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Volumn 1807, Issue 1, 2011, Pages 150-156

VDAC3 has differing mitochondrial functions in two types of striated muscles

Author keywords

ADP; Mitochondrial inner membrane; Mitochondrial outer membrane; VDAC

Indexed keywords

ADENOSINE DIPHOSPHATE; CYTOCHROME C OXIDASE; GLYCOLYTIC ENZYME; LUNG ENZYME; VOLTAGE DEPENDENT ANION CHANNEL 1; VOLTAGE DEPENDENT ANION CHANNEL 3;

EID: 78249279991     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.09.007     Document Type: Article
Times cited : (36)

References (53)
  • 1
    • 0028802746 scopus 로고
    • A hierarchy of ATP-consuming processes in mammalian cells
    • Buttgereit F., Brand M.D. A hierarchy of ATP-consuming processes in mammalian cells. Biochem. J. 1995, 312:163-167.
    • (1995) Biochem. J. , vol.312 , pp. 163-167
    • Buttgereit, F.1    Brand, M.D.2
  • 2
    • 0025007883 scopus 로고
    • Control of respiration and oxidative phosphorylation in isolated rat liver cells
    • Brown G.C., Lakin-Thomas P.L., Brand M.D. Control of respiration and oxidative phosphorylation in isolated rat liver cells. Eur. J. Biochem. 1990, 192:355-362.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 355-362
    • Brown, G.C.1    Lakin-Thomas, P.L.2    Brand, M.D.3
  • 3
    • 0345534388 scopus 로고
    • Role of the mitochondrial outer membrane in dynamic compartmentation of adenine nucleotides
    • Springer Verlag, Berlin Heidelberg, A. Azzi, K.A. Nalecz, M.J. Nalecz, L. Wojtczak (Eds.)
    • Gellerich F.N., Bohnensack R., Kunz W. Role of the mitochondrial outer membrane in dynamic compartmentation of adenine nucleotides. The Anion Carriers of the Mitochondrial Membranes 1989, 349-359. Springer Verlag, Berlin Heidelberg. A. Azzi, K.A. Nalecz, M.J. Nalecz, L. Wojtczak (Eds.).
    • (1989) The Anion Carriers of the Mitochondrial Membranes , pp. 349-359
    • Gellerich, F.N.1    Bohnensack, R.2    Kunz, W.3
  • 4
    • 0025801213 scopus 로고
    • In vivo regulation of mitochondrial respiration in cardiomyocytes: specific restriction for intracellular diffusion for ADP
    • Saks V.A., Belikova Y.O., Kuznetsov A.V. In vivo regulation of mitochondrial respiration in cardiomyocytes: specific restriction for intracellular diffusion for ADP. Biochim. Biophys. Acta 1991, 1074:302-311.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 302-311
    • Saks, V.A.1    Belikova, Y.O.2    Kuznetsov, A.V.3
  • 5
    • 0027324149 scopus 로고
    • Retarded diffusion of ADP in cardiomyocytes: possible role of mitochondrial outer membrane and creatine kinase in cellular regulation of oxidative phosphorylation
    • Saks V.A., Vasil'eva E., Belikova Y.O., Kuznetsov A.V., Lyapina S., Petrova L., Perov N.A. Retarded diffusion of ADP in cardiomyocytes: possible role of mitochondrial outer membrane and creatine kinase in cellular regulation of oxidative phosphorylation. Biochim. Biophys. Acta 1993, 1144:134-148.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 134-148
    • Saks, V.A.1    Vasil'eva, E.2    Belikova, Y.O.3    Kuznetsov, A.V.4    Lyapina, S.5    Petrova, L.6    Perov, N.A.7
  • 9
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function
    • Rostovtseva T., Colombini M. VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys J. 1997, 72:1954-1962.
    • (1997) Biophys J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 10
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: role of cytosolic proteins and mitochondrial lipids
    • Rostovtseva T.K., Bezrukov S.M. VDAC regulation: role of cytosolic proteins and mitochondrial lipids. J. Bioenerg. Biomembr. 2008, 40:163-170.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 12
    • 0027934365 scopus 로고
    • The importance of the outer mitochondrial compartment in regulation of energy metabolism
    • Brdiczka D., Wallimann T. The importance of the outer mitochondrial compartment in regulation of energy metabolism. Mol. Cell. Biochem. 1994, 133/134:69-83.
    • (1994) Mol. Cell. Biochem. , pp. 69-83
    • Brdiczka, D.1    Wallimann, T.2
  • 13
    • 0027965731 scopus 로고
    • The influence of the cytosolic oncotic pressure on the permeability of the mitochondrial outer membrane for ADP: implications for the kinetic properties of mitochondrial creatine kinase and for ADP channeling into the intermembrane space
