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Volumn 582, Issue 23-24, 2008, Pages 3445-3450

Stress-induced down-regulation of tumor-associated NADH oxidase during apoptosis in transformed cells

Author keywords

Apoptosis; Capsaicin; Down regulation; EGCg; Tumor associated NADH oxidase (tNOX); UVC

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 53049104152     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.09.008     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 0002231069 scopus 로고    scopus 로고
    • NADH oxidase: a multifunctional ectoprotein of the eukaryotic cell surface
    • Asard H., Bérczi A., and Caubergs R. (Eds), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Morré D.J. NADH oxidase: a multifunctional ectoprotein of the eukaryotic cell surface. In: Asard H., Bérczi A., and Caubergs R. (Eds). Plasma Membrane Redox Systems and their Role in Biological Stress and Disease (1998), Kluwer Academic Publishers, Dordrecht, The Netherlands 121-156
    • (1998) Plasma Membrane Redox Systems and their Role in Biological Stress and Disease , pp. 121-156
    • Morré, D.J.1
  • 2
    • 0033922168 scopus 로고    scopus 로고
    • Cell membrane redox systems and transformation
    • Chueh P.J. Cell membrane redox systems and transformation. Antiox. Redox Signal. 2 (2000) 177-187
    • (2000) Antiox. Redox Signal. , vol.2 , pp. 177-187
    • Chueh, P.J.1
  • 3
    • 0037133540 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface
    • Chueh P.J., Kim C., Cho N., Morré D.M., and Morré D.J. Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface. Biochemistry 41 (2002) 3732-3741
    • (2002) Biochemistry , vol.41 , pp. 3732-3741
    • Chueh, P.J.1    Kim, C.2    Cho, N.3    Morré, D.M.4    Morré, D.J.5
  • 4
    • 0037203806 scopus 로고    scopus 로고
    • A site-directed mutagenesis analysis of tNOX functional domains
    • Chueh P.J., Morré D.M., and Morré D.J. A site-directed mutagenesis analysis of tNOX functional domains. Biochim. Biophys. Acta 1594 (2002) 74-83
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 74-83
    • Chueh, P.J.1    Morré, D.M.2    Morré, D.J.3
  • 5
    • 0026772314 scopus 로고
    • Stimulation of NADH oxidase activity from rat liver plasma membranes by growth factors and hormones is decreased or absent with hepatoma plasma membranes
    • Bruno M., Brightman A.O., Lawrence J., Werderitsh D., Morré D.M., and Morré D.J. Stimulation of NADH oxidase activity from rat liver plasma membranes by growth factors and hormones is decreased or absent with hepatoma plasma membranes. Biochem. J. 284 (1992) 625-628
    • (1992) Biochem. J. , vol.284 , pp. 625-628
    • Bruno, M.1    Brightman, A.O.2    Lawrence, J.3    Werderitsh, D.4    Morré, D.M.5    Morré, D.J.6
  • 6
    • 0028960631 scopus 로고
    • Differential response of the NADH oxidase of plasma membranes of rat liver and hepatoma and HeLa cells to thiol reagents
    • Morré D.J., and Morré D.M. Differential response of the NADH oxidase of plasma membranes of rat liver and hepatoma and HeLa cells to thiol reagents. J. Bioenerg. Biomembr. 27 (1995) 137-144
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 137-144
    • Morré, D.J.1    Morré, D.M.2
  • 7
    • 0029608917 scopus 로고
