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Volumn 13, Issue 1, 2008, Pages 147-155

A molecular mechanism for mimosine-induced apoptosis involving oxidative stress and mitochondrial activation

Author keywords

Apoptosis; Mimosine; Mitochondria; Reactive oxygen species

Indexed keywords

ACETYLCYSTEINE; ALPHA TOCOPHEROL; ANTIOXIDANT; CASPASE 3; CYCLOSPORIN A; CYTOCHROME C; GLUTATHIONE; HYDROGEN PEROXIDE; MIMOSINE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 38049177594     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-007-0156-7     Document Type: Article
Times cited : (35)

References (36)
  • 1
    • 0030220017 scopus 로고    scopus 로고
    • Mimosine blocks cell cycle progression by chelating iron in asynchronous human breast cancer cells
    • Kristen NSK, Vulliet P (1996) Mimosine blocks cell cycle progression by chelating iron in asynchronous human breast cancer cells. Toxic App Pharm 139:356-364
    • (1996) Toxic App Pharm , vol.139 , pp. 356-364
    • Kristen, N.S.K.1    Vulliet, P.2
  • 2
    • 0014736370 scopus 로고
    • Effect of mimosine on the rat fetus
    • Dewreede S, Wayman O (1970) Effect of mimosine on the rat fetus. Teratology 3:21-27
    • (1970) Teratology , vol.3 , pp. 21-27
    • Dewreede, S.1    Wayman, O.2
  • 3
    • 0031585861 scopus 로고    scopus 로고
    • The dual effect of mimosine on DNA replication
    • Kalejta RF, Hamlin JL (1997) The dual effect of mimosine on DNA replication. Exp Cell Res 231:173-183
    • (1997) Exp Cell Res , vol.231 , pp. 173-183
    • Kalejta, R.F.1    Hamlin, J.L.2
  • 4
    • 0032192689 scopus 로고    scopus 로고
    • Mimosine, a toxin produced by the tree-legume Leucaena provides a nodulation competition advantage to mimosine-degrading Rhiobuim strains
    • Soedarjo M, Borthakur D (1998) Mimosine, a toxin produced by the tree-legume Leucaena provides a nodulation competition advantage to mimosine-degrading Rhiobuim strains. Appl Environ Microbiol 30:1605-1613
    • (1998) Appl Environ Microbiol , vol.30 , pp. 1605-1613
    • Soedarjo, M.1    Borthakur, D.2
  • 5
    • 0033602015 scopus 로고    scopus 로고
    • Mimosine arrests proliferating human cells before onset of DNA replication in a dose-dependent manner
    • Krude T (1999) Mimosine arrests proliferating human cells before onset of DNA replication in a dose-dependent manner. Exp Cell Res 247:148-159
    • (1999) Exp Cell Res , vol.247 , pp. 148-159
    • Krude, T.1
  • 6
    • 0028110330 scopus 로고
    • Mimosine inhibits viral DNA synthesis through ribonucleotide reductase
    • Dai Y, Gold B, Vishwantha JK, Rhode S (1994) Mimosine inhibits viral DNA synthesis through ribonucleotide reductase. Virology 205:210-216
    • (1994) Virology , vol.205 , pp. 210-216
    • Dai, Y.1    Gold, B.2    Vishwantha, J.K.3    Rhode, S.4
  • 7
    • 0028931706 scopus 로고
    • Mimosine differentially inhibits DNA replication and cell cycle progression in somatic cells compared to embryonic cells of Xenopus laevis
    • Wang Y, Zhao J, Clapper J, Martin LD, Du C, Devore ER et al (1995) Mimosine differentially inhibits DNA replication and cell cycle progression in somatic cells compared to embryonic cells of Xenopus laevis. Exp Cell Res 217:84-91
    • (1995) Exp Cell Res , vol.217 , pp. 84-91
    • Wang, Y.1    Zhao, J.2    Clapper, J.3    Martin, L.D.4    Du, C.5    Devore, E.R.6
  • 8
    • 0028952750 scopus 로고
    • Mimosine arrests DNA synthesis at replication forks by inhibiting deoxynucleotide metabolism
    • Gilbert DM, Neilson A, Miyazawa H, dePamphelis ML, Burhans WC (1995) Mimosine arrests DNA synthesis at replication forks by inhibiting deoxynucleotide metabolism. J Biol Chem 270:9597-9606
    • (1995) J Biol Chem , vol.270 , pp. 9597-9606
