메뉴 건너뛰기




Volumn 66, Issue 12, 2003, Pages 2301-2311

Induction of the mitochondrial permeability transition by selenium compounds mediated by oxidation of the protein thiol groups and generation of the superoxide

Author keywords

Apoptosis; Mitochondria; Mitochondria permeability transition; Selenium compounds; Superoxide anion

Indexed keywords

ANTINEOPLASTIC AGENT; CYTOCHROME C; GLUTATHIONE; OXYGEN RADICAL; SELENATE; SELENITE; SELENIUM DERIVATIVE; SELENOCYSTAMINE; SELENOCYSTINE; SELENODIOXIDE; SELENOMETHIONINE; SUPEROXIDE; THIOL GROUP; UNCLASSIFIED DRUG;

EID: 0344944226     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2003.08.021     Document Type: Article
Times cited : (100)

References (54)
  • 1
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., Reed J.C. Mitochondria and apoptosis. Science. 281:1998;1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 2
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M.O. The biochemistry of apoptosis. Nature. 407:2000;770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 3
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S., Robinson B.H. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem. Sci. 25:2000;502-508.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 4
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: Doubt no more
    • Susin S.A., Zamzami N., Kroemer G. Mitochondria as regulators of apoptosis: doubt no more. Biochim. Biophys. Acta. 1366:1998;151-165.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 6
    • 0034725989 scopus 로고    scopus 로고
    • The redox state of endogenous pyridine nucleotides can determine both the degree of mitochondrial oxidative stress and the solute selectivity of the permeability transition pore
    • Zago E.B., Castilho R.F., Vercesi A.E. The redox state of endogenous pyridine nucleotides can determine both the degree of mitochondrial oxidative stress and the solute selectivity of the permeability transition pore. FEBS Lett. 478:2000;29-33.
    • (2000) FEBS Lett. , vol.478 , pp. 29-33
    • Zago, E.B.1    Castilho, R.F.2    Vercesi, A.E.3
  • 7
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • Madesh M., Hajnoczky G. VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release. J. Cell Biol. 155:2001;1003-1015.
    • (2001) J. Cell Biol. , vol.155 , pp. 1003-1015
    • Madesh, M.1    Hajnoczky, G.2
  • 8
    • 0035917814 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and oxidative stress
    • Kowaltowski A.J., Castilho R.F., Vercesi A.E. Mitochondrial permeability transition and oxidative stress. FEBS Lett. 495:2001;12-15.
    • (2001) FEBS Lett. , vol.495 , pp. 12-15
    • Kowaltowski, A.J.1    Castilho, R.F.2    Vercesi, A.E.3
  • 9
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341(Pt 2):1999;233-249.
    • (1999) Biochem. J. , vol.341 , Issue.PT 2 , pp. 233-249
    • Crompton, M.1
  • 10
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas F., Jouaville L.S., Mazat J.P. Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell. 89:1997;1145-1153.
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 11
    • 0035917844 scopus 로고    scopus 로고
    • Curcumin induces the mitochondrial permeability transition pore mediated by membrane protein thiol oxidation
    • Morin D., Barthelemy S., Zini R., Labidalle S., Tillement J.P. Curcumin induces the mitochondrial permeability transition pore mediated by membrane protein thiol oxidation. FEBS Lett. 495:2001;131-136.
    • (2001) FEBS Lett. , vol.495 , pp. 131-136
    • Morin, D.1    Barthelemy, S.2    Zini, R.3    Labidalle, S.4    Tillement, J.P.5
  • 12
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J., Jones D.P. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273:1998;11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 13
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 275:1997;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
  • 17
    • 0032993576 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative diseases: The role of mitochondria
    • Tatton W.G., Olanow C.W. Apoptosis in neurodegenerative diseases: the role of mitochondria. Biochim. Biophys. Acta. 1410:1999;195-213.
