Mitochondrial Ca 2+ Transport and the Role of Intramitochondrial Ca 2+ in the Regulation of Energy Metabolism
Abstract
The mitochondrial inner membrane of all mammalian tissues, including brain tissues, has specific active transport systems for the uptake and egress of Ca2+. The primary role of this transport system is to relay changes in cytosolic [Ca2+], which stimulates energy-requiring processes in the cytosol (e.g. secretion), into the mitochondrial matrix where it stimulates several key steps in energy production. Thus using the same second-messenger molecule, the latter events allow energetic homeostasis to be maintained under conditions of cell stimulation. This appears to be brought about by a co-ordinated enhancement of steps throughout the pathways of oxidative phosphorylation, including substrate supply to the respiratory chain by dehydrogenase activation, activation of the respiratory chain itself by a mechanism which appears to involve changes in the matrix volume, and also possibly activation of the ATP synthetase where the release of a specific inhibitory subunit has been proposed.
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Inhibiting MPT pore opening may also prevent the loss of enzyme scavengers of ROS within the matrix that normally neutralizes ROS in the matrix.
“Inhibiting MPT pore opening may also prevent the loss of enzyme scavengers of ROS within the matrix that normally neutralizes ROS in the matrix (220).”
From Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function (2009) · cites this paper as [220]
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BackgroundRegulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 814 · see citing works
The possibility of neurotoxicity in the hippocampus in major depression: a primer on neuron death
Sapolsky, R. M. (2000) · Biological Psychiatry · doi:10.1016/s0006-3223(00)00971-9 · Cited by 699 · see citing works
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BackgroundWhite, R. J., & Reynolds, I. J. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05688.1996 · Cited by 592 · see citing works
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BackgroundStowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471 · see citing works
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Lee, A. L., Ogle, W. O., & Sapolsky, R. M. (2002) · Bipolar Disorders · doi:10.1034/j.1399-5618.2002.01144.x · Cited by 462 · see citing works
Crosstalk signaling between mitochondrial Ca2+ and ROS
Robert, F. F. (2009) · Frontiers in bioscience · doi:10.2741/3303 · Cited by 439 · see citing works
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Yuan, Y. A. N., Wei, C., Zhang, W., Cheng, H., & Jie, L. I. U. (2006) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2006.00390.x · Cited by 258 · see citing works
Crosstalk between calcium and reactive oxygen species signaling in cancer
Hempel, N., & Trebak, M. (2017) · Cell Calcium · doi:10.1016/j.ceca.2017.01.007 · Cited by 243 · see citing works
Hematopoietic Stem Cell Metabolism during Development and Aging
Nakamura‐Ishizu, A., Ito, K., & Suda, T. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.029 · Cited by 232 · see citing works
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Shergalis, A. G., Hu, S., Bankhead, A., & Neamati, N. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107525 · Cited by 194 · see citing works
White, R. J., & Reynolds, I. J. (1997) · The Journal of Physiology · doi:10.1113/jphysiol.1997.sp021839 · Cited by 188 · see citing works
NCLX: The mitochondrial sodium calcium exchanger
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“This is due largely to the [Ca]m sensitivity of key steps in energy production [1,2].”
The Complex Interplay between Mitochondria, ROS and Entire Cellular Metabolism
Kuznetsov, A. V., Margreiter, R., Ausserlechner, M. J., & Hagenbuchner, J. (2022) · Antioxidants · doi:10.3390/antiox11101995 · Cited by 168 · see citing works
Anderson, E. J., Rodríguez, E., Anderson, C. A., Thayne, K. A., Chitwood, W. R., & Kypson, A. P. (2010) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00932.2010 · Cited by 163 · see citing works
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The Interface Between ER and Mitochondria: Molecular Compositions and Functions.
