The role of Colchicine on actin polymerization dynamics: as a potent anti-angiogenic factor

References

• Abdolmaleki, Z., Arab, H.-A., Amanpour, S., & Muhammadnejad, S. (2016). Anti-angiogenic effects of ethanolic extract of Artemisia sieberi compared to its active substance, artemisinin. Revista Brasileira de Farmacognosia, 26(3), 326–333. https://doi.org/10.1016/j.bjp.2015.11.008
   Google Scholar
• Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindah, E. (2015). Gromacs: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX, 1-2, 19–25. https://doi.org/10.1016/j.softx.2015.06.001
   Google Scholar
• Arjonen, A., Kaukonen, R., & Ivaska, J. (2011). Filopodia and adhesion in cancer cell motility. Cell Adhesion & Migration, 5(5), 421–430. https://doi.org/10.4161/cam.5.5.17723
   PubMed Web of Science ®Google Scholar
• Barron, G. A., Goua, M., Wahle, K. W. J., & Bermano, G. (2017). Circulating levels of angiogenesis-related growth factors in breast cancer: A study to profile proteins responsible for tubule formation. Oncology Reports, 38(3), 1886–1894. https://doi.org/10.3892/or.2017.5803
   PubMed Web of Science ®Google Scholar
• Bayless, K. J., & Johnson, G. A. (2011). Role of the cytoskeleton in formation and maintenance of angiogenic sprouts. Journal of Vascular Research, 48(5), 369–385. https://doi.org/10.1159/000324751
   PubMed Web of Science ®Google Scholar
• Bielenberg, D. R., & Zetter, B. R. (2015). The contribution of angiogenesis to the process of metastasis. Cancer Journal, 21(4), 267–273. https://doi.org/10.1097/PPO.0000000000000138
   PubMed Web of Science ®Google Scholar
• Blackadar, C. B. (2016). Historical review of the causes of cancer. World Journal of Clinical Oncology, 7(1), 54–86. https://doi.org/10.5306/wjco.v7.i1.54
   PubMed Web of Science ®Google Scholar
• Borana, M. S., Mishra, P., Pissurlenkar, R. R. S., Hosur, R. V., & Ahmad, B. (2014). Curcumin and kaempferol prevent lysozyme fibril formation by modulating aggregation kinetic parameters. Biochimica et Biophysica Acta, 1844(3), 670–680. https://doi.org/10.1016/j.bbapap.2014.01.009
   PubMed Web of Science ®Google Scholar
• Carlsson, L., & Blikstad, I. (1981). Colchicine treatment of HeLa cells alters the G/F actin ratio. FEBS Letters, 124(2), 282–284. https://doi.org/10.1016/0014-5793(81)80156-1
   PubMed Web of Science ®Google Scholar
• Chamani, J. (2010). Energetic domains analysis of bovine α-lactalbumin upon interaction with copper and dodecyl trimethylammonium bromide. Journal of Molecular Structure, 979(1-3), 227–234. https://doi.org/10.1016/j.molstruc.2010.06.035
   Web of Science ®Google Scholar
• Chen, Y., Gou, X., Ke, X., Cui, H., & Chen, Z. (2012). Human tumor cells induce angiogenesis through positive feedback between CD147 and insulin-like growth factor-I. PLoS One, 7(7), e40965. https://doi.org/10.1371/journal.pone.0040965
   PubMed Web of Science ®Google Scholar
• Dalbeth, N., Lauterio, T. J., & Wolfe, H. R. (2014). Mechanism of action of colchicine in the treatment of gout. Clinical Therapeutics, 36(10), 1465–1479. https://doi.org/10.1016/j.clinthera.2014.07.017
   PubMed Web of Science ®Google Scholar
