메뉴 건너뛰기




Volumn 60, Issue 3, 2008, Pages 171-179

Citrinin induces apoptosis in mouse embryonic stem cells

Author keywords

Apoptosis; Calcium; Caspase; Citrinin; Nitric oxide; ROS

Indexed keywords

CALCIUM; CASPASE 3; CASPASE 9; CITRININ; CYTOCHROME C; HEAT SHOCK PROTEIN 90; NITRIC OXIDE; P21 ACTIVATED KINASE 2; PROTEIN BAX; PROTEIN BCL 2; RAF PROTEIN; RAS PROTEIN; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; ANTIINFECTIVE AGENT; P21 ACTIVATED KINASE;

EID: 44049089972     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.30     Document Type: Review
Times cited : (31)

References (89)
  • 2
    • 0038424492 scopus 로고    scopus 로고
    • CAST. Task Force Rep. No. 139. Council of Agricultural Science and Technology (CAST), Ames, IA
    • CAST. (2003) Mycotoxins: risks in plant, animal, and human systems. Task Force Rep. No. 139. Council of Agricultural Science and Technology (CAST), Ames, IA.
    • (2003) Mycotoxins: Risks in Plant, Animal, and Human Systems
  • 3
    • 0033921625 scopus 로고    scopus 로고
    • Co-occurrence of ochratoxin A and citrinin in cereals from Bulgarian villages with a history of Balkan endemic nephropathy
    • Vrabcheva, T., Usleber, E., Dietrich, R., and Martlbauer, E. (2000) Co-occurrence of ochratoxin A and citrinin in cereals from Bulgarian villages with a history of Balkan endemic nephropathy. J. Agric. Food Chem. 48, 2483-2488.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 2483-2488
    • Vrabcheva, T.1    Usleber, E.2    Dietrich, R.3    Martlbauer, E.4
  • 4
    • 11244318188 scopus 로고    scopus 로고
    • Evaluation of citrinin occurrence and cytotoxicity in Monascus fermentation products
    • Liu, B. H., Wu, T. S., Su, M. C., Chung, C. P., and Yu, F. Y. (2005) Evaluation of citrinin occurrence and cytotoxicity in Monascus fermentation products. J. Agric. Food Chem. 53, 170-175.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 170-175
    • Liu, B.H.1    Wu, T.S.2    Su, M.C.3    Chung, C.P.4    Yu, F.Y.5
  • 5
    • 0032811597 scopus 로고    scopus 로고
    • Mutagenicity of commercial Monascus fermentation products and the role of citrinin contamination
    • Sabater-Vilar, M., Maas, R. F., and Fink-Gremmels, J. (1999) Mutagenicity of commercial Monascus fermentation products and the role of citrinin contamination. Mutat. Res. 444, 7-16.
    • (1999) Mutat. Res. , vol.444 , pp. 7-16
    • Sabater-Vilar, M.1    Maas, R.F.2    Fink-Gremmels, J.3
  • 6
    • 0038640864 scopus 로고    scopus 로고
    • Hypolipidemic and anti-atherogenic effects of long-term cholestin (Monascus purpureus-fermented rice, red yeast rice) in cholesterol-fed rabbits
    • Wei, W., Li, C., Wang, Y., Su, H., Zhu, J., and Kritchevsky, D. (2003) Hypolipidemic and anti-atherogenic effects of long-term cholestin (Monascus purpureus-fermented rice, red yeast rice) in cholesterol-fed rabbits. J. Nutr. Biochem. 14, 314-318.
    • (2003) J. Nutr. Biochem. , vol.14 , pp. 314-318
    • Wei, W.1    Li, C.2    Wang, Y.3    Su, H.4    Zhu, J.5    Kritchevsky, D.6
  • 7
    • 0025860769 scopus 로고
    • The role of altered mitochondrial function in citrinin-induced toxicity to rat renal proximal tubule suspensions
    • Aleo, M. D., Wyatt, R. D., and Schnellmann, R. G. (1991) The role of altered mitochondrial function in citrinin-induced toxicity to rat renal proximal tubule suspensions. Toxicol. Appl. Pharmacol. 109, 455-463.
    • (1991) Toxicol. Appl. Pharmacol. , vol.109 , pp. 455-463
    • Aleo, M.D.1    Wyatt, R.D.2    Schnellmann, R.G.3
  • 8
    • 0027469915 scopus 로고
    • Experimental citrinin nephrotoxicosis in dogs: Renal function evaluation
    • Kogika, M. M., Hagiwara, M. K., and Mirandola, R. M. (1993) Experimental citrinin nephrotoxicosis in dogs: renal function evaluation. Vet. Hum. Toxicol. 35, 136-140.
