메뉴 건너뛰기




Volumn 3, Issue 10, 1997, Pages 674-685

Constitutive modulation of Raf-1 protein kinase is associated with differential gene expression of several known and unknown genes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE;

EID: 0031441241     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf03401706     Document Type: Article
Times cited : (19)

References (48)
  • 2
    • 0027049804 scopus 로고
    • The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases
    • Devary Y, Gottlieb RA, Smeal T, Karin M. (1992) The mammalian ultraviolet response is triggered by activation of Src tyrosine kinases. Cell 71: 1081-1091.
    • (1992) Cell , vol.71 , pp. 1081-1091
    • Devary, Y.1    Gottlieb, R.A.2    Smeal, T.3    Karin, M.4
  • 4
    • 0026641090 scopus 로고
    • Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro
    • Dent P, Haser W, Haystead TAG, Vincent LA, Roberts TM, Sturgill TW. (1992) Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro. Science 257: 1404-1407.
    • (1992) Science , vol.257 , pp. 1404-1407
    • Dent, P.1    Haser, W.2    Haystead, T.A.G.3    Vincent, L.A.4    Roberts, T.M.5    Sturgill, T.W.6
  • 5
    • 0027219329 scopus 로고
    • κB site-dependent induction of gene expression by diverse inducers of nuclear factor κB requires Raf-1
    • Finco T, Baldwin A. (1993) κB site-dependent induction of gene expression by diverse inducers of nuclear factor κB requires Raf-1. J. Biol. Chem. 268: 17676-17679.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17676-17679
    • Finco, T.1    Baldwin, A.2
  • 6
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ. (1995) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80: 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 8
    • 0030849058 scopus 로고    scopus 로고
    • Association of Grb2 with Sos and Ras with Raf-1 upon gamma irradiation of breast cancer cells
    • Suy S, Anderson WB, Dent P, Chang E, Kasid U. (1997) Association of Grb2 with Sos and Ras with Raf-1 upon gamma irradiation of breast cancer cells. Oncogene 15: 53-61.
    • (1997) Oncogene , vol.15 , pp. 53-61
    • Suy, S.1    Anderson, W.B.2    Dent, P.3    Chang, E.4    Kasid, U.5
  • 9
    • 0024545162 scopus 로고
    • Definition of the human raf amino-terminal regulatory region by deletion mutagenesis
    • Stanton VP, Nichols DW, Laudano AP, Cooper GM. (1989) Definition of the human raf amino-terminal regulatory region by deletion mutagenesis. Mol. Cell. Biol. 9: 639-647.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 639-647
    • Stanton, V.P.1    Nichols, D.W.2    Laudano, A.P.3    Cooper, G.M.4
  • 10
    • 0025277489 scopus 로고
    • Mutational activation of c-raf-1 and definition of the minimal transforming sequence
    • Heidecker G, Huleihel M, Cleveland JL, et al. (1990) Mutational activation of c-raf-1 and definition of the minimal transforming sequence. Mol. Cell. Biol. 10: 2503-2512.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2503-2512
    • Heidecker, G.1    Huleihel, M.2    Cleveland, J.L.3
  • 11
    • 0023186270 scopus 로고
    • The raf oncogene is associated with a radiation-resistant human laryngeal cancer
    • Kasid U, Pfeifer A, Weichselbaum RR, Dritschilo A, Mark GE. (1987) The raf oncogene is associated with a radiation-resistant human laryngeal cancer. Science 237: 1039-1041.
    • (1987) Science , vol.237 , pp. 1039-1041
    • Kasid, U.1    Pfeifer, A.2    Weichselbaum, R.R.3    Dritschilo, A.4    Mark, G.E.5
  • 12
    • 0031018758 scopus 로고    scopus 로고
    • Constitutive activation of Raf-1 correlates with morphological transformation and abrogation of tyrosine phosphorylation of distinct sets of proteins in human squamous carcinoma cells
    • Patel B, Ray S, Whiteside TLW, Kasid U. (1997) Constitutive activation of Raf-1 correlates with morphological transformation and abrogation of tyrosine phosphorylation of distinct sets of proteins in human squamous carcinoma cells. Mol. Carcinog. 18: 1-6.
