Cited by 287Alzheimer's disease research and treatmentsMitochondrial Function and PathologyDementia and Cognitive Impairment Research

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VDAC1, mitochondrial dysfunction, and Alzheimer’s disease

Shoshan-Barmatz, Varda, Nahon-Crystal, Edna, Shteinfer-Kuzmine, Anna, Gupta, Rajeev·2018·Pharmacological Research

DOI 10.1016/j.phrs.2018.03.010

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Abstract

Alzheimer's disease (AD) is an age-related neurodegenerative disorder. Although an accumulation of brain amyloid-β (Aβ) peptide and hyperphosphorylated tau protein have been implicated in the pathogenesis of AD, the etiology of the disease remains unclear. Mitochondrial dysfunction has been identified as an early event in AD pathogenesis and is reflected by reduced metabolism, disruption of Ca 2+ homeostasis, and increased levels of reactive oxygen species, lipid peroxidation, and apoptosis. The focus of this review is the involvement of mitochondrial dysfunction in AD, and specifically, the role of the voltage-dependent anion channel 1 (VDAC1), which has been linked to AD pathogenesis. VDAC1 is a multi-functional protein, expressed in the mitochondria and other cell compartments, including the plasma membrane. The protein regulates the main metabolic and energetic functions of the cell, including Ca 2+ homeostasis, oxidative stress, and mitochondria-mediated apoptosis. VDAC1 represents a hub protein that interacts with over 150 other proteins including phosphorylated tau, Aβ, and γ-secretase, and participates in their toxicity. The high levels of VDAC1 demonstrated post-mortem in the brains of AD patients and in amyloid precursor protein (APP) transgenic mice prompted the hypothesis that the protein may be associated with neuronal cell destruction since over-expression of VDAC1 triggers cell death. Thus, targeting mitochondrial dysfunction via VDAC1, to prevent this pro-apoptotic activity, could represent a novel strategy for inhibiting cell death. In addition, the review also discusses possible VDAC1 involvement in the link between AD and diabetes and the inverse association between cancer and AD.

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Rushworth, J. V., & Hooper, N. M. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/603052 · Cited by 234
The Voltage-Dependent Anion Channel: Characterization, Modulation, and Role in Mitochondrial Function in Cell Life and Death
Shoshan‐Barmatz, V., & Gincel, D. (2003) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:39:3:279 · Cited by 229
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Gradual Alteration of Mitochondrial Structure and Function by β-Amyloids: Importance of Membrane Viscosity Changes, Energy Deprivation, Reactive Oxygen Species Production, and Cytochrome c Release
Aleardi, A. M., Benard, G., Augereau, O., Malgat, M., Talbot, J.-C., Mazat, J., Letellier, T., Dachary-Prigent, J., Solaini, G., & Rossignol, R. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-6631-3 · Cited by 227
The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins
Abu-Hamad, S., Arbel, N., Calo, D., Arzoine, L., Israelson, A., Keinan, N., Ben-Romano, R., Friedman, O., & Shoshan-Barmatz, V. (2009) · Journal of Cell Science · doi:10.1242/jcs.040188 · Cited by 226
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Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
Zalk, R., Israelson, A., GARTY, E. S., Azoulay‐Zohar, H., & Shoshan‐Barmatz, V. (2005) · Biochemical Journal · doi:10.1042/bj20041356 · Cited by 226
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Hierarchical involvement of Bak, VDAC1 and Bax in cisplatin-induced cell death
Tajeddine, N., Galluzzi, L., Kepp, O., Hangen, E., Morselli, E., Senovilla, L., Araujo, N., Pinna, G., Larochette, N., Zamzami, N., et al. (2008) · Oncogene · doi:10.1038/onc.2008.63 · Cited by 217
Mitochondria in Neurodegeneration
Lezi, E., & Swerdlow, R. H. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_12 · Cited by 213
lncRNA H19/miR-675 axis regulates cardiomyocyte apoptosis by targeting VDAC1 in diabetic cardiomyopathy
Li, X., Wang, H., Yao, B., Xu, W., Chen, J., & Zhou, X. (2016) · Scientific Reports · doi:10.1038/srep36340 · Cited by 213
Early alterations in energy metabolism in the hippocampus of APPswe/PS1dE9 mouse model of Alzheimer's disease
Pedrós, I., Petrov, D., Allgaier, M., Sureda, F. X., Barroso, E., Beas‐Zárate, C., Auladell, C., Pallàs, M., Vázquez‐Carrera, M., Casadesús, G., et al. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.025 · Cited by 211
Mitochondria and Cell Bioenergetics: Increasingly Recognized Components and a Possible Etiologic Cause of Alzheimer's Disease
Swerdlow, R. H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4149 · Cited by 206
VDAC1: from structure to cancer therapy
Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 200
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Mitochondrial Dysfunction: The First Domino in Brain Aging and Alzheimer's Disease?
