Targeting VDAC-bound hexokinase II: a promising approach for concomitant anti-cancer therapy

Bibliography

• Wilson JE. Isozymes of mammalian hexokinase: structure, subcellular localization and metabolic function. J Exp Biol 2003;206(Pt 12):2049-57
   PubMedGoogle Scholar
• Warburg O, Wind F, Negelein E. The Metabolism of Tumors in the Body. J Gen Physiol 1927;8(6):519-30
   PubMedGoogle Scholar
• Bustamante E, Morris HP, Pedersen PL. Energy metabolism of tumor cells. Requirement for a form of hexokinase with a propensity for mitochondrial binding. J Biol Chem 1981;256(16):8699-704
   PubMed Web of Science ®Google Scholar
• Bustamante E, Pedersen PL. High aerobic glycolysis of rat hepatoma cells in culture: role of mitochondrial hexokinase. Proc Natl Acad Sci USA 1977;74(9):3735-9
   PubMedGoogle Scholar
• Nakashima RA, Mangan PS, Colombini M, Pedersen PL. Hexokinase receptor complex in hepatoma mitochondria: evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC. Biochemistry 1986;25(5):1015-21
   PubMedGoogle Scholar
• Nakashima RA, Paggi MG, Scott LJ, Pedersen PL. Purification and characterization of a bindable form of mitochondrial bound hexokinase from the highly glycolytic AS-30D rat hepatoma cell line. Cancer Res 1988;48(4):913-19
   PubMedGoogle Scholar
• Pastorino JG, Hoek JB. Regulation of hexokinase binding to VDAC. J Bioenerg Biomembr 2008;40(3):171-82
   PubMed Web of Science ®Google Scholar
• Mathupala SP, Ko YH, Pedersen PL. Hexokinase-2 bound to mitochondria: cancer's stygian link to the “Warburg Effect” and a pivotal target for effective therapy. Semin Cancer Biol 2009;19(1):17-24
   PubMedGoogle Scholar
• Lopez-Lazaro M. The warburg effect: why and how do cancer cells activate glycolysis in the presence of oxygen? Anticancer Agents Med Chem 2008;8(3):305-12
   PubMedGoogle Scholar
• Rodriguez-Enriquez S, Marin-Hernandez A, Gallardo-Perez JC, Moreno-Sanchez R. Kinetics of transport and phosphorylation of glucose in cancer cells. J Cell Physiol 2009;221(3):552-9
   PubMedGoogle Scholar
• Natsuizaka M, Ozasa M, Darmanin S, et al. Synergistic up-regulation of Hexokinase-2, glucose transporters and angiogenic factors in pancreatic cancer cells by glucose deprivation and hypoxia. Exp Cell Res 2007;313(15):3337-48
   PubMed Web of Science ®Google Scholar
• Brown RS, Goodman TM, Zasadny KR, et al. Expression of hexokinase II and Glut-1 in untreated human breast cancer. Nucl Med Biol 2002;29(4):443-53
   PubMedGoogle Scholar
• Pedersen PL. Voltage dependent anion channels (VDACs): a brief introduction with a focus on the outer mitochondrial compartment's roles together with hexokinase-2 in the "Warburg effect" in cancer. J Bioenerg Biomembr 2008;40(3):123-6
   PubMedGoogle Scholar
• Di Chiro G, DeLaPaz RL, Brooks RA, et al. Glucose utilization of cerebral gliomas measured by [18F] fluorodeoxyglucose and positron emission tomography. Neurology 1982;32(12):1323-9
   PubMed Web of Science ®Google Scholar
• Singh D, Miles K. Multiparametric PET/CT in oncology. Cancer Imaging 2012;12:336-44
   PubMedGoogle Scholar
• Hoogenboom BW, Suda K, Engel A, Fotiadis D. The supramolecular assemblies of voltage-dependent anion channels in the native membrane. J Mol Biol 2007;370(2):246-55
   PubMedGoogle Scholar
• Akanda N, Tofighi R, Brask J, et al. Voltage-dependent anion channels (VDAC) in the plasma membrane play a critical role in apoptosis in differentiated hippocampal neurons but not in neural stem cells. Cell Cycle 2008;7(20):3225-34
   PubMed Web of Science ®Google Scholar
