메뉴 건너뛰기




Volumn 281, Issue 1, 2002, Pages 148-156

Putrescine activates oxidative stress dependent apoptotic death in ornithine decarboxylase overproducing mouse myeloma cells

Author keywords

Apoptosis; Ornithine; Ornithine decarboxylase; Putrescine

Indexed keywords

AMINOGUANIDINE; ANTIOXIDANT; BUTYLATED HYDROXYANISOLE; CALCIUM CHELATING AGENT; CALCIUM ION; CASPASE 2; CASPASE INHIBITOR; CYTOCHROME C; EFLORNITHINE; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID(ACETOXYMETHYL) ESTER; INITIATION FACTOR 4G; MONOAMINE OXIDASE INHIBITOR; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; ORNITHINE DECARBOXYLASE; ORNITHINE DECARBOXYLASE INHIBITOR; PUTRESCINE; TERT BUTYLOXYCARBONYLASPARTYL FLUOROMETHYL KETONE; UNCLASSIFIED DRUG;

EID: 0036440584     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2002.5662     Document Type: Article
Times cited : (28)

References (36)
  • 2
    • 0023881236 scopus 로고
    • Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy
    • Pegg, A. E. (1988). Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res. 48, 759-774.
    • (1988) Cancer Res. , vol.48 , pp. 759-774
    • Pegg, A.E.1
  • 3
    • 0028800002 scopus 로고
    • Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells
    • Tobias, K. E., and Kahana, C. (1995). Exposure to ornithine results in excessive accumulation of putrescine and apoptotic cell death in ornithine decarboxylase overproducing mouse myeloma cells. Cell Growth Differ. 6, 1279-1285.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1279-1285
    • Tobias, K.E.1    Kahana, C.2
  • 4
    • 0031079677 scopus 로고    scopus 로고
    • Loss of intracellular putrescine pool-size regulation induces apoptosis
    • Xie, X., Tome, M. E., and Gerner, E. W. (1997). Loss of intracellular putrescine pool-size regulation induces apoptosis. Exp. Cell Res. 230, 386-392.
    • (1997) Exp. Cell Res. , vol.230 , pp. 386-392
    • Xie, X.1    Tome, M.E.2    Gerner, E.W.3
  • 5
    • 0031469938 scopus 로고    scopus 로고
    • Excess putrescine accumulation inhibits the formation of modified eukaryotic initiation factor 5A (eIF-5A) and induces apoptosis
    • Tome, M. E., Fiser, S. M., Payne, C. M., and Gerner, E. W. (1997). Excess putrescine accumulation inhibits the formation of modified eukaryotic initiation factor 5A (eIF-5A) and induces apoptosis. Biochem. J. 328, 847-854.
    • (1997) Biochem. J. , vol.328 , pp. 847-854
    • Tome, M.E.1    Fiser, S.M.2    Payne, C.M.3    Gerner, E.W.4
  • 6
    • 0028016495 scopus 로고
    • Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis
    • Packham, G., and Cleveland, J. L. (1994). Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis. Mol. Cell. Biol. 14, 5741-5747.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5741-5747
    • Packham, G.1    Cleveland, J.L.2
  • 7
    • 0032559188 scopus 로고    scopus 로고
    • Polyamine depletion protects HL-60 cells from 2-deoxy-D-ribose-induced apoptosis
    • Monti, M. G., Ghiaroni, S., Pernecco, L., Barbieri, D., Marverti, G., and Franceschi, C. (1998). Polyamine depletion protects HL-60 cells from 2-deoxy-D-ribose-induced apoptosis. Life Sci. 62, 799-806.
    • (1998) Life Sci. , vol.62 , pp. 799-806
    • Monti, M.G.1    Ghiaroni, S.2    Pernecco, L.3    Barbieri, D.4    Marverti, G.5    Franceschi, C.6
  • 8
    • 0032101936 scopus 로고    scopus 로고
    • Sensitization of tnf-induced apoptosis with polyamine synthesis inhibitors in different human and murine tumour cell lines
    • Penning, L. C., Schipper, R. G., Vercammen, D., Verhofstad, A. A., Denecker, T., Beyaert, R., and Vandenabeele, P. (1998). Sensitization of tnf-induced apoptosis with polyamine synthesis inhibitors in different human and murine tumour cell lines. Cytokine 10, 423-431.
