N-ω-chloroacetyl-l-ornithine, a new competitive inhibitor of ornithine decarboxylase, induces selective growth inhibition and cytotoxicity on human cancer cells versus normal cells

References

• Ferlay J, Shin HR, Bray F, et al. GLOBOCAN 2008, Cancer Incidence and Mortality Worldwide: IARC CancerBase No. 10. Lyon, France: International Agency for Research on Cancer; 2008. Available from: http://globocan.iarc.fr [last accessed 22 Oct 2013]
   Google Scholar
• Jemal A, Bray F, Center MM, et al. Global cancer statistics. CA Cancer J Clin 2011;6:69–90
   Google Scholar
• Seiler N. Thirty years of polyamine-related approaches to cancer therapy. Retrospect and prospect. Part 1. Selective enzyme inhibitors. Curr Drug Targets 2003;4:537–64
   Google Scholar
• Casero RA Jr, Marton LJ. Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases. Nat Rev Drug Discov 2007;6:373–90
   PubMed Web of Science ®Google Scholar
• Iyer AK, Singh A, Ganta S, Amiji MM. Role of integrated cancer nanomedicine in overcoming drug resistance. Adv Drug Deliv Rev 2013 65:1784–802
   PubMed Web of Science ®Google Scholar
• LaMuraglia GM, Lacaine F, Malt RA. High ornithine decarboxylase activity and polyamine levels in human colorectal neoplasia. Ann Surg 1986;204:89–93
   PubMed Web of Science ®Google Scholar
• Luk GD, Casero RA Jr. Polyamines in normal and cancer cells. Adv Enzyme Regul 1987;26:91–105
   PubMedGoogle Scholar
• Paz EA, Garcia-Huidobro J, Ignatenkos NA. Polyamines in cancer. Adv Clin Chem 2011;54:45–70
   PubMed Web of Science ®Google Scholar
• Soda KJ. The mechanisms by which polyamines accelerate tumor spread. Exp Clin Cancer Res 2011;30:95. doi: 10.1186/1756-9966-30-95
   PubMed Web of Science ®Google Scholar
• Shantz LM, Levin VA. Regulation of ornithine decarboxylase during oncogenic transformation: mechanisms and therapeutic potential. Amino Acids 2007;33:213–23
   PubMed Web of Science ®Google Scholar
• Nowotarski SL, Woster PM, Casero RA Jr. Polyamines and cancer: implications for chemotherapy and chemoprevention. Expert Rev Mol Med 2013;15:e3. doi: 10.1017/erm.2013.3
   PubMed Web of Science ®Google Scholar
• Russell D, Snyder SH. Amine synthesis in rapidly growing tissues: ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors. Proc Natl Acad Sci USA 1968;60:1420–7
   PubMed Web of Science ®Google Scholar
• Pegg AE, Shantz LM, Coleman CS. Ornithine decarboxylase as a target for chemoprevention. J Cell Biochem Suppl 1995;22:132–8
   PubMedGoogle Scholar
• Pegg AE, Feith DJ, Fong LY, et al. Transgenic mouse models for studies of the role of polyamines in normal, hypertrophic and neoplastic growth. Biochem Soc Trans 2003;31:356–60
   PubMed Web of Science ®Google Scholar
• Pegg AE. Regulation of ornithine decarboxylase. J Biol Chem 2006;281:14529–32
   PubMed Web of Science ®Google Scholar
• Verma AK. Inhibition of tumor promotion by dl-alpha-difluoromethylornithine, a specific irreversible inhibitor of ornithine decarboxylase. Basic Life Sci 1990;52:195–204
   PubMedGoogle Scholar
• Kubota S, Kiyosawa H, Nomura Y, et al. Ornithine decarboxylase overexpression in mouse 10T1/2 fibroblasts: cellular transformation and invasion. J Natl Cancer Inst 1997;89:567–71
   PubMed Web of Science ®Google Scholar
• Peralta Soler A, Gilliard G, Megosh L, et al. Polyamines regulate expression of the neoplastic phenotype in mouse skin. Cancer Res 1998;58:1654–9
   PubMed Web of Science ®Google Scholar
• Shantz LM, Pegg AE. Ornithine decarboxylase induction in transformation by H-Ras and RhoA. Cancer Res 1998;58:2748–53
   PubMed Web of Science ®Google Scholar
• Hurta RA. Altered ornithine decarboxylase and S-adenosylmethionine decarboxylase expression and regulation in mouse fibroblasts transformed with oncogenes or constitutively active Mitogen-Activated Protein (MAP) kinase kinase. Mol Cell Biochem 2000;215:81–92
   PubMed Web of Science ®Google Scholar
• Hardin MS, Mader R, Hurta RA. K-FGF mediated transformation and induction of metastatic potential involves altered ornithine decarboxylase and S-adenosylmethionine decarboxylase expression-role in cellular invasion. Mol Cell Biochem 2002;233:49–56