Lee, S., & Min, K. (2018) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2018.0438 · Cited by 157 · see citing works
Mitochondrial nitric oxide synthase
Brookes, P. S. (2003) · Mitochondrion · doi:10.1016/j.mito.2003.10.001 · Cited by 154 · see citing works
NAD(P)H fluorescence imaging of postsynaptic neuronal activation in murine hippocampal slices
Shuttleworth, C. W., Brennan, A. M., & Connor, J. A. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-08-03196.2003 · Cited by 151 · see citing works
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Dittami, G. M., Rajguru, S. M., Lasher, R. A., Hitchcock, R. W., & Rabbitt, R. D. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2010.198804 · Cited by 147 · see citing works
“Furthermore, as respiration in mitochondria has been linked to mitochondrial calcium cycling (McCormack & Denton, 1993), IR stimulation at 1862 nm wavelength could potentially provide an exogenous approach for controlling the oxidative metabolism in cells as has been reported for irradiation at…”
BackgroundHuntington’s Disease and Mitochondria
Farshbaf, M. J., & Ghaedi, K. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9766-1 · Cited by 148 · see citing works
“Ca2+ increases respiratory rate, upregulates the OXPHOS system, and elevates ATP synthesis by prompting PDH, isocitrate dehydrogenase, KGDH, and ATP synthase complex (McCormack and Denton 1993; Das and Harris 1990).”
Kovács, R., Schuchmann, S., Gabriel, S., Kann, O., Kardos, J., & Heinemann, U. (2002) · Journal of Neurophysiology · doi:10.1152/jn.00149.2002 · Cited by 146 · see citing works
Voltage-energized calcium-sensitive ATP production by mitochondria
Wescott, A. P., Kao, J. P. Y., Lederer, W. J., & Boyman, L. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0126-8 · Cited by 144 · see citing works
Rybalka, E., Timpani, C. A., Cooke, M. B., Williams, A. D., & Hayes, A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115763 · Cited by 143 · see citing works
Viruses as Modulators of Mitochondrial Functions
Anand, S. K., & Tikoo, S. K. (2013) · Advances in Virology · doi:10.1155/2013/738794 · Cited by 141 · see citing works
Functional Studies in Cultured Astrocytes
Hertz, L., Peng, L., & Lai, J. C. K. (1998) · Methods · doi:10.1006/meth.1998.0686 · Cited by 135 · see citing works
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Shoshan‐Barmatz, V., De, S., & Meir, A. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00060 · Cited by 122 · see citing works
Tadić, V., Prell, T., Lautenschläger, J., & Großkreutz, J. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00147 · Cited by 115 · see citing works
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Colegrove, S. L., Albrecht, M. A., & Friel, D. D. (2000) · The Journal of General Physiology · doi:10.1085/jgp.115.3.351 · Cited by 107 · see citing works
“One possibility arises in the context of Ca21-regulated mitochondrial ATP production (McCormack and Denton, 1993; Robb-Gaspers et al., 1998).”
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Zhou, Z., Matlib, M. A., & Bers, D. M. (1998) · The Journal of Physiology · doi:10.1111/j.1469-7793.1998.379bt.x · Cited by 105 · see citing works
“…(at physiological concentrations of Na¤ and Mg¥) have also typically shown very low Ca¥ uptake below 0·5 ìÒ medium [Ca¥], but with a sharp increase in Ca¥ uptake (and [Ca¥]m) starting between 0·5 and 1·5 ìÒ Ca¥ (Crompton, 1990; McCormack & Denton, 1993; Leisey, Grotyohann, Scott & Scaduto, 1993).”
BackgroundInfluentialChacon, E., Lemasters, J. J., Ohata, H., Harper, I. S., Trollinger, D. R., & Herman, B. A. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00138-x · Cited by 104 · see citing works
Kovács, R., Kardos, J., Heinemann, U., & Kann, O. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4000-04.2005 · Cited by 101 · see citing works
“…et al., 2000a,b; Duchen, 2000; Nicholls and Budd, 2000) and allows sensitive regulation of oxidative ATP synthesis as a result of Ca 2ϩ ion-dependent activation of mitochondrial dehydrogenases (McCormack and Denton , 1993; Robb-Gaspers et al., 1998; Jouaville et al., 1999; Kann et al., 2003a,b).”