    • (1998) Cytokine , vol.10 , pp. 423-431
    • Penning, L.C.1    Schipper, R.G.2    Vercammen, D.3    Verhofstad, A.A.4    Denecker, T.5    Beyaert, R.6    Vandenabeele, P.7
  • 9
    • 0031985423 scopus 로고    scopus 로고
    • The antiproliferative effect of HGF on hepatoma cells involves induction of apoptosis with increase in intracellular polyamine concentration levels
    • Yanagawa, K., Yamashita, T., Yada, K., Ohira, M., Ishikawa, T., Yano, Y., Otani, S., and Sowa, M. (1998). The antiproliferative effect of HGF on hepatoma cells involves induction of apoptosis with increase in intracellular polyamine concentration levels. Oncol. Rep. 5, 185-190.
    • (1998) Oncol. Rep. , vol.5 , pp. 185-190
    • Yanagawa, K.1    Yamashita, T.2    Yada, K.3    Ohira, M.4    Ishikawa, T.5    Yano, Y.6    Otani, S.7    Sowa, M.8
  • 10
    • 0031933606 scopus 로고    scopus 로고
    • Putrescine-stimulated intracellular Ca2+ release for invasiveness of rat ascites hepatoma cells
    • Ashida, Y., Ueno, A., Miwa, Y., Miyoshi, K., and Inoue, H. (1998). Putrescine-stimulated intracellular Ca2+ release for invasiveness of rat ascites hepatoma cells. Jpn. J. Cancer Res. 89, 67-75.
    • (1998) Jpn. J. Cancer Res. , vol.89 , pp. 67-75
    • Ashida, Y.1    Ueno, A.2    Miwa, Y.3    Miyoshi, K.4    Inoue, H.5
  • 11
    • 0027207101 scopus 로고
    • Inhibition of calcium signalling in murine splenocytes by polyamines: Differential effects on CD4 and CD8 T-cells
    • Thomas, T., Gunnia, U. B., Yurkow, E. J., Seibold, J. R., and Thomas, T. J. (1993). Inhibition of calcium signalling in murine splenocytes by polyamines: Differential effects on CD4 and CD8 T-cells. Biochem. J. 291, 378-381.
    • (1993) Biochem. J. , vol.291 , pp. 378-381
    • Thomas, T.1    Gunnia, U.B.2    Yurkow, E.J.3    Seibold, J.R.4    Thomas, T.J.5
  • 12
    • 0025865565 scopus 로고
    • Polyamine toxicity in Neurospora crassa: Protective role of the vacuole
    • Davis, R. H., and Ristow, J. L. (1991). Polyamine toxicity in Neurospora crassa: Protective role of the vacuole. Arch. Biochem. Biophys. 285, 306-311.
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 306-311
    • Davis, R.H.1    Ristow, J.L.2
  • 13
    • 0018293115 scopus 로고
    • Mechanism of toxicity of putrescine in Anacystis nidulans
    • Guarino, L. A., and Cohen, S. S. (1979). Mechanism of toxicity of putrescine in Anacystis nidulans. Proc. Natl. Acad. Sci. USA 76, 3660-3664.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3660-3664
    • Guarino, L.A.1    Cohen, S.S.2
  • 15
    • 0001547001 scopus 로고    scopus 로고
    • The role of polyamine catabolism in polyamine analogue-induced programmed cell death
    • Ha, H. C., Woster, P. M., Yager, J. D., and Casero, R. J. (1997). The role of polyamine catabolism in polyamine analogue-induced programmed cell death. Proc. Natl. Acad. Sci. USA 94, 11557-11562.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11557-11562
    • Ha, H.C.1    Woster, P.M.2    Yager, J.D.3    Casero, R.J.4
  • 16
    • 0030684153 scopus 로고    scopus 로고
    • Rapid induction of apoptosis by deregulated uptake of polyamine analogues
    • Hu, R. H., and Pegg, A. E. (1997). Rapid induction of apoptosis by deregulated uptake of polyamine analogues. Biochem. J. 328, 307-316.
    • (1997) Biochem. J. , vol.328 , pp. 307-316
    • Hu, R.H.1    Pegg, A.E.2
  • 18
    • 0021153314 scopus 로고
    • Isolation of cloned cDNA encoding mammalian ornithine decarboxylase
