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Volumn 300, Issue 3, 2011, Pages

Calcium-induced permeability transition in rat brain mitochondria is promoted by carbenoxolone through targeting connexin43

Author keywords

Liver mitochondria; Neuroprotection; Permeability transition pore

Indexed keywords

AMINO ACID; CALCIUM; CARBENOXOLONE; CONNEXIN 43; CYCLOSPORIN A; GAP JUNCTION PROTEIN; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; SERINE;

EID: 79952150276     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00061.2010     Document Type: Article
Times cited : (46)

References (44)
  • 4
    • 23844462432 scopus 로고    scopus 로고
    • 2+
    • DOI 10.1111/j.1471-4159.2005.03260.x
    • Azarashvili T, Krestinina O, Yurkov I, Evtodienko Y, Reiser G. High-affinity peripheral benzodiazepine receptor ligand, PK11195, regulates protein phosphorylation in rat brain mitochondria under control of Ca2+. J Neurochem 94: 1054-1062, 2005. (Pubitemid 41170592)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.4 , pp. 1054-1062
    • Azarashvili, T.1    Krestinina, O.2    Yurkov, I.3    Evtodienko, Y.4    Reiser, G.5
  • 5
    • 77956631199 scopus 로고    scopus 로고
    • The mitochondria permeability transition pore complex in the brain with interacting proteins - Promising targets for protection in neurodegenerative diseases
    • Azarashvili T, Stricker R, Reiser G. The mitochondria permeability transition pore complex in the brain with interacting proteins - promising targets for protection in neurodegenerative diseases. Biol Chem 391: 619-629.
    • Biol Chem , vol.391 , pp. 619-629
    • Azarashvili, T.1    Stricker, R.2    Reiser, G.3
  • 7
    • 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: 1127-1155, 1999. (Pubitemid 29473313)
    • (1999) Physiological Reviews , vol.79 , Issue.4 , pp. 1127-1155
    • Bernardi, P.1
  • 8
    • 0024592298 scopus 로고
    • Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues
    • DOI 10.1083/jcb.108.2.595
    • Beyer EC, Kistler J, Paul DL, Goodenough DA. Antisera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues. J Cell Biol 108: 595-605, 1989. (Pubitemid 19065855)
    • (1989) Journal of Cell Biology , vol.108 , Issue.2 , pp. 595-605
    • Beyer, E.C.1    Kistler, J.2    Paul, D.L.3    Goodenough, D.A.4
  • 10
    • 33745813297 scopus 로고    scopus 로고
    • Connexin 43 signalling and cardioprotection
    • DOI 10.1136/hrt.2005.066878
    • Boengler K, Schulz R, Heusch G. Connexin 43 signalling and cardioprotection. Heart 92: 1724-1727, 2006. (Pubitemid 44851310)
    • (2006) Heart , vol.92 , Issue.12 , pp. 1724-1727
    • Boengler, K.1    Schulz, R.2    Heusch, G.3
  • 12
    • 33846569548 scopus 로고    scopus 로고
    • 18beta-glycyrrhetinic acid promotes src interaction with connexin43 in rat cardiomyocytes
    • Chung TH, Wang SM, Chang YC, Chen YL, Wu JC. 18beta-glycyrrhetinic acid promotes src interaction with connexin43 in rat cardiomyocytes. J Cell Biochem 100: 653-664, 2007.
    • (2007) J Cell Biochem , vol.100 , pp. 653-664
    • Chung, T.H.1    Wang, S.M.2    Chang, Y.C.3    Chen, Y.L.4    Wu, J.C.5
  • 13
    • 0037281030 scopus 로고    scopus 로고
    • The carboxy-tail of connexin-43 localizes to the nucleus and inhibits cell growth
    • DOI 10.1023/A:1021152709313
    • Dang X, Doble BW, Kardami E. The carboxy-tail of connexin-43 localizes to the nucleus and inhibits cell growth. Mol Cell Biochem 242: 35-38, 2003. (Pubitemid 36240526)
    • (2003) Molecular and Cellular Biochemistry , vol.242 , Issue.1-2 , pp. 35-38
    • Dang, X.1    Doble, B.W.2    Kardami, E.3
  • 14
    • 21744457240 scopus 로고    scopus 로고
