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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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“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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“coli, purified (Figure 2M) and reconstituted into a PLB as described previously (Gincel et al., 2001).”
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“Ca 2 + plays a critical role in connecting the ER and mitochondria, where it is released in the ER through ITPRs and then transported to the outer mitochondrial membrane via the voltage-dependent anion channel (VDAC) [86].”
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“…(of which there are 3 subtypes (VDAC1-3)); although VDAC1 is predominantly implicated in mitochondrial Ca2+ dynamics, it was shown to selectively co-immunoprecipitate with inositol 1,4,5-trisphosphate receptors (IP3R; see later)(De Stefani et al., 2012; Gincel et al., 2001, Rapizzi et al., 2002).”
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“Nonetheless, the mammalian VDAC contains Ca2+ binding sites (Gincel et al. 2001).”
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“outer membrane and because of their location within the outer mitochondrial membrane, VDACs are the first regulators of Ca uptake into the mitochondria [115].”
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“56 – 59 The significant increase in cell viability and suppression of vacuolation observed after VDAC inhibition suggested that the Ca 2 + influx induced by the cannabinoid ratio could largely be attributed to VDAC modulation.”
BackgroundExploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore
Hoogerheide, D. P., Rostovtseva, T. K., & Bezrukov, S. M. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183643 · Cited by 20
Biophysical Properties of the Apoptosis-Inducing Plasma Membrane Voltage-Dependent Anion Channel
Akanda, N., & Elinder, F. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.080028 · Cited by 20
“This has also been reported for the VDACmt (22) and supports the idea that the VDACpl and the VDACmt are the same channel.”
BackgroundTrishna, S., Lavon, A., Shteinfer‐Kuzmine, A., Dafa-Berger, A., & Shoshan‐Barmatz, V. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.07.008 · Cited by 20
“Purified VDAC1 was reconstituted into a PLB, and single and multiple channel current recording and data analysis were carried out, as described previously.(97) Briefly, a PLB was prepared, and after one or a few channels were inserted into it, excess protein was”
Self-citationCalcium Flux across Plant Mitochondrial Membranes: Possible Molecular Players
Carraretto, L., Checchetto, V., Bortoli, S. D., Formentin, E., Costa, A., Szabó, I., & Teardo, E. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00354 · Cited by 18
“…as demonstrated both in vitro and in vivo for the mammalian Frontiers in Plant Science | www.frontiersin.org 2 March 2016 | Volume 7 | Article 354 protein (Gincel et al., 2001; Rapizzi et al., 2002; Bathori et al., 2006; Israelson et al., 2007; Rizzuto et al., 2009; Shoshan-Barmatz et al., 2010).”
BackgroundCalcium Signaling in the Liver
Amaya, M. J., & Nathanson, M. H. (2012) · Comprehensive physiology · doi:10.1002/cphy.c120013 · Cited by 111
Dyslipidemia alters sperm maturation and capacitation in LXR-null mice
Whitfield, M., Guiton, R., Rispal, J., Acar, N., Kocer, A., Drevet, J. R., & Saez, F. (2017) · Reproduction · doi:10.1530/rep-17-0467 · Cited by 16
Dong, S., Zhao, Y., Liu, H., Yang, X., & Wang, K. (2009) · BioMetals · doi:10.1007/s10534-009-9244-1 · Cited by 18
“(Gincel et al. 2001; Zoratti and Szabo 1995).”
Advances and Challenges in Modeling Cannabidiol Pharmacokinetics and Hepatotoxicity
Beers, J. L., Zhou, Z., & Jackson, K. D. (2024) · Drug Metabolism and Disposition · doi:10.1124/dmd.123.001435 · Cited by 18
VDAC blockage by phosphorothioate oligonucleotides and its implication in apoptosis
Tan, W. (2012) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.12.032 · Cited by 17
Kniss-James, A. S., Rivet, C. A., Chingozha, L., Lu, H., & Kemp, M. L. (2017) · Integrative Biology · doi:10.1039/c6ib00186f · Cited by 16
Leggio, L., Guarino, F., Magrì, A., Accardi, R., Reina, S., Specchia, V., Damiano, F., Tomasello, M. F., Tommasino, M., & Messina, A. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-23730-7 · Cited by 17
Nguyen, T. M. D., Klett, D., Filliatreau, L., & Combarnous, Y. (2019) · PLoS ONE · doi:10.1371/journal.pone.0217519 · Cited by 16
“These FLX effects on mitochondrial activities may also result from interaction with Voltage-dependent anion channels (VDAC) and conductance decreasing of a Ca channel [29] adenine nucleotides [30], other metabolites [31–32], as well as preventing PTP opening by preventing the release of accumulated Ca and by swelling…”
BackgroundMader, A., Abu‐Hamad, S., Arbel, N., Gutierr-Asuilar, M., & Shoshan‐Barmatz, V. (2010) · Biochemical Journal · doi:10.1042/bj20091338 · Cited by 13
Self-citationImaging mitochondrial calcium dynamics in the central nervous system
Serrat, R., Oliveira-Pinto, A., Marsicano, G., & Pouvreau, S. (2022) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2022.109560 · Cited by 13
Implications of SGLT Inhibition on Redox Signalling in Atrial Fibrillation
Bode, D., Semmler, L., Oeing, C. U., Alogna, A., Schiattarella, G. G., Pieske, B. M., Heinzel, F. R., & Hohendanner, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115937 · Cited by 11
E as in Enigma: The Mysterious Role of the Voltage-Dependent Anion Channel Glutamate E73
Rister, A. B., Gudermann, T. W., & Schredelseker, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010269 · Cited by 10
“had reported that VDAC transports Ca2+ into mitochondria and that this transport is sensitive to ruthenium red (RuR) [50], the same group reported in 2007 that Ca2+ competes with 25 μM azido ruthenium (AzRu) for a binding site involving E73 and E202 in a dose-dependent manner with a half-maximal effect at 100 μM [23].”
BackgroundWieloch, T. W., Mattiasson, G., Hansson, M. J., & Elmér, E. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_25 · Cited by 11
Atakpa‐Adaji, P., Ivanova, A., Kujawa, K., & Taylor, C. W. (2024) · Journal of Cell Science · doi:10.1242/jcs.261728 · Cited by 10
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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