    • (1993) Vet. Hum. Toxicol. , vol.35 , pp. 136-140
    • Kogika, M.M.1    Hagiwara, M.K.2    Mirandola, R.M.3
  • 9
    • 0020684746 scopus 로고
    • Tumorigenicity of citrinin in male F344 rats
    • DOI 10.1016/0304-3835(83)90165-9
    • Arai, M., and Hibino, T. (1983) Tumorigenicity of citrinin in male F344 rats. Cancer Lett. 17, 281-287. (Pubitemid 13194043)
    • (1983) Cancer Letters , vol.17 , Issue.3 , pp. 281-287
    • Arai, M.1    Hibino, T.2
  • 10
    • 0030345309 scopus 로고    scopus 로고
    • Citrinin-induced chromosomal abnormalities in the bone marrow cells of Mus musculus
    • Jeswal, P. (1996) Citrinin-induced chromosomal abnormalities in the bone marrow cells of Mus musculus. Cytobios 86, 29-33. (Pubitemid 126490372)
    • (1996) Cytobios , vol.1996 , Issue.344 , pp. 29-33
    • Jeswal, P.1
  • 11
    • 0031927107 scopus 로고    scopus 로고
    • Aneuploidogenic and clastogenic potential of the mycotoxins citrinin and patulin
    • DOI 10.1093/carcin/19.7.1313
    • Pfeiffer, E., Gross, K., and Metzler, M. (1998) Aneuploidogenic and clastogenic potential of the mycotoxins citrinin and patulin. Carcinogenesis 19, 1313-1318. (Pubitemid 28375385)
    • (1998) Carcinogenesis , vol.19 , Issue.7 , pp. 1313-1318
    • Pfeiffer, E.1    Gross, K.2    Metzler, M.3
  • 12
    • 0026524475 scopus 로고
    • Mechanism of citrinin-induced dysfunction of mitochondria. I. Effects on respiration, enzyme activities and membrane potential of renal cortical mitochondria
    • Chagas, G. M., Campello, A. P., and Kluppel, M. L. (1992) Mechanism of citrinin-induced dysfunction of mitochondria. I. Effects on respiration, enzyme activities and membrane potential of renal cortical mitochondria. J. Appl. Toxicol. 12, 123-129.
    • (1992) J. Appl. Toxicol. , vol.12 , pp. 123-129
    • Chagas, G.M.1    Campello, A.P.2    Kluppel, M.L.3
  • 13
    • 0028948215 scopus 로고
    • Mechanism of citrinin-induced dysfunction of mitochondria. III. Effects on renal cortical and liver mitochondrial swelling
    • Chagas, G. M., Oliveira, M. B., Campello, A. P., and Kluppel, M. L. (1995) Mechanism of citrinin-induced dysfunction of mitochondria. III. Effects on renal cortical and liver mitochondrial swelling. J. Appl. Toxicol. 15, 91-95.
    • (1995) J. Appl. Toxicol. , vol.15 , pp. 91-95
    • Chagas, G.M.1    Oliveira, M.B.2    Campello, A.P.3    Kluppel, M.L.4
  • 14
    • 0030773224 scopus 로고    scopus 로고
    • Mechanism of citrinin-induced dysfunction of mitochondria. V. Effect on the homeostasis of the reactive oxygen species
    • Ribeiro, S. M., Chagas, G. M., Campello, A. P., and Kluppel, M. L. (1997) Mechanism of citrinin-induced dysfunction of mitochondria. V. Effect on the homeostasis of the reactive oxygen species. Cell Biochem. Funct. 15, 203-209.
    • (1997) Cell Biochem. Funct. , vol.15 , pp. 203-209
    • Ribeiro, S.M.1    Chagas, G.M.2    Campello, A.P.3    Kluppel, M.L.4
  • 15
    • 34447262354 scopus 로고    scopus 로고
    • Effect of citrinin on mouse embryonic development in vitro and in vivo
    • Chan, W. H., and Shiao, N. H. (2007) Effect of citrinin on mouse embryonic development in vitro and in vivo. Reprod. Toxicol. 24, 120-125.
    • (2007) Reprod. Toxicol. , vol.24 , pp. 120-125
    • Chan, W.H.1    Shiao, N.H.2
  • 16
    • 34249782842 scopus 로고    scopus 로고
    • Citrinin induces apoptosis via a mitochondriadependent pathway and inhibition of survival signals in embryonic stem cells, and causes developmental injury in blastocysts
    • Chan, W. H. (2007) Citrinin induces apoptosis via a mitochondriadependent pathway and inhibition of survival signals in embryonic stem cells, and causes developmental injury in blastocysts. Biochem. J. 404, 317-326.