    • New, emerging roles for cardiac connexins. Mitochondrial Cx43 raises new questions
    • DOI 10.1016/j.cardiores.2005.05.026, PII S0008636305002804
    • Dhein S. New, emerging roles for cardiac connexins. Mitochondrial Cx43 raises new questions. Cardiovasc Res 67: 179-181, 2005. (Pubitemid 40943608)
    • (2005) Cardiovascular Research , vol.67 , Issue.2 , pp. 179-181
    • Dhein, S.1
  • 15
    • 0038142399 scopus 로고    scopus 로고
    • New roles for connexons
    • Ebihara L. New roles for connexons. News Physiol Sci 18: 100-103, 2003. (Pubitemid 36782798)
    • (2003) News in Physiological Sciences , vol.18 , Issue.JUNE , pp. 100-103
    • Ebihara, L.1
  • 17
    • 77951108497 scopus 로고    scopus 로고
    • Tissue-specific cross-reactivity of connexin32 antibodies: Problems and solutions unique to the central nervous system
    • Fowler SL, McLean AC, Bennett SA. Tissue-specific cross-reactivity of connexin32 antibodies: problems and solutions unique to the central nervous system. Cell Commun Adhes 16: 117-130, 2009.
    • (2009) Cell Commun Adhes , vol.16 , pp. 117-130
    • Fowler, S.L.1    McLean, A.C.2    Bennett, S.A.3
  • 20
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • Halestrap AP, McStay GP, Clarke SJ. The permeability transition pore complex: another view. Biochimie 84: 153-166, 2002.
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 21
    • 20044369560 scopus 로고    scopus 로고
    • Connexin-made channels as pharmacological targets
    • Herve JC, Sarrouilhe D. Connexin-made channels as pharmacological targets. Curr Pharm Des 11: 1941-1958, 2005.
    • (2005) Curr Pharm des , vol.11 , pp. 1941-1958
    • Herve, J.C.1    Sarrouilhe, D.2
  • 22
    • 0025959178 scopus 로고
    • Tissue-Specific Distribution of Differentially Phosphorylated Forms of Cx43
    • Kadle R, Zhang JT, Nicholson BJ. Tissue-specific distribution of differentially phosphorylated forms of Cx43. Mol Cell Biol 11: 363-369, 1991. (Pubitemid 21895214)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.1 , pp. 363-369
    • Kadle, R.1    Zhang, J.T.2    Nicholson, B.J.3
  • 23
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • DOI 10.1038/nature02229
    • Kokoszka JE, Waymire KG, Levy SE, Sligh JE, Cai J, Jones DP, MacGregor GR, Wallace DC. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 427: 461-465, 2004. (Pubitemid 38168501)
    • (2004) Nature , vol.427 , Issue.6973 , pp. 461-465
    • Kokoszka, J.E.1    Waymire, K.G.2    Levy, S.E.3    Sligh, J.E.4    Cai, J.5    Jones, D.P.6    MacGregor, G.R.7    Wallace, D.C.8
  • 24
    • 77957798880 scopus 로고    scopus 로고
    • Temporary sequestration of potassium by mitochondria in astrocytes
    • Kozoriz MG, Church J, Ozog MA, Naus CC, Krebs C. Temporary sequestration of potassium by mitochondria in astrocytes. J Biol Chem 285: 31107-31119.
    • J Biol Chem , vol.285 , pp. 31107-31119
    • Kozoriz, M.G.1    Church, J.2    Ozog, M.A.3    Naus, C.C.4    Krebs, C.5
  • 25
    • 0018338308 scopus 로고
    • Preparation of synaptic and nonsynaptic mitochondria from mammalian brain
    • Lai JC, Clark JB. Preparation of synaptic and nonsynaptic mitochondria from mammalian brain. Methods Enzymol 55: 51-60, 1979.
    • (1979) Methods Enzymol , vol.55 , pp. 51-60
    • Lai, J.C.1    Clark, J.B.2
  • 26
    • 0034717680 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication
    • DOI 10.1083/jcb.149.7.1503
    • Lampe PD, TenBroek EM, Burt JM, Kurata WE, Johnson RG, Lau AF. Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication. J Cell Biol 149: 1503-1512, 2000. (Pubitemid 30437622)
    • (2000) Journal of Cell Biology , vol.149 , Issue.7 , pp. 1503-1512
