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Volumn 275, Issue 2, 1999, Pages 180-186

Thrombin activates transcription factors Sp1, NF-κB, and CREB: Importance of the use of phosphatase inhibitors during nuclear protein extraction for the assessment of transcription factor DNA-binding activities

Author keywords

Dephosphorylation; EMSA; Phosphatase inhibitors; Thrombin; Transcription factors

Indexed keywords

AMINO ACIDS; CHEMICAL ACTIVATION; DNA; ELECTROPHORETIC MOBILITY; EXTRACTION; PHOSPHATASES; TRANSCRIPTION FACTORS;

EID: 0033571705     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.1999.4313     Document Type: Article
Times cited : (12)

References (38)
  • 1
    • 0032483574 scopus 로고    scopus 로고
    • TATA box mimicry by TFIID: Autoinhibition of pol II transcription
    • Burley S. K., Roeder R. G. TATA box mimicry by TFIID: Autoinhibition of pol II transcription. Cell. 94:1998;551-553.
    • (1998) Cell , vol.94 , pp. 551-553
    • Burley, S.K.1    Roeder, R.G.2
  • 2
    • 0032584643 scopus 로고    scopus 로고
    • An integrated model of the transcription complex in elongation, termination, and editing
    • von Hippel P. H. An integrated model of the transcription complex in elongation, termination, and editing. Science. 281:1998;660-665.
    • (1998) Science , vol.281 , pp. 660-665
    • Von Hippel, P.H.1
  • 3
    • 0030035436 scopus 로고    scopus 로고
    • Multiple steps in the regulation of transcription-factor level and activity
    • Calkhoven C. F., Ab G. Multiple steps in the regulation of transcription-factor level and activity. Biochem. J. 317:1996;329-342.
    • (1996) Biochem. J. , vol.317 , pp. 329-342
    • Calkhoven, C.F.1    Ab, G.2
  • 4
    • 0030768779 scopus 로고    scopus 로고
    • Regulation of transcription by proteins that control the cell cycle
    • Dynlacht B. D. Regulation of transcription by proteins that control the cell cycle. Nature. 389:1997;149-152.
    • (1997) Nature , vol.389 , pp. 149-152
    • Dynlacht, B.D.1
  • 5
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-κB
    • May M. J., Ghosh S. Signal transduction through NF-κB. Immunol. Today. 19:1998;80-88.
    • (1998) Immunol. Today , vol.19 , pp. 80-88
    • May, M.J.1    Ghosh, S.2
  • 6
    • 0030613758 scopus 로고    scopus 로고
    • NF-κB activation: The IκB kinase revealed?
    • Stancovski I., Baltimore D. NF-κB activation: The IκB kinase revealed? Cell. 91:1997;299-302.
    • (1997) Cell , vol.91 , pp. 299-302
    • Stancovski, I.1    Baltimore, D.2
  • 8
    • 0030848091 scopus 로고    scopus 로고
    • Cyclic AMP signalling and cellular proliferation: Regulation of CREB and CREM
    • Della F. M., Servillo G., Sassone C. P. Cyclic AMP signalling and cellular proliferation: Regulation of CREB and CREM. FEBS Lett. 410:1997;22-24.
    • (1997) FEBS Lett. , vol.410 , pp. 22-24
    • Della, F.M.1    Servillo, G.2    Sassone, C.P.3
  • 9
    • 0032525913 scopus 로고    scopus 로고
    • Cell cycle regulation of the transcriptional coactivators p300 an CREB binding protein
    • Snowden A. W., Perkins N. D. Cell cycle regulation of the transcriptional coactivators p300 an CREB binding protein. Biochem. Pharmacol. 55:1998;1947-1954.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1947-1954
    • Snowden, A.W.1    Perkins, N.D.2
  • 10
    • 0032546367 scopus 로고    scopus 로고
    • Coupling gene expression to cAMP signalling: Role of CREB and CREM
    • Sassone-Corsi P. Coupling gene expression to cAMP signalling: Role of CREB and CREM. Int. J. Biochem. Cell Biol. 30:1998;27-38.
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 27-38
    • Sassone-Corsi, P.1
  • 11
    • 0026497472 scopus 로고
    • Sp1 and the subfamily of zinc finger proteins with guanine-rich binding sites