• De Pinto V, Messina A, Lane DJ, Lawen A. Voltage-dependent anion-selective channel (VDAC) in the plasma membrane. FEBS Lett 2010;584(9):1793-9
   PubMed Web of Science ®Google Scholar
• Gonzalez-Gronow M, Ray R, Wang F, Pizzo SV. The voltage-dependent anion channel (VDAC) binds tissue-type plasminogen activator and promotes activation of plasminogen on the cell surface. J Biol Chem 2013;288(1):498-509
   PubMedGoogle Scholar
• Chandra D, Singh KK. Genetic insights into OXPHOS defect and its role in cancer. Biochim Biophys Acta 2011;1807(6):620-5
   PubMedGoogle Scholar
• Maldonado EN, Lemasters JJ. Warburg revisited: regulation of mitochondrial metabolism by voltage-dependent anion channels in cancer cells. J Pharmacol Exp Ther 2012;342(3):637-41
   PubMed Web of Science ®Google Scholar
• Smolkova K, Plecita-Hlavata L, Bellance N, et al. Waves of gene regulation suppress and then restore oxidative phosphorylation in cancer cells. Int J Biochem Cell Biol 2011;43(7):950-68
   PubMed Web of Science ®Google Scholar
• Azoulay-Zohar H, Israelson A, Abu-Hamad S, Shoshan-Barmatz V. In self-defence: hexokinase promotes voltage-dependent anion channel closure and prevents mitochondria-mediated apoptotic cell death. Biochem J 2004;377(Pt 2):347-55
   PubMedGoogle Scholar
• Tsujimoto Y, Shimizu S. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 2002;84(2-3):187-93
   PubMedGoogle Scholar
• Chowdhury I, Tharakan B, Bhat GK. Current concepts in apoptosis: the physiological suicide program revisited. Cell Mol Biol Lett 2006;11(4):506-25
   PubMedGoogle Scholar
• Korsmeyer SJ, Wei MC, Saito M, et al. Pro-apoptotic cascade activates BID, which oligomerizes BAK or BAX into pores that result in the release of cytochrome c. Cell Death Differ 2000;7(12):1166-73
   PubMed Web of Science ®Google Scholar
• Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997;91(4):479-89
   PubMed Web of Science ®Google Scholar
• Shoshan-Barmatz V, Mizrachi D. VDAC1: from structure to cancer therapy. Front Oncol 2012;2:164
   PubMedGoogle Scholar
• Chiara F, Castellaro D, Marin O, et al. Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels. PLoS One 2008;3(3):e1852
   PubMed Web of Science ®Google Scholar
• Shoshan-Barmatz V, Israelson A, Brdiczka D, Sheu SS. The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr Pharm Des 2006;12(18):2249-70
   PubMed Web of Science ®Google Scholar
• Shoshan-Barmatz V, De Pinto V, Zweckstetter M, et al. VDAC, a multi-functional mitochondrial protein regulating cell life and death. Mol Aspects Med 2010;31(3):227-85
   PubMed Web of Science ®Google Scholar
• Tsujimoto Y, Shimizu S. Role of the mitochondrial membrane permeability transition in cell death. Apoptosis 2007;12(5):835-40
   PubMed Web of Science ®Google Scholar
• Teijido O, Ujwal R, Hillerdal CO, et al. Affixing N-terminal alpha-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating. J Biol Chem 2012;287(14):11437-45
   PubMedGoogle Scholar
• Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000;20(3):929-35
   PubMed Web of Science ®Google Scholar
• Reed JC. Proapoptotic multidomain Bcl-2/Bax-family proteins: mechanisms, physiological roles, and therapeutic opportunities. Cell Death Differ 2006;13(8):1378-86
   PubMed Web of Science ®Google Scholar
• Kokoszka JE, Waymire KG, Levy SE, et al. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature 2004;427(6973):461-5
   PubMed Web of Science ®Google Scholar
• Baines CP, Kaiser RA, Sheiko T, et al. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol 2007;9(5):550-5
