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Volumn 290, Issue 10, 2015, Pages 6338-6348

The inhibitor protein (IF1) of the F1F0-ATPase modulates human osteosarcoma cell bioenergetics

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYST ACTIVITY; CELL MEMBRANES; CLONE CELLS; CYTOLOGY; DISEASES; ENZYME ACTIVITY; METABOLISM; MITOCHONDRIA; PROTEINS;

EID: 84924943426     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.631788     Document Type: Article
Times cited : (37)

References (49)
  • 1
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of cancer: The next generation
    • Hanahan, D., and Weinberg, R. A. (2011) Hallmarks of cancer: the next generation. Cell 144, 646-674
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 60249085118 scopus 로고    scopus 로고
    • Mitochondria in cancer: Not just innocent bystanders
    • Frezza, C., and Gottlieb, E. (2009) Mitochondria in cancer: not just innocent bystanders. Semin. Cancer Biol. 19, 4-11
    • (2009) Semin. Cancer Biol. , vol.19 , pp. 4-11
    • Frezza, C.1    Gottlieb, E.2
  • 5
    • 0033251088 scopus 로고    scopus 로고
    • Nucleotide sequence of cDNA coding the mitochondrial precursor protein of the ATPase inhibitor from humans
    • Ichikawa, N., Ushida, S., Kawabata, M., and Masazumi, Y. (1999) Nucleotide sequence of cDNA coding the mitochondrial precursor protein of the ATPase inhibitor from humans. Biosci. Biotechnol. Biochem. 63, 2225-2227
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2225-2227
    • Ichikawa, N.1    Ushida, S.2    Kawabata, M.3    Masazumi, Y.4
  • 6
    • 0026325774 scopus 로고
    • Control of mitochondrial ATP synthesis in the heart
    • Harris, D. A., and Das, A. M. (1991) Control of mitochondrial ATP synthesis in the heart. Biochem. J. 280, 561-573
    • (1991) Biochem. J. , vol.280 , pp. 561-573
    • Harris, D.A.1    Das, A.M.2
  • 7
    • 0026319258 scopus 로고
    • Regulation of the mitochondrial ATPase in situ in cardiac muscle: Role of the inhibitor subunit
    • Rouslin, W. (1991) Regulation of the mitochondrial ATPase in situ in cardiac muscle: role of the inhibitor subunit. J. Bioenerg. Biomembr. 23, 873-888
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 873-888
    • Rouslin, W.1
  • 8
    • 0031659950 scopus 로고    scopus 로고
    • Mitochondrial function as a determinant of recovery or death in cell response to injury
    • Di Lisa, F., and Bernardi, P. (1998) Mitochondrial function as a determinant of recovery or death in cell response to injury. Mol. Cell. Biochem. 184, 379-391
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 379-391
    • Di Lisa, F.1    Bernardi, P.2
  • 9
    • 25144478337 scopus 로고    scopus 로고
    • Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion
    • Solaini, G., and Harris, D. A. (2005) Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion. Biochem. J. 390, 377-394
    • (2005) Biochem. J. , vol.390 , pp. 377-394
    • Solaini, G.1    Harris, D.A.2
  • 11
    • 0026341287 scopus 로고
    • Effect of inhibition of the mitochondrial ATPase on net myocardial ATP in total ischemia
    • Jennings, R. B., Reimer, K. A., and Steenbergen, C. (1991) Effect of inhibition of the mitochondrial ATPase on net myocardial ATP in total ischemia. J. Mol. Cell. Cardiol. 23, 1383-1395
    • (1991) J. Mol. Cell. Cardiol. , vol.23 , pp. 1383-1395
    • Jennings, R.B.1    Reimer, K.A.2    Steenbergen, C.3
  • 15
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss, M., Hofhaus, G., Schröder, R. R., and Kühlbrandt, W. (2008) Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 27, 1154-1160
    • (2008) EMBO J. , vol.27 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schröder, R.R.3    Kühlbrandt, W.4
  • 16
    • 0021752396 scopus 로고