    • Berg J. M. Sp1 and the subfamily of zinc finger proteins with guanine-rich binding sites. Proc. Natl. Acad. Sci. USA. 89:1992;11109-11110.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11109-11110
    • Berg, J.M.1
  • 12
    • 0030973394 scopus 로고    scopus 로고
    • Casein kinase II-mediated phosphorylation of the C terminus of Sp1 decreases its DNA binding activity
    • Armstrong S. A., Barry D. A., Leggett R. W., Mueller C. R. Casein kinase II-mediated phosphorylation of the C terminus of Sp1 decreases its DNA binding activity. J. Biol. Chem. 272:1997;13489-13495.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13489-13495
    • Armstrong, S.A.1    Barry, D.A.2    Leggett, R.W.3    Mueller, C.R.4
  • 13
    • 0030771433 scopus 로고    scopus 로고
    • Modulation of transcription factor Sp1 by cAMP-dependent protein kinase
    • Rohlff C., Ahmad S., Borellini F., Lei J., Glazer R. I. Modulation of transcription factor Sp1 by cAMP-dependent protein kinase. J. Biol. Chem. 272:1997;21137-21141.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21137-21141
    • Rohlff, C.1    Ahmad, S.2    Borellini, F.3    Lei, J.4    Glazer, R.I.5
  • 14
    • 0030795465 scopus 로고    scopus 로고
    • Binding of phosphorylated Sp1 protein to tandem Sp1 binding sites regulates α2 integrin gene core promoter activity
    • Zutter M. M., Ryan E. E., Painter A. D. Binding of phosphorylated Sp1 protein to tandem Sp1 binding sites regulates α2 integrin gene core promoter activity. Blood. 90:1997;678-689.
    • (1997) Blood , vol.90 , pp. 678-689
    • Zutter, M.M.1    Ryan, E.E.2    Painter, A.D.3
  • 15
    • 0001484969 scopus 로고
    • Cellular effects of thrombin and their signalling pathways
    • Kanthou C., Benzakour B. Cellular effects of thrombin and their signalling pathways. Cell. Pharmacol. 2:1995;293-302.
    • (1995) Cell. Pharmacol. , vol.2 , pp. 293-302
    • Kanthou, C.1    Benzakour, B.2
  • 16
    • 0031744875 scopus 로고    scopus 로고
    • Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases
    • Dery O., Corvera C. U., Steinhoff M., Bunnett N. W. Proteinase-activated receptors: Novel mechanisms of signaling by serine proteases. Am. J. Physiol. 274:1998;C1429-52.
    • (1998) Am. J. Physiol. , vol.274
    • Dery, O.1    Corvera, C.U.2    Steinhoff, M.3    Bunnett, N.W.4
  • 17
    • 0028805435 scopus 로고
    • Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-gamma 1 in rat aortic smooth muscle cells
    • Rao G. N., Delafontaine P., Runge M. S. Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-gamma 1 in rat aortic smooth muscle cells. J. Biol. Chem. 270:1995;27871-27875.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27871-27875
    • Rao, G.N.1    Delafontaine, P.2    Runge, M.S.3
  • 18
    • 0028839210 scopus 로고
    • Thrombin receptor activating peptide (TRAP) stimulates mitogenesis, c-fos and PDGF-A gene expression in human vascular smooth muscle cells
    • Kanthou C., Benzakour O., Patel G., Deadman J., Kakkar V. V., Lupu F. Thrombin receptor activating peptide (TRAP) stimulates mitogenesis, c-fos and PDGF-A gene expression in human vascular smooth muscle cells. Thromb. Haemost. 74:1995;1340-1347.
    • (1995) Thromb. Haemost. , vol.74 , pp. 1340-1347
    • Kanthou, C.1    Benzakour, O.2    Patel, G.3    Deadman, J.4    Kakkar, V.V.5    Lupu, F.6
  • 19
    • 0028841444 scopus 로고
    • Structural domains of thrombin involved in the induction of mitogenesis in cultured human vascular smooth muscle cells
    • Kanthou C., Kanse S. M., Kakkar V. V., Benzakour O. Structural domains of thrombin involved in the induction of mitogenesis in cultured human vascular smooth muscle cells. Blood Coagul. Fibrin. 6:1995;634-642.