   PubMed Web of Science ®Google Scholar
• Malia TJ, Wagner G. NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL. Biochemistry 2007;46(2):514-25
   PubMedGoogle Scholar
• Wan KF, Chan SL, Sukumaran SK, et al. Chelerythrine induces apoptosis through a Bax/Bak-independent mitochondrial mechanism. J Biol Chem 2008;283(13):8423-33
   PubMedGoogle Scholar
• Majewski N, Nogueira V, Bhaskar P, et al. Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak. Mol Cell 2004;16(5):819-30
   PubMed Web of Science ®Google Scholar
• Rostovtseva TK, Tan W, Colombini M. On the role of VDAC in apoptosis: fact and fiction. J Bioenerg Biomembr 2005;37(3):129-42
   PubMedGoogle Scholar
• Robey RB, Hay N. Mitochondrial hexokinases, novel mediators of the antiapoptotic effects of growth factors and Akt. Oncogene 2006;25(34):4683-96
   PubMed Web of Science ®Google Scholar
• Robey RB, Hay N. Mitochondrial hexokinases: guardians of the mitochondria. Cell Cycle 2005;4(5):654-8
   PubMed Web of Science ®Google Scholar
• Pastorino JG, Hoek JB, Shulga N. Activation of glycogen synthase kinase 3beta disrupts the binding of hexokinase II to mitochondria by phosphorylating voltage-dependent anion channel and potentiates chemotherapy-induced cytotoxicity. Cancer Res 2005;65(22):10545-54
   PubMed Web of Science ®Google Scholar
• Tristan C, Shahani N, Sedlak TW, Sawa A. The diverse functions of GAPDH: views from different subcellular compartments. Cell Signal 2011;23(2):317-23
   PubMed Web of Science ®Google Scholar
• Sirover MA. Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J Cell Biochem 2012;113(7):2193-200
   PubMed Web of Science ®Google Scholar
• Krasnov GS, Dmitriev AA, Snezhkina AV, Kudryavtseva AV. Deregulation of glycolysis in cancer: glyceraldehyde-3-phosphate dehydrogenase as a therapeutic target. Expert Opin Ther Targets 2013;17(6):681-93
   PubMed Web of Science ®Google Scholar
• Zheng L, Roeder RG, Luo Y. S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component. Cell 2003;114(2):255-66
   PubMed Web of Science ®Google Scholar
• Thangima Zannat M, Bhattacharjee RB, Bag J. In the absence of cellular poly (A) binding protein, the glycolytic enzyme GAPDH translocated to the cell nucleus and activated the GAPDH mediated apoptotic pathway by enhancing acetylation and serine 46 phosphorylation of p53. Biochem Biophys Res Commun 2011;409(2):171-6
   PubMedGoogle Scholar
• Tarze A, Deniaud A, Le Bras M, et al. GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization. Oncogene 2007;26(18):2606-20
   PubMed Web of Science ®Google Scholar
• Hara MR, Agrawal N, Kim SF, et al. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 2005;7(7):665-74
   PubMed Web of Science ®Google Scholar
• Sen N, Hara MR, Ahmad AS, et al. GOSPEL: a neuroprotective protein that binds to GAPDH upon S-nitrosylation. Neuron 2009;63(1):81-91
   PubMedGoogle Scholar
• Martelli PL, D'Antonio M, Bonizzoni P, et al. ASPicDB: a database of annotated transcript and protein variants generated by alternative splicing. Nucleic Acids Res 2011;39(Database issue):D80-5
   PubMedGoogle Scholar
• Shionyu M, Yamaguchi A, Shinoda K, et al. AS-ALPS: a database for analyzing the effects of alternative splicing on protein structure, interaction and network in human and mouse. Nucleic Acids Res 2009;37(Database issue):D305-9
   PubMedGoogle Scholar
• Chen JQ, Russo J. Dysregulation of glucose transport, glycolysis, TCA cycle and glutaminolysis by oncogenes and tumor suppressors in cancer cells. Biochim Biophys Acta 2012;1826(2):370-84