    • Lampe, P.D.1    TenBroek, E.M.2    Burt, J.M.3    Kurata, W.E.4    Johnson, R.G.5    Lau, A.F.6
  • 27
    • 46349097952 scopus 로고    scopus 로고
    • Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore
    • Leung AW, Halestrap AP. Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore. Biochim Biophys Acta 1777: 946-952, 2008.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 946-952
    • Leung, A.W.1    Halestrap, A.P.2
  • 29
    • 67649772111 scopus 로고    scopus 로고
    • The role of mitochondrial transition pore, and its modulation, in traumatic brain injury and delayed neurodegeneration after TBI
    • Mazzeo AT, Beat A, Singh A, Bullock MR. The role of mitochondrial transition pore, and its modulation, in traumatic brain injury and delayed neurodegeneration after TBI. Exp Neurol 218: 363-370, 2009.
    • (2009) Exp Neurol , vol.218 , pp. 363-370
    • Mazzeo, A.T.1    Beat, A.2    Singh, A.3    Bullock, M.R.4
  • 31
    • 0344876141 scopus 로고    scopus 로고
    • Coupling of Astrocyte Connexins Cx26, Cx30, Cx43 to Oligodendrocyte Cx29, Cx32, Cx47: Implications from Normal and Connexin32 Knockout Mice
    • DOI 10.1002/glia.10278
    • Nagy JI, Ionescu AV, Lynn BD, Rash JE. Coupling of astrocyte connexins Cx26, Cx30, Cx43 to oligodendrocyte Cx29, Cx32, Cx47: implications from normal and connexin32 knockout mice. Glia 44: 205-218, 2003. (Pubitemid 37484472)
    • (2003) GLIA , vol.44 , Issue.3 , pp. 205-218
    • Nagy, J.I.1    Ionescu, A.-V.2    Lynn, B.D.3    Rash, J.E.4
  • 32
    • 33746207800 scopus 로고    scopus 로고
    • Translocation of connexin 43 to the inner mitochondrial membrane of cardiomyocytes through the heat shock protein 90-dependent TOM pathway and its importance for cardioprotection
    • DOI 10.1161/01.RES.0000230315.56904.de, PII 0000301220060707000015
    • Rodriguez-Sinovas A, Boengler K, Cabestrero A, Gres P, Morente M, Ruiz-Meana M, Konietzka I, Miro E, Totzeck A, Heusch G, Schulz R, Garcia-Dorado D. Translocation of connexin 43 to the inner mitochondrial membrane of cardiomyocytes through the heat shock protein 90-dependent TOM pathway and its importance for cardioprotection. Circ Res 99: 93-101, 2006. (Pubitemid 44297060)
    • (2006) Circulation Research , vol.99 , Issue.1 , pp. 93-101
    • Rodriguez-Sinovas, A.1    Boengler, K.2    Cabestrero, A.3    Gres, P.4    Morente, M.5    Ruiz-Meana, M.6    Konietzka, I.7    Miro, E.8    Totzeck, A.9    Heusch, G.10    Schulz, R.11    Garcia-Dorado, D.12
  • 35
    • 33746483243 scopus 로고    scopus 로고
    • Carbenoxolone inhibits junctional transfer and upregulates Connexin43 expression by a protein kinase A-dependent pathway
    • DOI 10.1002/jcb.20870
    • Sagar GD, Larson DM. Carbenoxolone inhibits junctional transfer and upregulates connexin43 expression by a protein kinase A-dependent pathway. J Cell Biochem 98: 1543-1551, 2006. (Pubitemid 44141858)
    • (2006) Journal of Cellular Biochemistry , vol.98 , Issue.6 , pp. 1543-1551
    • Sagar, G.D.V.1    Larson, D.M.2
  • 36
    • 0344585889 scopus 로고    scopus 로고
    • Glycyrrhetinic acid-induced permeability transition in rat liver mitochondria
    • DOI 10.1016/j.bcp.2003.08.023
    • Salvi M, Fiore C, Armanini D, Toninello A. Glycyrrhetinic acid-induced permeability transition in rat liver mitochondria. Biochem Pharmacol 66: 2375-2379, 2003. (Pubitemid 37456745)
    • (2003) Biochemical Pharmacology , vol.66 , Issue.12 , pp. 2375-2379
    • Salvi, M.1    Fiore, C.2    Armanini, D.3    Toninello, A.4
  • 37
    • 17744384311 scopus 로고    scopus 로고
    • Carbenoxolone induces oxidative stress in liver mitochondria, which is responsible for transition pore opening