    • (1997) Mol. Carcinog. , vol.18 , pp. 1-6
    • Patel, B.1    Ray, S.2    Whiteside, T.L.W.3    Kasid, U.4
  • 13
    • 0026647749 scopus 로고
    • Raf-1 activates MAP kinase-kinase
    • Kyriakis JM, App H, Zhang XF, et al. (1992) Raf-1 activates MAP kinase-kinase. Nature 358: 417-421.
    • (1992) Nature , vol.358 , pp. 417-421
    • Kyriakis, J.M.1    App, H.2    Zhang, X.F.3
  • 14
    • 0026596576 scopus 로고
    • Serum-, TPA-, and Ras-induced expression from AP-1/Ets-driven promoters requires Raf-1 kinase
    • Bruder JT, Heidecker G, Rapp UR. (1992) Serum-, TPA-, and Ras-induced expression from AP-1/Ets-driven promoters requires Raf-1 kinase. Genes Dev. 6: 545-556.
    • (1992) Genes Dev. , vol.6 , pp. 545-556
    • Bruder, J.T.1    Heidecker, G.2    Rapp, U.R.3
  • 15
    • 0025880813 scopus 로고
    • An inhibitory mutant of c-raf-1 blocks v-src-induced activation of the egr-1 promoter
    • Qureshi SA, Rim M, Bruder JT, et al. (1991) An inhibitory mutant of c-raf-1 blocks v-src-induced activation of the egr-1 promoter. J. Biol. Chem. 266: 20594-20597.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20594-20597
    • Qureshi, S.A.1    Rim, M.2    Bruder, J.T.3
  • 16
    • 0027482547 scopus 로고
    • Raf-1 protein kinase activates the NF-κB transcription factor by dissociating the cytoplasmic NF-κB-1κB complex
    • Shengfeng Li, Sedivy JM. (1993) Raf-1 protein kinase activates the NF-κB transcription factor by dissociating the cytoplasmic NF-κB-1κB complex. Proc. Natl. Acad. Sci. USA 90: 9247-9251.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9247-9251
    • Li, S.1    Sedivy, J.M.2
  • 17
    • 0024580323 scopus 로고
    • Effect of antisense c-raf-1 on tumor-igenicity and radiation sensitivity of a human squamous carcinoma
    • Kasid U, Pfeifer A, Brennan T, Beckett M, Weichselbaum RR, Dritschilo A, Mark G. (1989) Effect of antisense c-raf-1 on tumor-igenicity and radiation sensitivity of a human squamous carcinoma. Science 243: 1354-1356.
    • (1989) Science , vol.243 , pp. 1354-1356
    • Kasid, U.1    Pfeifer, A.2    Brennan, T.3    Beckett, M.4    Weichselbaum, R.R.5    Dritschilo, A.6    Mark, G.7
  • 18
    • 0029977448 scopus 로고    scopus 로고
    • Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against c-raf kinase
    • Monia B, Johnston JF, Geiger T, Muller M, Fabbro D. (1996) Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against c-raf kinase. Nature Med. 2: 668-675.
    • (1996) Nature Med. , vol.2 , pp. 668-675
    • Monia, B.1    Johnston, J.F.2    Geiger, T.3    Muller, M.4    Fabbro, D.5
  • 19
    • 0030894324 scopus 로고    scopus 로고
    • Inhibition of Raf-1 protein kinase by antisense phosphorothioate oligodeoxynucleotide is associated with sensitization of human laryngeal squamous carcinoma cells to gamma radiation
    • Soldatenkov VA, Dritschilo A, Wang F-H, Olah Z, Anderson WB, Kasid U. (1997) Inhibition of Raf-1 protein kinase by antisense phosphorothioate oligodeoxynucleotide is associated with sensitization of human laryngeal squamous carcinoma cells to gamma radiation. Cancer J. Sci. Am. 3: 13-20.