    • (2007) Biochem. J. , vol.404 , pp. 317-326
    • Chan, W.H.1
  • 17
    • 0028013360 scopus 로고
    • Azaphilones inhibit tumor promotion by 12-O-tetradecanoylphorbol-13- acetate in two-stage carcinogenesis in mice
    • Yasukawa, K., Takahashi, M., Natori, S., Kawai, K., Yamazaki, M., Takeuchi, M., and Takido, M. (1994) Azaphilones inhibit tumor promotion by 12-O-tetradecanoylphorbol-13-acetate in two-stage carcinogenesis in mice. Oncology 51, 108-112. (Pubitemid 24008651)
    • (1994) Oncology , vol.51 , Issue.1 , pp. 108-112
    • Yasukawa, K.1    Takahashi, M.2    Natori, S.3    Kawai -i, K.4    Yamazaki, M.5    Takeuchi, M.6    Takido, M.7
  • 18
    • 0029985406 scopus 로고    scopus 로고
    • Inhibitory effect of oral administration of monascus pigment on tumor promotion in two-stage carcinogenesis in mouse skin
    • Yasukawa, K., Takahashi, M., Yamanouchi, S., and Takido, M. (1996) Inhibitory effect of oral administration of Monascus pigment on tumor promotion in two-stage carcinogenesis in mouse skin. Oncology 53, 247-249. (Pubitemid 26131950)
    • (1996) Oncology , vol.53 , Issue.3 , pp. 247-249
    • Yasukawa, K.1    Takahashi, M.2    Yamanouchi, S.3    Takido, M.4
  • 19
    • 0032898925 scopus 로고    scopus 로고
    • Cholesterol-lowering effects of a proprietary Chinese red-yeast-rice dietary supplement
    • Heber, D., Yip, I., Ashley, J. M., Elashoff, D. A., Elashoff, R. M., and Go, V. L. (1999) Cholesterol-lowering effects of a proprietary Chinese red-yeast-rice dietary supplement. Am. J. Clin. Nutr. 69, 231-236.
    • (1999) Am. J. Clin. Nutr. , vol.69 , pp. 231-236
    • Heber, D.1    Yip, I.2    Ashley, J.M.3    Elashoff, D.A.4    Elashoff, R.M.5    Go, V.L.6
  • 20
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wyllie, A. H., and Currie, A. R. (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 21
    • 0018830636 scopus 로고
    • Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation
    • Wyllie, A. H. (1980) Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284, 555-556.
    • (1980) Nature , vol.284 , pp. 555-556
    • Wyllie, A.H.1
  • 24
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • DOI 10.1016/0076-6879(90)86093-B
    • Halliwell, B., and Gutteridge, J. M. (1990) Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186, 1-85. (Pubitemid 20279941)
    • (1990) Methods in Enzymology , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 25
    • 21344462243 scopus 로고    scopus 로고
    • Curcumin prevents methylglyoxal-induced oxidative stress and apoptosis in mouse embryonic stem cells and blastocysts
    • Hsuuw, Y. D., Chang, C. K., Chan, W. H., and Yu, J. S. (2005) Curcumin prevents methylglyoxal-induced oxidative stress and apoptosis in mouse embryonic stem cells and blastocysts. J. Cell. Physiol. 205, 379-386.
    • (2005) J. Cell. Physiol. , vol.205 , pp. 379-386
    • Hsuuw, Y.D.1    Chang, C.K.2    Chan, W.H.3    Yu, J.S.4
  • 26
    • 32044431692 scopus 로고    scopus 로고
    • Oxidative stress and apoptotic changes in murine splenocytes exposed to cadmium
    • DOI 10.1016/j.tox.2005.11.027, PII S0300483X05006001
    • Pathak, N., and Khandelwal, S. (2006) Oxidative stress and apoptotic changes in murine splenocytes exposed to cadmium. Toxicology 220, 26-36. (Pubitemid 43197626)
    • (2006) Toxicology , vol.220 , Issue.1 , pp. 26-36
    • Pathak, N.1    Khandelwal, S.2
  • 27
    • 28844463729 scopus 로고    scopus 로고
    • Tetrandrine-induced apoptosis in rat primary hepatocytes is initiated from mitochondria: Caspases and Endonuclease G (Endo G) pathway
    • DOI 10.1016/j.tox.2005.08.024, PII S0300483X05004348
    • Yan, C., Xin-Ming, Q., Li-Kun, G., Lin-Lin, L., Fang-Ping, C., Ying, X., Xiong-Fei, W., Xiang-Hong, L., and Jin, R. (2006) Tetrandrine-induced apoptosis in rat primary hepatocytes is initiated from mitochondria: caspases and endonuclease G (Endo G) pathway. Toxicology 218, 1-12. (Pubitemid 41774666)
    • (2006) Toxicology , vol.218 , Issue.1 , pp. 1-12
    • Yan, C.1    Xin-Ming, Q.2    Li-Kun, G.3    Lin-Lin, L.4    Fang-Ping, C.5    Ying, X.6    Xiong-Fei, W.7    Xiang-Hong, L.8    Jin, R.9
  • 28
    • 33750548225 scopus 로고    scopus 로고
    • Involvement of BH3-only proapoptotic proteins in mitochondrial-dependent Phenoxodiol-induced apoptosis of human melanoma cells
    • DOI 10.1097/01.cad.0000231484.17063.9a, PII 0000181320061100000005
    • Yu, F., Watts, R. N., Zhang, X. D., Borrow, J. M., and Hersey, P. (2006) Involvement of BH3-only proapoptotic proteins in mitochondrial-dependent phenoxodiol-induced apoptosis of human melanoma cells. Anticancer Drugs 17, 1151-1161. (Pubitemid 44673395)
    • (2006) Anti-Cancer Drugs , vol.17 , Issue.10 , pp. 1151-1161
    • Yu, F.1    Watts, R.N.2    Zhang, X.D.3    Borrow, J.M.4    Hersey, P.5
  • 29
    • 33845796488 scopus 로고    scopus 로고
    • Mitochondrial control of cell death induced by hyperosmotic stress
    • DOI 10.1007/s10495-006-0328-x
    • Criollo, A., Galluzzi, L., Chiara Maiuri, M., Tasdemir, E., Lavandero, S., and Kroemer, G. (2007) Mitochondrial control of cell death induced by hyperosmotic stress. Apoptosis 12, 3-18. (Pubitemid 46009500)
    • (2007) Apoptosis , vol.12 , Issue.1 , pp. 3-18
    • Criollo, A.1    Galluzzi, L.2    Chiara Maiuri, M.3    Tasdemir, E.4    Lavandero, S.5    Kroemer, G.6
  • 30
    • 29044432444 scopus 로고    scopus 로고
    • Citrinin induces apoptosis in HL-60 cells via activation of the mitochondrial pathway
    • Yu, F. Y., Liao, Y. C., Chang, C. H., and Liu, B. H. (2006) Citrinin induces apoptosis in HL-60 cells via activation of the mitochondrial pathway. Toxicol. Lett. 161, 143-151.
