The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
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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Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
Calcium, ATP, and ROS: a mitochondrial love-hate triangle
Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575
“Ca(2) , recent studies suggest that the outer membrane voltagedependent anion channel (VDAC) is a ruthenium red (RuRed)sensitive Ca(2) channel and thus serves to regulate Ca(2) entry to mitochondrial intermembrane space (60).”
BackgroundChaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
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
“Based on previous observations (Gincel et al., 2001; Csordas et al., 2002; Rapizzi et al., 2002; Israelson et al., 2005), we used VDAC1 as the start point for proteomic search of interacting proteins and for unraveling the molecular basis of mitochondrial Ca2+ homeostasis.”
BackgroundMethodMitochondrial creatine kinase in human health and disease
Schlattner, U., Tokarska-Schlattner, M., & Wallimann, T. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.09.004 · Cited by 641
“Possibly, the calcium signal is perceived through the interaction partner VDAC, where a specific Ca binding site has been identified [87].”
The mitochondrial permeability transition from in vitro artifact to disease target
Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05213.x · Cited by 627
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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