    • (1997) Cancer J. Sci. Am. , vol.3 , pp. 13-20
    • Soldatenkov, V.A.1    Dritschilo, A.2    Wang, F.-H.3    Olah, Z.4    Anderson, W.B.5    Kasid, U.6
  • 20
    • 0031450606 scopus 로고    scopus 로고
    • Antisense raf oligodeoxyribonucleotide is protected by liposomal encapsulation and inhibits Raf-1 protein expression in vitro and in vivo: Implication for gene therapy of radioresistant cancer
    • In press
    • Gokhale PC, Soldatenkov V, Wang F-H, Rahman A, Dritschilo A, Kasid U. (1997) Antisense raf oligodeoxyribonucleotide is protected by liposomal encapsulation and inhibits Raf-1 protein expression in vitro and in vivo: Implication for gene therapy of radioresistant cancer. Gene Therapy In press.
    • (1997) Gene Therapy
    • Gokhale, P.C.1    Soldatenkov, V.2    Wang, F.-H.3    Rahman, A.4    Dritschilo, A.5    Kasid, U.6
  • 21
    • 0345498292 scopus 로고    scopus 로고
    • Bcl-2 targets the protein kinase Raf-1 to mitochondria
    • Wang HG, Rapp UR, Reed JC. (1996) Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 87: 629-638.
    • (1996) Cell , vol.87 , pp. 629-638
    • Wang, H.G.1    Rapp, U.R.2    Reed, J.C.3
  • 22
    • 0026674886 scopus 로고
    • Differential display of eukaryotic mRNA by means of the polymerase chain reaction
    • Liang P, Pardee AB. (1992) Differential display of eukaryotic mRNA by means of the polymerase chain reaction. Science 257: 967-971.
    • (1992) Science , vol.257 , pp. 967-971
    • Liang, P.1    Pardee, A.B.2
  • 23
    • 0031147984 scopus 로고    scopus 로고
    • Identification of seven differentially displayed transcripts in human primary and matched metastatic head and neck squamous carcinoma cell lines: Implications in metastasis and/or radiation response
    • Patel S, Wang F-H, Whiteside TL, Kasid U. (1997) Identification of seven differentially displayed transcripts in human primary and matched metastatic head and neck squamous carcinoma cell lines: Implications in metastasis and/or radiation response. Eur J Cancer B Oral Oncol. 33: 197-203.
    • (1997) Eur J Cancer B Oral Oncol. , vol.33 , pp. 197-203
    • Patel, S.1    Wang, F.-H.2    Whiteside, T.L.3    Kasid, U.4
  • 24
    • 0024448596 scopus 로고
    • Biology, cytogenetics, and sensitivity to immunological effector cells of new head and neck squamous cell carcinoma lines
    • Heo DS, Synderman C, Gollin SM, et al. (1989) Biology, cytogenetics, and sensitivity to immunological effector cells of new head and neck squamous cell carcinoma lines. Cancer Res. 49: 5167-5175.
    • (1989) Cancer Res. , vol.49 , pp. 5167-5175
    • Heo, D.S.1    Synderman, C.2    Gollin, S.M.3
  • 26
    • 0025095405 scopus 로고
    • Cloning, expression, purification and biological activity of recombinant native and variant human α1-antichymotrypsins
    • Rubin H, Wang Z-M, Nickbarg EB, et al. (1990) Cloning, expression, purification and biological activity of recombinant native and variant human α1-antichymotrypsins. J. Biol. Chem. 265: 1199-1207.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1199-1207
    • Rubin, H.1    Wang, Z.-M.2    Nickbarg, E.B.3
  • 27
    • 0024600842 scopus 로고
    • Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1α
    • Uetsuki T, Naito A, Nagata S, Kaziro Y. (1989) Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1α. J. Biol. Chem. 264: 5791-5798.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5791-5798
    • Uetsuki, T.1    Naito, A.2    Nagata, S.3    Kaziro, Y.4
  • 28
    • 0028577311 scopus 로고
    • Molecular cloning and sequencing of a human cDNa encoding ornithine decarboxylase antizyme
    • Tewari ST, Qian Y, Thornton RD, et al. (1994) Molecular cloning and sequencing of a human cDNA encoding ornithine decarboxylase antizyme. Bichim. Biophys. Acta 1209: 293-295.
