Cited by 225Mitochondrial Function and PathologyCancer and biochemical researchCoenzyme Q10 studies and effects

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

Low Reserve of Cytochrome c Oxidase Capacity in Vivo in the Respiratory Chain of a Variety of Human Cell Types

Open access

Villani, Gaetano, Greco, Marilena, Papa, Sergio, Attardi, Giuseppe·1998·Journal of Biological Chemistry

Open this paper in CoChat — free account

Abstract

The question of whether and to what extent the in vivo cytochrome c oxidase (COX) capacity in mammalian cells exceeds that required to support respiration is still unresolved. In the present work, to address this question, a newly developed approach for measuring the rate of COX activity, either as an isolated step or as a respiratory chain-integrated step, has been applied to a variety of human cell types, including several tumor-derived semidifferentiated cell lines, as well as specialized cells removed from the organism. KCN titration assays, carried out on intact uncoupled cells, have clearly shown that the COX capacity is in low excess (16-40%) with respect to that required to support the endogenous respiration rate. Furthermore, measurements of O2 consumption rate supported by 0.4 mM tetramethyl-p-phenylenediamine in antimycin-inhibited uncoupled intact cells have given results that are fully consistent with those obtained in the KCN titration experiments. Similarly, KCN titration assays on digitonin-permeabilized cells have revealed a COX capacity that is nearly limiting (7-22% excess) for ADP + glutamate/malate-dependent respiration. The present observations, therefore, substantiate the conclusion that the in vivo control of respiration by COX is much tighter than has been generally assumed on the basis of experiments carried out on isolated mitochondria. This conclusion has important implications for understanding the role of physiological or pathological factors in affecting the COX threshold.

Integrity signals

Registry

Crossref · 10.1074/jbc.273.48.31829

Cites

47 of 47 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996) · Cell · doi:10.1016/s0092-8674(00)80085-9 · Cited by 5,167
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
Yang, J., Liu, X., Bhalla, K. N., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., & Wang, X. (1997) · Science · doi:10.1126/science.275.5303.1129 · Cited by 4,913
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
Kluck, R. M., Bossy‐Wetzel, E., Green, D. R., & Newmeyer, D. D. (1997) · Science · doi:10.1126/science.275.5303.1132 · Cited by 4,715
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Human Cells Lacking mtDNA: Repopulation with Exogenous Mitochondria by Complementation
King, M. P., & Attardi, G. M. (1989) · Science · doi:10.1126/science.2814477 · Cited by 1,685
Self-citation
A Linear Steady-State Treatment of Enzymatic Chains. General Properties, Control and Effector Strength
Heinrich, R., & Rapoport, T. A. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03318.x · Cited by 1,400
Human cells lacking mtDNA: repopulation with exogenous mitochondria by complementation
(1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90040-d · Cited by 1,386
Diseases of the mitochondrial DNA
Wallace, D. C. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.005523 · Cited by 1,319
Controlled synthesis of HBsAg in a differentiated human liver carcinoma-derived cell line
Aden, D. P., Fogel, A., Plotkin, S. A., Damjanov, I., & Knowles, B. B. (1979) · Nature · doi:10.1038/282615a0 · Cited by 1,317