• Daly, M. E., Makris, A., Reed, M., & Lewis, C. E. (2003). Hemostatic regulators of tumor angiogenesis: A source of antiangiogenic agents for cancer treatment? Journal of the National Cancer Institute, 95(22), 1660–1673. https://doi.org/10.1093/jnci/djg101
   PubMedGoogle Scholar
• Debreczeni, J. É., & Emsley, P. (2012). Handling ligands with Coot. Acta Crystallographica. Section D, Biological Crystallography, 68(Pt 4), 425–430. https://doi.org/10.1107/S0907444912000200
   PubMed Web of Science ®Google Scholar
• Dehghani Sani, F., Shakibapour, N., Beigoli, S., Sadeghian, H., Hosainzadeh, M., & Chamani, J. (2018). Changes in binding affinity between ofloxacin and calf thymus DNA in the presence of histone H1: Spectroscopic and molecular modeling investigations. Journal of Luminescence, 203, 599–608. https://doi.org/10.1016/j.jlumin.2018.06.083
   Web of Science ®Google Scholar
• Döme, B., Hendrix, M. J. C., Paku, S., Tóvári, J., & Tímár, J. (2007). Alternative vascularization mechanisms in cancer: Pathology and therapeutic implications. The American Journal of Pathology, 170(1), 1–15. https://doi.org/10.2353/ajpath.2007.060302
   PubMed Web of Science ®Google Scholar
• El Baba, N., Farran, M., Khalil, E. A., Jaafar, L., Fakhoury, I., & El-Sibai, M. (2020). The role of Rho GTPases in VEGF signaling in cancer cells. Analytical Cellular Pathology, 2020, 2097214. https://doi.org/10.1155/2020/2097214
   Web of Science ®Google Scholar
• Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010). Features and development of Coot. Acta Crystallographica Section D: Biological Crystallography, 66(Pt 4), 486–501. https://doi.org/10.1107/S0907444910007493
   PubMed Web of Science ®Google Scholar
• Ferlay, J., Soerjomataram, I., Ervik, M., Dikshit, R., & Eser, S., M. C. (2012). Cancer incidence and mortality worldwide: IARC CancerBase No. 11 Lyon, France. International Agency for Research on Cancer, GLOBOCAN, 136(5), E359–E386.
   Google Scholar
• Giordano, G., Febbraro, A., Venditti, M., Campidoglio, S., Olivieri, N., Raieta, K., Parcesepe, P., Imbriani, G. C., Remo, A., & Pancione, M. (2014). Targeting angiogenesis and tumor microenvironment in metastatic colorectal cancer: Role of aflibercept. Gastroenterology Research and Practice, 2014, 526178. https://doi.org/10.1155/2014/526178
   PubMed Web of Science ®Google Scholar
• Gourlay, C. W., Carpp, L. N., Timpson, P., Winder, S. J., & Ayscough, K. R. (2004). A role for the actin cytoskeleton in cell death and aging in yeast. The Journal of cell biology, 164(6), 803–809. https://doi.org/10.1083/jcb.200310148
   Google Scholar
• Haasdijk, R. A., Tempel, D., BüRgisser, P., van de Kamp, E. H. M., Blonden, L. A. J., Cheng, C., & Duckers, H. J. (2014). Klf7 regulates endothelial cell proliferation and differentiation in angiogenesis. In Angiogenesis the genetic regulation of vascular development (pp. 71–88). Erasmus Universiteit Rotterdam.
   Google Scholar
• Hardham, A. R., & Gunning, B. E. S. (1980). Some effects of colchicine on microtubules and cell division in roots of Azolla pinnata. Protoplasma, 102(1-2), 31–51. https://doi.org/10.1007/BF01276946
   Web of Science ®Google Scholar
• Hasbani, G. E., Jawad, A., & Uthman, I. (2019). Update on the management of colchicine resistant Familial Mediterranean Fever (FMF). Orphanet Journal of Rare Diseases, 14, 224.