    • Gellerich F.N., Kapischke M., Kunz W., Neumann W., Kuznetsov A., Brdiczka D., Nicolay K. The influence of the cytosolic oncotic pressure on the permeability of the mitochondrial outer membrane for ADP: implications for the kinetic properties of mitochondrial creatine kinase and for ADP channeling into the intermembrane space. Mol. Cell. Biochem. 1994, 133/134:85-104.
    • (1994) Mol. Cell. Biochem. , pp. 85-104
    • Gellerich, F.N.1    Kapischke, M.2    Kunz, W.3    Neumann, W.4    Kuznetsov, A.5    Brdiczka, D.6    Nicolay, K.7
  • 14
    • 0842323771 scopus 로고    scopus 로고
    • Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice
    • Dzeja P.P., Terzic A., Wieringa B. Phosphotransfer dynamics in skeletal muscle from creatine kinase gene-deleted mice. Mol. Cell. Biochem. 2004, 256/257:13-27.
    • (2004) Mol. Cell. Biochem. , pp. 13-27
    • Dzeja, P.P.1    Terzic, A.2    Wieringa, B.3
  • 15
    • 0032406769 scopus 로고    scopus 로고
    • Some new aspects of creatine kinase (CK): compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology
    • Wallimann T., Dolder M., Schlattner U., Eder M., Hornemann T., O'Gorman E., Ruck A., Brdiczka D. Some new aspects of creatine kinase (CK): compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology. Biofactors 1998, 8:229-234.
    • (1998) Biofactors , vol.8 , pp. 229-234
    • Wallimann, T.1    Dolder, M.2    Schlattner, U.3    Eder, M.4    Hornemann, T.5    O'Gorman, E.6    Ruck, A.7    Brdiczka, D.8
  • 16
    • 0029147509 scopus 로고
    • Muscle creatine kinase-deficient mice. II. Cardiac and skeletal muscles exhibit tissue-specific adaptation of the mitochondrial function
    • Veksler V.I., Kuznetsov A.V., Anflous K., Mateo P., van Deursen J., Wieringa B., Ventura-Clapier R. Muscle creatine kinase-deficient mice. II. Cardiac and skeletal muscles exhibit tissue-specific adaptation of the mitochondrial function. J. Biol. Chem. 1995, 270:19921-19929.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19921-19929
    • Veksler, V.I.1    Kuznetsov, A.V.2    Anflous, K.3    Mateo, P.4    van Deursen, J.5    Wieringa, B.6    Ventura-Clapier, R.7
  • 17
    • 0026585611 scopus 로고
    • Intracellular compartmentalization, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the "phosphocreatine circuit" for cellular energy homeostasis
    • Wallimann T., Wyss M., Brdiczka D., Nicolay K., Eppenberger H.M. Intracellular compartmentalization, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the "phosphocreatine circuit" for cellular energy homeostasis. Biochem. J. 1992, 281:21-40.
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 18
    • 0032581566 scopus 로고    scopus 로고
    • Characterization of rat porin isoforms: cloning of a cardiac type-3 variant encoding an additional methionine at its putative N-terminal region
    • Anflous K., Blondel O., Bernard A., Khrestchatiski M., Ventura-Clapier R. Characterization of rat porin isoforms: cloning of a cardiac type-3 variant encoding an additional methionine at its putative N-terminal region. Biochim. Biophys. Acta. 1998, 1399:47-50.
    • (1998) Biochim. Biophys. Acta. , vol.1399 , pp. 47-50
    • Anflous, K.1    Blondel, O.2    Bernard, A.3    Khrestchatiski, M.4    Ventura-Clapier, R.5
  • 19
    • 0027389308 scopus 로고
    • Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel
    • Blachly-Dyson E., Zambronicz E.B., Yu W.H., Adams V., MacCabe E.R., Adelman J., Colombini M., Forte M. Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel. J. Biol. Chem. 1993, 268:1835-1841.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1835-1841
    • Blachly-Dyson, E.1    Zambronicz, E.B.2    Yu, W.H.3    Adams, V.4    MacCabe, E.R.5    Adelman, J.6    Colombini, M.7    Forte, M.8
  • 21
    • 0027159339 scopus 로고
    • A mitochondrial porin cDNA predicts the existence of multiple human porins
    • Ha H., Hajek P., Bedwell D.M., Burrows P.D. A mitochondrial porin cDNA predicts the existence of multiple human porins. J. Biol. Chem. 1993, 268:12143-12149.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12143-12149
