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Volumn 60, Issue 11, 2000, Pages 2919-2925

Inhibition of translation initiation mediates the anticancer effect of the n-3 polyunsaturated fatty acid eicosapentaenoic acid

Author keywords

[No Author keywords available]

Indexed keywords

ICOSAPENTAENOIC ACID; OMEGA 3 FATTY ACID;

EID: 0343851156     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (104)

References (48)
  • 1
    • 0028203340 scopus 로고
    • Effect of eicosapentaenoic acid and other fatty acids on the growth in vitro of human pancreatic cancer cell lines
    • Falconer, J. S., Ross, J. A., Fearon, K. C., Hawkins, R. A., O'Riordain, M. G., and Carter, D. C. Effect of eicosapentaenoic acid and other fatty acids on the growth in vitro of human pancreatic cancer cell lines. Br. J. Cancer, 69: 826-832, 1994.
    • (1994) Br. J. Cancer , vol.69 , pp. 826-832
    • Falconer, J.S.1    Ross, J.A.2    Fearon, K.C.3    Hawkins, R.A.4    O'Riordain, M.G.5    Carter, D.C.6
  • 2
    • 0029822029 scopus 로고    scopus 로고
    • Cell cycle arrest and induction of apoptosis in pancreatic cancer cells exposed to eicosapentaenoic acid in vitro
    • Lai, P. B., Ross, J. A., Fearon, K. C., Anderson, J. D., and Carter, D. C. Cell cycle arrest and induction of apoptosis in pancreatic cancer cells exposed to eicosapentaenoic acid in vitro. Br. J. Cancer, 74: 1375-1383, 1996.
    • (1996) Br. J. Cancer , vol.74 , pp. 1375-1383
    • Lai, P.B.1    Ross, J.A.2    Fearon, K.C.3    Anderson, J.D.4    Carter, D.C.5
  • 3
    • 0032400501 scopus 로고    scopus 로고
    • Cell proliferation, apoptosis and accumulation of lipid droplets in U937-1 cells incubated with eicosapentaenoic acid
    • Finstad, H. S., Drevon, C. A., Kulseth, M. A., Synstad, A. V., Knudsen, E., and Kolset, S. O. Cell proliferation, apoptosis and accumulation of lipid droplets in U937-1 cells incubated with eicosapentaenoic acid. Biochem. J., 336: 451-459, 1998.
    • (1998) Biochem. J. , vol.336 , pp. 451-459
    • Finstad, H.S.1    Drevon, C.A.2    Kulseth, M.A.3    Synstad, A.V.4    Knudsen, E.5    Kolset, S.O.6
  • 4
    • 0030040547 scopus 로고    scopus 로고
    • Effect of free fatty acids on two-stage skin carcinogenesis in mice
    • Ramesh, G., and Das, U. N. Effect of free fatty acids on two-stage skin carcinogenesis in mice. Cancer Lett., 100: 199-209, 1996.
    • (1996) Cancer Lett. , vol.100 , pp. 199-209
    • Ramesh, G.1    Das, U.N.2
  • 5
    • 0027215979 scopus 로고
    • Kinetics of the inhibition of tumour growth in mice by eicosapentaenoic acid-reversal by linoleic acid
    • Hudson, E. A., Beck, S. A., and Tisdale, M. J. Kinetics of the inhibition of tumour growth in mice by eicosapentaenoic acid-reversal by linoleic acid. Biochem. Pharmacol., 45: 2189-2194, 1993.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 2189-2194
    • Hudson, E.A.1    Beck, S.A.2    Tisdale, M.J.3
  • 7
    • 0032939479 scopus 로고    scopus 로고
    • Essential fatty acids and their metabolites and cancer
    • Das, U. N. Essential fatty acids and their metabolites and cancer. Nutrition, 15: 239-241, 1999.
    • (1999) Nutrition , vol.15 , pp. 239-241
    • Das, U.N.1
  • 8
    • 0032052077 scopus 로고    scopus 로고
    • Essential fatty acids: Molecular and cellular basis of their anti-cancer action and clinical implications
    • Jiang, W. G., Bryce, R. P., and Horrobin, D. F. Essential fatty acids: molecular and cellular basis of their anti-cancer action and clinical implications. Crit. Rev. Oncol. Hematol., 27: 179-209, 1998.
    • (1998) Crit. Rev. Oncol. Hematol. , vol.27 , pp. 179-209
    • Jiang, W.G.1    Bryce, R.P.2    Horrobin, D.F.3
  • 9
    • 0020583793 scopus 로고
