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Volumn 1802, Issue 5, 2010, Pages 443-453

Mitochondrial bioenergetics and dynamics interplay in complex I-deficient fibroblasts

Author keywords

Bioenergetics; Mitochondrial disease; Mitochondrial dynamics; NDUFA1; NDUFV1

Indexed keywords

CELL PROTEIN; DYNAMIN RELATED PROTEIN 1; MITOCHONDRIAL PROTEIN; MITOFUSIN 2; PROTEIN NDUFA1; PROTEIN NDUFV1; PROTEIN OPA1; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 77950371493     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2010.02.001     Document Type: Article
Times cited : (70)

References (52)
  • 2
    • 0030298544 scopus 로고    scopus 로고
    • Isolation, mapping, and genomic structure of an X-linked gene for a subunit of human mitochondrial complex I
    • Zhuchenko O., Wehnert M., Bailey J., Sun Z.S., Lee C.C. Isolation, mapping, and genomic structure of an X-linked gene for a subunit of human mitochondrial complex I. Genomics 1996, 37:281-288.
    • (1996) Genomics , vol.37 , pp. 281-288
    • Zhuchenko, O.1    Wehnert, M.2    Bailey, J.3    Sun, Z.S.4    Lee, C.C.5
  • 3
    • 13044310136 scopus 로고    scopus 로고
    • The NDUFA1 gene product (MWFE protein) is essential for activity of complex I in mammalian mitochondria
    • Au H.C., Seo B.B., Matsuno-Yagi A., Yagi T., Scheffler I.E. The NDUFA1 gene product (MWFE protein) is essential for activity of complex I in mammalian mitochondria. Proc. Natl Acad. Sci. U. S. A. 1999, 96. 4354-4359.
    • (1999) Proc. Natl Acad. Sci. U. S. A. , vol.96 , pp. 4354-4359
    • Au, H.C.1    Seo, B.B.2    Matsuno-Yagi, A.3    Yagi, T.4    Scheffler, I.E.5
  • 4
    • 0037077251 scopus 로고    scopus 로고
    • Species specific and mutant MWFE proteins. Their effect on the assembly of a functional mammalian mitochondrial complex I
    • Yadava N., Potluri P., Smith E.N., Bisevac A., Scheffler I.E. Species specific and mutant MWFE proteins. Their effect on the assembly of a functional mammalian mitochondrial complex I. J. Biol. Chem. 2002, 277:21221-21230.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21221-21230
    • Yadava, N.1    Potluri, P.2    Smith, E.N.3    Bisevac, A.4    Scheffler, I.E.5
  • 5
    • 1842582613 scopus 로고    scopus 로고
    • Development and characterization of a conditional mitochondrial complex I assembly system
    • Yadava N., Houchens T., Potluri P., Scheffler I.E. Development and characterization of a conditional mitochondrial complex I assembly system. J. Biol. Chem. 2004, 279:12406-12413.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12406-12413
    • Yadava, N.1    Houchens, T.2    Potluri, P.3    Scheffler, I.E.4
  • 6
    • 2942726285 scopus 로고    scopus 로고
    • The phosphorylation of subunits of complex I from bovine heart mitochondria
    • Chen R., Fearnley I.M., Peak-Chew S.Y., Walker J.E. The phosphorylation of subunits of complex I from bovine heart mitochondria. J. Biol. Chem. 2004, 279:26036-26045.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26036-26045
    • Chen, R.1    Fearnley, I.M.2    Peak-Chew, S.Y.3    Walker, J.E.4
  • 7
    • 17644419961 scopus 로고    scopus 로고
    • Mass spectrometric identification of a novel phosphorylation site in subunit NDUFA10 of bovine mitochondrial complex I
    • Schilling B., Aggeler R., Schulenberg B., Murray J., Row R.H., Capaldi R.A., Gibson B.W. Mass spectrometric identification of a novel phosphorylation site in subunit NDUFA10 of bovine mitochondrial complex I. FEBS Lett. 2005, 579:2485-2490.
    • (2005) FEBS Lett. , vol.579 , pp. 2485-2490
    • Schilling, B.1    Aggeler, R.2    Schulenberg, B.3    Murray, J.4    Row, R.H.5    Capaldi, R.A.6    Gibson, B.W.7
  • 8
    • 39049110244 scopus 로고    scopus 로고
    • Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly
    • Yadava N., Potluri P., Scheffler I.E. Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Int. J. Biochem. Cell Biol. 2008, 40:447-460.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 447-460
    • Yadava, N.1    Potluri, P.2    Scheffler, I.E.3
  • 17
    • 2042459176 scopus 로고    scopus 로고
    • Altered mitochondrial structure and motion dynamics in living cells with energy metabolism defects revealed by real time microscope imaging
    • Pham N., Richardson T., Cameron J., Chue B., Robinson B.H. Altered mitochondrial structure and motion dynamics in living cells with energy metabolism defects revealed by real time microscope imaging. Microsc. Microanal. 2004, 10:247-260.