    • (1994) Bichim. Biophys. Acta , vol.1209 , pp. 293-295
    • Tewari, S.T.1    Qian, Y.2    Thornton, R.D.3
  • 29
    • 0026887870 scopus 로고
    • The biology and biochemistry of antichymotrypsin and its potential role as a therapeutic agent
    • Rubin H. (1992) The biology and biochemistry of antichymotrypsin and its potential role as a therapeutic agent. Biol. Chem. Hoppe-Seyler 373: 497-502.
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 497-502
    • Rubin, H.1
  • 30
    • 0029959819 scopus 로고    scopus 로고
    • Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents
    • Lotem J, Sachs L. (1996) Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents. Proc. Natl. Acad. Sci. USA 93: 12507-12512.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12507-12512
    • Lotem, J.1    Sachs, L.2
  • 31
    • 0029941477 scopus 로고    scopus 로고
    • Serine protease inhibitors (SERPINS) Where mechanism meets medicine
    • Rubin H. (1996) Serine protease inhibitors (SERPINS) Where mechanism meets medicine. Nature Med. 2: 632-633.
    • (1996) Nature Med. , vol.2 , pp. 632-633
    • Rubin, H.1
  • 33
    • 0004155427 scopus 로고
    • W.H. Freeman, New York
    • Stryer L. (1995) Biochemistry. W.H. Freeman, New York.
    • (1995) Biochemistry
    • Stryer, L.1
  • 34
    • 0025243540 scopus 로고
    • Neoplastic transformation is associated with coordinate induction of nuclear and cytoplasmic oxidative phosphorylation genes
    • Torroni A, Stepien G, Hodge JA, Wallace DC. (1990) Neoplastic transformation is associated with coordinate induction of nuclear and cytoplasmic oxidative phosphorylation genes. J. Biol. Chem. 265: 20589-20593.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20589-20593
    • Torroni, A.1    Stepien, G.2    Hodge, J.A.3    Wallace, D.C.4
  • 36
    • 0025824545 scopus 로고
    • Identification of genes that exhibit increased expression after flat reversion of NIH/3T3 cells transformed by human activated Ha-ras oncogene
    • Mullauer L, Suzuki H, Fujita M, Katabami M, Kuzumaki N. (1991) Identification of genes that exhibit increased expression after flat reversion of NIH/3T3 cells transformed by human activated Ha-ras oncogene. Cancer Lett. 59: 37-43.
    • (1991) Cancer Lett. , vol.59 , pp. 37-43
    • Mullauer, L.1    Suzuki, H.2    Fujita, M.3    Katabami, M.4    Kuzumaki, N.5
  • 37
    • 0026058530 scopus 로고
    • Interactions of bovine mitochondrial phenylalanyl-tRNA with ribosomes and elongation factors from mitochondria and bacteria
    • Kumazawa Y, Schwartzbach CJ, Liao HX, et al. (1991) Interactions of bovine mitochondrial phenylalanyl-tRNA with ribosomes and elongation factors from mitochondria and bacteria. Biochim. Biophys. Acta 1090: 167-172.
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 167-172
    • Kumazawa, Y.1    Schwartzbach, C.J.2    Liao, H.X.3
  • 38
    • 0026338694 scopus 로고
    • Rat elongation factor 1α: Sequence of cDNa from a highly metastatic fos-transferred cell line
    • Taniguchi S, Miyamoto S, Sadano H, Kobayashi H. (1991) Rat elongation factor 1α: Sequence of cDNA from a highly metastatic fos-transferred cell line. Nucl. Acids Res. 19: 6949.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 6949
    • Taniguchi, S.1    Miyamoto, S.2    Sadano, H.3    Kobayashi, H.4
  • 40
    • 0026700016 scopus 로고
    • Elongation factor-1α gene determines susceptibility to transformation
    • Tatsuka M, Mitsui H, Wada M, Nagata A, Nojima H, Okayama H. (1992) Elongation factor-1α gene determines susceptibility to transformation. Nature 359: 333-336.
