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Volumn 56, Issue 14, 1996, Pages 3265-3269

Regulation of ornithine decarboxylase in a transformed cell line that overexpresses translation initiation factor eIF-4E

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; INITIATION FACTOR; MESSENGER RNA; ORNITHINE DECARBOXYLASE; POLYAMINE;

EID: 0030011284     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (70)

References (29)
  • 1
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy
    • Pegg, A. E. Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy. Cancer Res., 48: 759-774, 1988.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 2
    • 0026555236 scopus 로고
    • Induction of ornithine decarboxylase in specific subpopulations of murine epidermal cells following multiple exposures to 12-O-tetradecanoylphorbol-13-acetate, merzerein and ethylphenylproprionate
    • Lond.
    • Gilmour, S. K , Robertson, F. M., Megosh, L , O'Connell, S. M , Mitchell, J., and O'Brien, T. G. Induction of ornithine decarboxylase in specific subpopulations of murine epidermal cells following multiple exposures to 12-O-tetradecanoylphorbol-13-acetate, merzerein and ethylphenylproprionate Carcinogenesis (Lond.), 13: 51-56, 1992.
    • (1992) Carcinogenesis , vol.13 , pp. 51-56
    • Gilmour, S.K.1    Robertson, F.M.2    Megosh, L.3    O'Connell, S.M.4    Mitchell, J.5    O'Brien, T.G.6
  • 3
    • 0026671825 scopus 로고
    • Ornithine decarboxylase as an enzyme target for therapy
    • McCann, P. P., and Pegg, A. E. Ornithine decarboxylase as an enzyme target for therapy Pharmacol. Ther., 54 195-215, 1992
    • (1992) Pharmacol. Ther. , vol.54 , pp. 195-215
    • McCann, P.P.1    Pegg, A.E.2
  • 4
    • 0026683752 scopus 로고
    • Ornithine decarboxylase activity is critical for cell transformation
    • Lond
    • Auvinen, M., Paasinen, A., Anderson, L. A., and Höltta, E. Ornithine decarboxylase activity is critical for cell transformation. Nature (Lond), 360 355-358, 1992.
    • (1992) Nature , vol.360 , pp. 355-358
    • Auvinen, M.1    Paasinen, A.2    Anderson, L.A.3    Höltta, E.4
  • 5
    • 0027263467 scopus 로고
    • Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression
    • Moshier, J S., Dosescu, J., Skunca, M., and Luk, G D Transformation of NIH/3T3 cells by ornithine decarboxylase overexpression. Cancer Res., 53: 2618-2622, 1993.
    • (1993) Cancer Res. , vol.53 , pp. 2618-2622
    • Moshier, J.S.1    Dosescu, J.2    Skunca, M.3    Luk, G.D.4
  • 7
    • 0025353859 scopus 로고
    • Regulation of rat ornithine decarboxylase mRNA translation by its 5′-untranslated region
    • Manzella, J. M , and Blackshear, P. J Regulation of rat ornithine decarboxylase mRNA translation by its 5′-untranslated region. J Biol. Chem., 265: 11817-11822, 1990
    • (1990) J Biol. Chem. , vol.265 , pp. 11817-11822
    • Manzella, J.M.1    Blackshear, P.J.2
  • 8
    • 0025277641 scopus 로고
    • The 5′- and 3′-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency
    • Grens, A., and Scheffler, I. E. The 5′- and 3′-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency. J. Biol. Chem., 265: 11810-11816, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11810-11816
    • Grens, A.1    Scheffler, I.E.2
  • 9
    • 0025268790 scopus 로고
    • Influence of the 5′-untranslated region of ornithine decarboxylase mRNA and spermidine on ornithine decarboxylase synthesis
    • Ito, K , Kashiwagi, K., Watanabe, S., Kameji, T., Hayashi, S., and Igarashi, K. Influence of the 5′-untranslated region of ornithine decarboxylase mRNA and spermidine on ornithine decarboxylase synthesis. J. Biol. Chem., 265: 13036-13041, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13036-13041