    • Gilbert, D.M.1    Neilson, A.2    Miyazawa, H.3    Depamphelis, M.L.4    Burhans, W.C.5
  • 10
    • 0028919255 scopus 로고
    • Mimosine, a novel inhibitor of DNA replication, binds to a 50 kDa protein in Chinese hamster cells
    • Mosca PJ, Lin HB, Hamlin JL (1995) Mimosine, a novel inhibitor of DNA replication, binds to a 50 kDa protein in Chinese hamster cells. Nuc Acids Res 23:261-268
    • (1995) Nuc Acids Res , vol.23 , pp. 261-268
    • Mosca, P.J.1    Lin, H.B.2    Hamlin, J.L.3
  • 12
    • 0027197906 scopus 로고
    • Hypusine. Its post-translational formation in eucaryotic initiation factor 5A and its potential role in cellular regulation
    • Park MH,Wolff EC, Folk JE (1993) Hypusine. Its post-translational formation in eucaryotic initiation factor 5A and its potential role in cellular regulation. Biofactors 4:95-104
    • (1993) Biofactors , vol.4 , pp. 95-104
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 14
    • 13244249801 scopus 로고    scopus 로고
    • 2 production as a mechanism for cell type-specific inhibition of tumor necrosis factor α-induced but not interleukin-1β induced IκB kinase complex/nuclear factor-κB activation
    • 2 production as a mechanism for cell type-specific inhibition of tumor necrosis factor α-induced but not interleukin-1β induced IκB kinase complex/nuclear factor-κB activation. J Biol Chem 280:2912-2923
    • (2004) J Biol Chem , vol.280 , pp. 2912-2923
    • Panopoulous, A.1    Harraz, M.2    Engelhardt, J.F.3    Zandi, E.4
  • 15
    • 0034738051 scopus 로고    scopus 로고
    • Treatment of mammalian cells with mimosine generates DNA breaks
    • Mikhailov I, Russev G, Anachkova B (2000) Treatment of mammalian cells with mimosine generates DNA breaks. Mut Res 459:299-306
    • (2000) Mut Res , vol.459 , pp. 299-306
    • Mikhailov, I.1    Russev, G.2    Anachkova, B.3
  • 16
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M (1999) The mitochondrial permeability transition pore and its role in cell death. Biochem J 341:233-249
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 17
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • Halestrap AP, McStay GP, Clarke SJ (2002) The permeability transition pore complex: another view. Biochimie 84:153-166
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 18
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC (2000) Mitochondrial control of cell death. Nat Med 6:513-519
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 19
    • 33745591102 scopus 로고    scopus 로고
    • Multiple pathways of cytochrome c relese from mitochondria in apoptosis
    • Gogvadze V, Orrenius S, Zhivotovsky B (2006) Multiple pathways of cytochrome c relese from mitochondria in apoptosis. Biochim Biophys Acta 1757:639-647
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 639-647
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 20
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF (2003) Mitochondrial formation of reactive oxygen species. J Physiol 552:335-344
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 21
    • 33644862368 scopus 로고    scopus 로고
    • JNK siganling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species
    • Shen HM, Liu ZG (2006) JNK siganling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species. Free Radic Biol Med 40:928-939
    • (2006) Free Radic Biol Med , vol.40 , pp. 928-939
    • Shen, H.M.1    Liu, Z.G.2
  • 22
    • 0035917814 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and oxidative stress
    • Kowaltowski AJ, Castilho RF, Vercesi AE (2001) Mitochondrial permeability transition and oxidative stress. FEBS Lett 495:12-15
    • (2001) FEBS Lett , vol.495 , pp. 12-15
    • Kowaltowski, A.J.1    Castilho, R.F.2    Vercesi, A.E.3
  • 23
    • 0032805804 scopus 로고    scopus 로고
    • Non-steroidal antiestrogens induce apoptosis in HL-60 and MOLT3 leukemic cells; Involvement of reactive oxygen radicals and protein kinase C
    • Hayon T, Dvilansky A, Oriev L, Nathan I (1999) Non-steroidal antiestrogens induce apoptosis in HL-60 and MOLT3 leukemic cells; involvement of reactive oxygen radicals and protein kinase C. Anticancer Res 19:2089-2093
    • (1999) Anticancer Res , vol.19 , pp. 2089-2093
    • Hayon, T.1    Dvilansky, A.2    Oriev, L.3    Nathan, I.4
  • 25
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
    • Zalk R, Israelson A, Garty ES, Azoulay-Zohar H, Shoshan-Barmatz V (2005) Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria. Biochem 386:73-83
    • (2005) Biochem , vol.386 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.S.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 26
    • 0025043947 scopus 로고
    • Microtiter plate assay for the measurement of glutathione and glutathione disulfide in large numbers of biological samples
    • Baker MA, Cerniglia GJ, Zaman A (1990) Microtiter plate assay for the measurement of glutathione and glutathione disulfide in large numbers of biological samples. Analy Biochem 190:360-365
    • (1990) Analy Biochem , vol.190 , pp. 360-365
    • Baker, M.A.1    Cerniglia, G.J.2    Zaman, A.3
  • 27
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like protease during Fas-mediated apoptosis
    • Enari M, Talanian RV, Wong WW, Nagata S (1996) Sequential activation of ICE-like and CPP32-like protease during Fas-mediated apoptosis. Nature 380:723-726
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 28
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf/Caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X (1997) Cytochrome c and dATP-dependent formation of Apaf/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
  • 29
    • 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
  • 32
    • 0028931345 scopus 로고
    • Iron chelators induce apoptosis in proliferating cells
    • Hileti D, Panayiotidis P, Hoffbrand AV (1995) Iron chelators induce apoptosis in proliferating cells. Br J Haematol 89:181-187
    • (1995) Br J Haematol , vol.89 , pp. 181-187
    • Hileti, D.1    Panayiotidis, P.2    Hoffbrand, A.V.3
  • 34
    • 0032078224 scopus 로고    scopus 로고
    • Mitochondrial respiratory enzymes are a major target of iron toxicity in rat heart cells
    • Link G, Saada A, Pinson A, Konijn AM, Hershko C (1998) Mitochondrial respiratory enzymes are a major target of iron toxicity in rat heart cells. J Lab Clin Med 131:466-474
    • (1998) J Lab Clin Med , vol.131 , pp. 466-474
    • Link, G.1    Saada, A.2    Pinson, A.3    Konijn, A.M.4    Hershko, C.5
  • 35
    • 0034064991 scopus 로고    scopus 로고
    • Susceptibiltiy to drug-induced apoptosis correlates with differential modulation of Bad, Bcl-2 and Bcl-xL protein levels
    • Tudor G, Aguilara A, Halverson DO, Laing ND, Sausville EA (2000) Susceptibiltiy to drug-induced apoptosis correlates with differential modulation of Bad, Bcl-2 and Bcl-xL protein levels. Cell Death Differ 6:574-586
    • (2000) Cell Death Differ , vol.6 , pp. 574-586
    • Tudor, G.1    Aguilara, A.2    Halverson, D.O.3    Laing, N.D.4    Sausville, E.A.5
  • 36
    • 8744313842 scopus 로고    scopus 로고
    • Cell cycle arrest at the initiation step of human chromosomal DNA replication causes DNA damage
    • Szuts D, Krude T (2004) Cell cycle arrest at the initiation step of human chromosomal DNA replication causes DNA damage. J Cell Sci 117:4897-4908
    • (2004) J Cell Sci , vol.117 , pp. 4897-4908
    • Szuts, D.1    Krude, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.