Mak, D. D., McBride, S. M. J., & Foskett, J. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22231 · Cited by 98 · see citing works
Jahangir, A., Özcan, C., Holmuhamedov, E., & Terzic, A. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00242-1 · Cited by 100 · see citing works
Brennan, A. M., Connor, J. A., & Shuttleworth, C. W. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600292 · Cited by 97 · see citing works
“Excitatory stimulation in hippocampal slices results in biphasic NAD(P)H fluorescence transients.”
BackgroundLi, X., Chlan‐Fourney, J., Juorio, A. V., Bennett, V. L., Shrikhande, S., Keegan, D. L., Jin, Q., & Boulton, A. A. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990401)56:1 · Cited by 57 · see citing works
Effects of NO on mitochondrial function in cardiomyocytes: Pathophysiological relevance
Davidson, S. M., & Duchen, M. R. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.01.019 · Cited by 91 · see citing works
Martinc, B., Grabnar, I., & Vovk, T. (2012) · Current Neuropharmacology · doi:10.2174/157015912804143504 · Cited by 88 · see citing works
Jahangir, A., Sagar, S., & Terzic, A. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00647.2007 · Cited by 88 · see citing works
Cummins, J. M. (2001) · Human Reproduction Update · doi:10.1093/humupd/7.2.217 · Cited by 86 · see citing works
Parra, V., Bravo, R., Norambuena‐Soto, I., Hernández-Fuentes, C. P., Gómez-Contreras, Á., Verdejo, H., Mellado, R., Chiong, M., Lavandero, S., & Castro, P. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.07.018 · Cited by 81 · see citing works
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BackgroundExcitatory Amino Acid Neurotoxicity
Gillessen, T., Budd, S. L., & Lipton, S. A. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0123-7_1 · Cited by 79 · see citing works
Cellular defenses against excitotoxic insults
Sapolsky, R. M. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00203.x · Cited by 79 · see citing works
“Commensurate with this, such uptake potently stimulates enzymes of oxidative phosphorylation (McCormack and Denton 1993).”
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Aydin, J., Andersson, D. C., Hänninen, S. L., Wredenberg, A., Tavi, P., Park, C. B., Larsson, N.-G., Bruton, J. D., & Westerblad, H. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddn355 · Cited by 75 · see citing works
Measurements of mitochondrial calcium in vivo
Pozzan, T., & Rudolf, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.11.012 · Cited by 75 · see citing works
The mechanism of MICU-dependent gating of the mitochondrial Ca2+uniporter
Garg, V., Suzuki, J., Paranjpe, I., Unsulangi, T., Boyman, L., Milescu, L. S., Lederer, W. J., & Kirichok, Y. (2021) · eLife · doi:10.7554/elife.69312 · Cited by 72 · see citing works
Im, Y. J., Perera, I. Y., Brglez, I., Davis, A. J., Stevenson, J. M., Phillippy, B. Q., Johannes, E., Allen, N. S., & Boss, W. F. (2007) · The Plant Cell · doi:10.1105/tpc.107.051367 · Cited by 71 · see citing works
“Changes in cytosolic calcium can directly affect mitochondria and stimulate respiration (McCormack et al., 1990; McCormack and Denton, 1993).”
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Booth, D. M., Mukherjee, R., Sutton, R., & Criddle, D. N. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3983 · Cited by 67 · see citing works
Marcu, R., Wiczer, B. M., Neeley, C. K., & Hawkins, B. J. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00068-14 · Cited by 62 · see citing works
“dehydrogenase, and oxoglutarate dehydrogenase (2) to speed mitochondrial NADH production (7, 29).”
