Rapamycin Inhibits Glioma Cells Growth and Promotes Autophagy by miR-26a-5p/DAPK1 Axis

References

• Weller M, Wick W, Aldape K, et al. Glioma. Nat Rev Dis Primers. 2015;1(1):15017. doi:10.1038/nrdp.2015.1727188790
   PubMed Web of Science ®Google Scholar
• Bush NAO, Chang SM, Berger MS. Current and future strategies for treatment of glioma. Neurosurg Rev. 2017;40(1):1–14. doi:10.1007/s10143-016-0709-827085859
   PubMed Web of Science ®Google Scholar
• Suryadevara CM, Verla T, Sanchez-Perez L, et al. Immunotherapy for malignant glioma. Surg Neurol Int. 2015;6(Suppl 1):S68. doi:10.4103/2152-7806.15134125722935
   PubMedGoogle Scholar
• Geering B. Death-associated protein kinase 2: regulator of apoptosis, autophagy and inflammation. Int J Biochem Cell Biol. 2015;65:151–154. doi:10.1016/j.biocel.2015.06.00126055515
   PubMed Web of Science ®Google Scholar
• Deiss LP, Feinstein E, Berissi H, Cohen O, Kimchi A. Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death. Genes Dev. 1995;9(1):15–30. doi:10.1101/gad.9.1.157828849
   PubMed Web of Science ®Google Scholar
• Bialik S, Bresnick AR, Kimchi A. DAP-kinase-mediated morphological changes are localization dependent and involve myosin-II phosphorylation. Cell Death Differ. 2004;11(6):631–644. doi:10.1038/sj.cdd.440138615002035
   PubMed Web of Science ®Google Scholar
• Wang S, Shi X, Li H, et al. DAPK1 signaling pathways in stroke: from mechanisms to therapies. Mol Neurobiol. 2017;54(6):4716–4722. doi:10.1007/s12035-016-0008-y27447806
   PubMed Web of Science ®Google Scholar
• Yuan W, Chen J, Shu Y, et al. Correlation of DAPK1 methylation and the risk of gastrointestinal cancer: a systematic review and meta-analysis. PLoS One. 2017;12(9):e0184959. doi:10.1371/journal.pone.018495928934284
   PubMed Web of Science ®Google Scholar
• Beermann J, Piccoli M-T, Viereck J, Non-coding TT. RNAs in development and disease: background, mechanisms, and therapeutic approaches. Physiol Rev. 2016;96(4):1297–1325. doi:10.1152/physrev.00041.201527535639
   PubMed Web of Science ®Google Scholar
• Acunzo M, Romano G, Wernicke D, Croce CM. MicroRNA and cancer–a brief overview. Adv Biol Regul. 2015;57:1–9. doi:10.1016/j.jbior.2014.09.01325294678
   PubMedGoogle Scholar
• Shah MY, Ferrajoli A, Sood AK, Lopez-Berestein G, Calin GA. MicroRNA therapeutics in cancer—an emerging concept. EBioMedicine. 2016;12:34–42. doi:10.1016/j.ebiom.2016.09.01727720213
   PubMed Web of Science ®Google Scholar
• Xia Z, Liu F, Zhang J, Liu L, Kyprianou N. Decreased expression of MiRNA-204-5p contributes to glioma progression and promotes glioma cell growth, migration and invasion. PLoS One. 2015;10(7):e0132399. doi:10.1371/journal.pone.013239926134825
   PubMed Web of Science ®Google Scholar
• Que T, Song Y, Liu Z, et al. Decreased miRNA-637 is an unfavorable prognosis marker and promotes glioma cell growth, migration and invasion via direct targeting Akt1. Oncogene. 2015;34(38):4952. doi:10.1038/onc.2014.41925597410