   PubMed Web of Science ®Google Scholar
• Yeung SJ, Pan J, Lee MH. Roles of p53, MYC and HIF-1 in regulating glycolysis - the seventh hallmark of cancer. Cell Mol Life Sci 2008;65(24):3981-99
   PubMed Web of Science ®Google Scholar
• Steelman LS, Chappell WH, Abrams SL, et al. Roles of the Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR pathways in controlling growth and sensitivity to therapy-implications for cancer and aging. Aging 2011;3(3):192-222
   PubMedGoogle Scholar
• Cairns RA, Harris IS, Mak TW. Regulation of cancer cell metabolism. Nat Rev Cancer 2011;11(2):85-95
   PubMed Web of Science ®Google Scholar
• Wieman HL, Wofford JA, Rathmell JC. Cytokine stimulation promotes glucose uptake via phosphatidylinositol-3 kinase/Akt regulation of Glut1 activity and trafficking. Mol Biol Cell 2007;18(4):1437-46
   PubMed Web of Science ®Google Scholar
• Dang CV, Le A, Gao P. MYC-induced cancer cell energy metabolism and therapeutic opportunities. Clin Cancer Res 2009;15(21):6479-83
   PubMed Web of Science ®Google Scholar
• Lewis BC, Prescott JE, Campbell SE, et al. Tumor induction by the c-Myc target genes rcl and lactate dehydrogenase A. Cancer Res 2000;60(21):6178-83
   PubMedGoogle Scholar
• Dang CV, Kim JW, Gao P, Yustein J. The interplay between MYC and HIF in cancer. Nat Rev Cancer 2008;8(1):51-6
   PubMed Web of Science ®Google Scholar
• Jose C, Bellance N, Rossignol R. Choosing between glycolysis and oxidative phosphorylation: a tumor's dilemma? Biochim Biophys Acta 2011;1807(6):552-61
   PubMed Web of Science ®Google Scholar
• Mathupala SP, Heese C, Pedersen PL. Glucose catabolism in cancer cells. The type II hexokinase promoter contains functionally active response elements for the tumor suppressor p53. J Biol Chem 1997;272(36):22776-80
   PubMed Web of Science ®Google Scholar
• Rempel A, Mathupala SP, Perdersen PL. Glucose catabolism in cancer cells: regulation of the Type II hexokinase promoter by glucose and cyclic AMP. FEBS Lett 1996;385(3):233-7
   PubMedGoogle Scholar
• Thomson DM, Herway ST, Fillmore N, et al. AMP-activated protein kinase phosphorylates transcription factors of the CREB family. J Appl Physiol 2008;104(2):429-38
   PubMedGoogle Scholar
• Moon JS, Jin WJ, Kwak JH, et al. Androgen stimulates glycolysis for de novo lipid synthesis by increasing the activities of hexokinase 2 and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 in prostate cancer cells. Biochem J 2011;433(1):225-33
   PubMedGoogle Scholar
• Abu-Hamad S, Zaid H, Israelson A, et al. Hexokinase-I protection against apoptotic cell death is mediated via interaction with the voltage-dependent anion channel-1: mapping the site of binding. J Biol Chem 2008;283(19):13482-90
   PubMedGoogle Scholar
• Craig TA, Ramachandran PL, Bergen HR III, et al. The regulation of apoptosis by the downstream regulatory element antagonist modulator/potassium channel interacting protein 3 (DREAM/KChIP3) through interactions with hexokinase I. Biochem Biophys Res Commun 2013;433(4):508-12
   PubMedGoogle Scholar
• Wyatt E, Wu R, Rabeh W, et al. Regulation and cytoprotective role of hexokinase III. PloS one 2010;5(11):e13823
   PubMed Web of Science ®Google Scholar
• Hooft L, van der Veldt AA, Hoekstra OS, et al. Hexokinase III, cyclin A and galectin-3 are overexpressed in malignant follicular thyroid nodules. Clin Endocrinol (Oxf) 2008;68(2):252-7
   PubMedGoogle Scholar
• Birney E, Stamatoyannopoulos JA, Dutta A, et al. Identification and analysis of functional elements in 1% of the human genome by the ENCODE pilot project. Nature 2007;447(7146):799-816