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Guillet, V., Chevrollier, A., Cassereau, J., Letournel, F., Guéguen, N., Richard, L., Desquiret‐Dumas, V., Verny, C., Procaccio, V., Amati‐Bonneau, P., et al. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.11.004 · Cited by 61 · see citing works
Luz, A. L., Godebo, T. R., Smith, L. L., Leuthner, T. C., Maurer, L. L., & Meyer, J. N. (2017) · Toxicology · doi:10.1016/j.tox.2017.05.018 · Cited by 58 · see citing works
“For example, posttranslation modifications (Hofer and Wenz 2014) or positive allosteric regulation (Das and Harris 1990; McCormack and Denton 1994) of OXPHOS may be playing a role; however, additional work is required to test this.”
BackgroundMitochondrial Protection by PARP Inhibition
Gallyas, F., & Sümegi, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082767 · Cited by 58 · see citing works
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BackgroundSingle Channel Characterization of the Mitochondrial Ryanodine Receptor in Heart Mitoplasts
Ryu, S.-Y., Beutner, G., Kinnally, K. W., Dirksen, R. T., & Sheu, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.245597 · Cited by 57 · see citing works
Kovacs, R., Schuchmann, S., Gabriel, S., Kardos, J., & Heinemann, U. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01505.x · Cited by 56 · see citing works
“As a result, the turnover in the tricarboxylic acid cycle is increased, which provides enhanced supply of NADH for a subsequent increase of ATP production (Duchen, 1992, 1999; McCormack & Denton, 1993; Bernardi, 1999; Schuchmann et al., 1999).”
BackgroundLosano, J. D. D. A., Angrimani, D. D. S. R., Leite, R. F., da Silva, B. D. C. S., Barnabé, V. H., & Nichi, M. (2018) · Zygote · doi:10.1017/s0967199418000242 · Cited by 54 · see citing works
Mitochondrial VDAC, the Na+/Ca2+ Exchanger, and the Ca2+ Uniporter in Ca2+ Dynamics and Signaling
Shoshan‐Barmatz, V., & De, S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55858-5_13 · Cited by 56 · see citing works
Gao, P., Yang, W., & Sun, L. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3120539 · Cited by 57 · see citing works
“Constitutive ERto-mitochondria Ca transfer throughMAMs is essential for the maintenance of optimal mitochondrial bioenergetics under physiological conditions [105], because Ca uptake by the mitochondria can facilitate the TCA cycle and oxidative phosphorylation at several sites, including at ATP synthase [106], α-keto…”
BackgroundAdiele, R. C., Stevens, D., & Kamunde, C. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs091 · Cited by 54 · see citing works
Heinemann, U., Buchheim, K., Gabriel, S., Kann, O., Kovacs, R., & Schuchmann, S. (2002) · Progress in brain research · doi:10.1016/s0079-6123(02)35019-2 · Cited by 53 · see citing works
Calcium dynamics: analyzing the Ca2+ regulatory network in intact cells
Friel, D. D., & Chiel, H. J. (2007) · Trends in Neurosciences · doi:10.1016/j.tins.2007.11.004 · Cited by 53 · see citing works
Ferreira, J. J., Cassina, A., Irigoyen, P., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102176 · Cited by 47 · see citing works
“Mitochondrial [Ca2+] is considered a central regulator of oxidative phosphorylation by mediating NADH production and controlling activity of pyruvate dehydrogenase, isocitrate dehydrogenase, and α-ketoglutarate dehydrogenase [8,40].”
BackgroundMolecular and biochemical regulation of skeletal muscle metabolism
Zumbaugh, M. D., Johnson, S., Shi, T. H., & Gerrard, D. E. (2022) · Journal of Animal Science · doi:10.1093/jas/skac035 · Cited by 53 · see citing works
Mitochondria-mediated damage to dopaminergic neurons in Parkinson's disease (Review)
Liu, X., Wang, Y., Yu, X., Li, D., & Li, G. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3255 · Cited by 45 · see citing works
“Ca2+ plays a crucial role in mitochondrial metabolism through the activation of numerous mitochondrial enzymes (88,89).”