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 195-213
    • Tatton, W.G.1    Olanow, C.W.2
  • 18
    • 0035034541 scopus 로고    scopus 로고
    • Apoptosis and liver diseases: Recent concepts of mechanism and significance
    • Ockner R.K. Apoptosis and liver diseases: recent concepts of mechanism and significance. J. Gastroenterol. Hepatol. 16:2001;248-260.
    • (2001) J. Gastroenterol. Hepatol. , vol.16 , pp. 248-260
    • Ockner, R.K.1
  • 19
    • 0029873387 scopus 로고    scopus 로고
    • Reactive oxygen species and programmed cell death
    • Jacobson M.D. Reactive oxygen species and programmed cell death. Trends Biochem. Sci. 21:1996;83-86.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 83-86
    • Jacobson, M.D.1
  • 21
    • 0035882266 scopus 로고    scopus 로고
    • Se-methylselenocysteine induces apoptosis mediated by reactive oxygen species in HL-60 cells
    • Jung U., Zheng X., Yoon S., Chung A. Se-methylselenocysteine induces apoptosis mediated by reactive oxygen species in HL-60 cells. Free Radic. Biol. Med. 31:2001;479-489.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 479-489
    • Jung, U.1    Zheng, X.2    Yoon, S.3    Chung, A.4
  • 22
    • 0035916436 scopus 로고    scopus 로고
    • 2 induces apoptosis with down-regulation of Bcl-2 and up-regulation of p53 expression in both immortal human hepatic cell line and hepatoma cell line
    • 2 induces apoptosis with down-regulation of Bcl-2 and up-regulation of p53 expression in both immortal human hepatic cell line and hepatoma cell line. Mutat. Res. 490:2001;113-121.
    • (2001) Mutat. Res. , vol.490 , pp. 113-121
    • Wei, Y.1    Cao, X.2    Ou, Y.3    Lu, J.4    Xing, C.5    Zheng, R.6
  • 23
    • 0035185334 scopus 로고    scopus 로고
    • Superoxide radical-initiated apoptotic signalling pathway in selenite-treated HepG2 cells: Mitochondria serve as the main target
    • Shen H.M., Yang C.F., Ding W.X., Liu J., Ong C.N. Superoxide radical-initiated apoptotic signalling pathway in selenite-treated HepG2 cells: mitochondria serve as the main target. Free Radic. Biol. Med. 30:2001;9-21.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 9-21
    • Shen, H.M.1    Yang, C.F.2    Ding, W.X.3    Liu, J.4    Ong, C.N.5
  • 24
    • 0028332519 scopus 로고
    • On the nature of selenium toxicity and carcinostatic activity
    • Spallholz J.E. On the nature of selenium toxicity and carcinostatic activity. Free Radic. Biol. Med. 17:1994;45-64.
    • (1994) Free Radic. Biol. Med. , vol.17 , pp. 45-64
    • Spallholz, J.E.1
  • 25
    • 0027500419 scopus 로고
    • Generation of reactive oxygen species from the reaction of selenium compounds with thiols and mammary tumor cells
    • Yan L., Spallholz J.E. Generation of reactive oxygen species from the reaction of selenium compounds with thiols and mammary tumor cells. Biochem. Pharmacol. 45:1993;429-437.
    • (1993) Biochem. Pharmacol. , vol.45 , pp. 429-437
    • Yan, L.1    Spallholz, J.E.2
  • 26
    • 0032557424 scopus 로고    scopus 로고
    • The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism
    • Kowaltowski A.J., Netto L.E., Vercesi A.E. The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition. Evidence for the participation of reactive oxygen species in this mechanism. J. Biol. Chem. 273:1998;12766-12769.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 27
    • 0026083843 scopus 로고
    • Chemical form of selenium, critical metabolites, and cancer prevention
    • Ip C., Hayes C., Budnick R.M., Ganther H.E. Chemical form of selenium, critical metabolites, and cancer prevention. Cancer Res. 51:1991;595-600.
    • (1991) Cancer Res. , vol.51 , pp. 595-600
    • Ip, C.1    Hayes, C.2    Budnick, R.M.3    Ganther, H.E.4
  • 28
    • 0036289628 scopus 로고    scopus 로고
    • Dysfunction of rat liver mitochondria by selenite: Induction of mitochondrial permeability transition through thiol-oxidation
    • Kim T.S., Jeong D.W., Yun B.Y., Kim I.Y. Dysfunction of rat liver mitochondria by selenite: induction of mitochondrial permeability transition through thiol-oxidation. Biochem. Biophys. Res. Commun. 294:2002;1130-1137.