    • (2006) Toxicol. Lett. , vol.161 , pp. 143-151
    • Yu, F.Y.1    Liao, Y.C.2    Chang, C.H.3    Liu, B.H.4
  • 31
    • 0028176651 scopus 로고
    • Oxidative stress as a mediator of apoptosis
    • Buttke, T. M., and Sandstrom, P. A. (1994) Oxidative stress as a mediator of apoptosis. Immunol. Today 15, 7-10.
    • (1994) Immunol. Today , vol.15 , pp. 7-10
    • Buttke, T.M.1    Sandstrom, P.A.2
  • 32
    • 16844368414 scopus 로고    scopus 로고
    • NO news is not necessarily good news in cancer
    • DOI 10.2174/1568009053202072
    • Ekmekcioglu, S., Tang, C. H., and Grimm, E. A. (2005) NO news is not necessarily good news in cancer. Curr. Cancer Drug Targets 5, 103-115. (Pubitemid 40488597)
    • (2005) Current Cancer Drug Targets , vol.5 , Issue.2 , pp. 103-115
    • Ekmekcioglu, S.1    Tang, C.-H.2    Grimm, E.A.3
  • 33
    • 13244255346 scopus 로고    scopus 로고
    • NO and transcriptional regulation: From signaling to death
    • Zhou, J., and Brune, B. (2005) NO and transcriptional regulation: from signaling to death. Toxicology 208, 223-233.
    • (2005) Toxicology , vol.208 , pp. 223-233
    • Zhou, J.1    Brune, B.2
  • 34
    • 5144230475 scopus 로고    scopus 로고
    • Nitric oxide signaling in colon cancer chemoprevention
    • Rao, C. V. (2004) Nitric oxide signaling in colon cancer chemoprevention. Mutat. Res. 555, 107-119.
    • (2004) Mutat. Res. , vol.555 , pp. 107-119
    • Rao, C.V.1
  • 35
    • 33749536207 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species and nitric oxide-mediated cancer cell apoptosis in 2-butylamino-2-demethoxyhypocrellin B photodynamic treatment
    • Lu, Z., Tao, Y., Zhou, Z., Zhang, J., Li, C., Ou, L., and Zhao, B. (2006) Mitochondrial reactive oxygen species and nitric oxide-mediated cancer cell apoptosis in 2-butylamino-2-demethoxyhypocrellin B photodynamic treatment. Free Radic. Biol. Med. 41, 1590-1605.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1590-1605
    • Lu, Z.1    Tao, Y.2    Zhou, Z.3    Zhang, J.4    Li, C.5    Ou, L.6    Zhao, B.7
  • 36
    • 33847078905 scopus 로고    scopus 로고
    • Tamoxifen induces oxidative stress and mitochondrial apoptosis via stimulating mitochondrial nitric oxide synthase
    • DOI 10.1158/0008-5472.CAN-06-3099
    • Nazarewicz, R. R., Zenebe, W. J., Parihar, A., Larson, S. K., Alidema, E., Choi, J., and Ghafourifar, P. (2007) Tamoxifen induces oxidative stress and mitochondrial apoptosis via stimulating mitochondrial nitric oxide synthase. Cancer Res. 67, 1282-1290. (Pubitemid 46270788)
    • (2007) Cancer Research , vol.67 , Issue.3 , pp. 1282-1290
    • Nazarewicz, R.R.1    Zenebe, W.J.2    Parihar, A.3    Larson, S.K.4    Alidema, E.5    Choi, J.6    Ghafourifar, P.7
  • 38
    • 1342282382 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase
    • Brookes, P. S. (2004) Mitochondrial nitric oxide synthase. Mitochondrion 3, 187-204.