    • Increased content of natural ATPase inhibitor in tumor mitochondria
    • Luciaková, K., and Kuzela, S. (1984) Increased content of natural ATPase inhibitor in tumor mitochondria. FEBS Lett. 177, 85-88
    • (1984) FEBS Lett. , vol.177 , pp. 85-88
    • Luciaková, K.1    Kuzela, S.2
  • 17
    • 0030669983 scopus 로고    scopus 로고
    • Oxidative phosphorylation enzymes in normal and neoplastic cell growth
    • Capuano, F., Guerrieri, F., and Papa, S. (1997) Oxidative phosphorylation enzymes in normal and neoplastic cell growth. J. Bioenerg. Biomembr. 29, 379-384
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 379-384
    • Capuano, F.1    Guerrieri, F.2    Papa, S.3
  • 20
    • 0018404130 scopus 로고
    • Stabilization of mitochondrial functions with digitonin
    • Kun, E., Kirsten, E., and Piper, W. N. (1979) Stabilization of mitochondrial functions with digitonin. Methods Enzymol. 55, 115-118
    • (1979) Methods Enzymol. , vol.55 , pp. 115-118
    • Kun, E.1    Kirsten, E.2    Piper, W.N.3
  • 21
    • 73249137166 scopus 로고    scopus 로고
    • Mitochondrial Complex I decrease is responsible for bioenergetic dysfunction in K-ras transformed cells
    • Baracca, A., Chiaradonna, F., Sgarbi, G., Solaini, G., Alberghina, L., and Lenaz, G. (2010) Mitochondrial Complex I decrease is responsible for bioenergetic dysfunction in K-ras transformed cells. Biochim. Biophys. Acta 1797, 314-323
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 314-323
    • Baracca, A.1    Chiaradonna, F.2    Sgarbi, G.3    Solaini, G.4    Alberghina, L.5    Lenaz, G.6
  • 23
  • 24
    • 0030853263 scopus 로고    scopus 로고
    • Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels
    • Zerbetto, E., Vergani, L., and Dabbeni-Sala, F. (1997) Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis 18, 2059-2064
    • (1997) Electrophoresis , vol.18 , pp. 2059-2064
    • Zerbetto, E.1    Vergani, L.2    Dabbeni-Sala, F.3
  • 26
    • 84877050463 scopus 로고    scopus 로고
    • Glucose plays a main role in human fibroblasts adaptation to hypoxia
    • Baracca, A., Sgarbi, G., Padula, A., and Solaini, G. (2013) Glucose plays a main role in human fibroblasts adaptation to hypoxia. Int. J. Biochem. Cell Biol. 45, 1356-1365
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 1356-1365
    • Baracca, A.1    Sgarbi, G.2    Padula, A.3    Solaini, G.4
  • 32
    • 84861562196 scopus 로고    scopus 로고
    • 1, to ATP homeostasis, cell growth, mitochondrial morphology, and cell viability
    • 1, to ATP homeostasis, cell growth, mitochondrial morphology, and cell viability. J. Biol. Chem. 287, 18781-18787
    • (2012) J. Biol. Chem. , vol.287 , pp. 18781-18787
    • Fujikawa, M.1    Imamura, H.2    Nakamura, J.3    Yoshida, M.4
  • 34
    • 0023836981 scopus 로고
    • The binding and release of the inhibitor protein are governed independently by ATP and membrane potential in ox-heart submitochondrial vesicles
    • Lippe, G., Sorgato, M. C., and Harris, D. A. (1988) The binding and release of the inhibitor protein are governed independently by ATP and membrane potential in ox-heart submitochondrial vesicles. Biochim. Biophys. Acta 933, 1-11
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 1-11
    • Lippe, G.1    Sorgato, M.C.2    Harris, D.A.3
  • 36
    • 0014961651 scopus 로고
    • Partial resolution of the enzyme catalyzing oxidative phosphorylation: XXII. Interaction between mitochondrial adenosine triphosphatase inhibitor and mitochondrial adenosine triphosphatase
    • Horstman, L. L., and Racker, E. (1970) Partial resolution of the enzyme catalyzing oxidative phosphorylation: XXII. interaction between mitochondrial adenosine triphosphatase inhibitor and mitochondrial adenosine triphosphatase. J. Biol. Chem. 245, 1336-1344