Benjamin, I. J., Guo, Y., Sathyanarayanan, S., et al. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01363.2006 · Cited by 45 · see citing works
“Since calcium is an important physiological stimulus for ATP synthesis (2, 15, 20, 21), then the abrogation of calcium signaling in DKO is predicted to decrease mitochondrial F1F0 ATP synthase.”
BackgroundKaram, C. N., Yi, J., Xiao, Y., Dhakal, K. R., Zhang, L., Li, X., Manno, C. D., Xu, J., Li, K., Cheng, H., et al. (2017) · Skeletal Muscle · doi:10.1186/s13395-017-0123-0 · Cited by 42 · see citing works
Calcium influx through the mitochondrial calcium uniporter holocomplex, MCUcx
Boyman, L., Greiser, M., & Lederer, W. J. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.10.015 · Cited by 42 · see citing works
“Our findings that [Ca]m partly controls ATP production by the mitochondria through only a few pivotal regulatory sites is new and is contrary to the large number of earlier publications that hypothesized many [Ca]m-sensitive regulatory sites [27-38].”
BackgroundResultMoon, S. H., Jenkins, C. M., Kiebish, M. A., Sims, H. F., Mancuso, D. J., & Gross, R. W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.373654 · Cited by 39 · see citing works
“resulting in TCA cycle activation (74,75) and stimulation of oxidative phosphorylation) are well known (76,77), mitochondrial Ca overload has been demonstrated to result in the generation of toxic reactive oxygen species (ROS) by accelerating uncoupling and the loss of antioxidants such as reduced glutathione after mP…”
BackgroundPérez-Liébana, I., Juaristi, I., González‐Sánchez, P., González-Moreno, L., Rial, E., Podunavac, M., Zakarian, A., Molgó, J., Vallejo‐Illarramendi, A., Mosqueira‐Martín, L., et al. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.1463-21.2022 · Cited by 37 · see citing works
Peruzzo, R., Costa, R., Bachmann, M., Leanza, L., & Szabó, I. (2020) · Cancers · doi:10.3390/cancers12092574 · Cited by 41 · see citing works
“The Krebs cycle enzymes α-ketoglutarate dehydrogenase and isocitrate dehydrogenase, as well as pyruvate dehydrogenase, are all Ca2+-dependent enzymes [40], thus also a mild increase in mitochondrial [Ca2+] results in elevated generation of ATP [41].”
BackgroundCarmichael, K., Sullivan, B. T., Lopez, E., Sun, L., & Cai, H. (2021) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2021.07 · Cited by 46 · see citing works
Mitochondria and calcium signaling in embryonic development
Cao, X., & Chen, Y. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.12.014 · Cited by 37 · see citing works
Hacker, K., & Medler, K. F. (2008) · Journal of Neurophysiology · doi:10.1152/jn.90534.2008 · Cited by 37 · see citing works
Molecular and Cellular Biology of Neuroprotection in the CNS
Alzheimer, C., Neuroprotection, O., Alzheimer, C., & Alzheimer, E. C. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0123-7 · Cited by 37 · see citing works
Alcohol Withdrawal and Cerebellar Mitochondria
Jung, M. E. (2014) · The Cerebellum · doi:10.1007/s12311-014-0598-8 · Cited by 35 · see citing works
“Ca activates enzymes of TCA cycle such as pyruvate dehydrogenase and α-ketoglutarate dehydrogenase [44] and helps provide electrons to the electron transport chain for ATP generation.”