Show all 47 references

Research works printed but not linked: 1

Biedler, 1973, Cancer Res., 33, 2643

Sorted by citations

Analysis of mitochondrial function in situ in permeabilized muscle fibers, tissues and cells
Kuznetsov, A. V., Veksler, V., Gellerich, F. N., Saks, V. A., Margreiter, R., & Kunz, W. S. (2008) · Nature Protocols · doi:10.1038/nprot.2008.61 · Cited by 839
Mitochondrial threshold effects
Rossignol, R., Faustin, B., Rocher, C., Malgat, M., Mazat, J., & Letellier, T. (2003) · Biochemical Journal · doi:10.1042/bj20021594 · Cited by 816
The inhibition of mitochondrial cytochrome oxidase by the gases carbon monoxide, nitric oxide, hydrogen cyanide and hydrogen sulfide: chemical mechanism and physiological significance
Cooper, C. E., & Brown, G. C. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9166-6 · Cited by 746
AIF deficiency compromises oxidative phosphorylation
Vahsen, N., Candé, C., Brière, J.-J., Bénit, P., Joza, N. A., Larochette, N., Mastroberardino, P. G., Péquignot, M. O., Casares, N., Lazar, V., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600461 · Cited by 633
HIF1α induced switch from bivalent to exclusively glycolytic metabolism during ESC‐to‐EpiSC/hESC transition
Zhou, W., Choi, M. P., Margineantu, D. H., Margaretha, L., Hesson, J., Cavanaugh, C., Blau, C. A., Horwitz, M. S., Hockenbery, D. M., Ware, C. B., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.71 · Cited by 555
The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis
Hüttemann, M., Pecina, P., Rainbolt, M., Sanderson, T. H., Kagan, V. E., Samavati, L., Doan, J. W., & Lee, I. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.01.010 · Cited by 522
Cyclic AMP Produced inside Mitochondria Regulates Oxidative Phosphorylation
Acín‐Pérez, R., Salazar, E., Kamenetsky, M., Buck, J., Levin, L. R., & Manfredi, G. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.012 · Cited by 465
High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain
Lin, M. T. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.2.133 · Cited by 366
Cytochrome c oxidase subunit IV is essential for assembly and respiratory function of the enzyme complex
Li, Y.-F., Park, J.-S., Deng, J., & Bai, Y. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9052-z · Cited by 342
Molecular Mechanisms and Therapeutic Effects of (−)-Epicatechin and Other Polyphenols in Cancer, Inflammation, Diabetes, and Neurodegeneration
Shay, J., Elbaz, H. A., Lee, I., Zielske, S. P., Malek, M. H., & Hüttemann, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/181260 · Cited by 289
Natural selection and the evolution of mtDNA-encoded peptides: evidence for intergenomic co-adaptation
Blier, P. U. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(01)02338-1 · Cited by 269
Mitochondrial energy metabolism is regulated via nuclear-coded subunits of cytochrome c oxidase
Kadenbach, B., Hüttemann, M., Arnold, S., Lee, I., & Bender, E. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00305-1 · Cited by 268
In vivo and in organello assessment of OXPHOS activities
Barrientos, A. (2002) · Methods · doi:10.1016/s1046-2023(02)00036-1 · Cited by 266
Ceramide Interaction with the Respiratory Chain of Heart Mitochondria
Di Paola, M., Cocco, T., & Lorusso, M. (2000) · Biochemistry · doi:10.1021/bi9924415 · Cited by 262
Mitochondrial Respiration and ATP Production Are Significantly Impaired in Striatal Cells Expressing Mutant Huntingtin
Milakovic, T., & Johnson, G. V. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504749200 · Cited by 259
Evaluation of the Mitochondrial Respiratory Chain and Oxidative Phosphorylation System Using Polarography and Spectrophotometric Enzyme Assays
Barrientos, A., Fontanesi, F., & Díaz, F. (2009) · Current Protocols in Human Genetics · doi:10.1002/0471142905.hg1903s63 · Cited by 251
Cytochrome c Oxidase and the Regulation of Oxidative Phosphorylation
Ludwig, B., Bender, E., Arnold, S., Hüttemann, M., Lee, I., & Kadenbach, B. (2001) · ChemBioChem · doi:10.1002/1439-7633(20010601)2:6 · Cited by 246
The subunit composition and function of mammalian cytochrome c oxidase