    • (1992) Nature , vol.359 , pp. 333-336
    • Tatsuka, M.1    Mitsui, H.2    Wada, M.3    Nagata, A.4    Nojima, H.5    Okayama, H.6
  • 41
    • 0027960230 scopus 로고
    • Characterization of the regulatory elements in the promoter of the human elongation factor-1α gene
    • Wakabayashi-Ito N, Nagata S. (1994) Characterization of the regulatory elements in the promoter of the human elongation factor-1α gene. J. Biol. Chem. 269: 29831-29837.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29831-29837
    • Wakabayashi-Ito, N.1    Nagata, S.2
  • 42
    • 0345955882 scopus 로고
    • Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction
    • Heller JS, Fong WF, Canellakis ES. (1976) Induction of a protein inhibitor to ornithine decarboxylase by the end products of its reaction. Proc. Natl. Acad. Sci. USA 73: 1858-1862.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1858-1862
    • Heller, J.S.1    Fong, W.F.2    Canellakis, E.S.3
  • 43
    • 0025325255 scopus 로고
    • Molecular genetics of polyamine synthesis in eukaryotic cells
    • Heby O, Persson L. (1990) Molecular genetics of polyamine synthesis in eukaryotic cells. Trends Biochem. Sci. 15: 153-158.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 153-158
    • Heby, O.1    Persson, L.2
  • 44
    • 0026683752 scopus 로고
    • Ornithine decarboxylase activity is critical for cell transformation
    • Auvinen M, Paasinen A, Andersson LC, Holtta E. (1992) Ornithine decarboxylase activity is critical for cell transformation. Nature 360: 355-358.
    • (1992) Nature , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Andersson, L.C.3    Holtta, E.4
  • 45
    • 0028790834 scopus 로고
    • Ornithine decarboxylase and ras induced cell transformations: Reversal by protein tyrosine kinase inhibitors and role of pp130CAS
    • Auvinen M, Paasinen-Sohns A, Hirai H, Andersson LC, Holtta E. (1995) Ornithine decarboxylase and ras induced cell transformations: Reversal by protein tyrosine kinase inhibitors and role of pp130CAS. Mol. Cell Biol. 15: 6513-6525.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 6513-6525
    • Auvinen, M.1    Paasinen-Sohns, A.2    Hirai, H.3    Andersson, L.C.4    Holtta, E.5
  • 46
    • 0031019072 scopus 로고    scopus 로고
    • Ornithine decarboxylase overexpression stimulates mitogen-activated protein kinase and anchorage-independent growth of human breast epithelial cells
    • Manni A, Wechter R, Gilmour S, Verderame MF, Mauger D, Demers LM. (1997) Ornithine decarboxylase overexpression stimulates mitogen-activated protein kinase and anchorage-independent growth of human breast epithelial cells. Int. J. Cancer 70: 175-182.
    • (1997) Int. J. Cancer , vol.70 , pp. 175-182
    • Manni, A.1    Wechter, R.2    Gilmour, S.3    Verderame, M.F.4    Mauger, D.5    Demers, L.M.6
  • 47
    • 0028089990 scopus 로고
    • Forced expression of antizyme abolishes ornithine decarboxylase activity, suppresses cellular levels of polyamines and inhibits cell growth
    • Murakami Y, Matsufuji S, Miyazaki Y, Hayashi SI. (1994) Forced expression of antizyme abolishes ornithine decarboxylase activity, suppresses cellular levels of polyamines and inhibits cell growth. Biochem. J. 304: 183-187.
    • (1994) Biochem. J. , vol.304 , pp. 183-187
    • Murakami, Y.1    Matsufuji, S.2    Miyazaki, Y.3    Hayashi, S.I.4
  • 48
    • 0030004102 scopus 로고    scopus 로고
    • Differential screening of gene expression difference enriched by differential display
    • Zhang H, Zhang R, Liang P. (1996) Differential screening of gene expression difference enriched by differential display. Nucl. Acids Res. 24: 2454-2455.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 2454-2455
    • Zhang, H.1    Zhang, R.2    Liang, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.