    • NADH oxidase activity of HeLa plasma membranes inhibited by the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N′-(4-chlorophenyl) urea (LY181984) at an external site
    • Morré D.J. NADH oxidase activity of HeLa plasma membranes inhibited by the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N′-(4-chlorophenyl) urea (LY181984) at an external site. Biochim. Biophys. Acta 1240 (1995) 201-208
    • (1995) Biochim. Biophys. Acta , vol.1240 , pp. 201-208
    • Morré, D.J.1
  • 8
    • 0028925916 scopus 로고
    • Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture
    • Morré D.J., Chueh P.J., and Morré D.M. Capsaicin inhibits preferentially the NADH oxidase and growth of transformed cells in culture. Proc. Natl. Acad. Sci. USA 92 (1995) 1831-1835
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1831-1835
    • Morré, D.J.1    Chueh, P.J.2    Morré, D.M.3
  • 9
    • 0030854118 scopus 로고    scopus 로고
    • A circulating form of NADH oxidase activity responsive to the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N′-(4-chlorophenyl)urea (LY181984) specific to sera of cancer patients
    • Morré D.J., and Reust T. A circulating form of NADH oxidase activity responsive to the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N′-(4-chlorophenyl)urea (LY181984) specific to sera of cancer patients. J. Bioenerg. Biomembr. 29 (1997) 281-289
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 281-289
    • Morré, D.J.1    Reust, T.2
  • 10
    • 0031570783 scopus 로고    scopus 로고
    • NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients
    • Morré D.J., Caldwell S., Mayorga A., Wu L.-Y., and Morré D.M. NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients. Arch. Biochim. Biophys. 342 (1997) 224-230
    • (1997) Arch. Biochim. Biophys. , vol.342 , pp. 224-230
    • Morré, D.J.1    Caldwell, S.2    Mayorga, A.3    Wu, L.-Y.4    Morré, D.M.5
  • 11
    • 0034308086 scopus 로고    scopus 로고
    • Preferential inhibition by (-)-epigallocatechin-3-gallate of the cell surface NADH oxidase and growth of transformed cells in culture
    • Morré D.J., Bridge A., Wu L.-Y., and Morré D.M. Preferential inhibition by (-)-epigallocatechin-3-gallate of the cell surface NADH oxidase and growth of transformed cells in culture. Biochem. Pharmacol. 60 (2000) 937-946
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 937-946
    • Morré, D.J.1    Bridge, A.2    Wu, L.-Y.3    Morré, D.M.4
  • 13
    • 34249714358 scopus 로고    scopus 로고
    • Effect of polyclonal antisera to recombinant tNOX protein on the growth of transformed cells
    • Chen C.F., Huang S., Liu S.C., and Chueh P.J. Effect of polyclonal antisera to recombinant tNOX protein on the growth of transformed cells. BioFactors 28 (2006) 119-133
    • (2006) BioFactors , vol.28 , pp. 119-133
    • Chen, C.F.1    Huang, S.2    Liu, S.C.3    Chueh, P.J.4
  • 14
    • 34247859081 scopus 로고    scopus 로고
    • Mouse embryonic fibroblast cells from transgenic mice overexpressing tNOX exhibit an altered growth and drug response phenotype
    • Yagiz K., Wu L.-Y., Kuntz C.P., Morré D.J., and Morré D.M. Mouse embryonic fibroblast cells from transgenic mice overexpressing tNOX exhibit an altered growth and drug response phenotype. J. Cell Biochem. 101 (2007) 295-306
    • (2007) J. Cell Biochem. , vol.101 , pp. 295-306
