메뉴 건너뛰기




Volumn 1683, Issue 1-3, 2004, Pages 22-32

Induction of antioxidant enzymes by FAK in a human leukemic cell line, HL-60

Author keywords

Anti apoptosis; Antioxidant enzyme; FAK; Lipid peroxidation; PHGPx; ROS

Indexed keywords

ANTIOXIDANT; CATALASE; FOCAL ADHESION KINASE; HYDROGEN PEROXIDE; MESSENGER RNA; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; REACTIVE OXYGEN METABOLITE;

EID: 3042656867     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2004.04.002     Document Type: Article
Times cited : (12)

References (38)
  • 2
    • 0037188927 scopus 로고    scopus 로고
    • GFP-FRNK disrupts focal adhesions and induces anoikis in neonatal rat ventricular myocytes
    • Heidkamp M.C., Bayer A.L., Kalina J.A., Eble D.M., Samarel A.M. GFP-FRNK disrupts focal adhesions and induces anoikis in neonatal rat ventricular myocytes. Circ. Res. 90:2000;1282-1289
    • (2000) Circ. Res. , vol.90 , pp. 1282-1289
    • Heidkamp, M.C.1    Bayer, A.L.2    Kalina, J.A.3    Eble, D.M.4    Samarel, A.M.5
  • 3
    • 0037064030 scopus 로고    scopus 로고
    • Dual inhibition of focal adhesion kinase and epidermal growth factor receptor pathways cooperatively induces death receptor-mediated apoptosis in human breast cancer cells
    • Golubovskaya V., Beviglia L., Xu L.H., Earp H.S., Craven R., Cance W. Dual inhibition of focal adhesion kinase and epidermal growth factor receptor pathways cooperatively induces death receptor-mediated apoptosis in human breast cancer cells. J. Biol. Chem. 277:2002;38978-38987
    • (2002) J. Biol. Chem. , vol.277 , pp. 38978-38987
    • Golubovskaya, V.1    Beviglia, L.2    Xu, L.H.3    Earp, H.S.4    Craven, R.5    Cance, W.6
  • 4
    • 0031590713 scopus 로고    scopus 로고
    • A Suppressive role of p125FAK protein tyrosine kinase in hydrogen peroxide-induced apoptosis of T98G cells
    • Sonoda Y., Kasahara T., Yokota-Aizu E., Ueno M., Watanabe S. A Suppressive role of p125FAK protein tyrosine kinase in hydrogen peroxide-induced apoptosis of T98G cells. Biochem. Biophys. Res. Commun. 241:1997;769-774
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 769-774
    • Sonoda, Y.1    Kasahara, T.2    Yokota-Aizu, E.3    Ueno, M.4    Watanabe, S.5
  • 5
    • 0034717285 scopus 로고    scopus 로고
    • Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60
    • Sonoda Y., Matsumoto Y., Funakoshi M., Yamamoto D., Hanks S.K., Kasahara T. Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60. J. Biol. Chem. 275:2000;16309-16315
    • (2000) J. Biol. Chem. , vol.275 , pp. 16309-16315
    • Sonoda, Y.1    Matsumoto, Y.2    Funakoshi, M.3    Yamamoto, D.4    Hanks, S.K.5    Kasahara, T.6
  • 9
    • 0036293621 scopus 로고    scopus 로고
    • Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-alpha-induced apoptosis in cultured mouse hepatocytes
    • Nagai H., Matsumaru K., Feng K., Kaplowitz G. Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-alpha-induced apoptosis in cultured mouse hepatocytes. Hepatology. 36:2002;55-64
    • (2002) Hepatology , vol.36 , pp. 55-64
    • Nagai, H.1    Matsumaru, K.2    Feng, K.3    Kaplowitz, G.4
  • 10
    • 0035900696 scopus 로고    scopus 로고
    • Opposite roles of selenium-dependent glutathione peroxidase-1 in superoxide generator diquat- and peroxynitrite-induced apoptosis and signaling
    • Fu Y., Sies H., Lei X.G. Opposite roles of selenium-dependent glutathione peroxidase-1 in superoxide generator diquat- and peroxynitrite-induced apoptosis and signaling. J. Biol. Chem. 276:2001;43004-43009
    • (2001) J. Biol. Chem. , vol.276 , pp. 43004-43009
    • Fu, Y.1    Sies, H.2    Lei, X.G.3
  • 11
    • 0028175470 scopus 로고    scopus 로고
    • Resistance to TNF-alpha adriamycin in the human breast cancer MCF-7 cell line: Relationship to MDR1, MnSOD, and TNF gene expression