   PubMed Web of Science ®Google Scholar
• Gu J, Lu Z, Ji C, et al. Melatonin inhibits proliferation and invasion via repression of miRNA-155 in glioma cells. Biomed Pharmacother. 2017;93:969–975. doi:10.1016/j.biopha.2017.07.01028724215
   PubMed Web of Science ®Google Scholar
• Yu J, Wu S-W, Wu W-P. A tumor-suppressive microRNA, miRNA-485-5p, inhibits glioma cell proliferation and invasion by down-regulating TPD52L2. Am J Transl Res. 2017;9(7):3336.28804551
   PubMed Web of Science ®Google Scholar
• Blagosklonny MV. Does rapamycin slow down time? Oncotarget. 2018;9(54):30210. doi:10.18632/oncotarget.2578830100983
   PubMedGoogle Scholar
• Lamming DW. Inhibition of the mechanistic target of rapamycin (mTOR)–rapamycin and beyond. Cold Spring Harb Perspect Med. 2016;6(5):a025924. doi:10.1101/cshperspect.a02592427048303
   PubMed Web of Science ®Google Scholar
• Petővári G, Hujber Z, Krencz I, et al. Targeting cellular metabolism using rapamycin and/or doxycycline enhances anti-tumour effects in human glioma cells. Cancer Cell Int. 2018;18(1):211. doi:10.1186/s12935-018-0710-030574020
   PubMed Web of Science ®Google Scholar
• Escalona-Rayo O, Fuentes-Vázquez P, Jardon-Xicotencatl S, García-Tovar CG, Mendoza-Elvira S, Quintanar-Guerrero D. Rapamycin-loaded polysorbate 80-coated PLGA nanoparticles: optimization of formulation variables and in vitro anti-glioma assessment. J Drug Deliv Sci Technol. 2019;52:488–499. doi:10.1016/j.jddst.2019.05.026
   Web of Science ®Google Scholar
• Hjelmeland AB, Lattimore KP, Fee BE, et al. The combination of novel low molecular weight inhibitors of RAF (LBT613) and target of rapamycin (RAD001) decreases glioma proliferation and invasion. Mol Cancer Ther. 2007;6(9):2449–2457. doi:10.1158/1535-7163.MCT-07-015517766837
   PubMed Web of Science ®Google Scholar
• Tanaka K, Sasayama T, Mizukawa K, et al. Specific mTOR inhibitor rapamycin enhances cytotoxicity induced by alkylating agent 1-(4-amino-2-methyl-5-pyrimidinyl)methyl-3-(2-chloroethyl)-3-nitrosourea (ACNU) in human U251 malignant glioma cells. J Neurooncol. 2007;84(3):233–244. doi:10.1007/s11060-007-9371-x17390104
   PubMed Web of Science ®Google Scholar
• Guo Y, Ren G. Effect of rapamycin on proliferation and apoptosis in human glioblastoma cell. J Shantou Univ Med Coll. 2015;28(2):65–67+62.
   Google Scholar
• Zhuang W-Z, Long L-M, Ji W-J, Liang Z-Q. Rapamycin induces differentiation of glioma stem/progenitor cells by activating autophagy. Chin J Cancer. 2011;30(10):712–720. doi:10.5732/cjc.011.1023421959048
   PubMedGoogle Scholar
• Yang P, Zhang J, Li Q, Ding Y, Ren J. Rapamycin combined with nimuatine suppresses growth and proliferation of human U87MG glioma cells. Acta Acad Med Militaris Tertlae. 2010;32(14):1529–1533.
