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Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function
Open accessAbstract
Mitochondria play a central role in energy metabolism, Ca2+ signalling, aging and cell death. To control cytosolic or mitochondrial Ca2+ concentration, mitochondria possess several Ca2+-transport systems across the inner membrane. However, the pathway for Ca2+ crossing the outer membrane has not been directly addressed. We report that purified voltage-dependent anion channel (VDAC) reconstituted into lipid bilayers or liposomes is highly permeable to Ca2+. VDAC contains Ca2+-binding sites that bind Ruthenium Red (RuR), La3+ and that RuR completely closed VDACs in single or multichannel experiments. Energized, freshly prepared mitochondria accumulate Ca2+ (500–700nmol/mg of protein), and subsequently released it. The release of Ca2+ is accompanied by cyclosporin A-inhibited swelling, suggesting activation of permeability transition pore (PTP). RuR and ruthenium amine binuclear complex, when added to mitochondria after Ca2+ accumulation has reached a maximal level and before PTP is activated, prevented the release of Ca2+ and the accompanied mitochondrial swelling. RuR also prevented PTP opening promoted by atractyloside, an adenine nucleotide translocase inhibitor. These results suggest that VDAC, located in the mitochondrial outer membrane, controls Ca2+ transport into and from the mitochondria, and that the inhibition of Ca2+ uptake by RuR and La3+ may result from their interaction with VDAC Ca2+-binding sites. Inhibition of PTP opening or assembly by RuR and ruthenium amine binuclear complex suggest the involvement of VDAC in PTP activity and/or regulation. The permeability of VDAC to Ca2+ and its binding of Ca2+, suggest that VDAC has a role in regulation of the mitochondrial Ca2+ homoeostasis.
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VDAC in the outer mitochondrial membrane is important for Ca2+ in- and outflux of mitochondria.
“It has been reported that VDAC located in the outer mitochondrial membrane is important for the in-and outflux of Ca 2ϩ of the mitochondria (43)”
From Simvastatin Effects on Skeletal Muscle (2013) · cites this paper as [43]
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Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413
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BackgroundMethodMitochondrial creatine kinase in human health and disease
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Self-citationChemotherapy: targeting the mitochondrial cell death pathway
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Tarze, A., Deniaud, A., Bras, M. L., Maillier, E., Mollé, D., Larochette, N., Zamzami, N., Jan, G., Kroemer, G., & Brenner, C. (2006) · Oncogene · doi:10.1038/sj.onc.1210074 · Cited by 354
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Self-citationThe expression level of the voltage-dependent anion channel controls life and death of the cell
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“The MCU inhibitors ruthenium red and Ru360 are known to specifically interact with the Ca2 binding site in VDAC (34, 35).”
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Self-citationSilencing VDAC1 Expression by siRNA Inhibits Cancer Cell Proliferation and Tumor Growth In Vivo
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Self-citationVDAC regulation of mitochondrial calcium flux: From channel biophysics to disease
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BackgroundSelf-citationThe regulation of OXPHOS by extramitochondrial calcium
Gellerich, F. N., Gizatullina, Z. Z., Trumbeckaitė, S., Nguyen, H. P., Pallas, T., Arandarčikaitė, O., Vielhaber, S., Seppet, E. K., & Striggow, F. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.005 · Cited by 129
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CGI1746 targets σ1R to modulate ferroptosis through mitochondria-associated membranes
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“VDAC1 located at ER–mitochondria contact sites mediates Ca 2+ transfer into the intermembrane space from the high Ca 2+ microdomain formed by IP 3 R 36,37 .”
Subcellular localization of VDAC in mitochondria and ER in the cerebellum
Shoshan‐Barmatz, V., Zalk, R., Gincel, D., & Vardi, N. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.02.009 · Cited by 109
“The voltage-dependent anion channel (VDAC) controls the passage of adenine nucleotides [1], Ca + [2], and other metabolites [3] into and from mitochondria.”
BackgroundSelf-citationCa2+-mediated regulation of VDAC1 expression levels is associated with cell death induction
Algor, S. W., Keinan, N., Ben-Hail, D., Arif, T., & Shoshan‐Barmatz, V. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.03.021 · Cited by 108
Self-citationNahon, E., Israelson, A., Abu-Hamad, S., & Shoshan-Barmatz, V. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.020 · Cited by 101
“However, these effects of fluoxetine on mitochondrial activities may result from interacting with VDAC and decreasing its conductance as a channel providing passage for Ca [19],”
BackgroundMethodInfluentialSelf-citationProbing the Outer Mitochondrial Membrane in Cardiac Mitochondria with Nanoparticles
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“CATR binds the C-state of the adenine nucleotide translocator and stimulates the PT pore (6,47,48); whereas alamethicin forms giant pores through both mitochondrial membranes (49,50).”