   PubMed Web of Science ®Google Scholar
• Gregersen LH, Jacobsen A, Frankel LB, et al. MicroRNA-143 down-regulates Hexokinase 2 in colon cancer cells. BMC Cancer 2012;12:232
   PubMed Web of Science ®Google Scholar
• Jiang S, Zhang LF, Zhang HW, et al. A novel miR-155/miR-143 cascade controls glycolysis by regulating hexokinase 2 in breast cancer cells. EMBO J 2012;31(8):1985-98
   PubMed Web of Science ®Google Scholar
• Peschiaroli A, Giacobbe A, Formosa A, et al. miR-143 regulates hexokinase 2 expression in cancer cells. Oncogene 2013;32(6):797-802
   PubMedGoogle Scholar
• Aggarwal BB, Vijayalekshmi RV, Sung B. Targeting inflammatory pathways for prevention and therapy of cancer: short-term friend, long-term foe. Clin Cancer Res 2009;15(2):425-30
   PubMed Web of Science ®Google Scholar
• Yu H, Pardoll D, Jove R. STATs in cancer inflammation and immunity: a leading role for STAT3. Nat Rev Cancer 2009;9(11):798-809
   PubMed Web of Science ®Google Scholar
• Davey GM, Heath WR, Starr R. SOCS1: a potent and multifaceted regulator of cytokines and cell-mediated inflammation. Tissue Antigens 2006;67(1):1-9
   PubMedGoogle Scholar
• Jiang S, Zhang HW, Lu MH, et al. MicroRNA-155 functions as an OncomiR in breast cancer by targeting the suppressor of cytokine signaling 1 gene. Cancer Res 2010;70(8):3119-27
   PubMed Web of Science ®Google Scholar
• Katabi MM, Chan HL, Karp SE, Batist G. Hexokinase type II: a novel tumor-specific promoter for gene-targeted therapy differentially expressed and regulated in human cancer cells. Hum Gene Ther 1999;10(2):155-64
   PubMed Web of Science ®Google Scholar
• Peng SY, Lai PL, Pan HW, et al. Aberrant expression of the glycolytic enzymes aldolase B and type II hexokinase in hepatocellular carcinoma are predictive markers for advanced stage, early recurrence and poor prognosis. Oncol Rep 2008;19(4):1045-53
   PubMed Web of Science ®Google Scholar
• Palmieri D, Fitzgerald D, Shreeve SM, et al. Analyses of resected human brain metastases of breast cancer reveal the association between up-regulation of hexokinase 2 and poor prognosis. Mol Cancer Res 2009;7(9):1438-45
   PubMed Web of Science ®Google Scholar
• Yasuda S, Arii S, Mori A, et al. Hexokinase II and VEGF expression in liver tumors: correlation with hypoxia-inducible factor 1 alpha and its significance. J Hepatol 2004;40(1):117-23
   PubMedGoogle Scholar
• Rho M, Kim J, Jee CD, et al. Expression of type 2 hexokinase and mitochondria-related genes in gastric carcinoma tissues and cell lines. Anticancer Res 2007;27(1A):251-8
   PubMedGoogle Scholar
• Qiu MZ, Han B, Luo HY, et al. Expressions of hypoxia-inducible factor-1alpha and hexokinase-II in gastric adenocarcinoma: the impact on prognosis and correlation to clinicopathologic features. Tumour Biol 2011;32(1):159-66
   PubMedGoogle Scholar
• Lyshchik A, Higashi T, Hara T, et al. Expression of glucose transporter-1, hexokinase-II, proliferating cell nuclear antigen and survival of patients with pancreatic cancer. Cancer Invest 2007;25(3):154-62
   PubMed Web of Science ®Google Scholar
• Vach W, Hoilund-Carlsen PF, Gerke O, Weber WA. Generating evidence for clinical benefit of PET/CT in diagnosing cancer patients. J Nucl Med 2011;52(Suppl 2):77S-85S
   PubMedGoogle Scholar
• Niekel MC, Bipat S, Stoker J. Diagnostic imaging of colorectal liver metastases with CT, MR imaging, FDG PET, and/or FDG PET/CT: a meta-analysis of prospective studies including patients who have not previously undergone treatment. Radiology 2010;257(3):674-84
