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Volumn 368, Issue 2, 2002, Pages 581-587

α1B-adrenergic receptor phosphorylation and desensitization induced by transforming growth factor-β

Author keywords

Adrenaline; Cross talk; Phosphoinositide 3 kinase; Protein kinase C

Indexed keywords

CELLS; ENZYME KINETICS; MUTAGENESIS;

EID: 0036882132     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021052     Document Type: Article
Times cited : (13)

References (46)
  • 1
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: An evolutionary success
    • Bockaert, J. and Pin, J. P. (1999) Molecular tinkering of G protein-coupled receptors: An evolutionary success. EMBO J. 18, 1723-1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 4
    • 0029874397 scopus 로고    scopus 로고
    • 1-adrenergic receptor subtypes. Molecular structure, function and signalling
    • 1-adrenergic receptor subtypes. Molecular structure, function and signalling. Circ. Res. 78, 737-749
    • (1996) Circ. Res. , vol.78 , pp. 737-749
    • Graham, R.M.1    Perez, D.M.2    Hwa, J.3    Piasck, M.T.4
  • 19
    • 0034574298 scopus 로고    scopus 로고
    • How cells read TGF-β signals
    • Massagué, J. (2000) How cells read TGF-β signals. Nat. Rev. Mol. Cell Biol. 1, 169-178
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 169-178
    • Massagué, J.1
  • 20
    • 0036467496 scopus 로고    scopus 로고
    • TGF-β signaling: Positive and negative effects on tumorigenesis
    • Wakefield, L. M. and Roberts, A. B. (2002) TGF-β signaling: Positive and negative effects on tumorigenesis. Curr. Opin. Genet. Dev. 12, 22-29
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 22-29
    • Wakefield, L.M.1    Roberts, A.B.2
  • 21
    • 0034104591 scopus 로고    scopus 로고
    • Smads as transcriptional co-modulators
    • Attisano, L. and Wrana, J. L. (2000) Smads as transcriptional co-modulators. Curr. Opin. Cell Biol. 12, 235-243
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 235-243
    • Attisano, L.1    Wrana, J.L.2
  • 22
    • 0037200041 scopus 로고    scopus 로고
    • Involvement of cell-cell interactions in the rapid stimulation of cas tyrosine phosphorylation and Src kinase activity by transforming growth factor-β1
    • Kim, J.-T. and Joo, C.-K. (2002) Involvement of cell-cell interactions in the rapid stimulation of cas tyrosine phosphorylation and Src kinase activity by transforming growth factor-β1. J. Biol. Chem. 277, 31938-31948
    • (2002) J. Biol. Chem. , vol.277 , pp. 31938-31948
    • Kim, J.-T.1    Joo, C.-K.2
  • 23
    • 0037127263 scopus 로고    scopus 로고
    • Transforming growth factor-β1 regulates Kir2.3 inward rectifier K+ channels via phospholipase C and protein kinase C-delta in reactive astrocytes from adult rat brain
    • Perillan, P. R., Chen, M., Potts, E. A. and Simard, J. M. (2002) Transforming growth factor-β1 regulates Kir2.3 inward rectifier K+ channels via phospholipase C and protein kinase C-delta in reactive astrocytes from adult rat brain. J. Biol. Chem. 277, 1974-1980
    • (2002) J. Biol. Chem. , vol.277 , pp. 1974-1980
    • Perillan, P.R.1    Chen, M.2    Potts, E.A.3    Simard, J.M.4
  • 24
    • 0032547233 scopus 로고    scopus 로고
    • Transforming growth factor-β1-induced activation of the raf-MEK-MAPK signaling pathway in rat lung fibroblasts via a PKC-dependent mechanism
    • Axmann, A., Seidel, D., Reimann, T., Hempel, U. and Wenzel, K.-W. (1998) Transforming growth factor-β1-induced activation of the raf-MEK-MAPK signaling pathway in rat lung fibroblasts via a PKC-dependent mechanism. Biochem. Biophys. Res. Commun. 249, 456-460
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 456-460
    • Axmann, A.1    Seidel, D.2    Reimann, T.3    Hempel, U.4    Wenzel, K.-W.5
  • 25
    • 0034711307 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase function is required for transforming growth factor β-mediated epithelial to mesenchymal transition and cell migration
    • Bakin, A. V., Tomlinson, A. K., Bhowmick, N. A., Moses, H. L. and Arteaga, C. L. (2000) Phosphatidylinositol 3-kinase function is required for transforming growth factor β-mediated epithelial to mesenchymal transition and cell migration. J. Biol. Chem. 275, 36803-36810