BackgroundVoltage-dependent anion channels are a key factor of male fertility
Kwon, W., Park, Y.-J., Mohamed, E. A., & Pang, M. (2012) · Fertility and Sterility · doi:10.1016/j.fertnstert.2012.09.021 · Cited by 99
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“In order to transfer Ca2+, a complex is formed between the ER-resident IP3R and voltagedependent anion channel 1 (VDAC1) in the outer mitochondrial membrane [161,163,164].”
BackgroundMitochondrial calcium channels
Hoppe, U. C. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.04.017 · Cited by 95
“The voltage dependent anion channel (VDAC) reconstituted in lipid bilayers was shown to conduct Ca in addition to monovalent ions [16].”
BackgroundGonzalez–Gronow, M., Kalfa, T. A., Johnson, C. E., Gawdi, G., & Pizzo, S. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303172200 · Cited by 94
Liu, H., Yuan, L., Yang, X., & Wang, K. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(03)00072-3 · Cited by 95
Hu, H., Guo, L., Overholser, J. P., & Wang, X. (2022) · Cells · doi:10.3390/cells11193174 · Cited by 97
“VDAC1 was shown to be highly permeable to Ca2+, and contains a binding site for ruthenium red, thereby inhibiting channel opening [96,97].”
BackgroundEnlargement and Contracture of C2-Ceramide Channels
Siskind, L. J., Davoody, A., Lewin, N., Marshall, S., & Colombini, M. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74588-3 · Cited by 92
“La(13) is a known inhibitor of various types of channels and transporters (Takata et al., 1966; Reed and Bygrave, 1974; Armstrong and Cota, 1990; Sparagna et al., 1995; Colvin, 1998; Colvin et al., 2000; Gincel et al., 2001).”
BackgroundInfluentialAnion Channels of Mitochondria
Ponnalagu, D., & Singh, H. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_39 · Cited by 90
“All the cells from prokaryotes to eukaryotes maintain a cytosolic pH of ~7.2, with concentration of potassium ions (K+) many fold higher than sodium (Na+) Correspondence to: Harpreet Singh. uthor M anuscript A uthor M anuscript A uthor M anuscript and calcium (Ca2+) ions (Bose et al. 2015; Prindle et al. 2015).”
BackgroundInfluentialMultistep and multitask Bax activation
Ghibelli, L., & Diederich, M. F. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.08.003 · Cited by 84
“VDAC pore is regulated by physico-chemical mechanisms such as voltage, which is maintained by trans-membrane potential, and by molecular mechanisms including phosphorylation and binding by cytosolic proteins (Chen et al., 2010; Gincel et al., 2001).”
BackgroundMitochondria and Energetic Depression in Cell Pathophysiology
Seppet, E. K., Puurand, M., Peetsalu, A., Gizatullina, Z. Z., Nguyen, H. P., Vielhaber, S., Wussling, M. H. P., Trumbeckaitė, S., Arandarčikaitė, O., Jerzembek, D., et al. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10052252 · Cited by 84
Shoshan‐Barmatz, V., & Israelson, A. (2005) · The Journal of Membrane Biology · doi:10.1007/s00232-005-0749-4 · Cited by 83
“... [32, 80], in SR, the organometallic hexavalent dye RuR and ruthenium amine binuclear complex, Ru360, known to specifically interact with Ca 2+ -binding proteins [80], induce VDAC channel closure in a time-dependent manner, and stabilize the channel in a completelyclosed state (Fig. 2). Thus, VDAC, as Ca 2+ transpo…”
InfluentialSelf-citationBouyer, G., Cueff, A., Égée, S., Kmiecik, J., Maksimova, Y. D., Glogowska, E., Gallagher, P. G., & Thomas, S. L. Y. (2011) · Blood · doi:10.1182/blood-2011-01-329300 · Cited by 79
VDAC1-interacting anion transport inhibitors inhibit VDAC1 oligomerization and apoptosis
Ben-Hail, D., & Shoshan-Barmatz, V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.04.002 · Cited by 80
Self-citationMitochondrial calcium at the synapse
Datta, S., & Jaiswal, M. (2021) · Mitochondrion · doi:10.1016/j.mito.2021.04.006 · Cited by 73
Localization of the voltage-dependent anion channel-1 Ca2+-binding sites
Israelson, A., Abu‐Hamad, S., Zaid, H., Nahon, E., & Shoshan‐Barmatz, V. (2006) · Cell Calcium · doi:10.1016/j.ceca.2006.06.005 · Cited by 79
“Similar to RuR [7] and Ru360 [8], AzRu decreased the hannel conductance of purified VDAC reconstituted into a lanar lipid bilayer (Fig.”
