메뉴 건너뛰기




Volumn 61, Issue 19-20, 2004, Pages 2664-2671

Influence of reactive oxygen species production by monoamine oxidase activity on aluminum-induced mitochondrial permeability transition

Author keywords

Aluminum; Mitochondria; Monoamine oxidase; Permeability transition; Tyramine

Indexed keywords

ALUMINUM; AMINE OXIDASE (FLAVIN CONTAINING); CATALASE; CYCLOSPORIN A; DITHIOERYTHRITOL; HYDROGEN PEROXIDE; N ETHYLMALEIMIDE; PYRIDINE NUCLEOTIDE; REACTIVE OXYGEN METABOLITE; THIOL GROUP; TYRAMINE;

EID: 9744221186     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4236-3     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 0017234506 scopus 로고
    • The dialysis encephalopathy syndrome: Possible aluminum intoxication
    • Alfrey A. C., LeGendre G. R. and Kaehny W. D. (1976) The dialysis encephalopathy syndrome: possible aluminum intoxication. N. Engl. J. Med. 294: 184-188
    • (1976) N. Engl. J. Med. , vol.294 , pp. 184-188
    • Alfrey, A.C.1    Legendre, G.R.2    Kaehny, W.D.3
  • 2
    • 0005973206 scopus 로고    scopus 로고
    • Aluminum induced oxidative events and its relation to inflammation: A role for the metal in Alzheimer's disease
    • Campbell A. and Bondy S. C. (2000) Aluminum induced oxidative events and its relation to inflammation: a role for the metal in Alzheimer's disease. Cell. Mol. Biol. 46: 721-730
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 721-730
    • Campbell, A.1    Bondy, S.C.2
  • 3
    • 0348002190 scopus 로고
    • Nicolini M., Zatta P. and Corani B. (eds), Raven Press, New York
    • Colombini M. (1991) In: Aluminum in Chemistry Biology and Medicine, pp. 33-43, Nicolini M., Zatta P. and Corani B. (eds), Raven Press, New York
    • (1991) Aluminum in Chemistry Biology and Medicine , pp. 33-43
    • Colombini, M.1
  • 4
    • 0003280444 scopus 로고
    • Chadwick D. J. and Wlielan J. (eds) Wiley, Chichester
    • Martin R. B. (1992) In: Aluminum in Biology and Medicine, pp. 5-18, Chadwick D. J. and Wlielan J. (eds) Wiley, Chichester
    • (1992) Aluminum in Biology and Medicine , pp. 5-18
    • Martin, R.B.1
  • 6
    • 0032701899 scopus 로고    scopus 로고
    • Effect of aluminum-induced Alzheimer like condition on oxidative energy metabolism in rat liver, brain and heart mitochondria
    • Swegert C. V., Dave K. R. and Katyare S. S. (1999) Effect of aluminum-induced Alzheimer like condition on oxidative energy metabolism in rat liver, brain and heart mitochondria. Mech. Ageing Dev. 112: 27-42
    • (1999) Mech. Ageing Dev. , vol.112 , pp. 27-42
    • Swegert, C.V.1    Dave, K.R.2    Katyare, S.S.3
  • 8
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M. and Szabò I. (1995) The mitochondrial permeability transition. Biochim. Biophys. Acta 1241: 139-176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabò, I.2
  • 9
    • 0033607443 scopus 로고    scopus 로고
    • Activation of monoamine oxidase type-B by aluminum in rat brain homogenate
    • Zatta P., Zambenedetti P. and Milanesi M. (1999) Activation of monoamine oxidase type-B by aluminum in rat brain homogenate. Neuroreport 10: 3645-3648
    • (1999) Neuroreport , vol.10 , pp. 3645-3648
    • Zatta, P.1    Zambenedetti, P.2    Milanesi, M.3
  • 11
    • 0036628855 scopus 로고    scopus 로고
    • Tyramine and monoamine oxidase inhibitors as modulators of the mitochondrial membrane permeability transition
    • Marcocci L., De Marchi U., Salvi M., Milella Z. G., Nocera S., Agostinelli et al. (2002) Tyramine and monoamine oxidase inhibitors as modulators of the mitochondrial membrane permeability transition. J. Membr. Biol. 188: 23-31
    • (2002) J. Membr. Biol. , vol.188 , pp. 23-31
    • Marcocci, L.1    De Marchi, U.2    Salvi, M.3    Milella, Z.G.4    Nocera, S.5    Agostinelli6
  • 12
    • 0035202117 scopus 로고    scopus 로고
    • Molecular characterization of monoamine oxidases a and B
    • Abell C. W. and Kwan S. W. (2000) Molecular characterization of monoamine oxidases A and B. Prog. Nucleic Acid Res. Mol. Biol. 65: 129-156
    • (2000) Prog. Nucleic Acid Res. Mol. Biol. , vol.65 , pp. 129-156
    • Abell, C.W.1    Kwan, S.W.2
  • 13
    • 0010357791 scopus 로고
    • Correlation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity with blood-brain barrier monoamine oxidase activity
    • Kalaria R. N., Mitchell M. J. and Harik S. I. (1987) Correlation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine neurotoxicity with blood-brain barrier monoamine oxidase activity. Proc. Natl. Acad. Sci. USA 84: 3521-3525
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3521-3525
    • Kalaria, R.N.1    Mitchell, M.J.2    Harik, S.I.3
  • 14
    • 0024571226 scopus 로고
    • Monoamine oxidase, brain ageing and degenerative diseases
    • Strolin-Benedetti, M. and Dosiert, P. (1989) Monoamine oxidase, brain ageing and degenerative diseases. Biochem. Pharmacol. 38: 555-561
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 555-561
    • Strolin-Benedetti, M.1    Dosiert, P.2
  • 15
    • 0016086409 scopus 로고
    • The absorptiometric determination of aluminum in water: A comparison of some chromogenic reagents and the development of an improved method
    • Dougan W. K. and Wilson A. E. (1974) The absorptiometric determination of aluminum in water: a comparison of some chromogenic reagents and the development of an improved method. Analyst 99: 413-430
    • (1974) Analyst , vol.99 , pp. 413-430
    • Dougan, W.K.1    Wilson, A.E.2
  • 16
    • 0000417081 scopus 로고
    • Intracellular distribution of enzymes. V. Further studies on the distribution of cytochrome c in rat homogenate
    • Schneider W. C. and Hogeboom G. H. (1950) Intracellular distribution of enzymes. V. Further studies on the distribution of cytochrome c in rat homogenate. J. Biol. Chem. 183: 123-128
    • (1950) J. Biol. Chem. , vol.183 , pp. 123-128
    • Schneider, W.C.1    Hogeboom, G.H.2
  • 17
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall A. G., Bardawill C. J. and Davi, M. M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177: 751-766
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    Davi, M.M.3
  • 19
    • 0036128974 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin reductase and thiol status
    • Bindoli A. and Rigobello M. P. (2002) Mitochondrial thioredoxin reductase and thiol status. Methods Enzymol. 347: 307-316
    • (2002) Methods Enzymol. , vol.347 , pp. 307-316
    • Bindoli, A.1    Rigobello, M.P.2
  • 20
    • 0014544548 scopus 로고
    • Ion-induced ultrastructural transformations in isolated mitochondria
    • Hackenbrock C. R. and Caplan A. I. (1969) Ion-induced ultrastructural transformations in isolated mitochondria. J. Cell. Biol. 42: 221-234
    • (1969) J. Cell. Biol. , vol.42 , pp. 221-234
    • Hackenbrock, C.R.1    Caplan, A.I.2
  • 21
    • 0023576056 scopus 로고
    • Voltage gating in VDAC is markedly inhibited by micromolar quantities of aluminum
    • Dill E. T., Holden M. J. and Colombini M. (1987) Voltage gating in VDAC is markedly inhibited by micromolar quantities of aluminum. J. Membr. Biol. 99: 187-196
    • (1987) J. Membr. Biol. , vol.99 , pp. 187-196
    • Dill, E.T.1    Holden, M.J.2    Colombini, M.3
  • 22
    • 0024978250 scopus 로고
    • Inhibition by aluminum hydroxide of the voltage-dependent closure of the mitochondrial channel, VDAC
    • Zhang D. W. and Colombini M. (1989) Inhibition by aluminum hydroxide of the voltage-dependent closure of the mitochondrial channel, VDAC. Biochim. Biophys. Acta 991: 68-78
    • (1989) Biochim. Biophys. Acta , vol.991 , pp. 68-78
    • Zhang, D.W.1    Colombini, M.2
  • 23
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • Beutner G., Ruck A., Riede B., Welte W. and Brdiczka D. (1996) Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 396: 189-195
    • (1996) FEBS Lett. , vol.396 , pp. 189-195
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 24
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore: Implication for regulation of permeability transition by the kinases
    • Beutner G., Ruck A., Riede B. and Brdiczka D. (1998) Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore: implication for regulation of permeability transition by the kinases. Biochim. Biophys. Acta. 1368: 7-18
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 25
    • 0028821028 scopus 로고
    • Ca(2+)-induced mitochondrial membrane permeabilization: Role of coenzyme Q redox state
    • Kowaltowski A. J., Castilho R. F. and Vercesi A. E. (1995) Ca(2+)-induced mitochondrial membrane permeabilization: role of coenzyme Q redox state. Am. J. Physiol. 269: C141-C147
    • (1995) Am. J. Physiol. , vol.269
    • Kowaltowski, A.J.1    Castilho, R.F.2    Vercesi, A.E.3
  • 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. and Vercesi A. E. (1998) The thiol-specific antioxidant enzyme prevents mitochondrial permeability transition: evidence for the participation of reactive oxygen species in this mechanism. J. Biol. Chem. 273: 12766-12769.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12766-12769
    • Kowaltowski, A.J.1    Netto, L.E.2    Vercesi, A.E.3
  • 27
    • 0037109064 scopus 로고    scopus 로고
    • Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore
    • McStay P., Clarke S. J. and Halestrap A. P. (2002) Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore. Biochem. J. 367: 541-548
    • (2002) Biochem. J. , vol.367 , pp. 541-548
    • McStay, P.1    Clarke, S.J.2    Halestrap, A.P.3
  • 28
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis; doubt no more
    • Susin S. A., Zamzami N. and Kroemer G. (1998) Mitochondria as regulators of apoptosis; doubt no more. Biochim. Biophys. Acta. 1366: 151-165
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 29
    • 0030592172 scopus 로고    scopus 로고
    • The permeability transition pore: Control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death
    • Bernardi P. (1996) The permeability transition pore: control points of a cyclosporin A-sensitive mitochondrial channel involved in cell death. Biochim. Biophys. Acta 1275: 5-9
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 5-9
    • Bernardi, P.1
  • 30
    • 0028938858 scopus 로고
    • Selective inhibition of the mitochondrial permeability transition pore at the oxidation-reduction sensitive dithiol by monobromobimane
    • Costantini P., Chernyak B. V., Petronilli V. and Bernardi P. (1995) Selective inhibition of the mitochondrial permeability transition pore at the oxidation-reduction sensitive dithiol by monobromobimane. FEBS Lett. 362: 239-242
    • (1995) FEBS Lett. , vol.362 , pp. 239-242
    • Costantini, P.1    Chernyak, B.V.2    Petronilli, V.3    Bernardi, P.4
  • 32
    • 0028154011 scopus 로고
    • 2+ from mitochondria without inactivating the mitochondrial inner-membrane pore
    • 2+ from mitochondria without inactivating the mitochondrial inner-membrane pore. Biochem. J. 297: 151-155
    • (1994) Biochem. J. , vol.297 , pp. 151-155
    • Reichman, N.1    Porteous, C.M.2    Murphy, M.P.3
  • 33
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K. F. and Kroemer G. (2001) Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3: E255-E263
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.2
  • 35
    • 0032749848 scopus 로고    scopus 로고
    • Mitochondrial physiology and pathology: Concepts of programmed death of organelles, cells and organisms
    • Skulachev V. P. (1999) Mitochondrial physiology and pathology: concepts of programmed death of organelles, cells and organisms. Mol. Aspects Med. 20: 139-184
    • (1999) Mol. Aspects Med. , vol.20 , pp. 139-184
    • Skulachev, V.P.1
  • 36
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cells: Shape changes, dislocations, fusion, and fission of mitochondria
    • Bereiter-Hahn, J. and Voth, M. (1994) Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria. Microsc. Res. Tech. 27: 198-219.
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voth, M.2
  • 37
    • 0032896640 scopus 로고    scopus 로고
    • Rat liver GTP-binding proteins mediate changes in mitochondrial membrane potential and organelle fusion
    • Cortese, J. D. (1999) Rat liver GTP-binding proteins mediate changes in mitochondrial membrane potential and organelle fusion. Am. J. Physiol. 276: C611-C620
    • (1999) Am. J. Physiol. , vol.276
    • Cortese, J.D.1
  • 38
    • 0032574956 scopus 로고    scopus 로고
    • Novel fluorescence membrane fusion assays reveal GTP-dependent fusogenic properties of outer mitochondrial membrane-derived proteins
    • Cortese J. D., Voglino L. A. and Hackenbrock C. R. (1998) Novel fluorescence membrane fusion assays reveal GTP-dependent fusogenic properties of outer mitochondrial membrane-derived proteins. Biochim. Biophys. Acta 1371: 185-198
    • (1998) Biochim. Biophys. Acta , vol.1371 , pp. 185-198
    • Cortese, J.D.1    Voglino, L.A.2    Hackenbrock, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.