    • (2004) Mitochondrion , vol.3 , pp. 187-204
    • Brookes, P.S.1
  • 39
    • 0037381787 scopus 로고    scopus 로고
    • Interactions among nitric oxide and Bcl-family proteins after MPP+ exposure of SH-SY5Y neural cells I. MPP+ increases mitochondrial NO and Bax protein
    • Dennis, J., and Bennett, J. P., Jr. (2003) Interactions among nitric oxide and Bcl-family proteins after MPP+ exposure of SH-SY5Y neural cells I. MPP+ increases mitochondrial NO and Bax protein. J. Neurosci. Res. 72, 76-88.
    • (2003) J. Neurosci. Res. , vol.72 , pp. 76-88
    • Dennis, J.1    Bennett Jr., J.P.2
  • 40
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • Elfering, S. L., Sarkela, T. M., and Giulivi, C. (2002) Biochemistry of mitochondrial nitric-oxide synthase. J. Biol. Chem. 277, 38079-38086.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 41
    • 0742323115 scopus 로고    scopus 로고
    • Mitochondrial calcium uptake stimulates nitric oxide production in mitochondria of bovine vascular endothelial cells
    • Dedkova, E. N., Ji, X., Lipsius, S. L., and Blatter, L. A. (2004) Mitochondrial calcium uptake stimulates nitric oxide production in mitochondria of bovine vascular endothelial cells. Am. J. Physiol. Cell Physiol. 286, C406-C415.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Dedkova, E.N.1    Ji, X.2    Lipsius, S.L.3    Blatter, L.A.4
  • 42
    • 1642634614 scopus 로고    scopus 로고
    • Nitric oxide: A potential inducer of adhesion-related apoptosis - Anoikis
    • Monteiro, H. P., Silva, E. F., and Stern, A. (2004) Nitric oxide: a potential inducer of adhesion-related apoptosis - anoikis. Nitric Oxide 10, 1-10.
    • (2004) Nitric Oxide , vol.10 , pp. 1-10
    • Monteiro, H.P.1    Silva, E.F.2    Stern, A.3
  • 44
    • 0033212190 scopus 로고    scopus 로고
    • Effects of BAPTA-AM and forskolin on apoptosis and cytochrome c release in photosensitized Chinese hamster V79 cells
    • Inanami, O., Yoshito, A., Takahashi, K., Hiraoka, W., and Kuwabara, M. (1999) Effects of BAPTA-AM and forskolin on apoptosis and cytochrome c release in photosensitized Chinese hamster V79 cells. Photochem. Photobiol. 70, 650-655.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 650-655
    • Inanami, O.1    Yoshito, A.2    Takahashi, K.3    Hiraoka, W.4    Kuwabara, M.5
  • 46
    • 21744449943 scopus 로고    scopus 로고
    • Nitric oxide as a modulator of apoptosis
    • Li, C. Q., and Wogan, G. N. (2005) Nitric oxide as a modulator of apoptosis. Cancer Lett. 226, 1-15.
    • (2005) Cancer Lett. , vol.226 , pp. 1-15
    • Li, C.Q.1    Wogan, G.N.2
  • 47
    • 0036782294 scopus 로고    scopus 로고
    • Nitric oxide modulates tumor cell death induced by photodynamic therapy through a cGMP-dependent mechanism
    • Gomes, E. R., Almeida, R. D., Carvalho, A. P., and Duarte, C. B. (2002) Nitric oxide modulates tumor cell death induced by photodynamic therapy through a cGMP-dependent mechanism. Photochem. Photobiol. 76, 423-430.
    • (2002) Photochem. Photobiol. , vol.76 , pp. 423-430
    • Gomes, E.R.1    Almeida, R.D.2    Carvalho, A.P.3    Duarte, C.B.4
  • 48
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonny, M. V. (2002) Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia 16, 455-462.
    • (2002) Leukemia , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 51
    • 4644228513 scopus 로고    scopus 로고
    • The farnesyl transferase inhibitor R115777 (Zarnestra) synergistically enhances growth inhibition and apoptosis induced on epidermoid cancer cells by zoledronic acid (Zometa) and pamidronate
    • DOI 10.1038/sj.onc.1207814
    • Caraglia, M., D'Alessandro, A. M., Marra, M., Giuberti, G., Vitale, G., Viscomi, C., Colao, A., Prete, S. D., Tagliaferri, P., Tassone, P., Budillon, A., Venuta, S., and Abbruzzese, A. (2004) The farnesyl transferase inhibitor R115777 (Zarnestra) synergistically enhances growth inhibition and apoptosis induced on epidermoid cancer cells by zoledronic acid (Zometa) and pamidronate. Oncogene 23, 6900-6913. (Pubitemid 39279991)
    • (2004) Oncogene , vol.23 , Issue.41 , pp. 6900-6913
    • Caraglia, M.1    D'Alessandro, A.M.2    Marra, M.3    Giuberti, G.4    Vitale, G.5    Viscomi, C.6    Colao, A.7    Del Prete, S.8    Tagliaferri, P.9    Tassone, P.10    Budillon, A.11    Venuta, S.12    Abbruzzese, A.13
  • 53
    • 21644466385 scopus 로고    scopus 로고
    • Electromagnetic fields at mobile phone frequency induce apoptosis and inactivation of the multi-chaperone complex in human epidermoid cancer cells
    • Caraglia, M., Marra, M., Mancinelli, F., D'Ambrosio, G., Massa, R., Giordano, A., Budillon, A., Abbruzzese, A., and Bismuto, E. (2005) Electromagnetic fields at mobile phone frequency induce apoptosis and inactivation of the multi-chaperone complex in human epidermoid cancer cells. J. Cell. Physiol. 204, 539-548.