   Google Scholar
• Lin X, Han L, Weng J, Wang K, Chen T. Rapamycin inhibits proliferation and induces autophagy in human neuroblastoma cells. Biosci Rep. 2018;38(6). doi:10.1042/BSR20181822
   Web of Science ®Google Scholar
• Singh P, Ravanan P, Talwar P. Death associated protein kinase 1 (DAPK1): a regulator of apoptosis and autophagy. Front Mol Neurosci. 2016;9:46. doi:10.3389/fnmol.2016.0004627445685
   PubMed Web of Science ®Google Scholar
• Zhang L, Tong X, Li J, et al. Apoptotic and autophagic pathways with relevant small-molecule compounds, in cancer stem cells. Cell Prolif. 2015;48(4):385–397. doi:10.1111/cpr.1219126013704
   PubMed Web of Science ®Google Scholar
• Karsli-Uzunbas G, Guo JY, Price S, et al. Autophagy is required for glucose homeostasis and lung tumor maintenance. Cancer Discov. 2014;4(8):914–927. doi:10.1158/2159-8290.CD-14-036324875857
   PubMed Web of Science ®Google Scholar
• Levy JMM, Towers CG, Thorburn A. Targeting autophagy in cancer. Nat Rev Cancer. 2017;17(9):528. doi:10.1038/nrc.2017.5328751651
   PubMed Web of Science ®Google Scholar
• Miyamoto K, Seki N, Matsushita R, et al. Tumour-suppressive miRNA-26a-5p and miR-26b-5p inhibit cell aggressiveness by regulating PLOD2 in bladder cancer. Br J Cancer. 2016;115(3):354. doi:10.1038/bjc.2016.17927310702
   PubMed Web of Science ®Google Scholar
• Ghanbari R, Mosakhani N, Asadi J, et al. Downregulation of plasma MiR-142-3p and MiR-26a-5p in patients with colorectal carcinoma. Iran J Cancer Prev. 2015;8(3):3. doi:10.17795/ijcp2329
   Google Scholar
• Guo K, Zheng S, Xu Y, Xu A, Chen B, Wen Y. Loss of miR-26a-5p promotes proliferation, migration, and invasion in prostate cancer through negatively regulating SERBP1. Tumour Biol. 2016;37(9):12843–12854. doi:10.1007/s13277-016-5158-z27449037
   PubMedGoogle Scholar
• Song Q, Liu B, Li X, et al. miR-26a-5p potentiates metastasis of human lung cancer cells by regulating ITGβ8-JAK2/STAT3 axis. Biochem Biophys Res Commun. 2018;501(2):494–500. doi:10.1016/j.bbrc.2018.05.02029746867
   PubMed Web of Science ®Google Scholar
• Mizushima N. Autophagy: process and function. Genes Dev. 2007;21(22):2861–2873. doi:10.1101/gad.159920718006683
   PubMed Web of Science ®Google Scholar
• Ichimura Y, Kirisako T, Takao T, et al. A ubiquitin-like system mediates protein lipidation. Nature. 2000;408(6811):488–492. doi:10.1038/3504411411100732
   PubMed Web of Science ®Google Scholar
• Nakatogawa H, Ichimura Y, Ohsumi YJC. Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. Cell. 2007;130(1):165–178. doi:10.1016/j.cell.2007.05.02117632063
   PubMed Web of Science ®Google Scholar
• Noda N, Ohsumi Y, Inagaki F. Atg8-family interacting motif crucial for selective autophagy. FEBS Lett. 2010;584(7):1379–1385. doi:10.1016/j.febslet.2010.01.01820083108
   PubMed Web of Science ®Google Scholar
• Kabeya Y, Mizushima N, Ueno T, et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 2000;19(21):5720–5728. doi:10.1093/emboj/19.21.572011060023
   PubMed Web of Science ®Google Scholar
• Kuma A, Matsui M, Mizushima NJA. LC3, an autophagosome marker, can be incorporated into protein aggregates independent of autophagy: caution in the interpretation of LC3 localization. Autophagy. 2007;3(4):323–328. doi:10.4161/auto.401217387262
   PubMed Web of Science ®Google Scholar
• Kimura S, Fujita N, Noda T, Yoshimori T. Monitoring autophagy in mammalian cultured cells through the dynamics of LC3. Methods Enzymol. 2009;452:1–12.19200872
   PubMed Web of Science ®Google Scholar
• Klionsky DJ, Abdelmohsen K, Abe A, et al. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy. 2016;12(1):1–222.26799652
   PubMed Web of Science ®Google Scholar