   PubMed Web of Science ®Google Scholar
• Jászai, J., & Schmidt, M. H. H. (2019). Trends and challenges in tumor anti-angiogenic therapies. Cells, 8(9), 7–11. https://doi.org/10.3390/cells8091102
   Web of Science ®Google Scholar
• Joo, Y. Y., Jang, J. W., Lee, S. W., Yoo, S. H., Kwon, J. H., Nam, S. W., Bae, S. H., Choi, J. Y., & Yoon, S. K. (2019). Circulating pro- and anti-angiogenic factors in multi-stage liver disease and hepatocellular carcinoma progression. Scientific Reports, 9(1), 9137–9138. https://doi.org/10.1038/s41598-019-45537-w
   PubMedGoogle Scholar
• Jung, H. I., Shin, I., Park, Y. M., Kang, K. W., & Ha, K. S. (1997). Colchicine activates actin polymerization by microtubule depolymerization. Molecules and Cells, 7(3), 431–437.
   PubMed Web of Science ®Google Scholar
• Lamalice, L., Le Boeuf, F., & Huot, J. (2007). Endothelial cell migration during angiogenesis. Circulation Research, 100(6), 782–794. https://doi.org/10.1161/01.RES.0000259593.07661.1e
   PubMed Web of Science ®Google Scholar
• Lang, L., Hou, Y., Chen, Y., Tu, G., Tao, J., Yang, D., Xi, L., Fu, L., Sun, K., Yin, J., Chen, R., Peng, M., Liu, S., & Liu, M. (2018). ATM-mediated phosphorylation of cortactin involved in actin polymerization promotes breast cancer cells migration and invasion. Cellular Physiology and Biochemistry, 51(6), 2972–2988. https://doi.org/10.1159/000496048
   PubMedGoogle Scholar
• Li, W. W., Li, V. W., Hutnik, M., & Chiou, A. S. (2012). Tumor angiogenesis as a target for dietary cancer prevention. Journal of Oncology, 2012, 879623 https://doi.org/10.1155/2012/879623
   PubMedGoogle Scholar
• Liantinioti, G., Argyris, A. A., Protogerou, A. D., & Vlachoyiannopoulos, P. (2018). The role of Colchicine in the treatment of autoinflammatory diseases. Current Pharmaceutical Design, 24(6), 690–694. https://doi.org/10.2174/1381612824666180116095658
   PubMed Web of Science ®Google Scholar
• Liotta, L. A., & Stetler-Stevenson, W. G. (1991). Tumor invasion and metastasis: An imbalance of positive and negative regulation. Cancer Research, 51(18 SUPPL), 327–336.
   Web of Science ®Google Scholar
• Little RE, S. C. (2009). The New England Journal of Medicine Downloaded from nejm.org at CARLETON UNIVERSITY on March 3, 2016. For Personal Use Only. No Other Uses without Permission. From the NEJM Archive. Copyright © 2009 Massachusetts Medical Society. All Rights Reserved.
   Google Scholar
• Liu, H., Pierre-Pierre, N., & Huo, Q. (2012). Dynamic light scattering for gold nanorod size characterization and study of nanorod-protein interactions. Gold Bulletin, 45(4), 187–195. https://doi.org/10.1007/s13404-012-0067-4
   Web of Science ®Google Scholar
• Lugano, R., Ramachandran, M., & Dimberg, A. (2020). Tumor angiogenesis: Causes, consequences, challenges and opportunities. Cellular and Molecular Life Sciences, 77(9), 1745–1770. https://doi.org/10.1007/s00018-019-03351-7
   PubMed Web of Science ®Google Scholar
• Ma, X., & Yu, H. (2006). Global burden of cancer. Yale Journal of Biology and Medicine, 79(3–4), 85–94.