   PubMed Web of Science ®Google Scholar
• Heby O, Persson L, Rentala M. Targeting the polyamine biosynthetic enzymes: a promising approach to therapy of African sleeping sickness, Chagas' disease, and leishmaniasis. Amino Acids 2007;33:359–66
   PubMed Web of Science ®Google Scholar
• Birkholtz LM, Williams M, Niemand J, et al. Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities. Biochem J 2011;438:229–44
   Google Scholar
• Vlastos AT, West LA, Atkinson EN, et al. Results of a phase II double-blinded randomized clinical trial of difluoromethylornithine for cervical intraepithelial neoplasia grades 2 to 3. Clin Cancer Res 2005;11:390–6
   PubMed Web of Science ®Google Scholar
• Messing E, Kim KM, Sharkey F, et al. Randomized prospective phase III trial of difluoromethylornithine vs placebo in preventing recurrence of completely resected low risk superficial bladder cancer. J Urol 2006;176:500–4
   PubMed Web of Science ®Google Scholar
• Correa-Basurto J, Rodríguez-Páez L, Aguiar-Moreno ES, et al. Computational and experimental evaluation of ornithine derivatives as ornithine decarboxylase inhibitors. Med Chem Res 2009;18:20–30
   Web of Science ®Google Scholar
• Larimore FS, Roon RJ. Possible site-specific reagent for the general amino acid transport system of Saccharomyces cerevisiae. Biochemistry 1978;17:431–6
   PubMed Web of Science ®Google Scholar
• Woodward JR, Kornberg HL. Membrane proteins associated with amino acid transport by yeast (Saccharomyces cerevisiae). Biochem J 1980;192:659–64
   PubMed Web of Science ®Google Scholar
• Woodward JR, Kornberg HL. Changes in membrane proteins associated with inhibition of the general amino acid permease of yeast (Saccharomyces cerevisiae). Biochem J 1981;196:531–6
   PubMed Web of Science ®Google Scholar
• Auvin S, Cochet O, Kucharczyk N, et al. Synthesis and evaluation of inhibitors for Escherichia coli glucosamine-6-phosphate synthase. Bioorg Chem 1991;19:143–51
   Web of Science ®Google Scholar
• Ono M, Inoue H, Suzuki F, Takeda Y. Studies of ornithine decarboxylase from the liver of thioacetamide treated rats. Purification and some properties. Biochem Biophys 1972;284:285–97
   Google Scholar
• Hayashi S. Ornithine decarboxylase (rat liver). In: Tabor H, Tabor CW, eds. Methods in enzymology. Vol. 94. Polyamines. New York (NY): Academic Press Inc.; 1983:154–8
   Google Scholar
• Stojan J. Enzyme inhibitors. In: Smith J, Simons C, eds. Enzymes and their inhibition. Boca Raton (FL): CRC Press; 2005:149–69
   Google Scholar
• Louis KS, Siegel AC. Cell viability analysis using trypan blue: manual and automated methods. Methods Mol Biol 2011;740:7–12
   PubMedGoogle Scholar
• Li S, Liang Y, Wu M, et al. The novel mTOR inhibitor CCI-779 (temsirolimus) induces antiproliferative effects through inhibition of mTOR in Bel-7402 liver cancer cells. Cancer Cell Int 2013;13:30
   PubMedGoogle Scholar
• Pegg AE. Mammalian polyamine metabolism and function. IUBMB Life 2009;6:880–94
   Google Scholar
• Pegg AE, Casero RA Jr. Current status of the polyamine research field. Methods Mol Biol 2011;720:3–35
   PubMedGoogle Scholar
• Wallace HM, Fraser AV, Hughes A. A perspective of polyamine metabolism. Biochem J 2003;376:1–14
   PubMed Web of Science ®Google Scholar
• Wallace HM, Fraser AV. Inhibitors of polyamine metabolism. Amino Acids 2004;26:353–65
   PubMed Web of Science ®Google Scholar
• Wu F, Grossenbacher D, Gehring H. New transition state-based inhibitor for human ornithine decarboxylase inhibits growth of tumor cells. Mol Cancer Ther 2007;6:1831–9
   PubMed Web of Science ®Google Scholar
• Wu F, Gehring H. Structural requirements for novel coenzyme-substrate derivatives to inhibit intracellular ornithine decarboxylase and cell proliferation. FASEB J 2009;23:565–74
   PubMed Web of Science ®Google Scholar
• Silva TM, Andersson S, Sukumaran SK, et al. Norspermidine and novel Pd(II) and Pt(II) polynuclear complexes of norspermidine as potential antineoplastic agents against breast cancer. PLoS One 2013;8:e55651
   Web of Science ®Google Scholar