Leuner, K., Hauptmann, S., Abdel-Kader, R. M., Scherping, I., Keil, U., Strosznajder, J. B., Eckert, A., & Müller, W. E. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1763 · Cited by 195
The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis.
Vyssokikh, M. Y., & Brdiczka, D. G. (2003) · Acta Biochimica Polonica · doi:10.18388/abp.2003_3693 · Cited by 189
Role of Mitochondrial Amyloid-β in Alzheimer's Disease
Chen, J. X., & Yan, S. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100357 · Cited by 188
A brief overview of amyloids and Alzheimer's disease
Ow, S., & Dunstan, D. E. (2014) · Protein Science · doi:10.1002/pro.2524 · Cited by 188
Intracellular Amyloid-β1–42, but Not Extracellular Soluble Amyloid-β Peptides, Induces Neuronal Apoptosis
Kienlen-Campard, P., Miolet, S., Tasiaux, B., & Octave, J.-N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200887200 · Cited by 187
Uncovering the role of VDAC in the regulation of cell life and death
Shoshan‐Barmatz, V., Keinan, N., & Zaid, H. (2008) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-008-9147-9 · Cited by 186
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A Greek Tragedy: The Growing Complexity of Alzheimer Amyloid Precursor Protein Proteolysis
Andrew, R. J., Kellett, K. A. B., Thinakaran, G., & Hooper, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.746032 · Cited by 186
Mitochondrial alterations near amyloid plaques in an Alzheimer’s disease mouse model
Xie, H., Guan, J., Borrelli, L. A., Xu, J., Serrano-Pozo, A., & Bacskai, B. J. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1836-13.2013 · Cited by 185
The Supramolecular Assemblies of Voltage-dependent Anion Channels in the Native Membrane
Hoogenboom, B. W., Suda, K., Engel, A. H., & Fotiadis, D. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.073 · Cited by 183
Mediation of the antiapoptotic activity of Bcl-xL protein upon interaction with VDAC1 protein
Arbel, N., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.345918 · Cited by 179
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The Role of Mitochondrial Porins and the Permeability Transition Pore in Learning and Synaptic Plasticity
Weeber, E. J., Levy, M., Sampson, M. J., Anflous, K., Armstrong, D. L., Brown, S. E., Sweatt, J. D., & Craigen, W. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201649200 · Cited by 179
Voltage-dependent Anion Channel-1 (VDAC-1) Contributes to ATP Release and Cell Volume Regulation in Murine Cells
Okada, S. F., O’Neal, W. K., Huang, P., Nicholas, R. A., Ostrowski, L. E., Craigen, W. J., Lazarowski, E. R., & Boucher, R. C. (2004) · The Journal of General Physiology · doi:10.1085/jgp.200409154 · Cited by 179
Voltage-dependent Anion Channel 1-based Peptides Interact with Hexokinase to Prevent Its Anti-apoptotic Activity
Arzoine, L., Zilberberg, N., Ben-Romano, R., & Shoshan‐Barmatz, V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803614200 · Cited by 178
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Cancer and Neurodegeneration: Between the Devil and the Deep Blue Sea
Plun‐Favreau, H., Lewis, P. A., Hardy, J., Martins, L. M., & Wood, N. W. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001257 · Cited by 176
Voltage‐dependent anion‐selective channel (VDAC) in the plasma membrane
Pinto, V. D., Messina, A. A., Lane, D. J. R., & Lawen, A. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.02.049 · Cited by 174
Tauopathies with parkinsonism: clinical spectrum, neuropathologic basis, biological markers, and treatment options
Ludolph, A. C., Kassubek, J., Landwehrmeyer, G. B., Mandelkow, E., Mandelkow, E., Burn, D. J., Caparros-Lefebvre, D., Frey, K. A., de Yébenes, J. G., Gasser, T., et al. (2009) · European Journal of Neurology · doi:10.1111/j.1468-1331.2008.02513.x · Cited by 174
Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer’s disease
Ferrer, I. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9243-5 · Cited by 172
NMR Structural Investigation of the Mitochondrial Outer Membrane Protein VDAC and Its Interaction with Antiapoptotic Bcl-xL
Malia, T., & Wagner, G. (2006) · Biochemistry · doi:10.1021/bi061577h · Cited by 170
VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress
Shoshan-Barmatz, V., N. Maldonado, E., & Krelin, Y. (2017) · Cell Stress · doi:10.15698/cst2017.10.104 · Cited by 170
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Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity
Arbel, N., & Shoshan-Barmatz, V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082990 · Cited by 168
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VDAC is a conserved element of death pathways in plant and animal systems
Godbole, A., Varghese, J., Sarin, A., & Mathew, M. K. (2003) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(03)00102-2 · Cited by 165
Signaling pathway cross talk in Alzheimer’s disease
Godoy, J. A., Ríos, J. A., Zolezzi, J. M., Braidy, N., & Inestrosa, N. C. (2014) · Cell Communication and Signaling · doi:10.1186/1478-811x-12-23 · Cited by 165
Supramolecular Assembly of VDAC in Native Mitochondrial Outer Membranes
Gonçalves, R. P., Buzhynskyy, N., Prima, V., Sturgis, J. N., & Scheuring, S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.063 · Cited by 163
Convergence of Amyloid-β and Tau Pathologies on Mitochondria In Vivo
Eckert, A., Schulz, K. L., Rhein, V. F., & Götz, J. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8109-5 · Cited by 160
Diagnosis and biomarkers of predementia in Alzheimer's disease
Forlenza, O. V., Diniz, B. S., & Gattaz, W. F. (2010) · BMC Medicine · doi:10.1186/1741-7015-8-89 · Cited by 160
Characterization of human VDAC isoforms: A peculiar function for VDAC3?
Pinto, V. D., Guarino, F., Guarnera, A., Messina, A. A., Reina, S., Tomasello, M. F., Palermo, V., & Mazzoni, C. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.031 · Cited by 159
Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins
Shi, Y., Chen, J., Weng, C., Chen, R., Zheng, Y., Chen, Q., & Tang, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00871-4 · Cited by 158
VDAC1 Is a Transplasma Membrane NADH-Ferricyanide Reductase
Baker, M. A., Lane, D. J. R., Ly, J. D., Pinto, V. D., & Lawen, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311020200 · Cited by 158
Novel Compounds Targeting the Mitochondrial Protein VDAC1 Inhibit Apoptosis and Protect against Mitochondrial Dysfunction
Ben-Hail, D., Begas-Shvartz, R., Shalev, M., Shteinfer-Kuzmine, A., Gruzman, A., Reina, S., De Pinto, V., & Shoshan-Barmatz, V. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.744284 · Cited by 158
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The involvement of lipid rafts in Alzheimer's disease (Review)
Cordy, J. M., Cordy, J. M., Hooper, N. M., & Turner, A. J. (2006) · Molecular Membrane Biology · doi:10.1080/09687860500496417 · Cited by 157
Apoptosis is regulated by the VDAC1 N-terminal region and by VDAC oligomerization: release of cytochrome c, AIF and Smac/Diablo
Shoshan‐Barmatz, V., Keinan, N., Abu‐Hamad, S., Tyomkin, D., & Aram, L. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.03.003 · Cited by 155
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Brain-specific knockdown of miR-29 results in neuronal cell death and ataxia in mice
Roshan, R., Shridhar, S., Sarangdhar, M. A., Banik, A., Chawla, M., Garg, M., Singh, V. P., & Pillai, B. (2014) · RNA · doi:10.1261/rna.044008.113 · Cited by 149
Mitochondrial import and degradation of amyloid-β peptide
Pinho, C. M., Teixeira, P. F., & Glaser, E. G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.007 · Cited by 149
Amyloid beta-induced glycogen synthase kinase 3β phosphorylated VDAC1 in Alzheimer's disease: Implications for synaptic dysfunction and neuronal damage
Reddy, P. H. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.06.012 · Cited by 147
The voltage-dependent anion channel 1 mediates amyloid β toxicity and represents a potential target for Alzheimer disease therapy
Smilansky, A., Dangoor, L., Nakdimon, I., Ben-Hail, D., Mizrachi, D., & Shoshan-Barmatz, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691493 · Cited by 143
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Mitochondrial VDAC1: Function in Cell Life and Death and a Target for Cancer Therapy
Shoshan‐Barmatz, V., & Golan, M. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712798992110 · Cited by 142
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Cytochrome c release from isolated rat liver mitochondria can occur independently of outer-membrane rupture: possible role of contact sites
Doran, E., & Halestrap, A. P. (2000) · Biochemical Journal · doi:10.1042/bj3480343 · Cited by 140
Truncated tau and Aβ cooperatively impair mitochondria in primary neurons
Quintanilla, R. A., Dolan, P. J., Jin, Y. N., & Johnson, G. V. W. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.02.007 · Cited by 139
Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.