Koo, B., Hong, D., Hong, H., Lim, H. K., Hoe, K., Won, M., Kim, Y., Berkowitz, D. E., & Ryoo, S. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0262-y · Cited by 34 · see citing works
Mitochondrial inhibitors activate influx of external Ca2+ in sea urchin sperm
Ardón, F., Rodríguez‐Miranda, E., Beltrán, C., Hernández‐Cruz, A., & Darszon, A. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.10.003 · Cited by 34 · see citing works
Lebrecht, D., Kirschner, J., Geist, A., Haberstroh, J., & Walker, U. A. (2009) · Cardiovascular Pathology · doi:10.1016/j.carpath.2009.06.006 · Cited by 34 · see citing works
Levine, M. S., Klapstein, G. J., Koppel, A. B., Gruen, E., Cepeda, C., Vargas, M. E., Jokel, E. S., Carpenter, E. M., Zanjani, H., Hurst, R. S., et al. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19991115)58:4 · Cited by 351 · see citing works
Sims, N. R. (1995) · Metabolic Brain Disease · doi:10.1007/bf02081026 · Cited by 33 · see citing works
MK801 decreases glutamate release and oxidative metabolism during hypoglycemic coma in piglets
Ichord, R., Johnston, M. V., & Traystman, R. J. (2001) · Developmental Brain Research · doi:10.1016/s0165-3806(01)00161-4 · Cited by 29 · see citing works
Lysosomal TRPML1 regulates mitochondrial function in hepatocellular carcinoma cells
Siow, W. X., Kabiri, Y., Tang, R., et al. (2022) · Journal of Cell Science · doi:10.1242/jcs.259455 · Cited by 28 · see citing works
“Mitochondrial Ca 2+ is important for the generation of ATP in these organelles (Hansford and Zorov, 1998; McCormack and Denton, 1993); nevertheless, Ca 2+ overloading is dangerous.”
Sahdeo, S., Tomilov, A. A., Komachi, K., Iwahashi, C., Datta, S., Hughes, O., Hagerman, P. J., & Cortopassi, G. A. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.07.002 · Cited by 28 · see citing works
“Thus gallamine-mediated inhibition of this pathway would lead to increased calcium release and potential mitochondrial uptake of calcium (McCormack and Denton, 1993).”
BackgroundMitochondrial Na+/Ca2+ exchanger, a new target for neuroprotection in rat hippocampal slices
Nicolau, S. M., Egea, J., López, M. G., & Garcı́a, A. G. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.028 · Cited by 26 · see citing works
Tominaga, M., Kurihara, H., Honda, S., Amakawa, G., Sakai, T., & Tomooka, Y. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03554.x · Cited by 26 · see citing works
Coupling of Electrical and Metabolic Activity During Epileptiform Discharges
Heinemann, U., Buchheim, K., Gabriel, S., et al. (2002) · Epilepsia · doi:10.1046/j.1528-1157.43.s.5.15.x · Cited by 24 · see citing works
Baron, K. T., Wang, G. J., Padua, R. A., Campbell, C., & Thayer, S. A. (2003) · Brain Research · doi:10.1016/j.brainres.2003.09.022 · Cited by 24 · see citing works
Nutrient sensing: TOR's Ragtime
Meijer, A. J., & Codogno, P. (2008) · Nature Cell Biology · doi:10.1038/ncb0808-881 · Cited by 23 · see citing works
Role of mitochondria in the immune response to cancer: a central role for Ca2+
Degasperi, G. R., Velho, J. A., Zecchin, K. G., de Souza, C. T., Velloso, L. A., Borecký, J., Castilho, R. F., & Vercesi, A. E. (2006) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-006-9000-y · Cited by 23 · see citing works
Glutathionylation of the L-type Ca2+ Channel in Oxidative Stress-Induced Pathology of the Heart
Johnstone, V., & Hool, L. C. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151019203 · Cited by 21 · see citing works