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 1130-1137
    • Kim, T.S.1    Jeong, D.W.2    Yun, B.Y.3    Kim, I.Y.4
  • 30
    • 1842296385 scopus 로고    scopus 로고
    • Effects of alterations in calcium homeostasis on apoptosis during neoplastic progression
    • Preston G.A., Barrett J.C., Biermann J.A., Murphy E. Effects of alterations in calcium homeostasis on apoptosis during neoplastic progression. Cancer Res. 57:1997;537-542.
    • (1997) Cancer Res. , vol.57 , pp. 537-542
    • Preston, G.A.1    Barrett, J.C.2    Biermann, J.A.3    Murphy, E.4
  • 32
    • 0033233483 scopus 로고    scopus 로고
    • Protein kinase Cδ targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector
    • Li L., Lorenzo P.S., Bogi K., Blumberg P.M., Yuspa S.H. Protein kinase Cδ targets mitochondria, alters mitochondrial membrane potential, and induces apoptosis in normal and neoplastic keratinocytes when overexpressed by an adenoviral vector. Mol. Cell Biol. 19:1999;8547-8558.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8547-8558
    • Li, L.1    Lorenzo, P.S.2    Bogi, K.3    Blumberg, P.M.4    Yuspa, S.H.5
  • 35
    • 0031172329 scopus 로고    scopus 로고
    • Influence of the redox state of pyridine nucleotides on mitochondrial sulfhydryl groups and permeability transition
    • Bindoli A., Callegaro M.T., Barzon E., Benetti M., Rigobello M.P. Influence of the redox state of pyridine nucleotides on mitochondrial sulfhydryl groups and permeability transition. Arch. Biochem. Biophys. 342:1997;22-28.
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 22-28
    • Bindoli, A.1    Callegaro, M.T.2    Barzon, E.3    Benetti, M.4    Rigobello, M.P.5
  • 36
    • 0035805115 scopus 로고    scopus 로고
    • In vitro effects of nicotine on mitochondrial respiration and superoxide anion generation
    • Cormier A., Morin C., Zini R., Tillement J.P., Lagrue G. In vitro effects of nicotine on mitochondrial respiration and superoxide anion generation. Brain Res. 900:2001;72-79.
    • (2001) Brain Res. , vol.900 , pp. 72-79
    • Cormier, A.1    Morin, C.2    Zini, R.3    Tillement, J.P.4    Lagrue, G.5
  • 37
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J.M., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:1969;6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 40
    • 0028239794 scopus 로고
    • The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents
    • Petronilli V., Costantini P., Scorrano L., Colonna R., Passamonti S., Bernardi P. The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. J. Biol. Chem. 269:1994;16638-16642.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 41
    • 0032031920 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c
    • Yang J.C., Cortopassi G.A. Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c. Free Radic. Biol. Med. 24:1998;624-631.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 624-631
    • Yang, J.C.1    Cortopassi, G.A.2
  • 42
    • 0027989826 scopus 로고
    • Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo
    • Faulkner K.M., Liochev S.I., Fridovich I. Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo. J. Biol. Chem. 269:1994;23471-23476.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23471-23476
    • Faulkner, K.M.1    Liochev, S.I.2    Fridovich, I.3
  • 43
    • 2442714587 scopus 로고    scopus 로고
    • Control of mitochondrial membrane potential and ROS formation by reversible phosphorylation of cytochrome c oxidase
    • Lee I., Bender E., Kadenbach B. Control of mitochondrial membrane potential and ROS formation by reversible phosphorylation of cytochrome c oxidase. Mol. Cell Biochem. 234-235:2002;63-70.
    • (2002) Mol. Cell Biochem. , vol.234-235 , pp. 63-70
    • Lee, I.1    Bender, E.2    Kadenbach, B.3
  • 44
    • 0035920192 scopus 로고    scopus 로고
    • Alloxan-induced mitochondrial permeability transition triggered by calcium, thiol oxidation, and matrix ATP
    • Sakurai K., Katoh M., Fujimoto Y. Alloxan-induced mitochondrial permeability transition triggered by calcium, thiol oxidation, and matrix ATP. J. Biol. Chem. 276:2001;26942-26946.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26942-26946