    • Yagiz, K.1    Wu, L.-Y.2    Kuntz, C.P.3    Morré, D.J.4    Morré, D.M.5
  • 15
    • 13444304185 scopus 로고    scopus 로고
    • TNOX is both necessary and sufficient as a cellular target for the anticancer actions of capsaicin and the green tea catechin (-)-epigallocatechin-3-gallate
    • Chueh P.J., Wu L.-Y., Morré D.M., and Morré D.J. TNOX is both necessary and sufficient as a cellular target for the anticancer actions of capsaicin and the green tea catechin (-)-epigallocatechin-3-gallate. BioFactors 20 (2004) 249-263
    • (2004) BioFactors , vol.20 , pp. 249-263
    • Chueh, P.J.1    Wu, L.-Y.2    Morré, D.M.3    Morré, D.J.4
  • 16
    • 36849021716 scopus 로고    scopus 로고
    • RNA interference targeting tNOX attenuates cell migration via a mechanism that involved membrane association of Rac
    • Liu S.C., Yang J.J., Shao K.N., and Chueh P.J. RNA interference targeting tNOX attenuates cell migration via a mechanism that involved membrane association of Rac. Biochem. Biophys. Res. Commun. 365 (2008) 672-677
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 672-677
    • Liu, S.C.1    Yang, J.J.2    Shao, K.N.3    Chueh, P.J.4
  • 17
    • 45849153496 scopus 로고    scopus 로고
    • The apoptotic effect of nanosilver is mediated by a ROS- and JNK-dependent mechanism involving the mitochondrial pathway in NIH3T3 cells
    • Hsin Y.H., Chen C.F., Huang S., Shih T.S., Lai P.S., and Chueh P.J. The apoptotic effect of nanosilver is mediated by a ROS- and JNK-dependent mechanism involving the mitochondrial pathway in NIH3T3 cells. Toxicol. Lett. 179 (2008) 130-139
    • (2008) Toxicol. Lett. , vol.179 , pp. 130-139
    • Hsin, Y.H.1    Chen, C.F.2    Huang, S.3    Shih, T.S.4    Lai, P.S.5    Chueh, P.J.6
  • 18
    • 0032104153 scopus 로고    scopus 로고
    • Oscillatory and steady laminar shear stress differentially affect human endothelial redox state: role of a superoxide-producing NADH oxidase
    • De Keulenaer G.W., Chappell D.C., Ishizaka N., Nerem R.M., Alexander R.W., and Griendling K.K. Oscillatory and steady laminar shear stress differentially affect human endothelial redox state: role of a superoxide-producing NADH oxidase. Circ. Res. 82 (1998) 1094-1101
    • (1998) Circ. Res. , vol.82 , pp. 1094-1101
    • De Keulenaer, G.W.1    Chappell, D.C.2    Ishizaka, N.3    Nerem, R.M.4    Alexander, R.W.5    Griendling, K.K.6
  • 19
    • 0842304283 scopus 로고    scopus 로고
    • Induction of apoptosis in leukemic cells by homovanillic acid derivative, capsaicin, through oxidative stress: implication of phosphorylation of p53 at Ser-15 residue by reactive oxygen species
    • Ito K., Nakazato T., Yamato K., Miyakawa Y., Yamada T., Hozumi N., Segawa K., Ikeda Y., and Kizaki M. Induction of apoptosis in leukemic cells by homovanillic acid derivative, capsaicin, through oxidative stress: implication of phosphorylation of p53 at Ser-15 residue by reactive oxygen species. Cancer Res. 64 (2004) 1071-1078
    • (2004) Cancer Res. , vol.64 , pp. 1071-1078
    • Ito, K.1    Nakazato, T.2    Yamato, K.3    Miyakawa, Y.4    Yamada, T.5    Hozumi, N.6    Segawa, K.7    Ikeda, Y.8    Kizaki, M.9
  • 20
    • 31444437266 scopus 로고    scopus 로고
    • Induction of apoptosis in prostate tumor PC-3 cells and inhibition of xenograft prostate tumor growth by the vanilloid capsaicin