    • Eskimo diets and diseases
    • Eskimo diets and diseases. Lancet, 21: 1139-1141, 1983.
    • (1983) Lancet , vol.21 , pp. 1139-1141
  • 10
    • 0024535082 scopus 로고
    • Fish consumption and breast cancer risk: An ecological study
    • Kaizer, L., Boyd, N. F., Kriukov, V., and Tritchler, D. Fish consumption and breast cancer risk: an ecological study. Nutr. Cancer, 12: 61-68, 1989.
    • (1989) Nutr. Cancer , vol.12 , pp. 61-68
    • Kaizer, L.1    Boyd, N.F.2    Kriukov, V.3    Tritchler, D.4
  • 14
    • 0028266931 scopus 로고
    • mRNA translation: Influence of the 5′ and 3′ untranslated regions
    • Sonenberg, N. mRNA translation: influence of the 5′ and 3′ untranslated regions. Curr. Opin. Genet. Dev., 4: 310-315, 1994.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 310-315
    • Sonenberg, N.1
  • 15
    • 0026342613 scopus 로고
    • An analysis of vertebrate mRNA sequences: Intimations of translational control
    • Kozak, M. An analysis of vertebrate mRNA sequences: intimations of translational control. J. Cell Biol., 115: 887-903, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 887-903
    • Kozak, M.1
  • 16
    • 0023350617 scopus 로고
    • The involvement of mRNA secondary structure in protein synthesis
    • Pelletier, T., and Sonenberg, N. The involvement of mRNA secondary structure in protein synthesis. Biochem. Cell Biol., 65: 576-581, 1987.
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 576-581
    • Pelletier, T.1    Sonenberg, N.2
  • 17
    • 0027140480 scopus 로고
    • Tumor suppression by RNA from the 3′ untranslated region of α-tropomyosin
    • Rastinejad, F., Conboy, M. J., Rando, T. A., and Blau, H. M. Tumor suppression by RNA from the 3′ untranslated region of α-tropomyosin. Cell, 75: 1107-1117, 1993.
    • (1993) Cell , vol.75 , pp. 1107-1117
    • Rastinejad, F.1    Conboy, M.J.2    Rando, T.A.3    Blau, H.M.4
  • 18
    • 0026701570 scopus 로고
    • Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase
    • Koromilas, A. E., Roy, S., Barber, G. N., Katze, M. G., and Sonenberg, N. Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase. Science (Washington DC), 257: 1685-1689, 1992.
    • (1992) Science (Washington DC) , vol.257 , pp. 1685-1689
    • Koromilas, A.E.1    Roy, S.2    Barber, G.N.3    Katze, M.G.4    Sonenberg, N.5
  • 19
    • 0029118217 scopus 로고
    • Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells
    • Donze, O., Jagus, R., Koromilas, A. E., Hershey, J. W., and Sonenberg, N. Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells. EMBO J., 14: 3828-3834, 1995.
    • (1995) EMBO J. , vol.14 , pp. 3828-3834
    • Donze, O.1    Jagus, R.2    Koromilas, A.E.3    Hershey, J.W.4    Sonenberg, N.5
  • 20
    • 0029740136 scopus 로고    scopus 로고
    • Expression of a translationally regulated, dominant-negative CCAAT/enhancer-binding protein β isoform and up-regulation of the eukaryotic translation initiation factor 2α are correlated with neoplastic transformation of mammary epithelial cells
    • Raught, B., Gingras, A-C., James, A., Medina, D., Sonenberg, N., and Rosen, J. M. Expression of a translationally regulated, dominant-negative CCAAT/enhancer-binding protein β isoform and up-regulation of the eukaryotic translation initiation factor 2α are correlated with neoplastic transformation of mammary epithelial cells. Cancer Res., 56: 4382-4386, 1996.
    • (1996) Cancer Res. , vol.56 , pp. 4382-4386
    • Raught, B.1    Gingras, A.-C.2    James, A.3    Medina, D.4    Sonenberg, N.5    Rosen, J.M.6
  • 21
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ cap
    • Lazaris-Karatzas, A., Montine, K. S., and Sonenberg, N. Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5′ 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