Carvalho, R. A., Rodrigues, T. B., Zhao, P., Jeffrey, F. M. H., Malloy, C. R., & Sherry, A. D. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00976.2003 · Cited by 21 · see citing works
Chaperones vs. oxidative stress in the pathobiology of ischemic stroke
Soldatov, V. O., Venediktov, A. A., Белых, А. Е., Piavchenko, G. A., Naimzada, M. D., Ogneva, N., Kartashkina, N. L., & Bushueva, O. Y. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1513084 · Cited by 22 · see citing works
The Effect Of NO Donor on Calcium Uptake and Reactive Nitrogen Species Production in Mitochondria
Ov, A., Kotsiuruba, A., Korkach, Y. P., Kolchinskaya, L. I., Nosar, V. I., Gavenauskas, B. L., Serebrovska, Z. O., Im, M., & Sagach, V. F. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000445616 · Cited by 20 · see citing works
Changes in mitochondrial functionality and calcium uptake in hypertensive rats as a function of age
Calderón‐Cortés, E., Cortés‐Rojo, C., Clemente‐Guerrero, M., et al. (2008) · Mitochondrion · doi:10.1016/j.mito.2008.04.005 · Cited by 20 · see citing works
“Accordingly, [Ca2+]i, is a second-messenger, implicated in the action of growth factors, hormones via transmitting signals to various kinases and enzymes (McCormack and Denton, 1993; Brini, 2003).”
BackgroundSpecific cyprinid HIF isoforms contribute to cellular mitochondrial regulation
Chen, J., Guan, L., Zou, M., He, S., Li, D., & Chi, W. (2020) · Scientific Reports · doi:10.1038/s41598-020-74210-w · Cited by 19 · see citing works
Hepatitis C virus, mitochondria and auto/mitophagy: Exploiting a host defense mechanism
Ruggieri, V. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i10.2624 · Cited by 19 · see citing works
Ammini, C. V., & Hauswirth, W. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6265 · Cited by 19 · see citing works
Harihar, S., & Welch, D. R. (2023) · Cancer and Metastasis Reviews · doi:10.1007/s10555-023-10090-6 · Cited by 18 · see citing works
“Several mitochondrial enzymes, α-ketoglutarate dehydrogenase, isocitrate dehydrogenase, and pyruvate dehydrogenase are calcium dependent [156]; therefore, by increasing mitochondrial calcium sequestration, KISS1 expression may promote tumor cell metabolic shift toward the Krebs cycle and OXPHOS.”
BackgroundRegulation of neuronal energy metabolism by calcium: Role of MCU and Aralar/malate-aspartate shuttle
del Arco, A., González-Moreno, L., Pérez-Liébana, I., et al. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119468 · Cited by 17 · see citing works
Mechanisms of Skeletal Muscle Weakness
Westerblad, H., Place, N., & Yamada, T. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-6366-6_16 · Cited by 16 · see citing works
- Authors
- McCormack, J. G., & Denton, R. M.
- Affiliations
- Heriot-Watt University (GB)
- Venue
- Developmental Neuroscience
- Publisher
- S. Karger AG
- Published
- 1994-08-18
- Volume
- 15
- Issue
- 3-5
- Pages
- 165-173
- ISSN
- 0378-5866 (ISSN-L)
- 1421-9859
- OpenAlex
- W1986720672
- Cited by
- 150
- References
- 0
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 5 · 2023: 5 · 2022: 6 · 2021: 5 · 2020: 8 · 2019: 4 · 2018: 3 · 2017: 9 · 2016: 6 · 2014: 7 · 2013: 3 · 2012: 5
- FWCI
- 1.14
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Developmental Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mitochondrial calcium transport, mitochondrial calcium, energy metabolism, inner mitochondrial membrane, oxidative phosphorylation, ATP synthase, intracellular calcium, brain mitochondria
- MeSH terms
- Animals, Biological Transport, Calcium, Energy Metabolism, Humans, Mitochondria
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