메뉴 건너뛰기




Volumn 10, Issue 2, 2010, Pages 151-157

Effects of α-mangostin on mitochondrial energetic metabolism

Author keywords

Mitochondrial permeability transition; Oxidative stress; Xanthone; Mangostin

Indexed keywords

ADENOSINE DIPHOSPHATE; ALPHA MANGOSTIN; CALCIUM; CYTOCHROME C OXIDASE; UNCLASSIFIED DRUG; XANTHONE DERIVATIVE;

EID: 76349117673     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mito.2009.12.140     Document Type: Article
Times cited : (31)

References (36)
  • 1
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 79 (1999) 1127-1155
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 2
    • 0015955670 scopus 로고
    • Spectrofluorometric analysis of hydrogen peroxide
    • Black M.J., and Brandt R.B. Spectrofluorometric analysis of hydrogen peroxide. Anal. Biochem. 58 (1974) 246-254
    • (1974) Anal. Biochem. , vol.58 , pp. 246-254
    • Black, M.J.1    Brandt, R.B.2
  • 3
    • 0029561991 scopus 로고
    • Inhibition of the mitochondrial permeability transition by cyclosporin A during long time frame experiments: relationship between pore opening and the activity of mitochondrial phospholipases
    • Broekemeier K.M., and Pfeiffer D.R. Inhibition of the mitochondrial permeability transition by cyclosporin A during long time frame experiments: relationship between pore opening and the activity of mitochondrial phospholipases. Biochemistry 34 (1995) 16440-16449
    • (1995) Biochemistry , vol.34 , pp. 16440-16449
    • Broekemeier, K.M.1    Pfeiffer, D.R.2
  • 4
    • 0037082357 scopus 로고    scopus 로고
    • {radical dot} signaling pathway and the transduction of nitrosative to oxidative cell signals: an alternative function for cytochrome c oxidase
    • {radical dot} signaling pathway and the transduction of nitrosative to oxidative cell signals: an alternative function for cytochrome c oxidase. Free Radical Biol. Med. 32 (2002) 370-374
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 370-374
    • Brookes, P.1    Darley-Usmar, V.M.2
  • 5
    • 0018837597 scopus 로고
    • Enhancement of hydrogen peroxide formation by protonophores and ionophores in antimycin-supplemented mitochondria
    • Cadenas E., and Boveris A. Enhancement of hydrogen peroxide formation by protonophores and ionophores in antimycin-supplemented mitochondria. Biochem. J. 188 (1980) 31-37
    • (1980) Biochem. J. , vol.188 , pp. 31-37
    • Cadenas, E.1    Boveris, A.2
  • 6
    • 0022385780 scopus 로고
    • Evidence for the involvement of dithiol groups in mitochondrial calcium transport: studies with cadmium
    • Chávez E., Briones R., Michel B., Bravo C., and Jay D. Evidence for the involvement of dithiol groups in mitochondrial calcium transport: studies with cadmium. Arch. Biochem. Biophys. 242 (1985) 493-497
    • (1985) Arch. Biochem. Biophys. , vol.242 , pp. 493-497
    • Chávez, E.1    Briones, R.2    Michel, B.3    Bravo, C.4    Jay, D.5
  • 7
    • 33947153951 scopus 로고    scopus 로고
    • Mitochondrial permeability transition relevance for apoptotic triggering in the post-ischemic heart
    • Correa F., Soto V., and Zazueta C. Mitochondrial permeability transition relevance for apoptotic triggering in the post-ischemic heart. Int. J. Biochem. Cell Biol. 39 (2007) 787-798
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 787-798
    • Correa, F.1    Soto, V.2    Zazueta, C.3
  • 8
    • 36748999905 scopus 로고    scopus 로고
    • Cardioprotective effect of alpha-mangostin, a xanthone derivative from mangosteen on tissue defense system against isoproterenol-induced myocardial infarction in rats
    • Devi Sampath P., and Vijayaraghavan K. Cardioprotective effect of alpha-mangostin, a xanthone derivative from mangosteen on tissue defense system against isoproterenol-induced myocardial infarction in rats. J. Biochem. Mol. Toxicol. 21 (2007) 336-339
    • (2007) J. Biochem. Mol. Toxicol. , vol.21 , pp. 336-339
    • Devi Sampath, P.1    Vijayaraghavan, K.2
  • 11