    • (2005) J. Cell. Physiol. , vol.204 , pp. 539-548
    • Caraglia, M.1    Marra, M.2    Mancinelli, F.3    D'Ambrosio, G.4    Massa, R.5    Giordano, A.6    Budillon, A.7    Abbruzzese, A.8    Bismuto, E.9
  • 54
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 55
    • 0034296394 scopus 로고    scopus 로고
    • Basic medical research award. the ubiquitin system
    • Hershko, A., Ciechanover, A., and Varshavsky, A. (2000) Basic medical research award. The ubiquitin system. Nat. Med. 6, 1073-1081.
    • (2000) Nat. Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 57
    • 0034979272 scopus 로고    scopus 로고
    • Mobile phones, heat shock proteins and cancer
    • DOI 10.1046/j.1432-0436.2001.670401.x
    • French, P. W., Penny, R., Laurence, J. A., and McKenzie, D. R. (2001) Mobile phones, heat shock proteins and cancer. Differentiation 67, 93-97. (Pubitemid 32575498)
    • (2001) Differentiation , vol.67 , Issue.4-5 , pp. 93-97
    • French, P.W.1    Penny, R.2    Laurence, J.A.3    McKenzie, D.R.4
  • 58
    • 0034715983 scopus 로고    scopus 로고
    • Physics and biology of mobile telephony
    • Hyland, G. J. (2000) Physics and biology of mobile telephony. Lancet 356, 1833-1836.
    • (2000) Lancet , vol.356 , pp. 1833-1836
    • Hyland, G.J.1
  • 59
    • 0036560770 scopus 로고    scopus 로고
    • Non-thermal activation of the hsp27/p38MAPK stress pathway by mobile phone radiation in human endothelial cells: Molecular mechanism for cancer- And blood-brain barrier-related effects
    • DOI 10.1046/j.1432-0436.2002.700207.x
    • Leszczynski, D., Joenvaara, S., Reivinen, J., and Kuokka, R. (2002) Non-thermal activation of the hsp27/p38MAPK stress pathway by mobile phone radiation in human endothelial cells: molecular mechanism for cancer- and blood-brain barrier-related effects. Differentiation 70, 120-129. (Pubitemid 38230562)
    • (2002) Differentiation , vol.70 , Issue.2-3 , pp. 120-129
    • Leszczynski, D.1    Joenvaara, S.2    Reivinen, J.3    Kuokka, R.4
  • 60
    • 0033529033 scopus 로고    scopus 로고
    • Molecular chaperones: The busy life of Hsp90
    • Mayer, M. P., and Bukau, B. (1999) Molecular chaperones: the busy life of Hsp90. Curr. Biol. 9, R322-R325.
    • (1999) Curr. Biol. , vol.9
    • Mayer, M.P.1    Bukau, B.2
  • 61
    • 0043288724 scopus 로고    scopus 로고
    • Heat shock protein 90 as a molecular target for cancer therapeutics
    • DOI 10.1016/S1535-6108(03)00029-1
    • Isaacs, J. S., Xu, W., and Neckers, L. (2003) Heat shock protein 90 as a molecular target for cancer therapeutics. Cancer Cell 3, 213-217. (Pubitemid 37443877)
    • (2003) Cancer Cell , vol.3 , Issue.3 , pp. 213-217
    • Isaacs, J.S.1    Xu, W.2    Neckers, L.3
  • 62
    • 0030759279 scopus 로고    scopus 로고
    • Kinase cascades regulating entry into apoptosis
    • Anderson, P. (1997) Kinase cascades regulating entry into apoptosis. Microbiol. Mol. Biol. Rev. 61, 33-46.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 33-46
    • Anderson, P.1
  • 63
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., and Greenberg, M. E. (1995) Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270, 1326-1331.
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 65
    • 0030614914 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase-mediated activation of interleukin-1β converting enzyme/CED-3-like protease during anticancer drug-induced apoptosis
    • Seimiya, H., Mashima, T., Toho, M., and Tsuruo, T. (1997) c-Jun NH2-terminal kinase-mediated activation of interleukin-1β converting enzyme/CED-3-like protease during anticancer drug-induced apoptosis. J. Biol. Chem. 272, 4631-4636.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4631-4636
    • Seimiya, H.1    Mashima, T.2    Toho, M.3    Tsuruo, T.4
  • 67
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • DOI 10.1016/0092-8674(94)90380-8
    • Derijard, B., Hibi, M., Wu, I. H., Barrett, T., Su, B., Deng, T., Karin, M., and Davis, R. J. (1994) JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76, 1025-1037. (Pubitemid 24106383)
    • (1994) Cell , vol.76 , Issue.6 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.-H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 68
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
    • Derijard, B., Raingeaud, J., Barrett, T., Wu, I. H., Han, J., Ulevitch, R. J., and Davis, R. J. (1995) Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267, 682-685.