Kadenbach, B., & Hüttemann, M. (2015) · Mitochondrion · doi:10.1016/j.mito.2015.07.002 · Cited by 250
Mitochondrial dysregulation and oxidative stress in patients with chronic kidney disease
Granata, S., Zaza, G., Simone, S., Villani, G., Latorre, D., Pontrelli, P., Carella, M., Schena, F. P., Grandaliano, G., & Pertosa, G. B. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-388 · Cited by 242
Self-citation
The possible role of cytochrome c oxidase in stress-induced apoptosis and degenerative diseases
Kadenbach, B., Arnold, S., Lee, I., & Hüttemann, M. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2003.06.005 · Cited by 238
Tissue‐specific regulation of cytochrome c by post‐translational modifications: respiration, the mitochondrial membrane potential, ROS, and apoptosis
Kalpage, H. A., Bazylianska, V., Recanati, M., Fite, A., Liu, J., Wan, J., Mantena, N., Malek, M. H., Podgorski, I., Heath, E., et al. (2018) · The FASEB Journal · doi:10.1096/fj.201801417r · Cited by 229
Complex IV – The regulatory center of mitochondrial oxidative phosphorylation
Kadenbach, B. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.10.004 · Cited by 224
Differentiation of SH-SY5Y cells to a neuronal phenotype changes cellular bioenergetics and the response to oxidative stress
Schneider, L. E., Giordano, S. S., Zelickson, B. R., Johnson, M. S., Benavides, G. A., Ouyang, X., Fineberg, N. S., Darley-Usmar, V. M., & Zhang, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.030 · Cited by 210
Characterization of Mitochondrial and Extra-mitochondrial Oxygen Consuming Reactions in Human Hematopoietic Stem Cells
Piccoli, C., Ria, R., Scrima, R., Cela, O., D'Aprile, A., Boffoli, D., Falzetti, F., Tabilio, A., & Capitanio, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500047200 · Cited by 209
cAMP-dependent Tyrosine Phosphorylation of Subunit I Inhibits Cytochrome c Oxidase Activity
Lee, I., Salomon, A. R., Ficarro, S. B., Mathes, I., Lottspeich, F., Grossman, L. I., & Hüttemann, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411335200 · Cited by 207
Tissue-specific mtDNA abundance from exome data and its correlation with mitochondrial transcription, mass and respiratory activity
D'Erchia, A. M., Atlante, A., Gadaleta, G., Pavesi, G., Chiara, M., De Virgilio, C., Manzari, C., Mastropasqua, F., Prazzoli, G. M., Picardi, E., et al. (2015) · Mitochondrion · doi:10.1016/j.mito.2014.10.005 · Cited by 197
Sequential Serum-dependent Activation of CREB and NRF-1 Leads to Enhanced Mitochondrial Respiration through the Induction of Cytochrome c
Herzig, R. P., Scacco, S., & Scarpulla, R. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.13134 · Cited by 197
Tissue-specific differences in mitochondrial activity and biogenesis
Fernández‐Vizarra, E., Enrı́quez, J. A., Martos, A. P., Montoya, J., & Fernández‐Silva, P. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.09.011 · Cited by 195
Acquisition of Temozolomide Chemoresistance in Gliomas Leads to Remodeling of Mitochondrial Electron Transport Chain
Oliva, C. R., Nozell, S. E., Diers, A. R., McClugage, S. G., Sarkaria, J. N., Markert, J. M., Darley-Usmar, V. M., Bailey, S. M., Gillespie, G. Y., Landar, A. L., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.147504 · Cited by 192
Protein Phosphorylation and Prevention of Cytochrome Oxidase Inhibition by ATP: Coupled Mechanisms of Energy Metabolism Regulation
Acin-Perez, R., Gatti, D. L., Bai, Y., & Manfredi, G. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.024 · Cited by 190
Tumor Necrosis Factor α Inhibits Oxidative Phosphorylation through Tyrosine Phosphorylation at Subunit I of Cytochrome c Oxidase
Samavati, L., Lee, I., Mathes, I., Lottspeich, F., & Hüttemann, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801954200 · Cited by 186
Cytochrome c Oxidase Activity Is a Metabolic Checkpoint that Regulates Cell Fate Decisions During T Cell Activation and Differentiation
Tarasenko, T. N., Pacheco, S. E., Koenig, M. K., Gómez‐Rodríguez, J., Kapnick, S. M., Díaz, F., Zerfas, P. M., Barca, E., Sudderth, J., DeBerardinis, R. J., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.05.007 · Cited by 186