Dermietzel, R., Hwang, T. K., Buettner, R., Hofer, A., Dotzler, E., Kremer, M., Deutzmann, R., THINNES, F. P., Fishman, G. I., & Spray, D. C. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.2.499 · Cited by 139
Mitochondria and Neurodegeneration
Petrozzi, L., Ricci, G., Giglioli, N. J., Siciliano, G., & Mancuso, M. (2007) · Bioscience Reports · doi:10.1007/s10540-007-9038-z · Cited by 139
Voltage‐dependent anion channel 1 is involved in endostatin‐induced endothelial cell apoptosis
Yuan, S., Fu, Y., Wang, X., Shi, H., Huang, Y., Song, X., Li, L., Song, N., & Luo, Y. (2008) · The FASEB Journal · doi:10.1096/fj.08-107417 · Cited by 137
Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics
Shoshan‐Barmatz, V., Krelin, Y., Shteinfer‐Kuzmine, A., & Arif, T. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00154 · Cited by 135
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Enhanced Expression of the Voltage-Dependent Anion Channel 1 (VDAC1) in Alzheimer's Disease Transgenic Mice: An Insight into the Pathogenic Effects of Amyloid-β
Cuadrado‐Tejedor, M., Vilariño, M., Cabodevilla, F., Río, J. D., Frechilla, D., & Pérez‐Mediavilla, A. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100966 · Cited by 134
Nuclear but not mitochondrial‐encoded oxidative phosphorylation genes are altered in aging, mild cognitive impairment, and Alzheimer's disease
Mastroeni, D., Khdour, O. M., Delvaux, E., Nolz, J., Olsen, G., Berchtold, N. C., Cotman, C. W., Hecht, S. M., & Coleman, P. D. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.003 · Cited by 134
Insulin dysfunction and Tau pathology
Khoury, N. B. E., Gratuze, M., Papon, M.-A., Bretteville, A., & Planel, E. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00022 · Cited by 133
Mitochondrial dysfunction and accumulation of the β-secretase-cleaved C-terminal fragment of APP in Alzheimer's disease transgenic mice
Devi, L., & Ohno, M. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.09.001 · Cited by 133
Connecting Alzheimer's disease to diabetes: Underlying mechanisms and potential therapeutic targets
Vieira, M. N. N., Lima‐Filho, R. A. S., & Felice, F. G. D. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.11.014 · Cited by 133
Altered Mitochondrial Sensitivity for ADP and Maintenance of Creatine-stimulated Respiration in Oxidative Striated Muscles from VDAC1-deficient Mice
Anflous, K., Armstrong, D. D., & Craigen, W. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006587200 · Cited by 132
Insights into Mitochondrial Dysfunction: Aging, Amyloid-β, and Tau–A Deleterious Trio
Schmitt, K., Grimm, A., Wilkaniec, A., Strosznajder, J. B., Götz, J., & Eckert, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4400 · Cited by 132
MicroRNA-7 Regulates the Function of Mitochondrial Permeability Transition Pore by Targeting VDAC1 Expression
Chaudhuri, A., Choi, D. C., Kabaria, S., Tran, A., & Junn, E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691352 · Cited by 132
Evidence for secretory pathway localization of a voltage-dependent anion channel isoform
Buettner, R., Papoutsoglou, G., Scemes, E., Spray, D. C., & Dermietzel, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3201 · Cited by 131
Metformin promotes tau aggregation and exacerbates abnormal behavior in a mouse model of tauopathy
Barini, E., Antico, O., Zhao, Y., Asta, F., Tucci, V., Catelani, T., Marotta, R., Xu, H., & Gasparini, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0082-7 · Cited by 126
A Mitocentric View of Alzheimer's Disease Suggests Multi-Faceted Treatments
Gibson, G. E., & Shi, Q. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100336 · Cited by 124
New perspectives on the role of tau in Alzheimer's disease. Implications for therapy
Medina, M., & Ávila, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.013 · Cited by 123
Porin Is Present in the Plasma Membrane Where It Is Concentrated in Caveolae and Caveolae-related Domains
Báthori, G., Parolini, I., Tombola, F., Szabó, I., Messina, A. A., Oliva, M., Pinto, V. D., Lisanti, M. P., Sargiacomo, M., & Zoratti, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.29607 · Cited by 121
