메뉴 건너뛰기




Volumn 41, Issue 1, 2006, Pages 41-45

A shortcut to mitochondrial signaling and pathology: A commentary on "Nonenzymatic formation of succinate in mitochondria under oxidative stress"

Author keywords

[No Author keywords available]

Indexed keywords

3 NITROPROPIONIC ACID; AMOBARBITAL; DIAZOXIDE; OXIDIZING AGENT; SUCCINIC ACID;

EID: 33745007332     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2006.03.019     Document Type: Note
Times cited : (11)

References (51)
  • 1
    • 27544477748 scopus 로고    scopus 로고
    • The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing
    • Kaelin Jr. W.G. The von Hippel-Lindau protein, HIF hydroxylation, and oxygen sensing. Biochem. Biophys. Res. Commun. 338 (2005) 627-638
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 627-638
    • Kaelin Jr., W.G.1
  • 2
    • 4143097031 scopus 로고    scopus 로고
    • Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity
    • Ardehali H., Chen Z., Ko Y., Mejia-Alvarez R., and Marban E. Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity. Proc. Natl. Acad. Sci. USA 101 (2004) 11880-11885
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11880-11885
    • Ardehali, H.1    Chen, Z.2    Ko, Y.3    Mejia-Alvarez, R.4    Marban, E.5
  • 7
    • 0000079144 scopus 로고
    • The role of citric acid in intermediate metabolism in mammals
    • Krebs H.A., and Johnson W.A. The role of citric acid in intermediate metabolism in mammals. Enzymologia 4 (1937) 148-156
    • (1937) Enzymologia , vol.4 , pp. 148-156
    • Krebs, H.A.1    Johnson, W.A.2
  • 8
    • 0030703154 scopus 로고    scopus 로고
    • Pyruvate protects neurons against hydrogen peroxide-induced toxicity
    • Desagher S., Glowinski J., and Premont J. Pyruvate protects neurons against hydrogen peroxide-induced toxicity. J. Neurosci. 17 (1997) 9060-9067
    • (1997) J. Neurosci. , vol.17 , pp. 9060-9067
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 9
    • 0025083143 scopus 로고
    • Importance of spontaneous alpha-ketoacid decarboxylation in experiments involving peroxide
    • Vlessis A.A., Bartos D., and Trunkey D. Importance of spontaneous alpha-ketoacid decarboxylation in experiments involving peroxide. Biochem. Biophys. Res. Commun. 170 (1990) 1281-1287
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1281-1287
    • Vlessis, A.A.1    Bartos, D.2    Trunkey, D.3
  • 10
    • 26444439977 scopus 로고    scopus 로고
    • Mitochondrial regulation of oxygen sensing
    • Bell E.L., Emerling B.M., and Chandel N.S. Mitochondrial regulation of oxygen sensing. Mitochondrion 5 (2005) 322-332
    • (2005) Mitochondrion , vol.5 , pp. 322-332
    • Bell, E.L.1    Emerling, B.M.2    Chandel, N.S.3
  • 11
    • 1642330709 scopus 로고    scopus 로고
    • Oxygen sensing and oxidant/redox-related pathways
    • Haddad J.J. Oxygen sensing and oxidant/redox-related pathways. Biochem. Biophys. Res. Commun. 316 (2004) 969-977
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 969-977
    • Haddad, J.J.1
  • 12
    • 11144251210 scopus 로고    scopus 로고
    • Hypoxic pulmonary vasoconstriction: redox events in oxygen sensing
    • Waypa G.B., and Schumacker P.T. Hypoxic pulmonary vasoconstriction: redox events in oxygen sensing. J. Appl. Physiol. 98 (2005) 404-414
    • (2005) J. Appl. Physiol. , vol.98 , pp. 404-414
    • Waypa, G.B.1    Schumacker, P.T.2
  • 13
    • 33744982959 scopus 로고    scopus 로고
    • The oxygen sensing signal cascade under the influence of reactive oxygen species
    • Acker H. The oxygen sensing signal cascade under the influence of reactive oxygen species. Philos. Trans. R. Soc. Lond B: Biol. Sci. 360 (2005) 2201-2210
    • (2005) Philos. Trans. R. Soc. Lond B: Biol. Sci. , vol.360 , pp. 2201-2210
    • Acker, H.1
  • 16
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • Bruick R.K., and McKnight S.L. A conserved family of prolyl-4-hydroxylases that modify HIF. Science 294 (2001) 1337-1340
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 19
    • 22244440847 scopus 로고    scopus 로고
    • Proline hydroxylation and gene expression