    • (2000) J. Biol. Chem. , vol.275 , pp. 36803-36810
    • Bakin, A.V.1    Tomlinson, A.K.2    Bhowmick, N.A.3    Moses, H.L.4    Arteaga, C.L.5
  • 26
    • 0031417544 scopus 로고    scopus 로고
    • TGF-β1 modulates EGF-stimulated phosphatidylinositol 3-kinase activity in human airway smooth muscle cells
    • Krymskaya, V. P., Hoffman, R., Eszterhas, A., Ciocca, V. and Panettieri, R. A. (1997) TGF-β1 modulates EGF-stimulated phosphatidylinositol 3-kinase activity in human airway smooth muscle cells. Am. J. Physiol. 273, L1220-L1227
    • (1997) Am. J. Physiol. , vol.273
    • Krymskaya, V.P.1    Hoffman, R.2    Eszterhas, A.3    Ciocca, V.4    Panettieri, R.A.5
  • 27
    • 0032868499 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for growth factor induced amino acid uptake by vascular smooth muscle cells
    • Higaki, M. and Shimokado, K. (1999) Phosphatidylinositol 3-kinase is required for growth factor induced amino acid uptake by vascular smooth muscle cells. Atherioscler. Thromb. Vasc. Biol. 19, 2127-2132
    • (1999) Atherioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2127-2132
    • Higaki, M.1    Shimokado, K.2
  • 29
    • 0029315177 scopus 로고
    • A simple procedure to increase efficiency of DEAE-dextran transfection of COS cells
    • González, A. L. and Joly, E. (1995) A simple procedure to increase efficiency of DEAE-dextran transfection of COS cells. Trends Genet. 11, 216-217
    • (1995) Trends Genet. , vol.11 , pp. 216-217
    • González, A.L.1    Joly, E.2
  • 31
    • 0020595443 scopus 로고
    • Changes in the level of inositol phosphates after agonist-dependent hydrolysis of membrane phospholipids
    • Berridge, M. J., Dawson, R. M. C., Downes, P., Heslop, J. P. and Irvine, R. F. (1983) Changes in the level of inositol phosphates after agonist-dependent hydrolysis of membrane phospholipids. Biochem. J. 212, 473-482
    • (1983) Biochem. J. , vol.212 , pp. 473-482
    • Berridge, M.J.1    Dawson, R.M.C.2    Downes, P.3    Heslop, J.P.4    Irvine, R.F.5
  • 33
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function and regulation
    • Newton, A. C. (1995) Protein kinase C: Structure, function and regulation. J. Biol. Chem. 270, 28495-28498
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 34
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK
    • Le Good, J. A., Ziegler, W. H., Parekh, D. B., Alessi, D. R., Cohen, P. and Parker, P. J. (1998) Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK. Science 281, 2042-2045
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 36
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies, S. P., Reddy, H., Caivano, M. and Cohen, P. (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351, 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 37
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinase
    • Wymann, M. P. and Pirola, L. (1998) Structure and function of phosphoinositide 3-kinase. Biochim. Biophys. Acta 1436, 127-150
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 40
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., Matter, W. F., Hui, K. Y. and Brown, R. F. (1994) A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269, 5241-5248
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 44
    • 0029802614 scopus 로고    scopus 로고
    • 2-adrenergic receptor in vivo on sites distinct from those phosphorylated in response to insulin
    • 2-adrenergic receptor in vivo on sites distinct from those phosphorylated in response to insulin. J. Biol. Chem. 271, 29347-29352
    • (1996) J. Biol. Chem. , vol.271 , pp. 29347-29352
    • Karoor, V.1    Malbon, C.C.2
  • 45
    • 0032875356 scopus 로고    scopus 로고
    • Physiological regulation of G protein-linked signaling
    • Morris, A. J. and Malbon, C. C. (1999) Physiological regulation of G protein-linked signaling. Physiol. Rev. 79, 1373-1430
    • (1999) Physiol. Rev. , vol.79 , pp. 1373-1430
    • Morris, A.J.1    Malbon, C.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.