Peroxisome proliferator-activated receptor-γ coactivator 1-α (PGC1α) is a metabolic regulator of intestinal epithelial cell fate
D’Errico, I., Salvatore, L., Murzilli, S., Sasso, G. L., Latorre, D., Martelli, N., Egorova, A. V., Polishuck, R. S., Madeyski-Bengtson, K., Lelliott, C. J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016354108 · Cited by 179
Self-citation
Effects of experimental weight perturbation on skeletal muscle work efficiency, fuel utilization, and biochemistry in human subjects
Goldsmith, R., Joanisse, D. R., Gallagher, D., Pavlovich, K., Shamoon, E., Leibel, R. L., & Rosenbaum, M. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00053.2009 · Cited by 171
Human Skin Keloid Fibroblasts Display Bioenergetics of Cancer Cells
Vincent, A. S., Phan, T. T., Mukhopadhyay, A., Lim, H. Y., Halliwell, B. B., & Wong, K. P. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5701107 · Cited by 170
Tissue-specific changes of mitochondrial functions in aged rats: Effect of a long-term dietary treatment with N-acetylcysteine
Cocco, T., Sgobbo, P., Clemente, M. T., Lopriore, B., Grattagliano, I., Paola, M. D., & Villani, G. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.034 · Cited by 157
Self-citation
Mitochondrial response to nutrient availability and its role in metabolic disease
Gao, A. W., Cantó, C., & Houtkooper, R. H. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201303782 · Cited by 148
Activation of Peroxisome Proliferator-Activated Receptor Pathway Stimulates the Mitochondrial Respiratory Chain and Can Correct Deficiencies in Patients’ Cells Lacking Its Components
Bastin, J., Aubey, F., Rötig, A., Münnich, A., & Djouadi, F. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-1701 · Cited by 148
Evaluation of Mitochondrial Respiratory Function in Small Biopsies of Liver
Kuznetsov, A. V., Strobl, D., Ruttmann, E., Königsrainer, A., Margreiter, R., & Gnaiger, E. (2002) · Analytical Biochemistry · doi:10.1006/abio.2002.5658 · Cited by 137
In vivo control of respiration by cytochrome c oxidase in human cells
Villani, G., & Attardi, G. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00303-8 · Cited by 127
Self-citation
Marked aging‐related decline in efficiency of oxidative phosphorylation in human skin fibroblasts
Gréco, M., Villani, G., Mazzucchelli, F., Bresolin, N., Papa, S., & Attardi, G. M. (2003) · The FASEB Journal · doi:10.1096/fj.02-1009fje · Cited by 122
Self-citation
MITOCHONDRIAL DNA VARIATION IS ASSOCIATED WITH MEASURABLE DIFFERENCES IN LIFE-HISTORY TRAITS AND MITOCHONDRIAL METABOLISM IN DROSOPHILA SIMULANS
Ballard, J. W. O., Melvin, R. G., Katewa, S. D., & Maas, K. (2007) · Evolution · doi:10.1111/j.1558-5646.2007.00133.x · Cited by 122
High-resolution respirometry–a modern tool in aging research
Hütter, E., Unterluggauer, H., Garedew, A., Jansen‐Dürr, P., & Gnaiger, E. (2005) · Experimental Gerontology · doi:10.1016/j.exger.2005.09.011 · Cited by 121
Polarographic Oxygen Sensors, the Oxygraph, and High‐Resolution Respirometry to Assess Mitochondrial Function
Gnaiger, E. (2008) · doi:10.1002/9780470372531.ch12 · Cited by 121
Mitochondrial defect and PGC-1α dysfunction in parkin-associated familial Parkinson's disease
Pacelli, C., Rasmo, D. D., Signorile, A., Grattagliano, I., Tullio, G. D., D’Orazio, A., Nico, B., Comi, G. P., Ronchi, D., Ferranini, E., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.12.022 · Cited by 119
Self-citation
Granzyme B can cause mitochondrial depolarization and cell death in the absence of BID, BAX, and BAK
Thomas, D. A., Scorrano, L., Putcha, G. V., Korsmeyer, S. J., & Ley, T. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261581498 · Cited by 120
Bioenergetics and cell death
Kushnareva, Y., & Newmeyer, D. D. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05633.x · Cited by 117
Loss of LRPPRC causes ATP synthase deficiency
Mourier, A., Ruzzenente, B., Brandt, T., Kühlbrandt, W., & Larsson, N. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddt652 · Cited by 117
The power of life—Cytochrome c oxidase takes center stage in metabolic control, cell signalling and survival