    • Kahana, C., and Nathans, D. (1984). Isolation of cloned cDNA encoding mammalian ornithine decarboxylase. Proc. Natl. Acad. Sci. USA 81, 3645-9.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3645-3649
    • Kahana, C.1    Nathans, D.2
  • 19
    • 0014726925 scopus 로고
    • Use of the dansyl reaction in biochemical analysis
    • Seiler, N. (1970). Use of the dansyl reaction in biochemical analysis. Methods Biochem. Anal. 18, 259-337.
    • (1970) Methods Biochem. Anal. , vol.18 , pp. 259-337
    • Seiler, N.1
  • 20
    • 0032481268 scopus 로고    scopus 로고
    • Over-expressed mitochondrial hinge protein, a cytochrome c-binding protein, accelerates apoptosis by enhancing the release of cytochrome c from mitochondria
    • Okazaki, M., Ishibashi, Y., Asoh, S., and Ohta, S. (1998). Over-expressed mitochondrial hinge protein, a cytochrome c-binding protein, accelerates apoptosis by enhancing the release of cytochrome c from mitochondria. Biochem. Biophys. Res. Commun. 243, 131-136.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 131-136
    • Okazaki, M.1    Ishibashi, Y.2    Asoh, S.3    Ohta, S.4
  • 22
    • 0032481114 scopus 로고    scopus 로고
    • Degradation of eukaryotic polypeptide chain initiation factor (eIF) 4G in response to induction of apoptosis in human lymphoma cell lines
    • Clemens, M. J., Bushell, M., and Morley, S. J. (1998). Degradation of eukaryotic polypeptide chain initiation factor (eIF) 4G in response to induction of apoptosis in human lymphoma cell lines. Oncogene 17, 2921-2931.
    • (1998) Oncogene , vol.17 , pp. 2921-2931
    • Clemens, M.J.1    Bushell, M.2    Morley, S.J.3
  • 23
    • 0031755021 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells
    • Marissen, W. E., and Lloyd, R. E. (1998). Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells. Mol. Cell. Biol. 18, 7565-7574.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7565-7574
    • Marissen, W.E.1    Lloyd, R.E.2
  • 24
    • 0032582744 scopus 로고    scopus 로고
    • Cleavage of translation initiation factor 4G (eIF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase
    • Morley, S. J., McKendrick, L., and Bushell, M. (1998). Cleavage of translation initiation factor 4G (eIF4G) during anti-Fas IgM-induced apoptosis does not require signalling through the p38 mitogen-activated protein (MAP) kinase. FEBS Lett. 438, 41-48.
    • (1998) FEBS Lett. , vol.438 , pp. 41-48
    • Morley, S.J.1    McKendrick, L.2    Bushell, M.3
  • 25
    • 0037134495 scopus 로고    scopus 로고
    • Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria
    • Guo, Y., Srinivasula, S. M., Druilhe, A., Fernandes-Alnemri, T., and Alnemri, E. S. (2002). Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J. Biol. Chem. 277, 13430-13437.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13430-13437
    • Guo, Y.1    Srinivasula, S.M.2    Druilhe, A.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5
  • 26
    • 0037177809 scopus 로고    scopus 로고
    • Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus
    • Paroni, G., Henderson, C., Schneider, C., and Brancolini, C. (2002). Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus. J. Biol. Chem. 277, 15147-15161.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15147-15161
    • Paroni, G.1    Henderson, C.2    Schneider, C.3    Brancolini, C.4
  • 27
    • 0030915095 scopus 로고    scopus 로고
    • Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis
    • Harvey, N. L., Butt, A. J., and Kumar, S. (1997). Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis. J. Biol. Chem. 272, 13134-13139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13134-13139