Mitochondrial Creatine Kinase in Contact Sites: Interaction with Porin and Adenine Nucleotide Translocase, Role in Permeability Transition and Sensitivity to Oxidative Damage
Dolder, M., Wendt, S., & Wallimann, T. (2001) · Neurosignals · doi:10.1159/000046878 · Cited by 117
Bidirectional interactions between diabetes and Alzheimer's disease
Shinohara, M., & Sato, N. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.04.020 · Cited by 117
The role of calcium in VDAC1 oligomerization and mitochondria-mediated apoptosis
Keinan, N., Pahima, H. T., Ben-Hail, D., & Shoshan‐Barmatz, V. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.017 · Cited by 116
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Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium
Schlattner, U., Dolder, M., Wallimann, T., & Tokarska-Schlattner, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106524200 · Cited by 114
The Role of Lipids in VDAC Oligomerization
Betaneli, V., Petrov, E. P., & Schwille, P. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.049 · Cited by 111
Tau-Based Therapeutic Approaches for Alzheimer's Disease - A Mini-Review
Boutajangout, A., & Wısnıewskı, T. (2014) · Gerontology · doi:10.1159/000358875 · Cited by 110
Ca2+-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
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Structure-based analysis of VDAC1: N-terminus location, translocation, channel gating and association with anti-apoptotic proteins
Geula, S., Ben-Hail, D., & Shoshan-Barmatz, V. (2012) · Biochemical Journal · doi:10.1042/bj20112079 · Cited by 105
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Structure-based Analysis of VDAC1 Protein
Geula, S., Naveed, H., Liang, J., & Shoshan-Barmatz, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.268920 · Cited by 97
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Interaction between NH2-tau fragment and Aβ in Alzheimer's disease mitochondria contributes to the synaptic deterioration
Amadoro, G., Corsetti, V., Atlante, A., Florenzano, F., Capsoni, S., Bussani, R., Mercanti, D., & Calissano, P. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.08.001 · Cited by 95
Pin1: A New Genetic Link between Alzheimers Disease, Cancer and Aging
Driver, J. A., & Lu, K. P. (2010) · Current Aging Science · doi:10.2174/1874609811003030158 · Cited by 92
Oligomerization of the Mitochondrial Protein VDAC1
Shoshan‐Barmatz, V., Mizrachi, D., & Keinan, N. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-386931-9.00011-8 · Cited by 91
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A NH2 Tau Fragment Targets Neuronal Mitochondria at AD Synapses: Possible Implications for Neurodegeneration
Amadoro, G., Corsetti, V., Stringaro, A., Colone, M., D’Aguanno, S., Meli, G., Ciotti, M. T., Sancesario, G., Cattaneo, A., Bussani, R., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100120 · Cited by 91
Molecular correlates of axonal and synaptic pathology in mouse models of Batten disease
Kielar, C., Wishart, T. M., Palmer, A., Dihanich, S., Wong, A. M., Macauley, S. L., Chan, C.-H., Sands, M. S., Pearce, D. A., Cooper, J. D., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp355 · Cited by 91
VDAC and ERα interaction in caveolae from human cortex is altered in Alzheimer's disease
Ramírez, C. M., González‐Gómez, M., Díaz, M. L., Alonso, R., Ferrer, I., Santpere, G., Puig, B., Meyer, G., & Marín, R. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.07.001 · Cited by 90
The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins
Hiller, S., & Wagner, G. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.07.013 · Cited by 90
The formation of prostaglandins in the postmortem cerebral cortex of Alzheimer-type dementia patients
Iwamoto, N., Kobayashi, K., & Kosaka, K. (1989) · Journal of Neurology · doi:10.1007/bf00314401 · Cited by 90
Is the mitochondrial outermembrane protein VDAC1 therapeutic target for Alzheimer's disease?