    • Sakurai, K.1    Katoh, M.2    Fujimoto, Y.3
  • 45
    • 0029849463 scopus 로고    scopus 로고
    • Identification and metabolism of selenocysteine-glutathione selenenyl sulfide (CySeSG) in small intestine of mice orally exposed to selenocystine
    • Hasegawa T., Okuno T., Nakamuro K., Sayato Y. Identification and metabolism of selenocysteine-glutathione selenenyl sulfide (CySeSG) in small intestine of mice orally exposed to selenocystine. Arch. Toxicol. 71:1996;39-44.
    • (1996) Arch. Toxicol. , vol.71 , pp. 39-44
    • Hasegawa, T.1    Okuno, T.2    Nakamuro, K.3    Sayato, Y.4
  • 46
    • 0026682519 scopus 로고
    • Glutathione oxidase activity of selenocystamine: A mechanistic study
    • Chaudiere J., Courtin O., Leclaire J. Glutathione oxidase activity of selenocystamine: a mechanistic study. Arch. Biochem. Biophys. 296:1992;328-336.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 328-336
    • Chaudiere, J.1    Courtin, O.2    Leclaire, J.3
  • 47
    • 0344142391 scopus 로고    scopus 로고
    • Selenium compounds have disparate abilities to impose oxidative stress and induce apoptosis
    • Stewart M.S., Spallholz J.E., Neldner K.H., Pence B.C. Selenium compounds have disparate abilities to impose oxidative stress and induce apoptosis. Free Radic. Biol. Med. 26:1999;42-48.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 42-48
    • Stewart, M.S.1    Spallholz, J.E.2    Neldner, K.H.3    Pence, B.C.4
  • 48
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10:2000;369-377.
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 49
    • 0034525374 scopus 로고    scopus 로고
    • The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability
    • Harris M.H., Thompson C.B. The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability. Cell Death Differ. 7:2000;1182-1191.
    • (2000) Cell Death Differ. , vol.7 , pp. 1182-1191
    • Harris, M.H.1    Thompson, C.B.2
  • 50
    • 0034523818 scopus 로고    scopus 로고
    • Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c
    • Korsmeyer S.J., Wei M.C., Saito M., Weiler S., Oh K.J., Schlesinger P.H. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ. 7:2000;1166-1173.
    • (2000) Cell Death Differ. , vol.7 , pp. 1166-1173
    • Korsmeyer, S.J.1    Wei, M.C.2    Saito, M.3    Weiler, S.4    Oh, K.J.5    Schlesinger, P.H.6
  • 51
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., Reed J.C. Mitochondrial control of cell death. Nat. Med. 6:2000;513-519.
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 52
    • 0032526940 scopus 로고    scopus 로고
    • The regulation of reactive oxygen species production during programmed cell death
    • Tan S., Sagara Y., Liu Y., Maher P., Schubert D. The regulation of reactive oxygen species production during programmed cell death. J. Cell Biol. 141:1998;1423-1432.
    • (1998) J. Cell Biol. , vol.141 , pp. 1423-1432
    • Tan, S.1    Sagara, Y.2    Liu, Y.3    Maher, P.4    Schubert, D.5
  • 53
    • 0029863399 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites
    • Costantini P., Chernyak B.V., Petronilli V., Bernardi P. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 271:1996;6746-6751.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6746-6751
    • Costantini, P.1    Chernyak, B.V.2    Petronilli, V.3    Bernardi, P.4
  • 54
    • 0035863104 scopus 로고    scopus 로고
    • Oxidation of pyridine nucleotides during Fas- and ceramide-induced apoptosis in Jurkat cells: Correlation with changes in mitochondria, glutathione depletion, intracellular acidification and caspase 3 activation
    • Gendron M.C., Schrantz N., Metivier D., Kroemer G., Maciorowska Z., Sureau F., Koester S., Petit P.X. Oxidation of pyridine nucleotides during Fas- and ceramide-induced apoptosis in Jurkat cells: correlation with changes in mitochondria, glutathione depletion, intracellular acidification and caspase 3 activation. Biochem. J. 353:2001;357-367.
    • (2001) Biochem. J. , vol.353 , pp. 357-367
    • Gendron, M.C.1    Schrantz, N.2    Metivier, D.3    Kroemer, G.4    MacIorowska, Z.5    Sureau, F.6    Koester, S.7    Petit, P.X.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.