    • DOI 10.1210/en.2004-1128
    • Salvi M, Fiore C, Battaglia V, Palermo M, Armanini D, Toninello A. Carbenoxolone induces oxidative stress in liver mitochondria, which is responsible for transition pore opening. Endocrinology 146: 2306-2312, 2005. (Pubitemid 40577518)
    • (2005) Endocrinology , vol.146 , Issue.5 , pp. 2306-2312
    • Salvi, M.1    Fiore, C.2    Battaglia, V.3    Palermo, M.4    Armanini, D.5    Toninello, A.6
  • 38
    • 33744494607 scopus 로고    scopus 로고
    • Connexin43 and ischemic preconditioning
    • DOI 10.1159/000092571, Cardiac Gap Junctions
    • Schulz R, Heusch G. Connexin43 and ischemic preconditioning. Adv Cardiol 42: 213-227, 2006. (Pubitemid 43805866)
    • (2006) Advances in Cardiology , vol.42 , pp. 213-227
    • Schulz, R.1    Heusch, G.2
  • 39
    • 0036716820 scopus 로고    scopus 로고
    • The connexin43 gap junction protein is phosphorylated by protein kinase A and protein kinase C: In vivo and in vitro studies
    • DOI 10.1023/A:1019902920693
    • Shah MM, Martinez AM, Fletcher WH. The connexin43 gap junction protein is phosphorylated by protein kinase A and protein kinase C: in vivo and in vitro studies. Mol Cell Biochem 238: 57-68, 2002. (Pubitemid 35023529)
    • (2002) Molecular and Cellular Biochemistry , vol.238 , Issue.1-2 , pp. 57-68
    • Shah, M.M.1    Martinez, A.-M.2    Fletcher, W.H.3
  • 40
    • 0025471534 scopus 로고
    • Rapid isolation of metabolically active mitochondria from rat brain and subregions using percoll density gradient centrifugation
    • Sims NR. Rapid isolation of metabolically active mitochondria from rat brain and subregions using Percoll density gradient centrifugation. J Neurochem 55: 698-707, 1990. (Pubitemid 120021648)
    • (1990) Journal of Neurochemistry , vol.55 , Issue.2 , pp. 698-707
    • Sims, N.R.1
  • 41
    • 64249170988 scopus 로고    scopus 로고
    • Connexin43 phosphorylation: Structural changes and biological effects
    • Solan JL, Lampe PD. Connexin43 phosphorylation: structural changes and biological effects. Biochem J 419: 261-272, 2009.
    • (2009) Biochem J , vol.419 , pp. 261-272
    • Solan, J.L.1    Lampe, P.D.2
  • 42
    • 20444411484 scopus 로고    scopus 로고
    • Connexin phosphorylation as a regulatory event linked to gap junction channel assembly
    • DOI 10.1016/j.bbamem.2004.09.013, PII S0005273604002445
    • Solan JL, Lampe PD. Connexin phosphorylation as a regulatory event linked to gap junction channel assembly. Biochim Biophys Acta 1711: 154-163, 2005. (Pubitemid 40799290)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1711 , Issue.2 SPEC. ISS , pp. 154-163
    • Solan, J.L.1    Lampe, P.D.2
  • 43
    • 0024787405 scopus 로고
    • Sequence and tissue distribution of a second protein of hepatic gap junctions, Cx26, as deduced from its cDNA
    • DOI 10.1083/jcb.109.6.3391
    • Zhang JT, Nicholson BJ. Sequence and tissue distribution of a second protein of hepatic gap junctions, Cx26, as deduced from its cDNA. J Cell Biol 109: 3391-3401, 1989. (Pubitemid 20017988)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 II , pp. 3391-3401
    • Zhang, J.-T.1    Nicholson, B.J.2
  • 44
    • 11144300815 scopus 로고    scopus 로고
    • Mitochondrial permeability transitions: How many doors to the house?
    • DOI 10.1016/j.bbabio.2004.10.006, PII S0005272804003007
    • Zoratti M, Szabo I, De Marchi U. Mitochondrial permeability transitions: how many doors to the house? Biochim Biophys Acta 1706: 40-52, 2005. (Pubitemid 40037759)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.1-2 , pp. 40-52
    • Zoratti, M.1    Szabo, I.2    De, M.U.3


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