   PubMedGoogle Scholar
• Mahadevan, V., & Hart, I. R. (1990). Metastasis and angiogenesis. Acta Oncologica, 29(1), 97–103. https://doi.org/10.3109/02841869009089997
   PubMed Web of Science ®Google Scholar
• McLoughlin, E. C., & O’Boyle, N. M. (2020). Correction: Colchicine-binding site inhibitors from chemistry to clinic: A review. Pharmaceuticals 2020, 13, 8. Pharmaceuticals, 13(4), 1–43. https://doi.org/10.3390/ph13040072
   Web of Science ®Google Scholar
• Mokaberi, P., Reyhani, V., Amiri-Tehranizadeh, Z., Saberi, M. R., Beigoli, S., Samandar, F., & Chamani, J. (2019). New insights into the binding behavior of lomefloxacin and human hemoglobin using biophysical techniques: Binary and ternary approaches. New Journal of Chemistry, 43(21), 8132–8145. https://doi.org/10.1039/C9NJ01048C
   Web of Science ®Google Scholar
• Moosavi-Movahedi, A. A., Chamani, J., Gharanfoli, M., & Hakimelahi, G. H. (2004). Differential scanning calorimetric study of the molten globule state of cytochrome c induced by sodium n-dodecyl sulfate. Thermochimica Acta, 409(2), 137–144. https://doi.org/10.1016/S0040-6031(03)00358-7
   Web of Science ®Google Scholar
• Nguyen, M. P., Lee, D., Lee, S. H., Lee, H. E., Lee, H. Y., & Lee, Y. M. (2015). Deguelin inhibits vasculogenic function of endothelial progenitor cells in tumor progression and metastasis via suppression of focal adhesion. Oncotarget, 6(18), 16588–16600. https://doi.org/10.18632/oncotarget.3752
   PubMedGoogle Scholar
• Nishida, N., Yano, H., Nishida, T., Kamura, T., & Kojiro, M. (2006). Angiogenesis in cancer. Vascular Health and Risk Management, 2(3), 213–219. https://doi.org/10.2147/vhrm.2006.2.3.213
   PubMedGoogle Scholar
• Otterbein, L. R., Graceffa, P., & Dominguez, R. (2001). The crystal structure of uncomplexed actin in the ADP state. Science, 293(5530), 708–711. https://doi.org/10.1126/science.1059700
   PubMed Web of Science ®Google Scholar
• Papakonstanti, E. A., & Stournaras, C. (2008). Cell responses regulated by early reorganization of actin cytoskeleton. FEBS Letters, 582(14), 2120–2127. https://doi.org/10.1016/j.febslet.2008.02.064
   PubMed Web of Science ®Google Scholar
• Pathak, S., Tripathi, S., Deori, N., Ahmad, B., Verma, H., Lokhande, R., Nagotu, S., & Kale, A. (2021). Effect of tetracycline family of antibiotics on actin aggregation, resulting in the formation of Hirano bodies responsible for neuropathological disorders. Journal of Biomolecular Structure & Dynamics, 39 (1), 218–236. https://doi.org/10.1080/07391102.2020.1717629
   Web of Science ®Google Scholar
• Perez-Iratxeta, C., & Andrade-Navarro, M. A. (2008). K2D2: Estimation of protein secondary structure from circular dichroism spectra. BMC Structural Biology, 8, 25–25. https://doi.org/10.1186/1472-6807-8-25
   PubMed Web of Science ®Google Scholar
• Pezzella, F. (2019). Pharmacogenetics implementation in the clinics: Information and guidelines for germline variants. Cancer Drug Resistance, 2, 595–607. https://doi.org/10.20517/cdr.2019.39
   PubMedGoogle Scholar
• Prager, G. W., Poettler, M., Unseld, M., & Zielinski, C. C. (2012). Angiogenesis in cancer: Anti-VEGF escape mechanisms. Translational Lung Cancer Research, 1(1), 14–25. https://doi.org/10.3978/j.issn.2218-6751.2011.11.02
   PubMedGoogle Scholar