  • 22
    • 0030443685 scopus 로고    scopus 로고
    • The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth
    • Rousseau, D., Gingras, A. C., Pause, A., and Sonenberg, N. The eIF4E-binding proteins 1 and 2 are negative regulators of cell growth. Oncogene, 13: 2415-2420, 1996.
    • (1996) Oncogene , vol.13 , pp. 2415-2420
    • Rousseau, D.1    Gingras, A.C.2    Pause, A.3    Sonenberg, N.4
  • 23
    • 0028897627 scopus 로고
    • Reduction of translation initiation factor 4E decreases the malignancy of ras-transformed cloned rat embryo fibroblasts
    • Graff, J. R., Boghaert, E. R., De Benedetti, A., Tudor, D. L., Zimmer, C. C., Chan, S. K., and Zimmer, S. G. Reduction of translation initiation factor 4E decreases the malignancy of ras-transformed cloned rat embryo fibroblasts. Int. J. Cancer, 60: 255-263, 1995.
    • (1995) Int. J. Cancer , vol.60 , pp. 255-263
    • Graff, J.R.1    Boghaert, E.R.2    De Benedetti, A.3    Tudor, D.L.4    Zimmer, C.C.5    Chan, S.K.6    Zimmer, S.G.7
  • 24
    • 0028605677 scopus 로고
    • Regulation of translation and cell growth by eIF-4E
    • Sonenberg, N. Regulation of translation and cell growth by eIF-4E. Biochimie, 76: 839-846, 1994.
    • (1994) Biochimie , vol.76 , pp. 839-846
    • Sonenberg, N.1
  • 25
    • 0025016922 scopus 로고
    • 2+ pool in T cells through a mechanism independent of phosphoinositide turnover
    • 2+ pool in T cells through a mechanism independent of phosphoinositide turnover. J. Biol. Chem., 265: 902-901, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 902-1901
    • Chow, S.C.1    Jondal, M.2
  • 29
    • 0030041884 scopus 로고    scopus 로고
    • Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E
    • Rousseau, D., Kaspar, R., Rosenwald, I., Gehrke, L., and Sonenberg, N. Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 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
  • 31
    • 0027215264 scopus 로고
    • Characterization of factors in routine laboratory protocols that significantly influence the Feulgen reaction
    • Kiss, R., Salmon, I., Camby, I., Gras, S., and Pasteels, J-L. Characterization of factors in routine laboratory protocols that significantly influence the Feulgen reaction. J. Histochem. Cytochem., 41: 935-945, 1993.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 935-945
    • Kiss, R.1    Salmon, I.2    Camby, I.3    Gras, S.4    Pasteels, J.-L.5
  • 32
    • 0027534681 scopus 로고
    • Relationship between proliferative activity and ploidy level in a series of 530 human brain tumors, including astrocytomas, meningiomas, schwannomas, and metastases
    • Salmon, I., and Kiss, R. Relationship between proliferative activity and ploidy level in a series of 530 human brain tumors, including astrocytomas, meningiomas, schwannomas, and metastases. Hum. Pathol., 24: 329-335, 1993.
    • (1993) Hum. Pathol. , vol.24 , pp. 329-335
    • Salmon, I.1    Kiss, R.2
  • 34
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • Berridge, M. J. Capacitative calcium entry. Biochem. J., 312: 1-11, 1995.
    • (1995) Biochem. J. , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 36
    • 0028825043 scopus 로고
    • Cytotoxic action of cis unsaturated fatty acids on human cervical carcinoma (HeLa) cells in vitro. Prostaglandins leukotrienes essent
    • Sagar, P. S., and Das, U. N. Cytotoxic action of cis unsaturated fatty acids on human cervical carcinoma (HeLa) cells in vitro. Prostaglandins Leukotrienes Essent. Fatty Acids, 53: 287-299, 1995.
    • (1995) Fatty Acids , vol.53 , pp. 287-299
    • Sagar, P.S.1    Das, U.N.2
  • 38
    • 0025326163 scopus 로고
    • Calcium-dependent regulation of protein synthesis in intact mammalian cells
    • Brostrom, C. O., and Brostrom, M. A. Calcium-dependent regulation of protein synthesis in intact mammalian cells. Annu. Rev. Physiol., 52: 577-590, 1990.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 577-590
    • Brostrom, C.O.1    Brostrom, M.A.2
  • 40
    • 0029067408 scopus 로고
    • Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis
    • Srivastava, S. P., Davies, M. V., and Kaufman, R. J. Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J. Biol. Chem., 270: 16619-16624, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16619-16624
    • Srivastava, S.P.1    Davies, M.V.2    Kaufman, R.J.3
  • 41
    • 0031961688 scopus 로고    scopus 로고
    • Regulation of translational initiation during cellular responses to stress
    • Brostrom, C. O., and Brostrom, M. A. Regulation of translational initiation during cellular responses to stress. Prog. Nucleic Acid Res. Mol. Biol., 58: 79-125, 1998.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.58 , pp. 79-125
    • Brostrom, C.O.1    Brostrom, M.A.2
  • 42
    • 0029968705 scopus 로고    scopus 로고
    • Initiation of protein synthesis in eukaryotic cells
    • Pain, V. M. Initiation of protein synthesis in eukaryotic cells. Eur. J. Biochem., 236: 747-771, 1996.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 747-771
    • Pain, V.M.1
  • 43
    • 0029013693 scopus 로고
    • Regulation of the interferon-inducible protein kinase PKR and (2′-5′) oligo (adenylate) synthetase by a catalytically inactive PKR mutant through competition for double-stranded RNA binding
    • Sharp, T. V., Xiao, Q., Justesen, J., Gewert, D. R., and Clemens, M. J. Regulation of the interferon-inducible protein kinase PKR and (2′-5′) oligo (adenylate) synthetase by a catalytically inactive PKR mutant through competition for double-stranded RNA binding. Eur. J. Biochem., 230: 97-103, 1995.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 97-103
    • Sharp, T.V.1    Xiao, Q.2    Justesen, J.3    Gewert, D.R.4    Clemens, M.J.5
  • 44
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P., Zhang, Y., and Ron, D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature (Lond.), 397: 271-174, 1999.
    • (1999) Nature (Lond.) , vol.397 , pp. 271-1174
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 45
    • 0016180710 scopus 로고
    • Model for the regulation of mRNA translation applied to haemoglobin synthesis
    • Lodish, H. F. Model for the regulation of mRNA translation applied to haemoglobin synthesis. Nature (Lond.), 251: 385-388, 1974.
    • (1974) Nature (Lond.) , vol.251 , pp. 385-388
    • Lodish, H.F.1
  • 46
    • 0019178883 scopus 로고
    • Mathematical modelling of translation of mRNA in eucaryotes; steady states, time-dependent processes and application to reticulocytes
    • Heinrich, R., and Rapoport, T. A. Mathematical modelling of translation of mRNA in eucaryotes; steady states, time-dependent processes and application to reticulocytes. J. Theor. Biol., 86: 279-313, 1980.
    • (1980) J. Theor. Biol. , vol.86 , pp. 279-313
    • Heinrich, R.1    Rapoport, T.A.2
  • 48
    • 0031878589 scopus 로고    scopus 로고
    • Dietary fish oil inhibits the expression of farnesyl protein transferase and colon tumor development in rodents
    • Singh, J., Hamid, R., and Reddy, B. S. Dietary fish oil inhibits the expression of farnesyl protein transferase and colon tumor development in rodents. Carcinogenesis (Lond.), 19: 985-989, 1998.
    • (1998) Carcinogenesis (Lond.) , vol.19 , pp. 985-989
    • Singh, J.1    Hamid, R.2    Reddy, B.S.3


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