    • (1995) Blood Coagul. Fibrin. , vol.6 , pp. 634-642
    • Kanthou, C.1    Kanse, S.M.2    Kakkar, V.V.3    Benzakour, O.4
  • 20
    • 0029894341 scopus 로고    scopus 로고
    • Evidence for cultured human vascular smooth muscle cell heterogeneity: Isolation of clonal cells and study of their growth characteristics
    • Benzakour O., Kanthou C., Kanse S. M., Scully M. F., Kakkar V. V., Cooper D. N. Evidence for cultured human vascular smooth muscle cell heterogeneity: Isolation of clonal cells and study of their growth characteristics. Thromb. Haemost. 75:1996;854-858.
    • (1996) Thromb. Haemost. , vol.75 , pp. 854-858
    • Benzakour, O.1    Kanthou, C.2    Kanse, S.M.3    Scully, M.F.4    Kakkar, V.V.5    Cooper, D.N.6
  • 22
    • 0017746140 scopus 로고
    • Distinction between smooth muscle, fibroblasts and endothelial cells in culture by the use of fluoresceinated antibodies against smooth muscle actin
    • Chamley J. H., Campbell G. R., Groschel S. U., Burnstock G. Distinction between smooth muscle, fibroblasts and endothelial cells in culture by the use of fluoresceinated antibodies against smooth muscle actin. Cell Tissue Res. 183:1977;153-166.
    • (1977) Cell Tissue Res. , vol.183 , pp. 153-166
    • Chamley, J.H.1    Campbell, G.R.2    Groschel, S.U.3    Burnstock, G.4
  • 23
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam J. D., Lebovitz R. M., Roeder R. G. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1983;1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 24
    • 0032539989 scopus 로고    scopus 로고
    • Phosphorylation of the cAMP response element binding protein CREB by cAMP-dependent protein kinase A and glycogen synthase kinase-3 alters DNA-binding affinity, conformation, and increases net charge
    • Bullock B. P., Habener J. F. Phosphorylation of the cAMP response element binding protein CREB by cAMP-dependent protein kinase A and glycogen synthase kinase-3 alters DNA-binding affinity, conformation, and increases net charge. Biochemistry. 37:1998;3795-3809.
    • (1998) Biochemistry , vol.37 , pp. 3795-3809
    • Bullock, B.P.1    Habener, J.F.2
  • 25
    • 0025037502 scopus 로고
    • GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase
    • Jackson S. P., MacDonald J. J., Lees M. S., Tjian R. GC box binding induces phosphorylation of Sp1 by a DNA-dependent protein kinase. Cell. 63:1990;155-165.
    • (1990) Cell , vol.63 , pp. 155-165
    • Jackson, S.P.1    MacDonald, J.J.2    Lees, M.S.3    Tjian, R.4
  • 26
    • 0027431749 scopus 로고
    • Inactivation of nuclear inhibitory polypeptides of protein phosphatase-1 (NIPP-1) by protein kinase A
    • Beullens M., Van E. A., Bollen M., Stalmans W. Inactivation of nuclear inhibitory polypeptides of protein phosphatase-1 (NIPP-1) by protein kinase A. J. Biol. Chem. 268:1993;13172-13177.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13172-13177
    • Beullens, M.1    Van, E.A.2    Bollen, M.3    Stalmans, W.4
  • 28
    • 0027221605 scopus 로고
    • Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation
    • Wadzinski B. E., Wheat W. H., Jaspers S., Peruski L. J., Lickteig R. L., Johnson G. L., Klemm D. J. Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation. Mol. Cell. Biol. 13:1993;2822-2834.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2822-2834
    • Wadzinski, B.E.1    Wheat, W.H.2    Jaspers, S.3    Peruski, L.J.4    Lickteig, R.L.5    Johnson, G.L.6    Klemm, D.J.7
  • 29
    • 0030025078 scopus 로고    scopus 로고
    • Involvement of pertussis toxin-sensitive and -insensitive G proteins in α-thrombin signalling on cultured human vascular smooth muscle cells