• Pralhad, T., Madhusudan, S., & Rajendrakumar, K. (2003). Concept, mechanisms and therapeutics of angiogenesis in cancer and other diseases. The Journal of Pharmacy and Pharmacology, 55(8), 1045–1053. https://doi.org/10.1211/0022357021819
   PubMed Web of Science ®Google Scholar
• Racherla, R., Mudhigeti, N., Kalawat, U., & Mohan, A. (2019). Trends of acute – Phase dengue at a tertiary care hospital, Tirupati, Andhra Pradesh India. The Journal of Clinical and Scientific Research, 7(4), 175. https://doi.org/10.4103/JCSR.JCSR
   Google Scholar
• Rajabi, M., & Mousa, S. A. (2017). The role of angiogenesis in cancer treatment. Biomedicines, 5(2), 34. https://doi.org/10.3390/biomedicines5020034
   Google Scholar
• Rodríguez-Caso, L., Reyes-Palomares, A., Sánchez-Jiménez, F., Quesada, A. R., & Medina, M. Á. (2012). What is known on angiogenesis-related rare diseases? A systematic review of literature. Journal of Cellular and Molecular Medicine, 16(12), 2872–2893. https://doi.org/10.1111/j.1582-4934.2012.01616.x
   PubMed Web of Science ®Google Scholar
• Saaristo, A., Karpanen, T., & Alitalo, K. (2000). Mechanisms of angiogenesis and their use in the inhibition of tumor growth and metastasis. Oncogene, 19(53), 6122–6129. https://doi.org/10.1038/sj.onc.1203969
   PubMed Web of Science ®Google Scholar
• Schindelin, J., Arganda-Carreras, I., Frise, E., Kaynig, V., Longair, M., Pietzsch, T., Preibisch, S., Rueden, C., Saalfeld, S., Schmid, B., Tinevez, J.-Y., White, D. J., Hartenstein, V., Eliceiri, K., Tomancak, P., & Cardona, A. (2012). Fiji: An open-source platform for biological-image analysis. Nature Methods, 9(7), 676–682. https://doi.org/10.1038/nmeth.2019
   PubMed Web of Science ®Google Scholar
• Schnittler, H., Taha, M., Schnittler, M. O., Taha, A. A., Lindemann, N., & Seebach, J. (2014). Actin filament dynamics and endothelial cell junctions: The Ying and Yang between stabilization and motion. Cell and Tissue Research, 355(3), 529–543. https://doi.org/10.1007/s00441-014-1856-2
   PubMed Web of Science ®Google Scholar
• Sharifi-Rad, M., Berkay Yılmaz, Y., Antika, G., Salehi, B., Tumer, T. B., Kulandaisamy Venil, C., Das, G., Patra, J. K., Karazhan, N., Akram, M., Iqbal, M., Imran, M., Sen, S., Acharya, K., Dey, A., & Sharifi-Rad, J. (2021). Phytochemical constituents, biological activities, and healthpromoting effects of the genus Origanum. Phytotherapy research : PTR, 35(1), 95–121. https://doi.org/10.1002/ptr.6785
   Google Scholar
• Skoufias, D. A., & Wilson, L. (1992). Mechanism of inhibition of microtubule polymerization by colchicine: Inhibitory potencies of unliganded colchicine and tubulin-colchicine complexes. Biochemistry, 31(3), 738–746. https://doi.org/10.1021/bi00118a015
   PubMed Web of Science ®Google Scholar
• Sohrabi, T., Hosseinzadeh, M., Beigoli, S., Saberi, M. R., & Chamani, J. (2018). Probing the binding of lomefloxacin to a calf thymus DNA-histone H1 complex by multi-spectroscopic and molecular modeling techniques. Journal of Molecular Liquids, 256, 127–138. https://doi.org/10.1016/j.molliq.2018.02.031
   Web of Science ®Google Scholar
• Solomon, E. I., Augustine, A. J., & Yoon, J. (2010). Rapid and efficient purification of actin from nonmuscle sources. Cell Motility and the Cytoskeleton, 39(30), 3921–3932. https://doi.org/10.1039/b800799c.O
   Google Scholar