    • 20044374408 scopus 로고    scopus 로고
    • On the role of the respiratory complex I on membrane permeability transition
    • García N., Correa F., and Chávez E. On the role of the respiratory complex I on membrane permeability transition. J. Bioenerg. Biomembr. 37 (2005) 17-23
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 17-23
    • García, N.1    Correa, F.2    Chávez, E.3
  • 12
    • 0032589515 scopus 로고    scopus 로고
    • 2+-stimulated generation of reactive oxygen species by the respiratory chain
    • 2+-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry 38 (1999) 13279-13287
    • (1999) Biochemistry , vol.38 , pp. 13279-13287
    • Grijalba, M.T.1    Vercesi, A.2    Schreier, S.3
  • 13
    • 0025292743 scopus 로고
    • Mechanism by which mitochondria transport calcium
    • Gunter T.E., and Pfeiffer D.R. Mechanism by which mitochondria transport calcium. Am. J. Physiol. 258 (1990) C755-C786
    • (1990) Am. J. Physiol. , vol.258
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 14
    • 33747081043 scopus 로고    scopus 로고
    • Toxicological studies of gambogic acid and its potential targets in experimental animals
    • Guo Q., Qi Q., You Q., Gu H., Zhao L., and Wu Z. Toxicological studies of gambogic acid and its potential targets in experimental animals. Basic Clin. Pharmacol. Toxicol. 99 (2006) 178-184
    • (2006) Basic Clin. Pharmacol. Toxicol. , vol.99 , pp. 178-184
    • Guo, Q.1    Qi, Q.2    You, Q.3    Gu, H.4    Zhao, L.5    Wu, Z.6
  • 15
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap A.P., Woodfield K.Y., and Connern C.P. Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272 (1997) 3346-3354
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 17
    • 33847114499 scopus 로고    scopus 로고
    • Quantitative and qualitative determination of six xanthones in Garcinia mangostana L. by LC-PDA and LC-ESI-MS
    • Ji X., Avula B., and Khan I.A. Quantitative and qualitative determination of six xanthones in Garcinia mangostana L. by LC-PDA and LC-ESI-MS. J. Pharm. Biomed. Anal. 43 (2007) 1270-1276
    • (2007) J. Pharm. Biomed. Anal. , vol.43 , pp. 1270-1276
    • Ji, X.1    Avula, B.2    Khan, I.A.3
  • 19
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li N., Ragheb K., Lawler G., Sturgis J., Rajwa B., Melendez J.A., and Robinson J.P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 278 (2003) 8516-8525
    • (2003) J. Biol. Chem. , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 22
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller F., Liu Y., and Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279 (2004) 49064-49073
    • (2004) J. Biol. Chem. , vol.279 , pp. 49064-49073
    • Muller, F.1    Liu, Y.2    Van Remmen, H.3
  • 23
    • 0028340683 scopus 로고
    • Magnesium ion modulates the sensitivity of the mitochondrial permeability transition pore to cyclosporine A and ADP
    • Novgodorov S., Gudz T., Brierly G., and Pfeiffer D. Magnesium ion modulates the sensitivity of the mitochondrial permeability transition pore to cyclosporine A and ADP. Arch. Biochem. Biophys. 311 (1994) 219-228
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 219-228
    • Novgodorov, S.1    Gudz, T.2    Brierly, G.3    Pfeiffer, D.4
  • 24
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H., Ohishi N., and Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem. 95 (1979) 351-358
    • (1979) Anal. Biochem. , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 25
    • 63949084185 scopus 로고    scopus 로고
    • The flavonoid quercetin induces changes in mitochondrial permeability transition by inhibiting adenine nucleotide translocase
    • Ortega R., and García N. The flavonoid quercetin induces changes in mitochondrial permeability transition by inhibiting adenine nucleotide translocase. J. Bioenerg. Biomembr. 41 (2009) 41-47
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 41-47
    • Ortega, R.1    García, N.2
  • 26
    • 21544476484 scopus 로고    scopus 로고
    • Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition
    • Pardo-Andreu G.L., Delgado R., Velho J.A., Curti C., and Vercesi A.E. Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition. Arch. Biochem. Biophys. 439 (2005) 184-193
    • (2005) Arch. Biochem. Biophys. , vol.439 , pp. 184-193
    • Pardo-Andreu, G.L.1    Delgado, R.2    Velho, J.A.3    Curti, C.4    Vercesi, A.E.5
  • 27
    • 29944444937 scopus 로고    scopus 로고
    • Vimang (Mangifera indica L. extract) induces permeability transition in isolated mitochondria, closely reproducing the effect of manfigerin, Vimang's main component
    • Pardo-Andreu G.L., Dorta D.J., Delgado R., Cavalheiro R.A., Santos A.C., Vercesi A.F., and Curti C. Vimang (Mangifera indica L. extract) induces permeability transition in isolated mitochondria, closely reproducing the effect of manfigerin, Vimang's main component. Chem. Biol. Interact. 159 (2006) 141-148
    • (2006) Chem. Biol. Interact. , vol.159 , pp. 141-148
    • Pardo-Andreu, G.L.1    Dorta, D.J.2    Delgado, R.3    Cavalheiro, R.A.4    Santos, A.C.5    Vercesi, A.F.6    Curti, C.7
  • 29
    • 0037010863 scopus 로고    scopus 로고
    • Interaction of genistein with the mitochondrial electron transport chain results in opening of the membrane transition pore
    • Salvi M., Brunati A.M., Clari G., and Toninello A. Interaction of genistein with the mitochondrial electron transport chain results in opening of the membrane transition pore. Biochim. Biophys. Acta 1556 (2002) 187-196
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 187-196
    • Salvi, M.1    Brunati, A.M.2    Clari, G.3    Toninello, A.4
  • 31
    • 0035242358 scopus 로고    scopus 로고
    • Palmitic acid opens a novel cyclosporin A-insensitive pore in the inner mitochondrial membrane
    • Sultan A., and Sokolove P.M. Palmitic acid opens a novel cyclosporin A-insensitive pore in the inner mitochondrial membrane. Arch. Biochem. Biophys. 386 (2001) 37-51
    • (2001) Arch. Biochem. Biophys. , vol.386 , pp. 37-51
    • Sultan, A.1    Sokolove, P.M.2
  • 32
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens J.F. Superoxide production by the mitochondrial respiratory chain. Biosci. Rep. 17 (1997) 3-8
    • (1997) Biosci. Rep. , vol.17 , pp. 3-8
    • Turrens, J.F.1
  • 33
    • 0242290783 scopus 로고    scopus 로고
    • Spontaneous changes in mitochondrial membrane potential in single isolated brain mitochondria
    • Vergun O., Votyakova T.V., and Reynolds I.J. Spontaneous changes in mitochondrial membrane potential in single isolated brain mitochondria. Biophys. J. 85 (2003) 3358-3366
    • (2003) Biophys. J. , vol.85 , pp. 3358-3366
    • Vergun, O.1    Votyakova, T.V.2    Reynolds, I.J.3
  • 34
    • 18144427184 scopus 로고    scopus 로고
    • 2+-induced permeabilization promotes free radical release from rat brain mitochondria with partially inhibited complex I
    • 2+-induced permeabilization promotes free radical release from rat brain mitochondria with partially inhibited complex I. J. Neurochem. 93 (2005) 526-537
    • (2005) J. Neurochem. , vol.93 , pp. 526-537
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 35
    • 0028279537 scopus 로고
    • On the role of ADP to increase the inhibitory effect of cyclosporin on mitochondrial membrane permeability transition
    • Zazueta C., Reyes-Vivas H., Corona N., Bravo C., and Chávez E. On the role of ADP to increase the inhibitory effect of cyclosporin on mitochondrial membrane permeability transition. Biochem. Mol. Biol. Int. 33 (1994) 385-392
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 385-392
    • Zazueta, C.1    Reyes-Vivas, H.2    Corona, N.3    Bravo, C.4    Chávez, E.5
  • 36
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., and Szabò I. The mitochondrial permeability transition. Biochim. Biophys. Acta 1241 (1995) 139-176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabò, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.