    • Sánchez A.M., Sánchez M.G., Malagarie-Cazenave S., Olea N., and Díaz-Laviada I. Induction of apoptosis in prostate tumor PC-3 cells and inhibition of xenograft prostate tumor growth by the vanilloid capsaicin. Apoptosis 11 (2006) 89-99
    • (2006) Apoptosis , vol.11 , pp. 89-99
    • Sánchez, A.M.1    Sánchez, M.G.2    Malagarie-Cazenave, S.3    Olea, N.4    Díaz-Laviada, I.5
  • 21
    • 4644295000 scopus 로고    scopus 로고
    • Capsaicin, a spicy component of hot pepper, induces apoptosis by activation of the peroxisome proliferators-activated receptor gamma in HT-29 human colon cancer cells
    • Kim C.S., Park W.H., Park J.Y., Kang J.H., Kim M.O., Kawada T., Yoo H., Han I.S., and Yu R. Capsaicin, a spicy component of hot pepper, induces apoptosis by activation of the peroxisome proliferators-activated receptor gamma in HT-29 human colon cancer cells. J. Med. Food 7 (2004) 267-273
    • (2004) J. Med. Food , vol.7 , pp. 267-273
    • Kim, C.S.1    Park, W.H.2    Park, J.Y.3    Kang, J.H.4    Kim, M.O.5    Kawada, T.6    Yoo, H.7    Han, I.S.8    Yu, R.9
  • 22
    • 34247898927 scopus 로고    scopus 로고
    • Involvement of AMPK signaling cascade in capsaicin-induced apoptosis of HT-29 colon cancer cells
    • Kim Y.M., Hwang J.T., Kwak D.W., Lee Y.K., and Park O.J. Involvement of AMPK signaling cascade in capsaicin-induced apoptosis of HT-29 colon cancer cells. Ann. NY Acad. Sci. 1095 (2007) 496-503
    • (2007) Ann. NY Acad. Sci. , vol.1095 , pp. 496-503
    • Kim, Y.M.1    Hwang, J.T.2    Kwak, D.W.3    Lee, Y.K.4    Park, O.J.5
  • 23
    • 33845789994 scopus 로고    scopus 로고
    • Apoptotic effect of EGCG in HT-29 colon cancer cells via AMPK signal pathway
    • Hwang J.T., Ha J., Park I.J., Lee S.K., Baik H.W., Kim Y.M., and Park O.J. Apoptotic effect of EGCG in HT-29 colon cancer cells via AMPK signal pathway. Cancer Lett. 247 (2007) 115-121
    • (2007) Cancer Lett. , vol.247 , pp. 115-121
    • Hwang, J.T.1    Ha, J.2    Park, I.J.3    Lee, S.K.4    Baik, H.W.5    Kim, Y.M.6    Park, O.J.7
  • 24
    • 17644401337 scopus 로고    scopus 로고
    • (-)-Epigallocatechin gallate and polyphenon E inhibit growth and activation of the epidermal growth factor receptor and human epidermal growth factor receptor-2 signaling pathways in human colon cancer cells
    • Shimizu M., Deguchi A., Lim J.T., Moriwaki H., Kopelovich L., and Weinstein I.B. (-)-Epigallocatechin gallate and polyphenon E inhibit growth and activation of the epidermal growth factor receptor and human epidermal growth factor receptor-2 signaling pathways in human colon cancer cells. Clin. Cancer Res. 11 (2005) 2735-2746
    • (2005) Clin. Cancer Res. , vol.11 , pp. 2735-2746
    • Shimizu, M.1    Deguchi, A.2    Lim, J.T.3    Moriwaki, H.4    Kopelovich, L.5    Weinstein, I.B.6
  • 25
    • 0042423355 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate-induced stress signals in HT-29 human colon adenocarcinoma cells
    • Chen C., Shen G., Hebbar V., Hu R., Owuor E.D., and Kong A.N. Epigallocatechin-3-gallate-induced stress signals in HT-29 human colon adenocarcinoma cells. Carcinogenesis 24 (2003) 1369-1378
    • (2003) Carcinogenesis , vol.24 , pp. 1369-1378
    • Chen, C.1    Shen, G.2    Hebbar, V.3    Hu, R.4    Owuor, E.D.5    Kong, A.N.6
  • 27
    • 33847313631 scopus 로고    scopus 로고