    • Ha, H.1    Hajek, P.2    Bedwell, D.M.3    Burrows, P.D.4
  • 22
    • 0029925099 scopus 로고    scopus 로고
    • Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms
    • Sampson M.J., Lovell R.S., Craigen W.J. Isolation, characterization, and mapping of two mouse mitochondrial voltage-dependent anion channel isoforms. Genomics 1996, 33:283-288.
    • (1996) Genomics , vol.33 , pp. 283-288
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 23
    • 0030586893 scopus 로고    scopus 로고
    • A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8
    • Sampson M.J., Lovell R.S., Davison D.B., Craigen W.J. A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8. Genomics 1996, 36:192-196.
    • (1996) Genomics , vol.36 , pp. 192-196
    • Sampson, M.J.1    Lovell, R.S.2    Davison, D.B.3    Craigen, W.J.4
  • 24
    • 0032514888 scopus 로고    scopus 로고
    • A novel isoform of the mitochondrial outer membrane protein VDAC3 via alternative splicing of a 3-base exon
    • Sampson M.J., Ross L., Decker W.K., Craigen W.J. A novel isoform of the mitochondrial outer membrane protein VDAC3 via alternative splicing of a 3-base exon. J. Biol. Chem. 1998, 273:30482-30486.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30482-30486
    • Sampson, M.J.1    Ross, L.2    Decker, W.K.3    Craigen, W.J.4
  • 25
    • 0032886205 scopus 로고    scopus 로고
    • Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis
    • Decker W.K., Boules K.R., Schatte E.C., Towbin J.A., Craigen W.J. Revised fine mapping of the human voltage-dependent anion channel loci by radiation hybrid analysis. Mamm. Genome 1999, 10:1041-1042.
    • (1999) Mamm. Genome , vol.10 , pp. 1041-1042
    • Decker, W.K.1    Boules, K.R.2    Schatte, E.C.3    Towbin, J.A.4    Craigen, W.J.5
  • 26
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltage-dependent anion channel gene family, conserved structure and function
    • Sampson M.J., Lovell R.S., Craigen W.J. The murine voltage-dependent anion channel gene family, conserved structure and function. J. Biol. Chem. 1997, 272:18966-18973.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18966-18973
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 27
    • 0035910495 scopus 로고    scopus 로고
    • Altered mitochondrial sensitivity for ADP and maintenance of creatine stimulated respiration in oxidative striated muscles from VDAC1 deficient mice
    • Anflous K., Armstrong D., Craigen W.J. Altered mitochondrial sensitivity for ADP and maintenance of creatine stimulated respiration in oxidative striated muscles from VDAC1 deficient mice. J. Biol. Chem. 2001, 276:1954-1960.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1954-1960
    • Anflous, K.1    Armstrong, D.2    Craigen, W.J.3
  • 30
    • 52449097233 scopus 로고    scopus 로고
    • Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions
    • Craigen W.J., Graham B.H. Genetic strategies for dissecting mammalian and Drosophila voltage-dependent anion channel functions. J. Bioenerg. Biomembr. 2008, 40:207-212.
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 207-212
    • Craigen, W.J.1    Graham, B.H.2
  • 31
    • 0023255871 scopus 로고
    • Mitochondrial respiratory parameters in cardiac tissue: a novel method of assessment by using saponin-skinned fibers
    • Veksler V.I., Kuznetsov A.V., Sharov V.G., Kapelko V.I., Saks V.A. Mitochondrial respiratory parameters in cardiac tissue: a novel method of assessment by using saponin-skinned fibers. Biochim. Biophys. Acta 1987, 892:191-196.
    • (1987) Biochim. Biophys. Acta , vol.892 , pp. 191-196
    • Veksler, V.I.1    Kuznetsov, A.V.2    Sharov, V.G.3    Kapelko, V.I.4    Saks, V.A.5
  • 32
    • 0034049927 scopus 로고    scopus 로고
    • The tissue-specific, alternatively spliced single ATG exon of the type 3 voltage-dependent anion channel gene does not create a truncated protein isoform in vivo
    • Decker W.K., Craigen W.J. The tissue-specific, alternatively spliced single ATG exon of the type 3 voltage-dependent anion channel gene does not create a truncated protein isoform in vivo. Mol. Genet. Metab. 2000, 70:69-74.
    • (2000) Mol. Genet. Metab. , vol.70 , pp. 69-74
    • Decker, W.K.1    Craigen, W.J.2
  • 33