Arnold, S. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.05.003 · Cited by 117
ANT2 Isoform Required for Cancer Cell Glycolysis
Chevrollier, A., Loiseau, D., Chabi, B., Rénier, G., Douay, O., Malthièry, Y., & Stepien, G. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-8642-5 · Cited by 116
Tight Control of Respiration by NADH Dehydrogenase ND5 Subunit Gene Expression in Mouse Mitochondria
Bai, Y., Shakeley, R. M., & Attardi, G. M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.805-815.2000 · Cited by 115
Self-citation
Phosphorylations and Acetylations of Cytochrome c Control Mitochondrial Respiration, Mitochondrial Membrane Potential, Energy, ROS, and Apoptosis
Morse, P. T., Arroum, T., Wan, J., Pham, L., Vaishnav, A., Bell, J., Pavelich, L., Malek, M. H., Sanderson, T. H., Edwards, B. F. P., et al. (2024) · Cells · doi:10.3390/cells13060493 · Cited by 113
Phosphorylation and Kinetics of Mammalian Cytochrome c Oxidase
Helling, S., Vogt, S. K., Rhiel, A., Ramzan, R., Wen, L., Marcus, K., & Kadenbach, B. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800137-mcp200 · Cited by 107
Phosphorylation of Mammalian Cytochrome c and Cytochrome c Oxidase in the Regulation of Cell Destiny: Respiration, Apoptosis, and Human Disease
Hüttemann, M., Lee, I., Grossman, L. I., Doan, J. W., & Sanderson, T. H. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_10 · Cited by 111
A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels
Peserico, A., Chiacchiera, F., Grossi, V., Matrone, A., Latorre, D., Simonatto, M., Fusella, A., Ryall, J. G., Finley, L. W. S., Haigis, M. C., et al. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1244-6 · Cited by 108
Self-citation
New Control of Mitochondrial Membrane Potential and ROS Formation A Hypothesis
Lee, I., Bender, E., Arnold, S., & Kadenbach, B. (2001) · Biological Chemistry · doi:10.1515/bc.2001.198 · Cited by 105
Remodeling pathway control of mitochondrial respiratory capacity by temperature in mouse heart: electron flow through the Q-junction in permeabilized fibers
Lemieux, H., Blier, P. U., & Gnaiger, E. (2017) · Scientific Reports · doi:10.1038/s41598-017-02789-8 · Cited by 101
Genetic defects of cytochrome c oxidase assembly
Pecina, P., Houšt'ková, H., Zeman, J., & Houštěk, J. (2004) · Physiological Research · doi:10.33549/physiolres.930000.53.s213 · Cited by 100
Mitochondrial dysfunction in a neural cell model of spinal muscular atrophy
Acsádi, G., Lee, I., Li, X., Khaidakov, M., Pecinová, A., Parker, G. C., & Hüttemann, M. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22106 · Cited by 102
The role of the electron transport chain in immunity
Yin, M., & O’Neill, L. A. J. (2021) · The FASEB Journal · doi:10.1096/fj.202101161r · Cited by 102
Flux Control of Cytochrome c Oxidase in Human Skeletal Muscle
Kunz, W. S., Kudin, A. P., Vielhaber, S., Elger, C. E., Attardi, G. M., & Villani, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004833200 · Cited by 96
Self-citation
Mitochondria in the human heart
Lemieux, H., & Hoppel, C. L. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9211-0 · Cited by 93
Control by cytochromecoxidase of the cellular oxidative phosphorylation system depends on the mitochondrial energy state
Piccoli, C., Scrima, R., Boffoli, D., & Capitanio, N. (2006) · Biochemical Journal · doi:10.1042/bj20060077 · Cited by 92
Low micromolar concentrations of the superoxide probe MitoSOX uncouple neural mitochondria and inhibit complex IV
Roelofs, B. A., Ge, S. X., Studlack, P. E., & Polster, B. M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.05.032 · Cited by 92
Two independent respiratory chains adapt OXPHOS performance to glycolytic switch
Fernández‐Vizarra, E., López-Calcerrada, S., Sierra‐Magro, A., Pérez‐Pérez, R., Formosa, L. E., Hock, D. H., Illescas, M., Peñas, A., Brischigliaro, M., Ding, S., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.09.005 · Cited by 83
Mitochondrial respiration and membrane potential are regulated by the allosteric ATP-inhibition of cytochrome c oxidase