Reddy, P. H. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.09.003 · Cited by 88
Modes of Aβ toxicity in Alzheimer’s disease
Götz, J., Eckert, A., Matamales, M., Ittner, L. M., & Liu, X. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0750-2 · Cited by 87
Voltage-dependent anion channel (VDAC) participates in amyloid beta-induced toxicity and interacts with plasma membrane estrogen receptor α in septal and hippocampal neurons
Marín, R., Ramírez, C. M., Marin, R., Ramírez, C. M., González‐Gómez, M., González-Muñoz, E., Antonio Zorzano, A., Camps, M., Alonso, R., & Díaz, M. L. (2007) · Molecular Membrane Biology · doi:10.1080/09687860601055559 · Cited by 86
Mitochondrial Abnormalities in Alzheimer’s Disease
Silva, D. F., Selfridge, J. E., Lu, J., E, L., Cardoso, S. M., & Swerdlow, R. H. (2012) · Advances in Pharmacology · doi:10.1016/b978-0-12-394816-8.00003-9 · Cited by 86
Impaired peripheral glucose homeostasis and Alzheimer's disease
Wijesekara, N., Gonçalves, R. A., Felice, F. G. D., & Fraser, P. E. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.11.027 · Cited by 84
Each mammalian mitochondrial outer membrane porin protein is dispensable: effects on cellular respiration
Wu, S., Sampson, M. J., Decker, W. K., & Craigen, W. J. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00120-2 · Cited by 83
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
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VDAC1-based peptides: novel pro-apoptotic agents and potential therapeutics for B-cell chronic lymphocytic leukemia
Prezma, T., Shteinfer‐Kuzmine, A., Admoni, L., Raviv, Z., Sela, I., Levi, I., & Shoshan‐Barmatz, V. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.316 · Cited by 77
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Reduced VDAC1 Protects Against Alzheimer's Disease, Mitochondria, and Synaptic Deficiencies
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Shoshan-Barmatz, 2008, VDAC, the voltage-dependent anion channel: function, regulation & mitochondrial signaling in cell life and death, Cell Sci., 4, 74

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See all 287

Authors: Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R.
Affiliations: Ben-Gurion University of the Negev (IL)
ORCID: Gupta, Rajeev
Venue: Pharmacological Research
Publisher: Elsevier BV
Published: 2018-05
Volume: 131
Pages: 87-101
ISSN: 1043-6618 (ISSN-L)
DOI: 10.1016/j.phrs.2018.03.010
OpenAlex: W2790842992
Cited by: 286
References: 233
Citations by year: 2026: 44 · 2025: 46 · 2024: 38 · 2023: 40 · 2022: 43 · 2021: 33 · 2020: 20 · 2019: 13 · 2018: 9
FWCI: 2.46
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Pharmacological Research (publishedVersion)
PubMed (publishedVersion)
Funders: Phil and Sima Needleman Funds
Israel Science Foundation (307/13)
National Institute for Biotechnology in the Negev
Ben-Gurion University
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: Alzheimer's disease, VDAC1, mitochondrial dysfunction, voltage-dependent anion channel, amyloid-beta, tau hyperphosphorylation, calcium homeostasis, oxidative stress, mitochondrial apoptosis, gamma-secretase, amyloid precursor protein, diabetes mellitus, cancer, neurodegeneration
MeSH terms: Alzheimer Disease, Animals, Calcium, Gene Expression Regulation, Humans, Mitochondria, Models, Molecular, Apoptosis, Voltage-Dependent Anion Channel 1, Protein Interaction Maps

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VDAC1, mitochondrial dysfunction, and Alzheimer’s disease

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