    • Kaelin W.G. Proline hydroxylation and gene expression. Annu. Rev. Biochem. 74 (2005) 115-128
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 115-128
    • Kaelin, W.G.1
  • 23
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation
    • Mansfield K.D., Guzy R.D., Pan Y., Young R.M., Cash T.P., Schumacker P.T., and Simon M.C. Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation. Cell Metab. 1 (2005) 393-399
    • (2005) Cell Metab. , vol.1 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3    Young, R.M.4    Cash, T.P.5    Schumacker, P.T.6    Simon, M.C.7
  • 24
    • 0017697003 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates
    • Tuderman L., Myllyla R., and Kivirikko K.I. Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates. Eur. J. Biochem. 80 (1977) 341-348
    • (1977) Eur. J. Biochem. , vol.80 , pp. 341-348
    • Tuderman, L.1    Myllyla, R.2    Kivirikko, K.I.3
  • 25
    • 0017742181 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence
    • Myllyla R., Tuderman L., and Kivirikko K.I. Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence. Eur. J. Biochem. 80 (1977) 349-357
    • (1977) Eur. J. Biochem. , vol.80 , pp. 349-357
    • Myllyla, R.1    Tuderman, L.2    Kivirikko, K.I.3
  • 26
    • 28544446058 scopus 로고    scopus 로고
    • Mitochondrial tumour suppressors: a genetic and biochemical update
    • Gottlieb E., and Tomlinson I.P. Mitochondrial tumour suppressors: a genetic and biochemical update. Nat. Rev. Cancer 5 (2005) 857-866
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 857-866
    • Gottlieb, E.1    Tomlinson, I.P.2
  • 32
    • 24144467846 scopus 로고    scopus 로고
    • ROS: really involved in oxygen sensing
    • Kaelin Jr. W.G. ROS: really involved in oxygen sensing. Cell Metab. 1 (2005) 357-358
    • (2005) Cell Metab. , vol.1 , pp. 357-358
    • Kaelin Jr., W.G.1
  • 33
    • 0036401499 scopus 로고    scopus 로고
    • Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion
    • Sadek H.A., Humphries K.M., Szweda P.A., and Szweda L.I. Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion. Arch. Biochem. Biophys. 406 (2002) 222-228
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 222-228
    • Sadek, H.A.1    Humphries, K.M.2    Szweda, P.A.3    Szweda, L.I.4
  • 34
    • 4344645827 scopus 로고    scopus 로고
    • The redox regulation of intermediary metabolism by a superoxide-aconitase rheostat
    • Armstrong J.S., Whiteman M., Yang H., and Jones D.P. The redox regulation of intermediary metabolism by a superoxide-aconitase rheostat. Bioessays 26 (2004) 894-900
    • (2004) Bioessays , vol.26 , pp. 894-900
    • Armstrong, J.S.1    Whiteman, M.2    Yang, H.3    Jones, D.P.4
  • 35
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal
    • Humphries K.M., and Szweda L.I. Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 37 (1998) 15835-15841
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 36
    • 29644442625 scopus 로고    scopus 로고
    • Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1
    • Lu H., Dalgard C.L., Mohyeldin A., McFate T., Tait A.S., and Verma A. Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J. Biol. Chem. 280 (2005) 41928-41939
    • (2005) J. Biol. Chem. , vol.280 , pp. 41928-41939
    • Lu, H.1    Dalgard, C.L.2    Mohyeldin, A.3    McFate, T.4    Tait, A.S.5    Verma, A.6
  • 37
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia
    • Kim J.W., Tchernyshyov I., Semenza G.L., and Dang C.V. HIF-1-mediated expression of pyruvate dehydrogenase kinase: a metabolic switch required for cellular adaptation to hypoxia. Cell Metab. 3 (2006) 177-185
    • (2006) Cell Metab. , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 38
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou I., Cairns R.A., Fontana L., Lim A.L., and Denko N.C. HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metab. 3 (2006) 187-197
    • (2006) Cell Metab. , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 39
    • 0020824623 scopus 로고
    • Kinetics of the inhibition of succinate dehydrogenase in bull adrenal cortex by malonate and oxaloacetate