Ramzan, R., Staniek, K., Kadenbach, B., & Vogt, S. K. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.06.005 · Cited by 91
Knockdown of Human Oxa1l Impairs the Biogenesis of F1Fo-ATP Synthase and NADH:Ubiquinone Oxidoreductase
Stibůrek, L., Fornůsková, D., Wenchich, L., Pejznochová, M., Hansíková, H., & Zeman, J. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.044 · Cited by 91
The oxidative damage theory of aging
Lin, M. T., & Flint Beal, M. (2003) · Clinical Neuroscience Research · doi:10.1016/s1566-2772(03)00007-0 · Cited by 89
T3 increases mitochondrial ATP production in oxidative muscle despite increased expression of UCP2 and -3
Short, K. R., Nygren, J., Barazzoni, R., Levine, J. A., & Nair, K. S. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.5.e761 · Cited by 88
Molecular evolution of aerobic energy metabolism in primates.
Grossman, L. I., Schmidt, T. R., Wildman, D. E., & Goodman, M. (2001) · Molecular Phylogenetics and Evolution · doi:10.1006/mpev.2000.0890 · Cited by 86
A second mechanism of respiratory control
Kadenbach, B., & Arnold, S. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00229-x · Cited by 86
What do mitochondrial diseases teach us about normal mitochondrial functions... that we already knew: threshold expression of mitochondrial defects
Mazat, J., Rossignol, R., Malgat, M., Rocher, C., Faustin, B., & Letellier, T. (2001) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00236-x · Cited by 85
PGC-1s in the Spotlight with Parkinson’s Disease
Piccinin, E., Sardanelli, A. M., Seibel, P., Moschetta, A., Cocco, T., & Villani, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073487 · Cited by 85
Self-citation
Regulation of mitochondrial oxidative phosphorylation through tight control of cytochrome c oxidase in health and disease – Implications for ischemia/reperfusion injury, inflammatory diseases, diabetes, and cancer
Pham, L., Arroum, T., Wan, J., Pavelich, L., Bell, J., Morse, P. T., Lee, I., Grossman, L. I., Sanderson, T. H., Malek, M. H., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103426 · Cited by 92
Control of Respiration by Cytochrome c Oxidase in Intact Cells
Dalmonte, M. E., Forte, E., Genova, M. L., Giuffrè, A., Sarti, P., & Lenaz, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.050146 · Cited by 81
Cytochrome c oxidase regulates endogenous nitric oxide availability in respiring cells: A possible explanation for hypoxic vasodilation
Palacios‐Callender, M., Hollis, V., Mitchison, M., Frakich, N., Unitt, D. C., & Moncada, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709440104 · Cited by 80
An intragenic suppressor in the cytochrome c oxidase I gene of mouse mitochondrial DNA
Acín‐Pérez, R. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg021 · Cited by 78
Effect of coenzyme Q10 on the mitochondrial function of skin fibroblasts from Parkinson patients
Winkler‐Stuck, K., Wiedemann, F. R., Wallesch, C., & Kunz, W. S. (2004) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2004.02.003 · Cited by 77
Cytochrome c oxidase subunit 4 isoform 2‐knockout mice show reduced enzyme activity, airway hyporeactivity, and lung pathology
Hüttemann, M., Lee, I., Gao, X., Pecina, P., Pecinová, A., Liu, J., Aras, S., Sommer, N., Sanderson, T. H., Tost, M., et al. (2012) · The FASEB Journal · doi:10.1096/fj.11-203273 · Cited by 76
Lactate oxidation in human skeletal muscle mitochondria
Jacobs, R. A., Meinild, A., Nordsborg, N. B., & Lundby, C. (2013) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00476.2012 · Cited by 77
Cytochrome c Oxidase and Its Role in Neurodegeneration and Neuroprotection
Arnold, S. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3573-0_13 · Cited by 77
In Vivo Regulation of Oxidative Phosphorylation in Cells Harboring a Stop-codon Mutation in Mitochondrial DNA-encoded Cytochrome c Oxidase Subunit I
D’Aurelio, M., Pallotti, F., Barrientos, A., Gajewski, C. D., Kwong, J. Q., Bruno, C., Beal, M. F., & Manfredi, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106429200 · Cited by 71
Transcription of mammalian cytochrome c oxidase subunit IV‐2 is controlled by a novel conserved oxygen responsive element