    • 33847135285 scopus 로고    scopus 로고
    • VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles
    • Anflous-Pharayra K., Cai Z.J., Craigen W.J. VDAC1 serves as a mitochondrial binding site for hexokinase in oxidative muscles. Biochim. Biophys. Acta 2007, 1767:136-142.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 136-142
    • Anflous-Pharayra, K.1    Cai, Z.J.2    Craigen, W.J.3
  • 34
    • 0036321382 scopus 로고    scopus 로고
    • Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients
    • Wiedemann F.R., Manfredi G., Mawrin C., Flint Beal M., Schon E.A. Mitochondrial DNA and respiratory chain function in spinal cords of ALS patients. J. Neurochem. 2002, 80:616-625.
    • (2002) J. Neurochem. , vol.80 , pp. 616-625
    • Wiedemann, F.R.1    Manfredi, G.2    Mawrin, C.3    Flint Beal, M.4    Schon, E.A.5
  • 35
    • 0014059118 scopus 로고
    • An electron-transport system associated with the outer membrane of liver mitochondria, A biochemical and morphological study
    • Sottocasa G.L., Kuylenstierna B., Ernster L., Bergstrand A. An electron-transport system associated with the outer membrane of liver mitochondria, A biochemical and morphological study. J. Cell Biol. 1967, 32:415-438.
    • (1967) J. Cell Biol. , vol.32 , pp. 415-438
    • Sottocasa, G.L.1    Kuylenstierna, B.2    Ernster, L.3    Bergstrand, A.4
  • 38
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: gene regulation and functional significance
    • (Review)
    • Schiaffino S., Reggiani C. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 1996, 76:371-423. (Review).
    • (1996) Physiol. Rev. , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 43
    • 0030050144 scopus 로고    scopus 로고
    • Identification of porin as a binding site for MAP2
    • Linden M., Karlsson G. Identification of porin as a binding site for MAP2. Biochem. Biophys. Res. Commun. 1996, 218:833-836.
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 833-836
    • Linden, M.1    Karlsson, G.2
  • 46
    • 0031944106 scopus 로고    scopus 로고
    • Ultrastructural alterations in encephalomyopathies of mitochondrial origin
    • Bonilla E., Tanji K. Ultrastructural alterations in encephalomyopathies of mitochondrial origin. Biofactors 1998, 7:231-236.
    • (1998) Biofactors , vol.7 , pp. 231-236
    • Bonilla, E.1    Tanji, K.2
  • 47
    • 9644276918 scopus 로고    scopus 로고
    • Respiratory chain defects: what do we know for sure about their consequences in vivo?
    • Briere J.J., Chretien D., Benit P., Rustin P. Respiratory chain defects: what do we know for sure about their consequences in vivo?. Biochim. Biophys. Acta 2004, 1659:172-177.
    • (2004) Biochim. Biophys. Acta , vol.1659 , pp. 172-177
    • Briere, J.J.1    Chretien, D.2    Benit, P.3    Rustin, P.4
  • 48
    • 0034728096 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain disorders II: neurodegenerative disorders and nuclear gene defects
    • Leonard J.V., Schapira A.H.V. Mitochondrial respiratory chain disorders II: neurodegenerative disorders and nuclear gene defects. Lancet 2000, 355:389-394.
    • (2000) Lancet , vol.355 , pp. 389-394
    • Leonard, J.V.1    Schapira, A.H.V.2
  • 49
    • 78249235652 scopus 로고    scopus 로고
    • Mitochondrial Encephalomyopathies regulation and functional significance
    • (Review)
    • Oldfors A., Tulinius M. Mitochondrial Encephalomyopathies regulation and functional significance. J. Neurop. Exp. Neurol. Physiol. Rev. 2003, 76:371-423. (Review).
    • (2003) J. Neurop. Exp. Neurol. Physiol. Rev. , vol.76 , pp. 371-423
    • Oldfors, A.1    Tulinius, M.2
  • 50
    • 2942562564 scopus 로고    scopus 로고
    • Mitochondrial disorders: prevalence, myths and advances
    • Thorburn D.R. Mitochondrial disorders: prevalence, myths and advances. J. Inherit. Metab. Dis. 2004, 27:349-362.
    • (2004) J. Inherit. Metab. Dis. , vol.27 , pp. 349-362
    • Thorburn, D.R.1
  • 51
    • 0036361291 scopus 로고    scopus 로고
    • Animal models for mitochondrial diseases
    • Wallace D.C. Animal models for mitochondrial diseases. Meth. Mol. Biol. 2002, 197:3-54.
    • (2002) Meth. Mol. Biol. , vol.197 , pp. 3-54
    • Wallace, D.C.1


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