    • (2004) Microsc. Microanal. , vol.10 , pp. 247-260
    • Pham, N.1    Richardson, T.2    Cameron, J.3    Chue, B.4    Robinson, B.H.5
  • 18
    • 25444446126 scopus 로고    scopus 로고
    • Mitochondrial network complexity and pathological decrease in complex I activity are tightly correlated in isolated human complex I deficiency
    • Koopman W., Visch H.J., Verkaart S., van den Heuvel L., Smeitink J., Willems P. Mitochondrial network complexity and pathological decrease in complex I activity are tightly correlated in isolated human complex I deficiency. Am. J. Physiol. Cell Physiol. 2005, 289:881-890.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289 , pp. 881-890
    • Koopman, W.1    Visch, H.J.2    Verkaart, S.3    van den Heuvel, L.4    Smeitink, J.5    Willems, P.6
  • 19
    • 43049115673 scopus 로고    scopus 로고
    • Modulation of mitocondrial morphology by bioenergetics defects in primary human fibroblasts
    • Guillery O., Malka F., Frachon P., Milea D., Rojo M., Lombès A. Modulation of mitocondrial morphology by bioenergetics defects in primary human fibroblasts. Neuromusc. Dis. 2008, 18:319-330.
    • (2008) Neuromusc. Dis. , vol.18 , pp. 319-330
    • Guillery, O.1    Malka, F.2    Frachon, P.3    Milea, D.4    Rojo, M.5    Lombès, A.6
  • 20
    • 54949153170 scopus 로고    scopus 로고
    • Biogenesis and dynamics of mitochondria during the cell cycle: significance of 3′ UTRs
    • Martínez-Díez M., Santamaría G., Ortega A.D., Cuezva J.M. Biogenesis and dynamics of mitochondria during the cell cycle: significance of 3′ UTRs. PLoS One 2006, 1:e107.
    • (2006) PLoS One , vol.1
    • Martínez-Díez, M.1    Santamaría, G.2    Ortega, A.D.3    Cuezva, J.M.4
  • 21
    • 34247526419 scopus 로고    scopus 로고
    • Mitochondrial dynamics in disease
    • Chan D.C. Mitochondrial dynamics in disease. N. Engl. J. Med. 2007, 356. 1707-1709.
    • (2007) N. Engl. J. Med. , vol.356 , pp. 1707-1709
    • Chan, D.C.1
  • 22
    • 48249134804 scopus 로고    scopus 로고
    • Mitochondrial fluidity matters. Focus on, inherited complex I deficiency is associated with faster protein diffusion in the matrix of moving mitochondria
    • Benard G., Rossignol R. Mitochondrial fluidity matters. Focus on, inherited complex I deficiency is associated with faster protein diffusion in the matrix of moving mitochondria. Am. J. Physiol. Cell Physiol. 2008, 294:C1123.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.294
    • Benard, G.1    Rossignol, R.2
  • 26
    • 0034845691 scopus 로고    scopus 로고
    • Thyroid hormone regulates oxidative phosphorylation in the cerebral cortex and striatum of neonatal rats
    • Martínez B., del Hoyo P., Martín M.A., Arenas J., Pérez-Castillo A., Santos A. Thyroid hormone regulates oxidative phosphorylation in the cerebral cortex and striatum of neonatal rats. J. Neurochem. 2001, 78:1054-1063.
    • (2001) J. Neurochem. , vol.78 , pp. 1054-1063
    • Martínez, B.1    del Hoyo, P.2    Martín, M.A.3    Arenas, J.4    Pérez-Castillo, A.5    Santos, A.6
  • 27
    • 67349179026 scopus 로고    scopus 로고
    • Quantification of mitocondrial DNA copy number: pre-analytical factors
    • Andreu A.L., Martínez R., Martí R., García-Arumi E. Quantification of mitocondrial DNA copy number: pre-analytical factors. Mitochondrion 2009, 9:242-246.
    • (2009) Mitochondrion , vol.9 , pp. 242-246
    • Andreu, A.L.1    Martínez, R.2    Martí, R.3    García-Arumi, E.4
  • 29
    • 0020625894 scopus 로고
    • Flow cytometric studies of oxidative product formation by neutrophils: a graded response to membrane stimulation
    • Bass D.A., Parce J.W., Dchatelet L.R., Szejda P., Seeds M.C., Thomas M. Flow cytometric studies of oxidative product formation by neutrophils: a graded response to membrane stimulation. J. Immunol. 1983, 130:1910-1917.
    • (1983) J. Immunol. , vol.130 , pp. 1910-1917
    • Bass, D.A.1    Parce, J.W.2    Dchatelet, L.R.3    Szejda, P.4    Seeds, M.C.5    Thomas, M.6
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 68949148655 scopus 로고    scopus 로고
    • Capacity of oxidative phosphorilation in human skeletal muscle, new perspectives of mitochondrial physiology
    • Gnaiger E. Capacity of oxidative phosphorilation in human skeletal muscle, new perspectives of mitochondrial physiology. Int. J. Biochem. Cell Biol. 2009, 41:1837-1845.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1837-1845
