immunol. 149, 2759-2764.
    • (1992) J. Immunol. , vol.149 , pp. 2759-2764
    • Rosales, C.1    Gresham, H.D.2    Brown, E.J.3
  • 27
    • 0033485642 scopus 로고    scopus 로고
    • Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47
    • Seiffert, M., Cant, C., Chen, Z., Rappold, I., Brugger, W., Kanz, L., Brown, E.J., Ullrich, A., and Buhring, H.J. (1999). Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47. Blood 94, 3633-3643.
    • (1999) Blood , vol.94 , pp. 3633-3643
    • Seiffert, M.1    Cant, C.2    Chen, Z.3    Rappold, I.4    Brugger, W.5    Kanz, L.6    Brown, E.J.7    Ullrich, A.8    Buhring, H.J.9
  • 28
    • 0032549527 scopus 로고    scopus 로고
    • Growth hormone regulation of SIRP and SHP-2 tyrosyl phosphorylation and association
    • Stofega, M.R., Wang, H., Ullrich, A., and 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
  • 29
    • 0032502706 scopus 로고    scopus 로고
    • Roles of the complex formation of SHPS-1 with SHP-2 in insulin-stimulated mitogen-activated protein kinase activation
    • Takada, T., et al. (1998). Roles of the complex formation of SHPS-1 with SHP-2 in insulin-stimulated mitogen-activated protein kinase activation. J. Biol. Chem. 273, 9234-9242.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9234-9242
    • Takada, T.1
  • 30
    • 0029894305 scopus 로고    scopus 로고
    • Expression of dominant negative mutant SHPTP2 attenuates phosphatidylinositol 3′-kinase activity via modulation of phosphorylation of insulin receptor substrate-1
    • Ugi, S., Maegawa, H., Kashiwagi, A., Adachi, M., Olefsky, J.M., and Kikkawa, R. (1996). Expression of dominant negative mutant SHPTP2 attenuates phosphatidylinositol 3′-kinase activity via modulation of phosphorylation of insulin receptor substrate-1. J. Biol. Chem. 271, 12595-12602.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12595-12602
    • Ugi, S.1    Maegawa, H.2    Kashiwagi, A.3    Adachi, M.4    Olefsky, J.M.5    Kikkawa, R.6
  • 31
    • 0033846993 scopus 로고    scopus 로고
    • CD47 is a ligand for rat macrophage membrane signal regulatory protein SIRP (OX41) and human SIRPalpha 1
    • Vernon-Wilson, E.F., Kee, W.J., Willis, A.C., Barclay, A.N., Simmons, D.L., and Brown, M.H. (2000). CD47 is a ligand for rat macrophage membrane signal regulatory protein SIRP (OX41) and human SIRPalpha 1. Eur. J. Immunol. 30, 2130-2137.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 2130-2137
    • Vernon-Wilson, E.F.1    Kee, W.J.2    Willis, A.C.3    Barclay, A.N.4    Simmons, D.L.5    Brown, M.H.6
  • 32
    • 0035921728 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP-2 is required for mediating phosphatidylinositol 3-kinase/Akt activation by growth factors
    • Wu, C.J., O'Rourke, D.M., Feng, G.S., Johnson, G.R., Wang, Q., and Greene, M.I. (2001). The tyrosine phosphatase SHP-2 is required for mediating phosphatidylinositol 3-kinase/Akt activation by growth factors. Oncogene 20, 6018-6025.
    • (2001) Oncogene , vol.20 , pp. 6018-6025
    • Wu, C.J.1    O'Rourke, D.M.2    Feng, G.S.3    Johnson, G.R.4    Wang, Q.5    Greene, M.I.6
  • 34
    • 0028896991 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling
    • Yamauchi, K., Milarski, K.L., Saltiel, A.R., and Pessin, J.E. (1995). Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc. Natl. Acad. Sci USA 92, 664-668.
    • (1995) Proc. Natl. Acad. Sci USA , vol.92 , pp. 664-668
    • Yamauchi, K.1    Milarski, K.L.2    Saltiel, A.R.3    Pessin, J.E.4
  • 35
    • 0036533494 scopus 로고    scopus 로고
    • Interaction between Src homology 2 domain bearing protein tyrosine phosphatase substrate-1 and CD47 mediates the adhesion of human B lymphocytes to nonactivated endothelial cells
    • Yoshida, et al. (2002). Interaction between Src homology 2 domain bearing protein tyrosine phosphatase substrate-1 and CD47 mediates the adhesion of human B lymphocytes to nonactivated endothelial cells. J. Immunol. 168, 3213-3220.
    • (2002) J. Immunol. , vol.168 , pp. 3213-3220
    • Yoshida1
  • 36
    • 0036258332 scopus 로고    scopus 로고
    • Receptor-specific regulation of phosphatidylinositol 3′-kinase activation by the protein tyrosine phosphatase Shp2
    • Zhang, S.Q., Tsiaras, W.G., Araki, T., Wen, G., Minichiello, L., Klein, R., and Neel, B.G. (2002). Receptor-specific regulation of phosphatidylinositol 3′-kinase activation by the protein tyrosine phosphatase Shp2. Mol. Cell. Biol. 22, 4062-4072.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4062-4072
    • Zhang, S.Q.1    Tsiaras, W.G.2    Araki, T.3    Wen, G.4    Minichiello, L.5    Klein, R.6    Neel, B.G.7
  • 37
    • 0032530109 scopus 로고    scopus 로고
    • Blocking ligand occupancy of the alphaVbeta3 integrin inhibits insulin-like growth factor I signaling in vascular smooth muscle cells
    • Zheng, B., and Clemmons, D.R. (1998). Blocking ligand occupancy of the alphaVbeta3 integrin inhibits insulin-like growth factor I signaling in vascular smooth muscle cells. Proc. Natl. Acad. Sci. USA 95, 11217-11222.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11217-11222
    • Zheng, B.1    Clemmons, D.R.2
  • 38
    • 0034922869 scopus 로고    scopus 로고
    • Targeted overexpression of IGF-I in smooth muscle cells of transgenic mice enhances neointimal formation through increased proliferation and cell migration after intraarterial injury
    • Zhu, B., Zhao, G., Witte, D.P., Hui, D.Y., and Fagin, J.A. (2001). Targeted overexpression of IGF-I in smooth muscle cells of transgenic mice enhances neointimal formation through increased proliferation and cell migration after intraarterial injury. Endocrinology 142, 3598-3606.
    • (2001) Endocrinology , vol.142 , pp. 3598-3606
    • Zhu, B.1    Zhao, G.2    Witte, D.P.3    Hui, D.Y.4    Fagin, J.A.5


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