Hüttemann, M., Lee, I., Liu, J., & Grossman, L. I. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06093.x · Cited by 69
Dinitrophenol-induced mitochondrial uncoupling in vivo triggers respiratory adaptation in HepG2 cells
Desquiret‐Dumas, V., Loiseau, D., Jacques, C. D. G., Douay, O., Malthièry, Y., Ritz, P., & Roussel, D. (2005) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2005.11.005 · Cited by 73
A CMC1‐knockout reveals translation‐independent control of human mitochondrial complex IV biogenesis
Bourens, M., & Barrientos, A. (2017) · EMBO Reports · doi:10.15252/embr.201643103 · Cited by 69
Oxygen Tolerance and Coupling of Mitochondrial Electron Transport
Campian, J. L., Qian, M., Gao, X., & Eaton, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406685200 · Cited by 69
The C57Bl/6 mouse serves as a suitable model of human skeletal muscle mitochondrial function
Jacobs, R. A., Díaz, V., Meinild, A., Gassmann, M., & Lundby, C. (2012) · Experimental Physiology · doi:10.1113/expphysiol.2012.070037 · Cited by 68
Metabolic consequences of a novel missense mutation of the mtDNA CO I gene
Varlamov, D. A. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.16.1797 · Cited by 68
Regulation of Mammalian 13-Subunit Cytochrome c Oxidase and Binding of other Proteins: Role of NDUFA4
Kadenbach, B. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.09.003 · Cited by 70
Cytoskeleton and regulation of mitochondrial function: the role of beta-tubulin II
Kuznetsov, A. V., Javadov, S. A., Guzun, R., Grimm, M. F., & Saks, V. A. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00082 · Cited by 67
Betaine is a positive regulator of mitochondrial respiration
Lee, I. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.12.005 · Cited by 66
PGC-1α/β upregulation is associated with improved oxidative phosphorylation in cells harboring nonsense mtDNA mutations
Srivastava, S., Barrett, J. N., & Moraes, C. T. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm045 · Cited by 64
A comparative assessment of mitochondrial function in epimastigotes and bloodstream trypomastigotes of Trypanosoma cruzi
Gonçalves, R. L. S., Barreto, R. F. S. M., Polycarpo, C. R., Gadelha, F. R., de Castro, S. L., & de Oliveira, M. F. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9398-8 · Cited by 60
Thermal sensitivity of mitochondrial functions in permeabilized muscle fibers from two populations of Drosophila simulans with divergent mitotypes
Pichaud, N., Ballard, J. W. O., Tanguay, R. M., & Blier, P. U. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00542.2010 · Cited by 62
Does apoptosis‐inducing factor (AIF) have both life and death functions in cells?
Porter, A. G., & Urbano, A. (2006) · BioEssays · doi:10.1002/bies.20444 · Cited by 58
Gender-specific role of mitochondria in the vulnerability of 6-hydroxydopamine-treated mesencephalic neurons
Misiak, M., Beyer, C., & Arnold, S. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.04.009 · Cited by 55
Mitochondrial Outer Membrane Permeability Change and Hypersensitivity to Digitonin Early in Staurosporine-induced Apoptosis
Duan, S., Hájek, P., Lin, C. P., Shin, S. K., Attardi, G. M., & Chomyn, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209269200 · Cited by 55
Self-citation
The biological foundation of the genetic association of TOMM40 with late-onset Alzheimer's disease
Zeitlow, K., Charlambous, L., Ng, I., Gagrani, S., Mihovilovic, M., Luo, S., Rock, D. L., Saunders, A. M., Roses, A. D., & Gottschalk, W. K. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.07.031 · Cited by 56
Functional alteration of cytochrome c oxidase by SURF1 mutations in Leigh syndrome
Pecina, P., Čapková, M., Chowdhury, S. R., Drahota, Z., Dubot, A., Pecinová, A., Hansíková, H., Houšt'ková, H., Zeman, J., Godinot, C., et al. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(03)00127-3 · Cited by 54
Tight control of mitochondrial membrane potential by cytochrome c oxidase
Pacelli, C., Latorre, D., Cocco, T., Capuano, F., Kukat, C., Seibel, P., & Villani, G. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.12.004 · Cited by 53
Self-citation