    • Mandrik K.A., Vonsovich V.A., and Vinogradov V.V. Kinetics of the inhibition of succinate dehydrogenase in bull adrenal cortex by malonate and oxaloacetate. Ukr. Biokhim. Zh. 55 (1983) 503-506
    • (1983) Ukr. Biokhim. Zh. , vol.55 , pp. 503-506
    • Mandrik, K.A.1    Vonsovich, V.A.2    Vinogradov, V.V.3
  • 40
    • 0015511326 scopus 로고
    • Tightly bound oxalacetate and the activation of succinate dehydrogenase
    • Kearney E.B., Ackrell B.A., and Mayr M. Tightly bound oxalacetate and the activation of succinate dehydrogenase. Biochem. Biophys. Res. Commun. 49 (1972) 1115-1121
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 1115-1121
    • Kearney, E.B.1    Ackrell, B.A.2    Mayr, M.3
  • 41
    • 0016710467 scopus 로고
    • Mechanism of the reductive activation of succinate dehydrogenase
    • Ackrell B.A., Kearney E.B., and Edmondson D. Mechanism of the reductive activation of succinate dehydrogenase. J. Biol. Chem. 250 (1975) 7114-7119
    • (1975) J. Biol. Chem. , vol.250 , pp. 7114-7119
    • Ackrell, B.A.1    Kearney, E.B.2    Edmondson, D.3
  • 42
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium
    • Murry C.E., Jennings R.B., and Reimer K.A. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 74 (1986) 1124-1136
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 43
    • 20644434910 scopus 로고    scopus 로고
    • Mitochondrial K(ATP) channels in cell survival and death
    • Ardehali H., and O'Rourke B. Mitochondrial K(ATP) channels in cell survival and death. J. Mol. Cell. Cardiol. 39 (2005) 7-16
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 7-16
    • Ardehali, H.1    O'Rourke, B.2
  • 44
    • 1542619245 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of signal transduction in ischemic preconditioning
    • Otani H. Reactive oxygen species as mediators of signal transduction in ischemic preconditioning. Antioxid. Redox. Signal. 6 (2004) 449-469
    • (2004) Antioxid. Redox. Signal. , vol.6 , pp. 449-469
    • Otani, H.1
  • 45
    • 31344444853 scopus 로고    scopus 로고
    • de Paula, J. G.; Santos, C. C.; Ferranti, R.; Laurindo, F. R.; Kowaltowski, A. J. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial K(+) channel activity
    • Facundo H.T., and Carreira R.S. de Paula, J. G.; Santos, C. C.; Ferranti, R.; Laurindo, F. R.; Kowaltowski, A. J. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial K(+) channel activity. Free Radic. Biol. Med. 40 (2006) 469-479
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 469-479
    • Facundo, H.T.1    Carreira, R.S.2
  • 47
    • 29244441132 scopus 로고    scopus 로고
    • Blockade of electron transport before cardiac ischemia with the reversible inhibitor amobarbital protects rat heart mitochondria
    • Chen Q., Hoppel C.L., and Lesnefsky E.J. Blockade of electron transport before cardiac ischemia with the reversible inhibitor amobarbital protects rat heart mitochondria. J. Pharmacol. Exp. Ther. 316 (2006) 200-207
    • (2006) J. Pharmacol. Exp. Ther. , vol.316 , pp. 200-207
    • Chen, Q.1    Hoppel, C.L.2    Lesnefsky, E.J.3
  • 48
    • 25444497278 scopus 로고    scopus 로고
    • The concept of synthetic lethality in the context of anticancer therapy
    • Kaelin Jr. W.G. The concept of synthetic lethality in the context of anticancer therapy. Nat. Rev. Cancer 5 (2005) 689-698
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 689-698
    • Kaelin Jr., W.G.1
  • 49
    • 2442683201 scopus 로고    scopus 로고
    • Physiology: orphan detectors of metabolism
    • Hebert S.C. Physiology: orphan detectors of metabolism. Nature 429 (2004) 143-145
    • (2004) Nature , vol.429 , pp. 143-145
    • Hebert, S.C.1
  • 50
    • 18044383110 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in cardiovascular disease
    • Ballinger S.W. Mitochondrial dysfunction in cardiovascular disease. Free Radic. Biol. Med. 38 (2005) 1278-1295
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1278-1295
    • Ballinger, S.W.1
  • 51
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): physiological and pathological implications. Pflugers Arch. 447 (2004) 689-709
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.