   PubMed Web of Science ®Google Scholar
• Monteil J, Mahmoudi N, Leobon S, et al. Chemotherapy response evaluation in metastatic colorectal cancer with FDG PET/CT and CT scans. Anticancer Res 2009;29(7):2563-8
   PubMedGoogle Scholar
• Nakajo M, Kajiya Y, Tani A, et al. (1)(8)FDG PET for grading malignancy in thymic epithelial tumors: significant differences in (1)(8)FDG uptake and expression of glucose transporter-1 and hexokinase II between low and high-risk tumors: preliminary study. Eur J Radiol 2012;81(1):146-51
   PubMedGoogle Scholar
• Warning K, Hildebrandt MG, Kristensen B, Ewertz M. Utility of 18FDG-PET/CT in breast cancer diagnostics–a systematic review. Dan Med Bull 2011;58(7):A4289
   PubMedGoogle Scholar
• Bhattacharya SK. Inhibition of liver hexokinase by dehydroascorbic acid and alloxan. Nature 1959;184(Suppl 21):1638-40
   PubMedGoogle Scholar
• Nesbakken R, Eldjarn L. The inhibition of hexokinase by disulphides. Biochem J 1963;87(3):526-32
   PubMedGoogle Scholar
• Newsholme EA, Rolleston FS, Taylor K. Inhibition of brain hexokinase by glucose 6-phosphate. Biochem J 1967;104(3):47P
   PubMedGoogle Scholar
• Liu X, Kim CS, Kurbanov FT, et al. Dual mechanisms for glucose 6-phosphate inhibition of human brain hexokinase. J Biol Chem 1999;274(44):31155-9
   PubMedGoogle Scholar
• Chuang JH, Chou MH, Tai MH, et al. 2-Deoxyglucose treatment complements the cisplatin- or BH3-only mimetic-induced suppression of neuroblastoma cell growth. Int J Biochem Cell Biol 2013;45(5):944-51
   PubMedGoogle Scholar
• Maschek G, Savaraj N, Priebe W, et al. 2-deoxy-D-glucose increases the efficacy of adriamycin and paclitaxel in human osteosarcoma and non-small cell lung cancers in vivo. Cancer Res 2004;64(1):31-4
   PubMed Web of Science ®Google Scholar
• Gupta S, Mathur R, Dwarakanath BS. The glycolytic inhibitor 2-deoxy-D-glucose enhances the efficacy of etoposide in ehrlich ascites tumor-bearing mice. Cancer Biol Ther 2005;4(1):87-94
   PubMedGoogle Scholar
• Oudard S, Carpentier A, Banu E, et al. Phase II study of lonidamine and diazepam in the treatment of recurrent glioblastoma multiforme. J Neurooncol 2003;63(1):81-6
   PubMedGoogle Scholar
• De Lena M, Lorusso V, Latorre A, et al. Paclitaxel, cisplatin and lonidamine in advanced ovarian cancer. A phase II study. Eur J Cancer 2001;37(3):364-8
   PubMed Web of Science ®Google Scholar
• Angioli R, Janicek M, Sevin B, et al. Use of lonidamine to potentiate the effect of cisplatin and carboplatin on platinum resistant human ovarian cancer cells. Int J Oncol 1997;11(4):777-80
   PubMedGoogle Scholar
• Biroccio A, Del Bufalo D, Fanciulli M, et al. bcl-2 inhibits mitochondrial metabolism and lonidamine-induced apoptosis in adriamycin-resistant MCF7 cells. Int J Cancer 1999;82(1):125-30
   PubMedGoogle Scholar
• Li YC, Fung KP, Kwok TT, et al. Mitochondrial targeting drug lonidamine triggered apoptosis in doxorubicin-resistant HepG2 cells. Life Sci 2002;71(23):2729-40
   PubMedGoogle Scholar
• Calvino E, Estan MC, Simon GP, et al. Increased apoptotic efficacy of lonidamine plus arsenic trioxide combination in human leukemia cells. Reactive oxygen species generation and defensive protein kinase (MEK/ERK, Akt/mTOR) modulation. Biochem Pharmacol 2011;82(11):1619-29
   PubMedGoogle Scholar
• Milane L, Duan Z, Amiji M. Therapeutic efficacy and safety of paclitaxel/lonidamine loaded EGFR-targeted nanoparticles for the treatment of multi-drug resistant cancer. PLoS One 2011;6(9):e24075
   PubMed Web of Science ®Google Scholar