    • Ito, K.1    Kashiwagi, K.2    Watanabe, S.3    Kameji, T.4    Hayashi, S.5    Igarashi, K.6
  • 10
    • 0023853724 scopus 로고
    • Increased efficiency of translation of ornithine decarboxylase mRNA in mitogen-activated lymphocytes
    • White, M. W., Kameji, T., Pegg, A. E., and Morris, D. R. Increased efficiency of translation of ornithine decarboxylase mRNA in mitogen-activated lymphocytes. Eur. J Biochem., 170: 87-92, 1987.
    • (1987) Eur. J Biochem. , vol.170 , pp. 87-92
    • White, M.W.1    Kameji, T.2    Pegg, A.E.3    Morris, D.R.4
  • 11
    • 0027432343 scopus 로고
    • Increased phosphorylation of eukaryotic initiation factor 4α during early activation of T lymphocytes correlates with increased initiation factor 4F complex formation
    • Morley, S. J., Rau, M , Kay, J. E., and Pain, V. M. Increased phosphorylation of eukaryotic initiation factor 4α during early activation of T lymphocytes correlates with increased initiation factor 4F complex formation. Eur. J. Biochem., 218: 39-48, 1993
    • (1993) Eur. J. Biochem. , vol.218 , pp. 39-48
    • Morley, S.J.1    Rau, M.2    Kay, J.E.3    Pain, V.M.4
  • 12
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5α cap
    • Lazaris-Karatzas, A., Montine, K S., and Sonenberg, N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5α cap. Nature (Lond.), 345: 544-547, 1990.
    • (1990) Nature (Lond.) , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.S.2    Sonenberg, N.3
  • 13
    • 0028271504 scopus 로고
    • Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation
    • Shantz, L. M , and Pegg, A. E. Overproduction of ornithine decarboxylase caused by relief of translational repression is associated with neoplastic transformation Cancer Res , 54: 2313-2316, 1994.
    • (1994) Cancer Res , vol.54 , pp. 2313-2316
    • Shantz, L.M.1    Pegg, A.E.2
  • 14
    • 0023707798 scopus 로고
    • Control of ornithine decarboxylase in α-difluoromethylornithine-resistant L1210 cells by polyamines and synthetic analogues
    • Pegg, A. E., Madhubala, R , Karneji, T., and Bergeron, R. J Control of ornithine decarboxylase in α-difluoromethylornithine-resistant L1210 cells by polyamines and synthetic analogues. J. Biol Chem , 263: 11008-11014, 1988
    • (1988) J. Biol Chem , vol.263 , pp. 11008-11014
    • Pegg, A.E.1    Madhubala, R.2    Karneji, T.3    Bergeron, R.J.4
  • 17
    • 0028071521 scopus 로고
    • Role of the 5′-untranslated region of mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine
    • Shantz, L M , Viswanath, R and Pegg, A. E. Role of the 5′-untranslated region of mRNA in the synthesis of S-adenosylmethionine decarboxylase and its regulation by spermine. Biochem. J., 302: 765-772, 1994.
    • (1994) Biochem. J. , vol.302 , pp. 765-772
    • Shantz, L.M.1    Viswanath, R.2    Pegg, A.E.3
  • 19
    • 0028126506 scopus 로고
    • PHAS-I as a link between mitogen-activated protein kinase and translation initiation
    • Washington DC
    • Lin, T-A , Kong, X., Haystead, T A , Pause, A., Belsham, G , Sonenberg, N., and Lawrence, J. C. PHAS-I as a link between mitogen-activated protein kinase and translation initiation. Science (Washington DC), 266: 653-656, 1994
    • (1994) Science , vol.266 , pp. 653-656
    • Lin, T.-A.1    Kong, X.2    Haystead, T.A.3    Pause, A.4    Belsham, G.5    Sonenberg, N.6    Lawrence, J.C.7
  • 20
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function
    • Pause, A , Belsham, G. J., Gingras, A-C., Donzé, O , Lin T-A., Lawrence, J C., and Sonenberg, N. Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5′-cap function. Nature (Lond), 371: 762-767, 1994