    • (1995) Science , vol.267 , pp. 682-685
    • Derijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu, I.H.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 69
    • 0028558986 scopus 로고
    • Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun
    • Sanchez, I., Hughes, R. T., Mayer, B. J., Yee, K., Woodgett, J. R., Avruch, J., Kyriakis, J. M., and Zon, L. I. (1994) Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun. Nature 372, 794-798.
    • (1994) Nature , vol.372 , pp. 794-798
    • Sanchez, I.1    Hughes, R.T.2    Mayer, B.J.3    Yee, K.4    Woodgett, J.R.5    Avruch, J.6    Kyriakis, J.M.7    Zon, L.I.8
  • 70
    • 0028670788 scopus 로고
    • Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
    • Yan, M., Dai, T., Deak, J. C., Kyriakis, J. M., Zon, L. I., Woodgett, J. R., and Templeton, D. J. (1994) Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1. Nature 372, 798-800.
    • (1994) Nature , vol.372 , pp. 798-800
    • Yan, M.1    Dai, T.2    Deak, J.C.3    Kyriakis, J.M.4    Zon, L.I.5    Woodgett, J.R.6    Templeton, D.J.7
  • 72
    • 0034306285 scopus 로고    scopus 로고
    • Apoptotic signalling cascade in photosensitized human epidermal carcinoma A431 cells: Involvement of singlet oxygen, c-Jun N-terminal kinase, caspase-3 and p21-activated kinase 2
    • Chan, W. H., Yu, J. S., and Yang, S. D. (2000) Apoptotic signalling cascade in photosensitized human epidermal carcinoma A431 cells: involvement of singlet oxygen, c-Jun N-terminal kinase, caspase-3 and p21-activated kinase 2. Biochem. J. 351, 221-232.
    • (2000) Biochem. J. , vol.351 , pp. 221-232
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 73
    • 0141529729 scopus 로고    scopus 로고
    • Curcumin inhibits UV irradiation-induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells
    • Chan, W. H., Wu, C. C., and Yu, J. S. (2003) Curcumin inhibits UV irradiation-induced oxidative stress and apoptotic biochemical changes in human epidermoid carcinoma A431 cells. J. Cell. Biochem. 90, 327-338.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 327-338
    • Chan, W.H.1    Wu, C.C.2    Yu, J.S.3
  • 74
    • 26444609711 scopus 로고    scopus 로고
    • Effect of resveratrol on high glucose-induced stress in human leukemia K562 cells
    • Chan, W. H. (2005) Effect of resveratrol on high glucose-induced stress in human leukemia K562 cells. J. Cell. Biochem. 94, 1267-1279.
    • (2005) J. Cell. Biochem. , vol.94 , pp. 1267-1279
    • Chan, W.H.1
  • 75
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • DOI 10.1126/science.276.5318.1571
    • Rudel, T., and Bokoch, G. M. (1997) Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276, 1571-1574. (Pubitemid 27255323)
    • (1997) Science , vol.276 , Issue.5318 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 76
    • 0031443641 scopus 로고    scopus 로고
    • Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis
    • Lee, N., MacDonald, H., Reinhard, C., Halenbeck, R., Roulston, A., Shi, T., and Williams, L. T. (1997) Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis. Proc. Natl. Acad. Sci. USA 94, 13642-13647.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13642-13647
    • Lee, N.1    MacDonald, H.2    Reinhard, C.3    Halenbeck, R.4    Roulston, A.5    Shi, T.6    Williams, L.T.7
  • 77
    • 0032531273 scopus 로고    scopus 로고
    • Proteolytic cleavage and activation of PAK2 during UV irradiation-induced apoptosis in A431 cells
    • Tang, T. K., Chang, W. C., Chan, W. H., Yang, S. D., Ni, M. H., and Yu, J. S. (1998) Proteolytic cleavage and activation of PAK2 during UV irradiation-induced apoptosis in A431 cells. J. Cell. Biochem. 70, 442-454.
    • (1998) J. Cell. Biochem. , vol.70 , pp. 442-454
    • Tang, T.K.1    Chang, W.C.2    Chan, W.H.3    Yang, S.D.4    Ni, M.H.5    Yu, J.S.6
  • 78
    • 0032931817 scopus 로고    scopus 로고
    • PAK2 is cleaved and activated during hyperosmotic shock-induced apoptosis via a caspase-dependent mechanism: Evidence for the involvement of oxidative stress
    • Chan, W. H., Yu, J. S., and Yang, S. D. (1999) PAK2 is cleaved and activated during hyperosmotic shock-induced apoptosis via a caspase-dependent mechanism: evidence for the involvement of oxidative stress. J. Cell. Physiol. 178, 397-408.
    • (1999) J. Cell. Physiol. , vol.178 , pp. 397-408
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 79
    • 0031105660 scopus 로고    scopus 로고
    • Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells
    • Sells, M. A., Knaus, U. G., Bagrodia, S., Ambrose, D. M., Bokoch, G. M., and Chernoff, J. (1997) Human p21-activated kinase (Pak1) regulates actin organization in mammalian cells. Curr. Biol. 7, 202-210.
    • (1997) Curr. Biol. , vol.7 , pp. 202-210
    • Sells, M.A.1    Knaus, U.G.2    Bagrodia, S.3    Ambrose, D.M.4    Bokoch, G.M.5    Chernoff, J.6
  • 80
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • DOI 10.1038/367040a0
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z. S., and Lim, L. (1994) A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367, 40-46. (Pubitemid 24038530)
    • (1994) Nature , vol.367 , Issue.6458 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.-S.4    Lim, L.5
  • 81
    • 0029134875 scopus 로고
    • Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation
    • Benner, G. E., Dennis, P. B., and Masaracchia, R. A. (1995) Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation. J. Biol. Chem. 270, 21121-21128.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21121-21128
    • Benner, G.E.1    Dennis, P.B.2    Masaracchia, R.A.3
  • 82
    • 0029915841 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of the cytostatic G protein-activated protein kinase PAK I
    • Jakobi, R., Chen, C. J., Tuazon, P. T., and Traugh, J. A. (1996) Molecular cloning and sequencing of the cytostatic G protein-activated protein kinase PAK I. J. Biol. Chem. 271, 6206-6211.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6206-6211
    • Jakobi, R.1    Chen, C.J.2    Tuazon, P.T.3    Traugh, J.A.4
  • 83
    • 0032529116 scopus 로고    scopus 로고
    • Identification of the regulatory autophosphorylation site of autophosphorylation-dependent protein kinase (auto-kinase). Evidence that autokinase belongs to a member of the p21-activated kinase family
    • Yu, J. S., Chen, W. J., Ni, M. H., Chan, W. H., and Yang, S. D. (1998) Identification of the regulatory autophosphorylation site of autophosphorylation-dependent protein kinase (auto-kinase). Evidence that autokinase belongs to a member of the p21-activated kinase family. Biochem. J. 334 (Pt 1), 121-131.
    • (1998) Biochem. J. , vol.334 , Issue.PART 1 , pp. 121-131
    • Yu, J.S.1    Chen, W.J.2    Ni, M.H.3    Chan, W.H.4    Yang, S.D.5
  • 84
    • 0028846513 scopus 로고
    • Activation of mitogen-activated protein kinase cascades by p21-activated protein kinases in cell-free extracts of Xenopus oocytes
    • Polverino, A., Frost, J., Yang, P., Hutchison, M., Neiman, A. M., Cobb, M. H., and Marcus, S. (1995) Activation of mitogen-activated protein kinase cascades by p21-activated protein kinases in cell-free extracts of Xenopus oocytes. J. Biol. Chem. 270, 26067-26070.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26067-26070
    • Polverino, A.1    Frost, J.2    Yang, P.3    Hutchison, M.4    Neiman, A.M.5    Cobb, M.H.6    Marcus, S.7
  • 85
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang, S., Han, J., Sells, M. A., Chernoff, J., Knaus, U. G., Ulevitch, R. J., and Bokoch, G. M. (1995) Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J. Biol. Chem. 270, 23934-23936.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 86
    • 0029950672 scopus 로고    scopus 로고
    • Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members
    • Frost, J. A., Xu, S., Hutchison, M. R., Marcus, S., and Cobb, M. H. (1996) Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members. Mol. Cell. Biol. 16, 3707-3713.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3707-3713
    • Frost, J.A.1    Xu, S.2    Hutchison, M.R.3    Marcus, S.4    Cobb, M.H.5
  • 87
    • 0031830188 scopus 로고    scopus 로고
    • Heat shock stress induces cleavage and activation of PAK2 in apoptotic cells
    • Chan, W. H., Yu, J. S., and Yang, S. D. (1998) Heat shock stress induces cleavage and activation of PAK2 in apoptotic cells. J. Protein Chem. 17, 485-494.
    • (1998) J. Protein Chem. , vol.17 , pp. 485-494
    • Chan, W.H.1    Yu, J.S.2    Yang, S.D.3
  • 88
    • 33847078455 scopus 로고    scopus 로고
    • Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-Jun N-terminal kinase, caspase-3, and p21-activated kinase 2
    • Chan, W. H., Wu, H. J., and Shiao, N. H. (2007) Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-Jun N-terminal kinase, caspase-3, and p21-activated kinase 2. J. Cell. Biochem. 100, 1056-1069.
    • (2007) J. Cell. Biochem. , vol.100 , pp. 1056-1069
    • Chan, W.H.1    Wu, H.J.2    Shiao, N.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.