    • (1970) J. Biol. Chem. , vol.245 , pp. 1336-1344
    • Horstman, L.L.1    Racker, E.2
  • 37
    • 0022430817 scopus 로고
    • 1-ATPase and its naturally occurring inhibitor protein. Studies using a specific anti-inhibitor antibody
    • 1-ATPase and its naturally occurring inhibitor protein. Studies using a specific anti-inhibitor antibody. Biochim. Biophys. Acta 806, 64-74
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 64-74
    • Husain, I.1    Jackson, P.J.2    Harris, D.A.3
  • 38
    • 0026529759 scopus 로고
    • Purification and characterization of adenosine triphosphatase from eel liver mitochondria
    • Baracca, A., Degli Esposti, M., Parenti Castelli, G., and Solaini, G. (1992) Purification and characterization of adenosine triphosphatase from eel liver mitochondria. Comp. Biochem. Physiol. 101B, 421-426
    • (1992) Comp. Biochem. Physiol. , vol.101 B , pp. 421-426
    • Baracca, A.1    Degli Esposti, M.2    Parenti Castelli, G.3    Solaini, G.4
  • 39
    • 84896691807 scopus 로고    scopus 로고
    • Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation
    • Chaban, Y., Boekema, E. J., Dudkina, N. V. (2014) Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation. Biochim. Biophys. Acta 1837, 418-426
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 418-426
    • Chaban, Y.1    Boekema, E.J.2    Dudkina, N.V.3
  • 42
    • 0019889799 scopus 로고
    • Proton-adenosinetriphosphatase complex of rat liver mitochondria: Effect of energy state on its interaction with the adenosinetriphosphatase inhibitory peptide
    • Schwerzmann, K., and Pedersen, P. L. (1981) Proton-adenosinetriphosphatase complex of rat liver mitochondria: effect of energy state on its interaction with the adenosinetriphosphatase inhibitory peptide. Biochemistry 20, 6305-6311
    • (1981) Biochemistry , vol.20 , pp. 6305-6311
    • Schwerzmann, K.1    Pedersen, P.L.2
  • 44
    • 46349087708 scopus 로고    scopus 로고
    • The study of the pathogenic mechanism of mitochondrial diseases provides information on basic bioenergetics
    • Solaini, G., Harris, D. A., Lenaz, G., Sgarbi, G., and Baracca, A. (2008) The study of the pathogenic mechanism of mitochondrial diseases provides information on basic bioenergetics. Biochim. Biophys. Acta 1777, 941-945
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 941-945
    • Solaini, G.1    Harris, D.A.2    Lenaz, G.3    Sgarbi, G.4    Baracca, A.5
  • 45
    • 59049097778 scopus 로고    scopus 로고
    • Respiratory complex I dysfunction due to mitochondrial DNA mutations shifts the voltage threshold for opening of the permeability transition pore toward resting levels
    • Porcelli, A. M., Angelin, A., Ghelli, A., Mariani, E., Martinuzzi, A., Carelli, V., Petronilli, V., Bernardi, P., and Rugolo, M. (2009) Respiratory complex I dysfunction due to mitochondrial DNA mutations shifts the voltage threshold for opening of the permeability transition pore toward resting levels. J. Biol. Chem. 284, 2045-2052
    • (2009) J. Biol. Chem. , vol.284 , pp. 2045-2052
    • Porcelli, A.M.1    Angelin, A.2    Ghelli, A.3    Mariani, E.4    Martinuzzi, A.5    Carelli, V.6    Petronilli, V.7    Bernardi, P.8    Rugolo, M.9
  • 46
    • 84873120174 scopus 로고    scopus 로고
    • The ATP synthase: The understood, the uncertain and the unknown
    • Walker, J. E. (2013) The ATP synthase: the understood, the uncertain and the unknown. Biochem. Soc. Trans. 41, 1-16
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1-16
    • Walker, J.E.1
  • 49
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase: A splendid molecular machine
    • Boyer, P. D. (1997) The ATP synthase: a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.