• Sonavane, S., Haider, S. Z., Kumar, A., & Ahmad, B. (2017). Hemin is able to disaggregate lysozyme amyloid fibrils into monomers. Biochimica et Biophysica Acta. Proteins and Proteomics, 1865(11 Pt A), 1315–1325. https://doi.org/10.1016/j.bbapap.2017.07.017
   PubMed Web of Science ®Google Scholar
• Stevenson, R. P., Veltman, D., & Machesky, L. M. (2012). Actin-bundling proteins in cancer progression at a glance. Journal of Cell Science, 125(Pt 5), 1073–1079. https://doi.org/10.1242/jcs.093799
   PubMed Web of Science ®Google Scholar
• Sun, B., Fang, Y., Li, Z., Chen, Z., & Xiang, J. (2015). Role of cellular cytoskeleton in epithelial-mesenchymal transition process during cancer progression. Biomedical Reports, 3(5), 603–610. https://doi.org/10.3892/br.2015.494
   PubMed Web of Science ®Google Scholar
• Sund, M., & Kalluri, R. (2008). Endogenous inhibitors of angiogenesis. Tumor Angiogenesis: Basic Mechanisms and Cancer Therapy, 10, 215–231. https://doi.org/10.1007/978-3-540-33177-3_12
   Google Scholar
• Tolentino, L. K. S., Justine Enrico, E. G., Listanco, R. L. M., Anthony Ramirez, M. M., Renon, T. L. U., & Rikko Samson, M. B. (2019). Development of fertile egg detection and incubation system using image processing and automatic candling [Paper presentation]. IEEE Region 10 Annual International Conference, Proceedings/TENCON, 2018-October (April), 701–706. https://doi.org/10.1109/TENCON.2018.8650320
   Google Scholar
• Trott, O., & Olson, A. J. (2010). AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem., 31, 455–461. http://doi.org/10.1002/jcc.21334
   Google Scholar
• Vandecandelaere, A., Martin, S. R., & Engelborghs, Y. (1997). Response of microtubules to the addition of colchicine and tubulin-colchicine: Evaluation of models for the interaction of drugs with microtubules. The Biochemical Journal, 323(1), 189–196. https://doi.org/10.1042/bj3230189
   PubMedGoogle Scholar
• Wang, D., Xie, Y., Yan, M., Pan, Q., Liang, Y., & Sun, X. (2019). Colchicine causes prenatal cell toxicity and increases tetraploid risk. BMC Pharmacology & Toxicology, 20(1), 66–68. https://doi.org/10.1186/s40360-019-0365-z
   PubMed Web of Science ®Google Scholar
• Wang, Z., Dabrosin, C., Yin, X., Fuster, M. M., Arreola, A., Rathmell, W. K., Generali, D., Nagaraju, G. P., El-Rayes, B., Ribatti, D., Chen, Y. C., Honoki, K., Fujii, H., Georgakilas, A. G., Nowsheen, S., Amedei, A., Niccolai, E., Amin, A., Ashraf, S. S., … Jensen, L. D. (2015). Broad targeting of angiogenesis for cancer prevention and therapy. Seminars in Cancer Biology, 35 Suppl, S224–S243. https://doi.org/10.1016/j.semcancer.2015.01.001
   PubMed Web of Science ®Google Scholar
• Wiedemann, C., Bellstedt, P., & Görlach, M. (2013). CAPITO-a web server-based analysis and plotting tool for circular dichroism data . Bioinformatics, 29(14), 1750–1757. https://doi.org/10.1093/bioinformatics/btt278
   PubMed Web of Science ®Google Scholar
• Yamazaki, D., Kurisu, S., & Takenawa, T. (2005). Regulation of cancer cell motility through actin reorganization. Cancer Science, 96(7), 379–386. https://doi.org/10.1111/j.1349-7006.2005.00062.x
   PubMed Web of Science ®Google Scholar
• Zuazo-Gaztelu, I., & Casanovas, O. (2018). Unraveling the role of angiogenesis in cancer ecosystems. Frontiers in Oncology, 8(JUL), 213–248. https://doi.org/10.3389/fonc.2018.00248
   PubMedGoogle Scholar