    • Kanthou C., Kanse S. M., Kakkar V. V., Benzakour O. Involvement of pertussis toxin-sensitive and -insensitive G proteins in α-thrombin signalling on cultured human vascular smooth muscle cells. Cell. Signal. 8:1996;59-66.
    • (1996) Cell. Signal. , vol.8 , pp. 59-66
    • Kanthou, C.1    Kanse, S.M.2    Kakkar, V.V.3    Benzakour, O.4
  • 30
    • 0031722950 scopus 로고    scopus 로고
    • Role of Ca2+/calmodulin-dependent phosphatase 2B in thrombin-induced endothelial cell contractile responses
    • Verin A. D., Cooke C., Herenyiova M., Patterson C. E., Garcia J. G. Role of Ca2+/calmodulin-dependent phosphatase 2B in thrombin-induced endothelial cell contractile responses. Am. J. Physiol. 275:1998;L788-99.
    • (1998) Am. J. Physiol. , vol.275
    • Verin, A.D.1    Cooke, C.2    Herenyiova, M.3    Patterson, C.E.4    Garcia, J.G.5
  • 31
    • 0032555506 scopus 로고    scopus 로고
    • Thrombin inactivates myosin light chain phosphatase via Rho and its target Rho kinase in human endothelial cells
    • Essler M., Amano M., Kruse H. J., Kaibuchi K., Weber P. C., Aepfelbacher M. Thrombin inactivates myosin light chain phosphatase via Rho and its target Rho kinase in human endothelial cells. J. Biol. Chem. 273:1998;21867-21874.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21867-21874
    • Essler, M.1    Amano, M.2    Kruse, H.J.3    Kaibuchi, K.4    Weber, P.C.5    Aepfelbacher, M.6
  • 32
    • 0029069226 scopus 로고
    • Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertussis toxin-sensitive heterotrimeric G-protein
    • Li R. Y., Gaits F., Ragab A., Ragab-Thomas J. M., Chap H. Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertussis toxin-sensitive heterotrimeric G-protein. EMBO J. 14:1995;2519-2526.
    • (1995) EMBO J. , vol.14 , pp. 2519-2526
    • Li, R.Y.1    Gaits, F.2    Ragab, A.3    Ragab-Thomas, J.M.4    Chap, H.5
  • 33
    • 0031043514 scopus 로고
    • Protein tyrosine phosphatase SHP-1 fails to associate with cytoskeleton but is normally phosphorylated upon thrombin stimulation of thrombasthenic platelets
    • Li R. Y., Gaits F., Ragab-Thomas J. M., Maclouf J., Caen J. P., Levy-Toledano S., Chap H. Protein tyrosine phosphatase SHP-1 fails to associate with cytoskeleton but is normally phosphorylated upon thrombin stimulation of thrombasthenic platelets. Thromb. Haemost. 77:1977;150-154.
    • (1977) Thromb. Haemost. , vol.77 , pp. 150-154
    • Li, R.Y.1    Gaits, F.2    Ragab-Thomas, J.M.3    Maclouf, J.4    Caen, J.P.5    Levy-Toledano, S.6    Chap, H.7
  • 34
    • 0030068660 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinases type I, II ad IV
    • 2+/calmodulin-dependent protein kinases type I, II ad IV. J. Biol. Chem. 271:1996;3066-3073.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3066-3073
    • Sun, P.1    Lou, L.2    Maurer, R.A.3
  • 35
    • 0026353468 scopus 로고
    • DNA contacts probed by modification protection and interference studies
    • Wissmann A., Hillen W. DNA contacts probed by modification protection and interference studies. Methods Enzymol. 208:1991;365-379.
    • (1991) Methods Enzymol. , vol.208 , pp. 365-379
    • Wissmann, A.1    Hillen, W.2
  • 36
  • 38
    • 0029036655 scopus 로고
    • Evaluation of the use of the luciferase-reporter-gene for gene-regulation studies involving cyclic AMP-elevating agents
    • Benzakour O., Kanthou C., Dennehy U., al H. A., Berg L. P., Kakkar V. V., Cooper D. N. Evaluation of the use of the luciferase-reporter-gene for gene-regulation studies involving cyclic AMP-elevating agents. Biochem. J. 309:1995;385-387.
    • (1995) Biochem. J. , vol.309 , pp. 385-387
    • Benzakour, O.1    Kanthou, C.2    Dennehy, U.3    Al, H.A.4    Berg, L.P.5    Kakkar, V.V.6    Cooper, D.N.7


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