Authors: Villani, G., Greco, M., Papa, S., & Attardi, G.
Affiliations: California Institute of Technology (US)
University of Bari Aldo Moro (IT)
Corresponding author: Villani, Gaetano
Attardi, Giuseppe
ORCID: Villani, Gaetano
Papa, Sergio
Attardi, Giuseppe
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1998-11
Volume: 273
Issue: 48
Pages: 31829-31836
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.273.48.31829
OpenAlex: W2109528024
Cited by: 225
References: 47
Citations by year: 2026: 6 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 2 · 2021: 7 · 2020: 5 · 2019: 2 · 2018: 6 · 2017: 6 · 2016: 7 · 2015: 6 · 2014: 12 · 2013: 10 · 2012: 11
FWCI: 3.25
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 8011 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion)
Funders: National Institute of General Medical Sciences (GM11726)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Keywords: cytochrome c oxidase, electron transport chain, oxygen consumption, tetramethyl-p-phenylenediamine, digitonin-permeabilized cells, uncoupled respiration, cancer cell lines, human cell types
MeSH terms: Adenosine Diphosphate, Cell Differentiation, Cell Line, Cell Membrane Permeability, Electron Transport Complex IV, Digitonin, Carcinoma, Hepatocellular, Humans, Kinetics, Liver Neoplasms, Lung Neoplasms, Malates, Mitochondria, Multiple Myeloma, Neuroblastoma, Oxygen Consumption, Potassium Cyanide, Osteosarcoma, Tetramethylphenylenediamine, Tumor Cells, Cultured, Glutamic Acid

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Low Reserve of Cytochrome c Oxidase Capacity in Vivo in the Respiratory Chain of a Variety of Human Cell Types

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks