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Volumn 13, Issue 15, 1999, Pages 2284-2298

Cyclin B-dependent kinase and caspase-1 activation precedes mitochondrial dysfunction in fumarylacetoacetate-induced apoptosis

Author keywords

Caspase; Cell cycle; Cell death; Cytochrome c; Glutathione

Indexed keywords

ACETOACETIC ACID DERIVATIVE; ACETYLCYSTEINE; BUTHIONINE SULFOXIMINE; CASPASE 3; CASPASE INHIBITOR; CYCLIN B; CYCLIN DEPENDENT KINASE; CYTOCHROME C; DNA; GLUTATHIONE; INTERLEUKIN 1BETA CONVERTING ENZYME; SUCCINYLACETONE; TYROSINE;

EID: 0032797275     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.13.15.2284     Document Type: Article
Times cited : (58)

References (49)
  • 2
    • 0025061932 scopus 로고
    • Different molecular basis for fumarylacetoacetate hydrolase deficiency in the two clinical forms of hereditary tyrosinemia (type 1)
    • Tanguay, R. M., Valet, J. P., Lescault, A., Duband, J. L., Laberge, C., Lettre, F., and Plante, M. (1990) Different molecular basis for fumarylacetoacetate hydrolase deficiency in the two clinical forms of hereditary tyrosinemia (type 1). Am. J. Hum. Genet. 47, 308-316
    • (1990) Am. J. Hum. Genet. , vol.47 , pp. 308-316
    • Tanguay, R.M.1    Valet, J.P.2    Lescault, A.3    Duband, J.L.4    Laberge, C.5    Lettre, F.6    Plante, M.7
  • 3
    • 0026474437 scopus 로고
    • Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a french canadian patient
    • Phaneuf, D., Lambert, M., Laframboise, R., Mitchell, G., Lettre, F., and Tanguay, R. M. (1992) Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient. J. Clin. Invest. 90, 1185-1192
    • (1992) J. Clin. Invest. , vol.90 , pp. 1185-1192
    • Phaneuf, D.1    Lambert, M.2    Laframboise, R.3    Mitchell, G.4    Lettre, F.5    Tanguay, R.M.6
  • 4
    • 0030966950 scopus 로고    scopus 로고
    • Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: Overview
    • St-Louis, M., and Tanguay, R. M. (1997) Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview. Hum. Mutat. 9, 291-299
    • (1997) Hum. Mutat. , vol.9 , pp. 291-299
    • St-Louis, M.1    Tanguay, R.M.2
  • 5
    • 0000362736 scopus 로고
    • Hypertyrosinemia
    • (Scriver, C. R., Beaudet, A. L., Sly, W. S., and Valle, D., eds) McGraw-Hill, New York
    • Mitchell, G. A., Lambert, M., and Tanguay, R. M. (1995) Hypertyrosinemia. In The Metabolic and Molecular Bases of Inherited Disease (Scriver, C. R., Beaudet, A. L., Sly, W. S., and Valle, D., eds) pp. 1077-1106, McGraw-Hill, New York
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1077-1106
    • Mitchell, G.A.1    Lambert, M.2    Tanguay, R.M.3
  • 6
    • 0017106109 scopus 로고
    • The occurrence of hepatoma in the chronic form of hereditary tyrosinemia
    • Weinberg, A., Mize, C., and Worthen, H. (1976) The occurrence of hepatoma in the chronic form of hereditary tyrosinemia J. Pediatr. 88, 434-438
    • (1976) J. Pediatr. , vol.88 , pp. 434-438
    • Weinberg, A.1    Mize, C.2    Worthen, H.3
  • 8
    • 0022851104 scopus 로고
    • Hereditary tyrosinemias (type 1): A new vista on tyrosine toxicity and cancer
    • (Poirier, L. A., Newberne, P. M., and Pariza, M. W., eds) Plenum Press, New York
    • Laberge, C., Lescault, A., and Tanguay, R. M. (1986) Hereditary tyrosinemias (type 1): a new vista on tyrosine toxicity and cancer. In Essential Nutrients in Carcinogennis (Poirier, L. A., Newberne, P. M., and Pariza, M. W., eds) pp. 209-221, Plenum Press, New York
    • (1986) Essential Nutrients in Carcinogennis , pp. 209-221
    • Laberge, C.1    Lescault, A.2    Tanguay, R.M.3
  • 10
    • 0031555866 scopus 로고    scopus 로고
    • The mutagenicity of the tyrosine metabolite, fumarylacetoacetate, is enhanced by glutathione depletion
    • Jorquera, R., and Tanguay, R. M. (1997) The mutagenicity of the tyrosine metabolite, fumarylacetoacetate, is enhanced by glutathione depletion. Biochem, Biophys. Res. Commun. 232, 42-48
    • (1997) Biochem, Biophys. Res. Commun. , vol.232 , pp. 42-48
    • Jorquera, R.1    Tanguay, R.M.2
  • 11
    • 9844238697 scopus 로고    scopus 로고
    • Complete rescue of lethal albino c14CoS mice by null mutation of 4-hydroxyphenylpyruvate dioxygenase and induction of apoptosis of hepatocytes in these mice by in vivo retrieval of the tyrosine catabolic pathway
    • Endo, F., Kubo, S., Awata, H., Kiwaki, K., Katoh, H., Kanegae, Y., Saito, I., Miyazaki, J., Yamamoto, T., Jakobs, C., Hattori, S., and Matsuda, I. (1997) Complete rescue of lethal albino c14CoS mice by null mutation of 4-hydroxyphenylpyruvate dioxygenase and induction of apoptosis of hepatocytes in these mice by in vivo retrieval of the tyrosine catabolic pathway. J. Biol. Chem. 272, 24426-24432
    • (1997) J. Biol. Chem. , vol.272 , pp. 24426-24432
    • Endo, F.1    Kubo, S.2    Awata, H.3    Kiwaki, K.4    Katoh, H.5    Kanegae, Y.6    Saito, I.7    Miyazaki, J.8    Yamamoto, T.9    Jakobs, C.10    Hattori, S.11    Matsuda, I.12
  • 13
    • 0026756172 scopus 로고
    • Deficiency of an enzyme of tyrosine metabolism underlies altered gene expression in newborn liver of lethal albino mice
    • Ruppert, S., Kelsey, G., Schedl, A., Schmid, E., Thies, E., and Schutz, G. (1992) Deficiency of an enzyme of tyrosine metabolism underlies altered gene expression in newborn liver of lethal albino mice, Genes Dev. 6, 1430-1443
    • (1992) Genes Dev. , vol.6 , pp. 1430-1443
    • Ruppert, S.1    Kelsey, G.2    Schedl, A.3    Schmid, E.4    Thies, E.5    Schutz, G.6
  • 14
    • 0001081346 scopus 로고
    • Enzymes involved in conversion of tyrosine to acetoacetate
    • Edwards, S. W., and Knox, W. E. (1955) Enzymes involved in conversion of tyrosine to acetoacetate. Methods Enzymol. 2, 292-300
    • (1955) Methods Enzymol. , vol.2 , pp. 292-300
    • Edwards, S.W.1    Knox, W.E.2
  • 15
    • 0025189329 scopus 로고
    • A reversible arrest point in the late g1 phase of the mammalian cell cycle
    • Lalande, M. (1990) A reversible arrest point in the late G1 phase of the mammalian cell cycle. Exp. Cell Res. 186, 332-339
    • (1990) Exp. Cell Res. , vol.186 , pp. 332-339
    • Lalande, M.1
  • 16
    • 0027261147 scopus 로고
    • The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents
    • Gorczyca, W., Gong, J., Ardelt, B., Traganos, F., and Darzynkiewicz., Z. (1993) The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents. Cancer Res. 53, 3186-3192
    • (1993) Cancer Res. , vol.53 , pp. 3186-3192
    • Gorczyca, W.1    Gong, J.2    Ardelt, B.3    Traganos, F.4
  • 17
    • 0002230857 scopus 로고
    • Morphological and biochemical assays of apoptosis
    • Duke, R. C., and Cohen, J. J. (1992) Morphological and biochemical assays of apoptosis. Curr. Prot. Immunol. 1, 3.17.1-3.17.16
    • (1992) Curr. Prot. Immunol. , vol.1 , pp. 3171-31716
    • Duke, R.C.1    Cohen, J.J.2
  • 18
    • 0028323164 scopus 로고
    • A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry
    • Gong, J., Traganos, F., and Darzynkiewicz, Z. (1994) A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry. Anal. Biorhem. 218, 314-319
    • (1994) Anal. Biorhem. , vol.218 , pp. 314-319
    • Gong, J.1    Traganos, F.2    Darzynkiewicz, Z.3
  • 19
    • 0028809690 scopus 로고
    • Arrest at the G2/M transition of the cell cycle by protein-tyrosine phosphatase inhibition: Studies on a neuronal and a glial cell line
    • Faure, R., Vincent, M., Dufour, M., Shaver, A., and Posner, B. (1995) Arrest at the G2/M transition of the cell cycle by protein-tyrosine phosphatase inhibition: studies on a neuronal and a glial cell line. J. Cell. Biochem. 59, 389-401
    • (1995) J. Cell. Biochem. , vol.59 , pp. 389-401
    • Faure, R.1    Vincent, M.2    Dufour, M.3    Shaver, A.4    Posner, B.5
  • 20
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochromer from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R., and Newmeyer, D. D. (1997) The release of cytochromer from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275, 1132-1136
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 21
    • 0025690822 scopus 로고
    • Analysis of the membrane potential of rat-and mouseliver mitochondria by flow cytometry and possible applications
    • Petit, P. X., O'Connor, J. E., Grunwald, D., and Brown, S. C. (1990) Analysis of the membrane potential of rat-and mouseliver mitochondria by flow cytometry and possible applications. Eur. J. Biochem. 194, 389-397
    • (1990) Eur. J. Biochem. , vol.194 , pp. 389-397
    • Petit, P.X.1    O'Connor, J.E.2    Grunwald, D.3    Brown, S.C.4
  • 23
    • 0029099358 scopus 로고
    • Involvement of NAD-poly(ADP-ribose) metabolism in p53 regulation and its consequences
    • Whitacre, C., Hashimoto, H., Tsai, M., Chatterjec, S., Berger, S., and Berger, N. (1995) Involvement of NAD-poly(ADP-ribose) metabolism in p53 regulation and its consequences. Cancer Res. 55, 3697-3701
    • (1995) Cancer Res. , vol.55 , pp. 3697-3701
    • Whitacre, C.1    Hashimoto, H.2    Tsai, M.3    Chatterjec, S.4    Berger, S.5    Berger, N.6
  • 24
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse, P. (1990) Universal control mechanism regulating onset of M-phase. Nature (London) 344, 503-508
    • (1990) Nature (London) , vol.344 , pp. 503-508
    • Nurse, P.1
  • 25
    • 0029981099 scopus 로고    scopus 로고
    • Sequential dephosphorylation of p34(cdc2) on Thr-14 and Tyr-15 at the prophase/metaphase transition
    • Borgne, A., and Meijer, L. (1996) Sequential dephosphorylation of p34(cdc2) on Thr-14 and Tyr-15 at the prophase/metaphase transition. J. Biol. Chem. 271, 27847-27854
    • (1996) J. Biol. Chem. , vol.271 , pp. 27847-27854
    • Borgne, A.1    Meijer, L.2
  • 28
    • 0030897988 scopus 로고    scopus 로고
    • Substrate and inhibitor specificity of interleukin-1β-converting enzyme and related caspases
    • Margolin, N., Raybuck, S. A., Wilson, K. P., Chen, W., Fox, T., Gu, Y., and Livingston, D. J. (1997) Substrate and inhibitor specificity of interleukin-1β-converting enzyme and related caspases. J. Biol. Chem. 272, 7223-7228
    • (1997) J. Biol. Chem. , vol.272 , pp. 7223-7228
    • Margolin, N.1    Raybuck, S.A.2    Wilson, K.P.3    Chen, W.4    Fox, T.5    Gu, Y.6    Livingston, D.J.7
  • 29
    • 0030002801 scopus 로고    scopus 로고
    • Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32
    • Slee, E. A., Zhu, H., Chow, S. C., MacFarlane, M., Nicholson, D. W., and Cohen, G. M. (1996) Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32. Biochem. J. 315, 21-24
    • (1996) Biochem. J. , vol.315 , pp. 21-24
    • Slee, E.A.1    Zhu, H.2    Chow, S.C.3    MacFarlane, M.4    Nicholson, D.W.5    Cohen, G.M.6
  • 30
    • 0031921562 scopus 로고    scopus 로고
    • Commitment and effector phases of the physiological cell death pathway elucidated with respect to Bcl-2 caspase, and cyclin-dependent kinase activities
    • Harvey, K. J., Blomquist, J. F., and Ucker, D. S. (1998) Commitment and effector phases of the physiological cell death pathway elucidated with respect to Bcl-2 caspase, and cyclin-dependent kinase activities. Mol. Cell. Biol. 18, 2912-2922
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2912-2922
    • Harvey, K.J.1    Blomquist, J.F.2    Ucker, D.S.3
  • 31
    • 0033601746 scopus 로고    scopus 로고
    • Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner
    • Slee, E., Harte, M., Kluck, R., Wolf, B., Casiano, C., Newmeyer, D., Wang, H., Reed, J., Nicholson, D., Alnemri, E., Green, D., and Martin, S. (1999) Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J. Cell Biol. 144, 281-292
    • (1999) J. Cell Biol. , vol.144 , pp. 281-292
    • Slee, E.1    Harte, M.2    Kluck, R.3    Wolf, B.4    Casiano, C.5    Newmeyer, D.6    Wang, H.7    Reed, J.8    Nicholson, D.9    Alnemri, E.10    Green, D.11    Martin, S.12
  • 32
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATH and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATH and cytochrome c. Cell 86, 147-157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 33
    • 0030741528 scopus 로고    scopus 로고
    • Cytochromec activation of CPP32-like proteolysis plays a critical role in a xenopus cell-free apoptosis system
    • Kluck, R. M., Martin, S. J., Hoffman, B. M., Zhou, J. S., Green, D. R., and Newmeyer, D. D. (1997) Cytochromec activation of CPP32-like proteolysis plays a critical role in a Xenopus cell-free apoptosis system. EMBO J. 16, 4639-4649
    • (1997) EMBO J. , vol.16 , pp. 4639-4649
    • Kluck, R.M.1    Martin, S.J.2    Hoffman, B.M.3    Zhou, J.S.4    Green, D.R.5    Newmeyer, D.D.6
  • 34
    • 0027485950 scopus 로고
    • Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor
    • Deckwerth, T. L., and Johnson, E. M. (1993) Temporal analysis of events associated with programmed cell death (apoptosis) of sympathetic neurons deprived of nerve growth factor. J. Cell Biol. 123, 1207-1222
    • (1993) J. Cell Biol. , vol.123 , pp. 1207-1222
    • Deckwerth, T.L.1    Johnson, E.M.2
  • 35
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochromec release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel, E., Newmeyer, D. D., and Green, D. R. (1998) Mitochondrial cytochromec release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMKO J. 17, 37-49
    • (1998) EMKO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 36
  • 38
    • 0029661896 scopus 로고    scopus 로고
    • Requirement of p34cdc2 kinase for apoptosis mediated by the Fas/APO-1 receptor and interleukiu 1β-converting enzymerelated proteases
    • Yao, S.-L., McKenna, K. A., Sharkis, S. J., and Bedi, A. (1996) Requirement of p34cdc2 kinase for apoptosis mediated by the Fas/APO-1 receptor and interleukiu 1β-converting enzymerelated proteases. Cancer Res. 56, 4551-4555
    • (1996) Cancer Res. , vol.56 , pp. 4551-4555
    • Yao, S.-L.1    McKenna, K.A.2    Sharkis, S.J.3    Bedi, A.4
  • 39
    • 0028094424 scopus 로고
    • The role of cell cycle progression in cisplatin-induced apoptosis in chinese hamster ovary cells
    • Demarcq, C., Bunch, R., Creswell, D., and Eastman, A. (1994) The role of cell cycle progression in cisplatin-induced apoptosis in Chinese hamster ovary cells. Cell Growth Differ. 5, 983-993
    • (1994) Cell Growth Differ. , vol.5 , pp. 983-993
    • Demarcq, C.1    Bunch, R.2    Creswell, D.3    Eastman, A.4
  • 40
    • 0028873880 scopus 로고