    • Gnaiger, E.1
  • 35
    • 1542297737 scopus 로고    scopus 로고
    • A switch in metabolism precedes increased mitochondrial biogenesis in respiratory chain-deficient mouse hearts
    • Hansson A., Nicole N., Dufour E., Rantanen A., Hultenby K., Clayton D.A., Wiborn R., Larsson N.G. A switch in metabolism precedes increased mitochondrial biogenesis in respiratory chain-deficient mouse hearts. PNAS 2004, 101:3136-3141.
    • (2004) PNAS , vol.101 , pp. 3136-3141
    • Hansson, A.1    Nicole, N.2    Dufour, E.3    Rantanen, A.4    Hultenby, K.5    Clayton, D.A.6    Wiborn, R.7    Larsson, N.G.8
  • 42
    • 71849096530 scopus 로고    scopus 로고
    • Mitochondria as ATP consumers in cellular pathology
    • Chinopoulos C., Adam-Vizi V. Mitochondria as ATP consumers in cellular pathology. Biochim. Biophys. Acta 2010, 1802:221-227.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 221-227
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 43
    • 0018386209 scopus 로고
    • Evidence that glutamine, not sugar, is the major energy source for cultured HeLa cells
    • Reitzer L.J., Wice B.M., Kennell D. Evidence that glutamine, not sugar, is the major energy source for cultured HeLa cells. J. Biol. Chem. 1979, 254:2669-2676.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2669-2676
    • Reitzer, L.J.1    Wice, B.M.2    Kennell, D.3
  • 44
    • 0034646656 scopus 로고    scopus 로고
    • Very rare complementation between mitochondria carrying different mitochondrial DNA mutations points to intrinsic genetic autonomy of the organelles in cultures human cells
    • Enriquez J.A., Cabezas-Herrera J., Bayona-Bafaluy M.P., Attardi G. Very rare complementation between mitochondria carrying different mitochondrial DNA mutations points to intrinsic genetic autonomy of the organelles in cultures human cells. J. Biol. Chem. 2000, 275:11207-11215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11207-11215
    • Enriquez, J.A.1    Cabezas-Herrera, J.2    Bayona-Bafaluy, M.P.3    Attardi, G.4
  • 45
    • 0026457218 scopus 로고
    • Nonviability of cells with oxidative defects in galactose medium: a screening test for affected patient fibroblasts
    • Robinson B.H., Petrova-Benedict R., Buncic J.R., Wallace D.C. Nonviability of cells with oxidative defects in galactose medium: a screening test for affected patient fibroblasts. Biochem. Med. Metab. Biol. 1992, 48:122-126.
    • (1992) Biochem. Med. Metab. Biol. , vol.48 , pp. 122-126
    • Robinson, B.H.1    Petrova-Benedict, R.2    Buncic, J.R.3    Wallace, D.C.4
  • 47
    • 51749084230 scopus 로고    scopus 로고
    • Ultrastructure of the mitochondrion and its bearing on function and bioenergetics
    • Benard G., Rossignol R. Ultrastructure of the mitochondrion and its bearing on function and bioenergetics. Antioxid. Redox Signal. 2008, 10:1313-1342.
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1313-1342
    • Benard, G.1    Rossignol, R.2
  • 48
    • 46649095406 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation and energetic status are reflected by morphology of mitochondrial network in INS-1E and HEP-G2 cells viewed by 4Pi microscopy
    • Plecitá-Hlavatá L., Lessard M., Santorová J., Bewersdorf J., Jezek P. Mitochondrial oxidative phosphorylation and energetic status are reflected by morphology of mitochondrial network in INS-1E and HEP-G2 cells viewed by 4Pi microscopy. Biochim. Biophys. Acta 2008, 1777:834-846.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 834-846
    • Plecitá-Hlavatá, L.1    Lessard, M.2    Santorová, J.3    Bewersdorf, J.4    Jezek, P.5
  • 49
    • 49349102894 scopus 로고    scopus 로고
    • Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view
    • Twig G., Hyde B., Shirihai O.S. Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view. Biochim. Biophys. Acta 2008, 1777:1902-1907.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1902-1907
    • Twig, G.1    Hyde, B.2    Shirihai, O.S.3
  • 51
    • 0036906665 scopus 로고    scopus 로고
    • Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins
    • Legros F., Lombès A., Frachon P., Rojo M. Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell 2002, 13:4343-4354.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4343-4354
    • Legros, F.1    Lombès, A.2    Frachon, P.3    Rojo, M.4
  • 52
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417:1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.