    • Down-regulation of survivin by ultraviolet C radiation is dependent on p53 and results in G(2)-M arrest in A549 cells
    • Ikeda M., Okamoto I., Tamura K., Satoh T., Yonesaka K., Fukuoka M., and Nakagawa K. Down-regulation of survivin by ultraviolet C radiation is dependent on p53 and results in G(2)-M arrest in A549 cells. Cancer Lett. 248 (2007) 292-298
    • (2007) Cancer Lett. , vol.248 , pp. 292-298
    • Ikeda, M.1    Okamoto, I.2    Tamura, K.3    Satoh, T.4    Yonesaka, K.5    Fukuoka, M.6    Nakagawa, K.7
  • 28
    • 34547949167 scopus 로고    scopus 로고
    • Translational repression of MCL-1 couples stress-induced eIF2 alpha phosphorylation to mitochondrial apoptosis initiation
    • Fritsch R.M., Sclneider G., Saur D., Scheibel M., and Schmid R.M. Translational repression of MCL-1 couples stress-induced eIF2 alpha phosphorylation to mitochondrial apoptosis initiation. J. Boil. Chem. 282 (2007) 22551-22562
    • (2007) J. Boil. Chem. , vol.282 , pp. 22551-22562
    • Fritsch, R.M.1    Sclneider, G.2    Saur, D.3    Scheibel, M.4    Schmid, R.M.5
  • 29
    • 35348954836 scopus 로고    scopus 로고
    • UVC inhibits HIF-1alpha protein translation by a DNA damage- and topoisomerase I-independent pathway
    • Rapisarda A., and Melillo G. UVC inhibits HIF-1alpha protein translation by a DNA damage- and topoisomerase I-independent pathway. Oncogene 26 (2007) 6875-6884
    • (2007) Oncogene , vol.26 , pp. 6875-6884
    • Rapisarda, A.1    Melillo, G.2
  • 30
    • 0033553421 scopus 로고    scopus 로고
    • Down-regulation of tumor necrosis factor alpha expression by activating transcription factor 2 increases UVC-induced apoptosis of late-stage melanoma cells
    • Ivanov V.N., and Ronai Z. Down-regulation of tumor necrosis factor alpha expression by activating transcription factor 2 increases UVC-induced apoptosis of late-stage melanoma cells. J. Biol. Chem. 274 (1999) 14079-14089
    • (1999) J. Biol. Chem. , vol.274 , pp. 14079-14089
    • Ivanov, V.N.1    Ronai, Z.2
  • 33
    • 35848942129 scopus 로고    scopus 로고
    • Fbw7 and Usp28 regulate myc protein stability in response to DNA damage
    • Popov N., Herold S., Llamazares M., Schülein C., and Eilers M. Fbw7 and Usp28 regulate myc protein stability in response to DNA damage. Cell Cycle 6 (2007) 2327-2331
    • (2007) Cell Cycle , vol.6 , pp. 2327-2331
    • Popov, N.1    Herold, S.2    Llamazares, M.3    Schülein, C.4    Eilers, M.5
  • 34
    • 33748753391 scopus 로고    scopus 로고
    • UV induces p21 rapid turnover independently of ubiquitin and Skp2
    • Lee H., Zeng S.X., and Lu H. UV induces p21 rapid turnover independently of ubiquitin and Skp2. J. Biol. Chem. 281 (2006) 26876-26883
    • (2006) J. Biol. Chem. , vol.281 , pp. 26876-26883
    • Lee, H.1    Zeng, S.X.2    Lu, H.3
  • 35
    • 33644834349 scopus 로고    scopus 로고
    • Cleavage of epidermal growth factor receptor by caspase during apoptosis is independent of its internalization
    • He Y.Y., Huang J.L., and Chignell C.F. Cleavage of epidermal growth factor receptor by caspase during apoptosis is independent of its internalization. Oncogene 25 (2006) 1521-1531
    • (2006) Oncogene , vol.25 , pp. 1521-1531
    • He, Y.Y.1    Huang, J.L.2    Chignell, C.F.3


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