    • Unscheduled activation of cyclin B1/Cdc2 kinase in human promyelocytic leukemia cell line HL60 cells undergoing apoptosis induced by DNA damage
    • Shimizu, T., O'Connor, P., Kohn, K., and Pommier, Y. (1995) Unscheduled activation of cyclin B1/Cdc2 kinase in human promyelocytic leukemia cell line HL60 cells undergoing apoptosis induced by DNA damage. Cancer Res. 55, 228-231
    • (1995) Cancer Res. , vol.55 , pp. 228-231
    • Shimizu, T.1    O'Connor, P.2    Kohn, K.3    Pommier, Y.4
  • 41
    • 0026444481 scopus 로고
    • Relationships between cdc2 kinase, DNA cross-linking, and cell cycle perturbations induced by nitrogen mustard
    • O'Connor, P., Ferris, D., White, G., Pines, J., Hunter, T., Longo, D., and Kohn, K. (1992) Relationships between cdc2 kinase, DNA cross-linking, and cell cycle perturbations induced by nitrogen mustard. Cell Growth Differ. 3, 43-52
    • (1992) Cell Growth Differ. , vol.3 , pp. 43-52
    • O'Connor, P.1    Ferris, D.2    White, G.3    Pines, J.4    Hunter, T.5    Longo, D.6    Kohn, K.7
  • 42
    • 0028345613 scopus 로고
    • Cell cycle control and cancer chemotherapy
    • Kohn, K., Jackman, J., and O'Connor, P. (1994) Cell cycle control and cancer chemotherapy. J. Cell. Biochem. 54, 440-452
    • (1994) J. Cell. Biochem. , vol.54 , pp. 440-452
    • Kohn, K.1    Jackman, J.2    O'Connor, P.3
  • 43
    • 0030768948 scopus 로고    scopus 로고
    • Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase
    • Furnari, B., Rhind, N., and Russell, P. (1997) Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase. Science 277, 1495-1497
    • (1997) Science , vol.277 , pp. 1495-1497
    • Furnari, B.1    Rhind, N.2    Russell, P.3
  • 44
    • 0030665150 scopus 로고    scopus 로고
    • The role of cdc2 feedback loop control in the DNA damage checkpoint in mammalian cells
    • Poon, R. Y. C., Chau, M. S., Yamashita, K., and Hunter, T. (1997) The role of cdc2 feedback loop control in the DNA damage checkpoint in mammalian cells. Cancer Res. 57, 5168-5178
    • (1997) Cancer Res. , vol.57 , pp. 5168-5178
    • Poon, R.Y.C.1    Chau, M.S.2    Yamashita, K.3    Hunter, T.4
  • 46
    • 0032534748 scopus 로고    scopus 로고
    • Redox regulation of caspase-3(-like) protease activity: Regulatory roles of thioredoxin and cytochromec
    • Ueda, S., Nakamura, H., Masutani, H., Sasada, T., Yonehara, S., Takabayashi, A., Yamaoka, Y., and Yodoi, J. (1998) Redox regulation of caspase-3(-like) protease activity: regulatory roles of thioredoxin and cytochromec. J. Immunol. 161, 6689-6695
    • (1998) J. Immunol. , vol.161 , pp. 6689-6695
    • Ueda, S.1    Nakamura, H.2    Masutani, H.3    Sasada, T.4    Yonehara, S.5    Takabayashi, A.6    Yamaoka, Y.7    Yodoi, J.8
  • 48
    • 0032514740 scopus 로고    scopus 로고
    • Deficient DNA-ligase activity in the metabolic disease tyrosinemia type 1
    • Prieto-Alamo, M. J., and Laval, F. (1998) Deficient DNA-ligase activity in the metabolic disease tyrosinemia type 1. Proc. Natl Acad. Sci. USA 95, 12614-12618
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12614-12618
    • Prieto-Alamo, M.J.1    Laval, F.2
  • 49
    • 0019409236 scopus 로고
    • Induction and repair of single-strand DNA breaks after irradiation of human fibroblasts deficient in glutathione
    • Edgren, M., Revesz, L., and Larsson, A. (1981) Induction and repair of single-strand DNA breaks after irradiation of human fibroblasts deficient in glutathione. Int. J. Radiat. Biol. 40, 355-363
    • (1981) Int. J. Radiat. Biol. , vol.40 , pp. 355-363
    • Edgren, M.1    Revesz, L.2    Larsson, A.3


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