InfluentialSelf-citationIntracellular Ca2 + Imbalance Critically Contributes to Paraptosis
Kim, E., Lee, D. M., Seo, M. J., Lee, H. J., & Choi, K. S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.607844 · Cited by 80
Sander, P., Gudermann, T. W., & Schredelseker, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020946 · Cited by 84
“This was based on several lines of evidence: (i) a Ca2+ induced shift in electrophoretic mobility of VDAC1, (ii) a blockade of the channel by La3+, which could be reversed by the addition of EGTA, and (iii) an inhibition of the channel by ruthenium derivatives such as RuR, Ru360 [3], or AzRu [56] that was reversed by…”
BackgroundMethodMitochondrial ryanodine receptors and other mitochondrial Ca2+ permeable channels
Ryu, S.-Y., Beutner, G., Dirksen, R. T., Kinnally, K. W., & Sheu, S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.032 · Cited by 80
“Both VDAC cationic and anionic conductance states are blocked by ruthenium red and lanthanides [60,68].”
BackgroundTikunov, A. P., Johnson, C. B., Pediaditakis, P., Markevich, N. I., Macdonald, J. M., Lemasters, J. J., & Holmuhamedov, E. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.01.008 · Cited by 74
Mitostasis, Calcium and Free Radicals in Health, Aging and Neurodegeneration
Godoy, J. A., Ríos, J. A., Picón-Pagès, P., Herrera-Fernández, V., Swaby, B., Crepin, G., Vicente, R., Fernández‐Fernández, J. M., & Muñoz, F. J. (2021) · Biomolecules · doi:10.3390/biom11071012 · Cited by 73
“The alteration of MAMs yields to the lack of Ca 2+ homeostasis and mitochondrial biogenesis impairment [97,116,120,121].”
BackgroundFunctional interaction of endothelial nitric oxide synthase with a voltage-dependent anion channel
Sun, J., & Liao, J. K. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202260999 · Cited by 72
C-terminal Lysines Determine Phospholipid Interaction of Sarcomeric Mitochondrial Creatine Kinase
Schlattner, U., Gehring, F., Vernoux, N., Tokarska-Schlattner, M., Neumann, D., Marcillat, O., Vial, C., & Wallimann, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314158200 · Cited by 71
Antonenkov, V. D., Isomursu, A., Mennerich, D., Vapola, M. H., Weiher, H., Kietzmann, T., & Hiltunen, J. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.608083 · Cited by 69
“An estimation of the Ca(2) /Cl permeability ratio was done as described (20).”
MethodJang, B., Kim, E., Choi, J.-K., et al. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080388 · Cited by 70
VDAC Modulation of Cancer Metabolism: Advances and Therapeutic Challenges
Heslop, K. A., Milesi, V., & Maldonado, E. N. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.742839 · Cited by 77
Peroxisomal plant metabolism – an update on nitric oxide, Ca2+ and the NADPH recycling network
Corpas, F. J., & Barroso, J. B. (2017) · Journal of Cell Science · doi:10.1242/jcs.202978 · Cited by 65
“Ca can move through membranes using voltage-dependent anion channels, among others (Gincel et al., 2001; Jammes et al., 2011).”
Background
Metadata
- Authors
- GINCEL, D., ZAID, H., & SHOSHAN-BARMATZ, V.
- Affiliations
- Ben-Gurion University of the Negev (IL)
- Department of Life Sciences and Zlotowski Center for Neuroscience, Ben Gurion University of the Negev, Beer Sheva, P.O.B. 653, 84105 Israel
- ORCID
- ZAID, Hilal
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2001-08-08
- Volume
- 358
- Issue
- 1
- Pages
- 147-155
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1222042
- OpenAlex
- W2012135330
- Cited by
- 396
- References
- 0
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 15 · 2023: 9 · 2022: 18 · 2021: 28 · 2020: 14 · 2019: 12 · 2018: 12 · 2017: 21 · 2016: 22 · 2015: 9 · 2014: 19 · 2013: 14 · 2012: 20
- FWCI
- 4.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (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 › Ion channel regulation and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- voltage-dependent anion channel, mitochondrial outer membrane, calcium transport, calcium binding sites, ruthenium red, lanthanum, mitochondrial permeability transition pore, mitochondrial calcium homeostasis, mitochondrial swelling, cyclosporine, atractyloside, adenine nucleotide translocase, calcium release
- MeSH terms
- Animals, Anions, Binding Sites, Calcium, Dose-Response Relationship, Drug, Electrophoresis, Polyacrylamide Gel, Humans, Intracellular Membranes, Ion Channels, Kinetics, Lanthanum, Lipid Bilayers, Liposomes, Mitochondria, Mitochondria, Liver, Models, Biological, Protein Binding, Ruthenium Red, Time Factors, Models, Statistical, Signal Transduction, Cyclosporine, Porins, Voltage-Dependent Anion Channels, Rats
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