    • Zyad A., Benard J., Tursz T., Clarke R., Chouaib S. Resistance to TNF-alpha adriamycin in the human breast cancer MCF-7 cell line: relationship to MDR1, MnSOD, and TNF gene expression. Cancer Res. 54:2002;825-831
    • (2002) Cancer Res. , vol.54 , pp. 825-831
    • Zyad, A.1    Benard, J.2    Tursz, T.3    Clarke, R.4    Chouaib, S.5
  • 12
    • 0032855506 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway
    • Nomura K., Imai H., Koumura T., Arai M., Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway. J. Biol. Chem. 274:1999;29294-29302
    • (1999) J. Biol. Chem. , vol.274 , pp. 29294-29302
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Arai, M.4    Nakagawa, Y.5
  • 14
    • 0025218905 scopus 로고
    • Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′,7′-dichlorofluorescin
    • Rothe G., Valet G. Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′, 7′-dichlorofluorescin. J. Leukoc. Biol. 47:1990;440-448
    • (1990) J. Leukoc. Biol. , vol.47 , pp. 440-448
    • Rothe, G.1    Valet, G.2
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95:1979;351-358
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 18
    • 0020549171 scopus 로고
    • Glutathione peroxidase, glutathione reductase, glutathione S-transferase and g-glutamyl-transpeptidase activities in human early pregnancy placenta
    • Di-Ilio C., Polidoro G., Arduini A., Muccini A., Federici G. Glutathione peroxidase, glutathione reductase, glutathione S-transferase and g-glutamyl-transpeptidase activities in human early pregnancy placenta. Biochem. Med. 29:1983;143-148
    • (1983) Biochem. Med. , vol.29 , pp. 143-148
    • Di-Ilio, C.1    Polidoro, G.2    Arduini, A.3    Muccini, A.4    Federici, G.5
  • 19
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • Flohe L., Gunzler W.A. Assays of glutathione peroxidase. Methods Enzymol. 105:1984;114-121
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohe, L.1    Gunzler, W.A.2
  • 20
    • 0021288878 scopus 로고
    • Superoxide dismutase assays
    • Flohe L., Otting F. Superoxide dismutase assays. Methods Enzymol. 105:1984;93-104
    • (1984) Methods Enzymol. , vol.105 , pp. 93-104
    • Flohe, L.1    Otting, F.2
  • 21
    • 0031939746 scopus 로고    scopus 로고
    • Suppression of leukotriene formation in RBL-2H3 cells that overexpressed phospholipid hydroperoxide glutathione peroxidase
    • Imai H., Narashima K., Arai M., Sakamoto H., Chiba N., Nakagawa Y. Suppression of leukotriene formation in RBL-2H3 cells that overexpressed phospholipid hydroperoxide glutathione peroxidase. J. Biol. Chem. 273:1998;1990-1997
    • (1998) J. Biol. Chem. , vol.273 , pp. 1990-1997
    • Imai, H.1    Narashima, K.2    Arai, M.3    Sakamoto, H.4    Chiba, N.5    Nakagawa, Y.6
  • 22
    • 0033521693 scopus 로고    scopus 로고
    • Validation of the peroxidative indicators, cis-parinaric acid and parinaroyl-phospholipids, in a model system and cultured cardiac myocytes
    • Drummen G.P., Op den Kamp J.A., Post J.A. Validation of the peroxidative indicators, cis-parinaric acid and parinaroyl-phospholipids, in a model system and cultured cardiac myocytes. Biochim. Biophys. Acta. 1436:1999;370-382
    • (1999) Biochim. Biophys. Acta. , vol.1436 , pp. 370-382
    • Drummen, G.P.1    Op Den Kamp, J.A.2    Post, J.A.3
  • 25
    • 0034840464 scopus 로고    scopus 로고
    • Cloning of phospholipid hydroperoxide glutathione peroxidase (PHGPx) as an anti-apoptotic and growth promoting gene of Burkitt lymphoma cells
    • Brielmeier M., Bechet J.M., Suppmann S., Conrad M., Laux G., Bornkamm G.W. Cloning of phospholipid hydroperoxide glutathione peroxidase (PHGPx) as an anti-apoptotic and growth promoting gene of Burkitt lymphoma cells. BioFactors. 14:2001;179-190
    • (2001) BioFactors , vol.14 , pp. 179-190
    • Brielmeier, M.1    Bechet, J.M.2    Suppmann, S.3    Conrad, M.4    Laux, G.5    Bornkamm, G.W.6
  • 26
    • 0032935722 scopus 로고    scopus 로고
    • Selenocysteine-containing proteins in mammals
    • Gladyshew V.N., Hatfield D.L. Selenocysteine-containing proteins in mammals. J. Biomed. Sci. 6:1999;151-160
    • (1999) J. Biomed. Sci. , vol.6 , pp. 151-160
    • Gladyshew, V.N.1    Hatfield, D.L.2
  • 27
    • 0027419580 scopus 로고
    • Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone
    • Weitzel F., Wendel A. Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone. J. Biol. Chem. 268:1993;6288-6293
    • (1993) J. Biol. Chem. , vol.268 , pp. 6288-6293
    • Weitzel, F.1    Wendel, A.2
  • 30
    • 0035827635 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha selectively induces MnSOD expression via mitochondria-to-nucleus signaling, whereas interleukin-1beta utilizes an alternative pathway
    • Rogers R.J., Monnier J.M., Nick H.S. Tumor necrosis factor-alpha selectively induces MnSOD expression via mitochondria-to-nucleus signaling, whereas interleukin-1beta utilizes an alternative pathway. J. Biol. Chem. 276:2001;20419-20427
    • (2001) J. Biol. Chem. , vol.276 , pp. 20419-20427
    • Rogers, R.J.1    Monnier, J.M.2    Nick, H.S.3
  • 31
    • 0033214460 scopus 로고    scopus 로고
    • Bombesin and platelet-derived growth factor induce association of endogenous focal adhesion kinase with Src in intact Swiss 3T3 cells
    • Salazar E.P., Rozengurt E. Bombesin and platelet-derived growth factor induce association of endogenous focal adhesion kinase with Src in intact Swiss 3T3 cells. J. Biol. Chem. 274:1999;28371-28378
    • (1999) J. Biol. Chem. , vol.274 , pp. 28371-28378
    • Salazar, E.P.1    Rozengurt, E.2
  • 32
    • 0034079862 scopus 로고    scopus 로고
    • Free radicals and antioxidants in the year 2000. a historical look to the future
    • Gutteridge J.M., Halliwell B. Free radicals and antioxidants in the year 2000. A historical look to the future. Ann. N.Y. Acad. Sci. 899:2000;136-147
    • (2000) Ann. N.Y. Acad. Sci. , vol.899 , pp. 136-147
    • Gutteridge, J.M.1    Halliwell, B.2
  • 33
    • 0030615325 scopus 로고    scopus 로고
    • Overexpression of Bcl-2 inhibits UVA-mediated immediate apoptosis in rat 6 fibroblasts: Evidence for the involvement of Bcl-2 as an antioxidant
    • Pourzand C., Rossier G., Reelfs O., Borner C., Tyrrell R.M. Overexpression of Bcl-2 inhibits UVA-mediated immediate apoptosis in rat 6 fibroblasts: evidence for the involvement of Bcl-2 as an antioxidant. Cancer Res. 57:1997;1405-1411
    • (1997) Cancer Res. , vol.57 , pp. 1405-1411
    • Pourzand, C.1    Rossier, G.2    Reelfs, O.3    Borner, C.4    Tyrrell, R.M.5
  • 35
    • 0035894104 scopus 로고    scopus 로고
    • Effect of overexpression of Bcl-2 on cellular oxidative damage, nitric oxide production, antioxidant defenses, and the proteasome
    • Lee M., Hyun D., Marshall K., Ellerby L.M., Bredesen D.E., Jenner P., Halliwell B. Effect of overexpression of Bcl-2 on cellular oxidative damage, nitric oxide production, antioxidant defenses, and the proteasome. Free Radic. Biol. Med. 31:2001;1550-1559
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1550-1559
    • Lee, M.1    Hyun, D.2    Marshall, K.3    Ellerby, L.M.4    Bredesen, D.E.5    Jenner, P.6    Halliwell, B.7
  • 38
    • 0041529697 scopus 로고    scopus 로고
    • An endogenous inhibitor of focal adhesion kinase blocks Rac1/JNK but not Ras/ERK-dependent signaling in vascular smooth muscle cells
    • Sundberg L.J., Galante L.M., Bill H.M., Mack C.P., Taylor J.M. An endogenous inhibitor of focal adhesion kinase blocks Rac1/JNK but not Ras/ERK-dependent signaling in vascular smooth muscle cells. J. Biol. Chem. 278:2003;29783-29791
    • (2003) J. Biol. Chem. , vol.278 , pp. 29783-29791
    • Sundberg, L.J.1    Galante, L.M.2    Bill, H.M.3    MacK, C.P.4    Taylor, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.