• Cardaci S, Desideri E, Ciriolo MR. Targeting aerobic glycolysis: 3-bromopyruvate as a promising anticancer drug. J Bioenerg Biomembr 2012;44(1):17-29
   PubMedGoogle Scholar
• Ganapathy-Kanniappan S, Kunjithapatham R, Geschwind JF. Anticancer efficacy of the metabolic blocker 3-bromopyruvate: specific molecular targeting. Anticancer Res 2013;33(1):13-20
   PubMed Web of Science ®Google Scholar
• Tang Z, Yuan S, Hu Y, et al. Over-expression of GAPDH in human colorectal carcinoma as a preferred target of 3-bromopyruvate propyl ester. J Bioenerg Biomembr 2012;44(1):117-25
   PubMedGoogle Scholar
• Ganapathy-Kanniappan S, Vali M, Kunjithapatham R, et al. 3-bromopyruvate: a new targeted antiglycolytic agent and a promise for cancer therapy. Curr Pharm Biotechnol 2010;11(5):510-17
   PubMed Web of Science ®Google Scholar
• Yu SJ, Yoon JH, Yang JI, et al. Enhancement of hexokinase II inhibitor-induced apoptosis in hepatocellular carcinoma cells via augmenting ER stress and anti-angiogenesis by protein disulfide isomerase inhibition. J Bioenerg Biomembr 2012;44(1):101-15
   PubMedGoogle Scholar
• Yu SJ, Yoon JH, Lee JH, et al. Inhibition of hypoxia-inducible carbonic anhydrase-IX enhances hexokinase II inhibitor-induced hepatocellular carcinoma cell apoptosis. Acta Pharmacol Sin 2011;32(7):912-20
   PubMed Web of Science ®Google Scholar
• Galluzzi L, Kepp O, Tajeddine N, Kroemer G. Disruption of the hexokinase-VDAC complex for tumor therapy. Oncogene 2008;27(34):4633-5
   PubMed Web of Science ®Google Scholar
• Rosano C. Molecular model of hexokinase binding to the outer mitochondrial membrane porin (VDAC1): implication for the design of new cancer therapies. Mitochondrion 2011;11(3):513-19
   PubMedGoogle Scholar
• Chen Z, Zhang H, Lu W, Huang P. Role of mitochondria-associated hexokinase II in cancer cell death induced by 3-bromopyruvate. Biochim Biophys Acta 2009;1787(5):553-60
   PubMed Web of Science ®Google Scholar
• Chang JM, Chung JW, Jae HJ, et al. Local toxicity of hepatic arterial infusion of hexokinase II inhibitor, 3-bromopyruvate: in vivo investigation in normal rabbit model. Acad Radiol 2007;14(1):85-92
   PubMedGoogle Scholar
• Arzoine L, Zilberberg N, Ben-Romano R, Shoshan-Barmatz V. Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity. J Biol Chem 2009;284(6):3946-55
   PubMed Web of Science ®Google Scholar
• Penso J, Beitner R. Clotrimazole and bifonazole detach hexokinase from mitochondria of melanoma cells. Eur J Pharmacol 1998;342(1):113-17
   PubMed Web of Science ®Google Scholar
• Goldin N, Arzoine L, Heyfets A, et al. Methyl jasmonate binds to and detaches mitochondria-bound hexokinase. Oncogene 2008;27(34):4636-43
   PubMedGoogle Scholar
• Raviv Z, Cohen S, Reischer-Pelech D. The anti-cancer activities of jasmonates. Cancer Chemother Pharmacol 2013;71(2):275-85
   PubMedGoogle Scholar
• Klippel S, Jakubikova J, Delmore J, et al. Methyljasmonate displays in vitro and in vivo activity against multiple myeloma cells. Br J Haematol 2012;159(3):340-51
   PubMedGoogle Scholar
• Cohen S, Flescher E. Methyl jasmonate: a plant stress hormone as an anti-cancer drug. Phytochemistry 2009;70(13-14):1600-9
   PubMed Web of Science ®Google Scholar
• Reischer D, Heyfets A, Shimony S, et al. Effects of natural and novel synthetic jasmonates in experimental metastatic melanoma. Br J Pharmacol 2007;150(6):738-49
   PubMedGoogle Scholar
• Tsumura H, Akimoto M, Kiyota H, et al. Gene expression profiles in differentiating leukemia cells induced by methyl jasmonate are similar to those of cytokinins and methyl jasmonate analogs induce the differentiation of human leukemia cells in primary culture. Leukemia 2009;23(4):753-60