    • (1994) Nature (Lond) , vol.371 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.-C.3    Donzé, O.4    Lin, T.-A.5    Lawrence, J.C.6    Sonenberg, N.7
  • 21
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. The scanning model for translation: an update. J Cell Biol., 108: 229-241, 1989
    • (1989) J Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 22
    • 0030041884 scopus 로고    scopus 로고
    • Translation initiation of ornithine decarboxylase and nucleoplasmic transport of cyclin D1 are increased in cells overexpressing eukaryotic initiation factor eIF-4E
    • Rousseau, D , Kaspar, R , Rosenwald, I , Gehrke, L , and Sonenberg, N Translation initiation of ornithine decarboxylase and nucleoplasmic transport of cyclin D1 are increased in cells overexpressing eukaryotic initiation factor eIF-4E. Proc. Natl. Acad. Sci USA, 93: 1065-1070, 1996
    • (1996) Proc. Natl. Acad. Sci USA , vol.93 , pp. 1065-1070
    • Rousseau, D.1    Kaspar, R.2    Rosenwald, I.3    Gehrke, L.4    Sonenberg, N.5
  • 23
    • 0026649391 scopus 로고
    • Specific protein binding to a conserved region of the ornithine decarboxylase mRNA 5′-untranslated region
    • Manzella, J. M., and Blackshear, P J. Specific protein binding to a conserved region of the ornithine decarboxylase mRNA 5′-untranslated region. J. Biol. Chem , 267: 7077-7082, 1992.
    • (1992) J. Biol. Chem , vol.267 , pp. 7077-7082
    • Manzella, J.M.1    Blackshear, P.J.2
  • 24
    • 0023886318 scopus 로고
    • The mechanism of ornithine decarboxylase deregulation in c-Ha-ras oncogene-transformed NIH 3T3 cells
    • Holttä, E , Sistonen, L., and Alitalo, K. The mechanism of ornithine decarboxylase deregulation in c-Ha-ras oncogene-transformed NIH 3T3 cells. J Biol. Chem , 263: 4500-4507, 1988.
    • (1988) J Biol. Chem , vol.263 , pp. 4500-4507
    • Holttä, E.1    Sistonen, L.2    Alitalo, K.3
  • 25
    • 0023836862 scopus 로고
    • Dissociation of c-fos from ODC expression and neuronal differentiation in a PC12 subline stably transfected with an inducible N-ras oncogene
    • Guerrero, I , Pellicer, A , and Alitalo, K. Dissociation of c-fos from ODC expression and neuronal differentiation in a PC12 subline stably transfected with an inducible N-ras oncogene Biochem. Biophys. Res Commun , 150: 1185-1192, 1988.
    • (1988) Biochem. Biophys. Res Commun , vol.150 , pp. 1185-1192
    • Guerrero, I.1    Pellicer, A.2    Alitalo, K.3
  • 26
    • 0023880427 scopus 로고
    • Effect of polyamine depletion on c-myc expression in human colon carcinoma cells
    • Celano, P., Baylin, S. B., Giardello, F. M , Nelkin, B. D , and Casero, R A Effect of polyamine depletion on c-myc expression in human colon carcinoma cells. J Biol. Chem., 263: 5491-5494, 1988
    • (1988) J Biol. Chem. , vol.263 , pp. 5491-5494
    • Celano, P.1    Baylin, S.B.2    Giardello, F.M.3    Nelkin, B.D.4    Casero, R.A.5
  • 28
    • 0028799607 scopus 로고
    • Rapid and regulated degradation of ornithine decarboxylase
    • Hayashi, S-I , and Murakami, Y Rapid and regulated degradation of ornithine decarboxylase Biochem. J., 306: 1-10, 1995.
    • (1995) Biochem. J. , vol.306 , pp. 1-10
    • Hayashi, S.-I.1    Murakami, Y.2
  • 29
    • 0021071962 scopus 로고
    • Effect of 1,3-diaminopropane on ornithine decarboxylase enzyme protein in thioacetamide-treated rat liver
    • Seely, J E , and Pegg, A E Effect of 1,3-diaminopropane on ornithine decarboxylase enzyme protein in thioacetamide-treated rat liver Biochem J. 216: 701-707, 1983
    • (1983) Biochem J. , vol.216 , pp. 701-707
    • Seely, J.E.1    Pegg, A.E.2


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