    • Harvey, N.L.1    Butt, A.J.2    Kumar, S.3
  • 28
    • 0035877605 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3
    • Paroni, G., Henderson, C., Schneider, C., and Brancolini, C. (2001). Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3. J. Biol. Chem. 276, 21907-21915.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21907-21915
    • Paroni, G.1    Henderson, C.2    Schneider, C.3    Brancolini, C.4
  • 29
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., and Wang, X. (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 30
    • 0026675519 scopus 로고
    • Peroxide inactivates calcium pumps in pig coronary artery
    • Grover, A. K., Samson, S. E., and Fomin, V. P. (1992). Peroxide inactivates calcium pumps in pig coronary artery. Am. J. Physiol. 263, H537-H543.
    • (1992) Am. J. Physiol. , vol.263
    • Grover, A.K.1    Samson, S.E.2    Fomin, V.P.3
  • 31
    • 0028981159 scopus 로고
    • Amyloid beta-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death
    • Mark, R. J., Hensley, K., Butterfield, D. A., and Mattson, M. P. (1995). Amyloid beta-peptide impairs ion-motive ATPase activities: Evidence for a role in loss of neuronal Ca2+ homeostasis and cell death. J. Neurosci. 15, 6239-6249.
    • (1995) J. Neurosci. , vol.15 , pp. 6239-6249
    • Mark, R.J.1    Hensley, K.2    Butterfield, D.A.3    Mattson, M.P.4
  • 32
    • 0031020993 scopus 로고    scopus 로고
    • Amyloid beta-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation
    • Mark, R. J., Pang, Z., Geddes, J. W., Uchida, K., and Mattson, M. P. (1997). Amyloid beta-peptide impairs glucose transport in hippocampal and cortical neurons: Involvement of membrane lipid peroxidation. J. Neurosci. 17, 1046-1054.
    • (1997) J. Neurosci. , vol.17 , pp. 1046-1054
    • Mark, R.J.1    Pang, Z.2    Geddes, J.W.3    Uchida, K.4    Mattson, M.P.5
  • 33
    • 0031977191 scopus 로고    scopus 로고
    • The role of calcium in apoptosis
    • Nicotera, P., and Orrenius, S. (1998). The role of calcium in apoptosis. Cell Calcium 23, 173-180.
    • (1998) Cell Calcium , vol.23 , pp. 173-180
    • Nicotera, P.1    Orrenius, S.2
  • 34
    • 0011736559 scopus 로고    scopus 로고
    • Modifications and oxidation of lipids and proteins in human serum detected by thermochemiluminescence
    • Shnizer, S., Kagan, T., Lanir, A., Maor, I., and Reznick, A. (2002). Modifications and oxidation of lipids and proteins in human serum detected by thermochemiluminescence. Luminescence 17, 1-7.
    • (2002) Luminescence , vol.17 , pp. 1-7
    • Shnizer, S.1    Kagan, T.2    Lanir, A.3    Maor, I.4    Reznick, A.5
  • 35
    • 0032571567 scopus 로고    scopus 로고
    • Inhibition of caspase activity induces a switch from apoptosis to necrosis
    • Lemaire, C., Andreau, K., Souvannavong, V., and Adam, A. (1998). Inhibition of caspase activity induces a switch from apoptosis to necrosis. FEBS Lett. 425, 266-270.
    • (1998) FEBS Lett. , vol.425 , pp. 266-270
    • Lemaire, C.1    Andreau, K.2    Souvannavong, V.3    Adam, A.4
  • 36
    • 0033524857 scopus 로고    scopus 로고
    • A comparative study of apoptosis and necrosis in HepG2 cells: Oxidant-induced caspase inactivation leads to necrosis
    • Samali, A., Nordgren, H., Zhivotovsky, B., Peterson, E., and Orrenius, S. (1999). A comparative study of apoptosis and necrosis in HepG2 cells: Oxidant-induced caspase inactivation leads to necrosis. Biochem. Biophys. Res. Commun. 255, 6-11.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 6-11
    • Samali, A.1    Nordgren, H.2    Zhivotovsky, B.3    Peterson, E.4    Orrenius, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.