   PubMedGoogle Scholar
• Kashiwagi Y, Kato N, Sassa T, et al. Cotylenin A inhibits cell proliferation and induces apoptosis and PAX6 mRNA transcripts in retinoblastoma cell lines. Mol Vis 2010;16:970-82
   PubMedGoogle Scholar
• Elia U, Flescher E. PI3K/Akt pathway activation attenuates the cytotoxic effect of methyl jasmonate toward sarcoma cells. Neoplasia 2008;10(11):1303-13
   PubMedGoogle Scholar
• Kachadourian R, Brechbuhl HM, Ruiz-Azuara L, et al. Casiopeina IIgly-induced oxidative stress and mitochondrial dysfunction in human lung cancer A549 and H157 cells. Toxicology 2010;268(3):176-83
   PubMedGoogle Scholar
• Marin-Hernandez A, Gallardo-Perez JC, Lopez-Ramirez SY, et al. Casiopeina II-gly and bromo-pyruvate inhibition of tumor hexokinase, glycolysis, and oxidative phosphorylation. Arch Toxicol 2012;86(5):753-66
   PubMedGoogle Scholar
• Wei L, Dai Q, Zhou Y, et al. Oroxylin A sensitizes non-small cell lung cancer cells to anoikis via glucose-deprivation-like mechanisms: c-Src and hexokinase II. Biochim Biophys Acta 2013;1830(6):3835-45
   PubMed Web of Science ®Google Scholar
• Wei L, Zhou Y, Dai Q, et al. Oroxylin A induces dissociation of hexokinase II from the mitochondria and inhibits glycolysis by SIRT3-mediated deacetylation of cyclophilin D in breast carcinoma. Cell Death Dis 2013;4:e601
   PubMed Web of Science ®Google Scholar
• Smith TA, Appleyard MV, Sharp S, et al. Response to trastuzumab by HER2 expressing breast tumour xenografts is accompanied by decreased Hexokinase II, glut1 and [18F]-FDG incorporation and changes in 31P-NMR-detectable phosphomonoesters. Cancer Chemother Pharmacol 2013;71(2):473-80
   PubMedGoogle Scholar
• Kim JE, Ahn BC, Hwang MH, et al. Combined RNA interference of hexokinase II and (131)I-sodium iodide symporter gene therapy for anaplastic thyroid carcinoma. J Nucl Med 2011;52(11):1756-63
   PubMedGoogle Scholar
• Ward LS, Santarosa PL, Granja F, et al. Low expression of sodium iodide symporter identifies aggressive thyroid tumors. Cancer Lett 2003;200(1):85-91
   PubMed Web of Science ®Google Scholar
• Li W, Ain KB. Human sodium-iodide symporter (hNIS) gene expression is inhibited by a trans-active transcriptional repressor, NIS-repressor, containing PARP-1 in thyroid cancer cells. Endocr Relat Cancer 2010;17(2):383-98
   PubMedGoogle Scholar
• Lee YL, Lee YJ, Ahn SJ, et al. Combined radionuclide-chemotherapy and in vivo imaging of hepatocellular carcinoma cells after transfection of a triple-gene construct, NIS, HSV1-sr39tk, and EGFP. Cancer Lett 2010;290(1):129-38
   PubMedGoogle Scholar
• Peng Q, Zhou J, Zhou Q, et al. Silencing hexokinase II gene sensitizes human colon cancer cells to 5-fluorouracil. Hepatogastroenterology 2009;56(90):355-60
   PubMedGoogle Scholar
• Fantin VR, St-Pierre J, Leder P. Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell 2006;9(6):425-34
   PubMed Web of Science ®Google Scholar
• Wang ZY, Loo TY, Shen JG, et al. LDH-A silencing suppresses breast cancer tumorigenicity through induction of oxidative stress mediated mitochondrial pathway apoptosis. Breast Cancer Res Treat 2012;131(3):791-800
   PubMed Web of Science ®Google Scholar
• Shen YC, Ou DL, Hsu C, et al. Activating oxidative phosphorylation by a pyruvate dehydrogenase kinase inhibitor overcomes sorafenib resistance of hepatocellular carcinoma. Br J Cancer 2013;108(1):72-81
   PubMed Web of Science ®Google Scholar