• Trujillo JG, Ceballos G, Yanez R, Joseph-Nathan P. Regioselective synthesis of (+)-S-2-amino-5-iodoacetamidopentanoic and (+)-S-2-amino-6-iodoacetamidohexanoic acids. Synth Comm 1991;21:683–91
   Web of Science ®Google Scholar
• Rodríguez-Páez L, Neri CD, Baeza RI, Wong RC. La δ-N-yodoactil ornitina y la ε-N-yodoacetil lisina como inhibidores irreversibles dirigidos al sitio activo de la ornitina descarboxilasa. An Esc Nac Cienc Biol Mex 1998;44:99–115
   Google Scholar
• Trujillo-Ferrara J, Koizumi G, Muñoz O, et al. Antitumor effect and toxicity of two new active-site-directed irreversible ornithine decarboxylase and extrahepatic arginase inhibitors. Cancer Lett 1992;67:193–7
   PubMed Web of Science ®Google Scholar
• Sjoerdsma A, Schechter PJ. Chemotherapeutic implications of polyamine biosynthesis inhibition. Clin Pharmacol Ther 1984;35:287–300
   PubMed Web of Science ®Google Scholar
• Williams-Ashman HG, Coppoc GL, Weber G. Imbalance in ornithine metabolism in hepatomas of different growth rates as expressed in formation of putrescine, spermidine, and spermine. Cancer Res 1972;32:1924–32
   PubMed Web of Science ®Google Scholar
• Russell DH. Ornithine decarboxylase as a biological and pharmacological tool. Pharmacology 1980;20:117–29
   PubMed Web of Science ®Google Scholar
• Ichimura S, Hamana K, Nenoi M. Significant increases in steady states of putrescine and spermidine/spermine N1-acetyltranserase mRNA in HeLa cells accompanied by growth arrest. Biochem Biophys Res Commun 1998;243:518–21
   PubMed Web of Science ®Google Scholar
• Pyronnet S, Pradayrol L, Sonenberg N. Alternative splicing facilitates internal ribosome entry on the ornithine decarboxylase mRNA. Cell Mol Life Sci 2005;62:1267–74
   PubMed Web of Science ®Google Scholar
• Deng W, Jiang X, Mei Y, et al. Role of ornithine decarboxylase in breast cancer. Acta Biochim Biophys Sin 2008;40:235–43
   Google Scholar
• Verma AJ. Polyamines and cancer. In: Wang J-Y, Casero RA Jr, eds. Polyamine cell signaling. Totowa (NJ): Humana Press; 2010:313–28
   Google Scholar
• Lundgren DW, Prokay SL. Glucose elevates ornithine decarboxylase expression in vero cells. J Cell Physiol 1988;137:469–75
   PubMed Web of Science ®Google Scholar
• Marverti G, Ligabue A, Lombardi A, et al. Modulation of the expression of folate cycle enzymes and polyamine metabolism by berberine in cisplatin-sensitive and -resistant human ovarian cancer cells. Int J Oncol 2013;43:1269–80
   PubMed Web of Science ®Google Scholar
• Pera PJ, Kramer DL, Sufrin JR, Porter CW. Comparison of the biological effects of four irreversible inhibitors of ornithine decarboxylase in two murine lymphocytic leukemia cell lines. Cancer Res 1986;46:1148–54
   PubMed Web of Science ®Google Scholar
• Sunkara PS, Chang CC, Prakash NJ, Lachmann PJ. Effect of inhibition of polyamine biosynthesis by dl-alpha-difluoromethylornithine on the growth and melanogenesis of B16 melanoma in vitro and in vivo. Cancer Res 1985;45:4067–70
   PubMed Web of Science ®Google Scholar
• Samal K, Zhao P, Kendzicky A, et al. AMXT-1501, a novel polyamine transport inhibitor, synergizes with DFMO in inhibiting neuroblastoma cell proliferation by targeting both ornithine decarboxylase and polyamine transport. Int J Cancer 2013;133:1323–33
   PubMed Web of Science ®Google Scholar
• Wu F, Gehring H. Structural requirements for novel coenzyme-substrate derivatives to inhibit intracellular ornithine decarboxylase and cell proliferation. FASEB J 2009;23:565–74
   PubMed Web of Science ®Google Scholar
• Zou C, Vlastos AT, Yang L, et al. Effects of difluoromethylornithine on growth inhibition and apoptosis in human cervical epithelial and cancerous cell lines. Gynecol Oncol 2002;85:266–73
   PubMed Web of Science ®Google Scholar
• Glikman P, Manni A, Demers L, Bartholomew M. Polyamine involvement in the growth of hormone-responsive and -resistant human breast cancer cells in culture. Cancer Res 1989;49:1371–6
   PubMed Web of Science ®Google Scholar
• Li M, Li Q, Zhang YH, et al. Antitumor effects and preliminary systemic toxicity of ANISpm in vivo and in vitro. Anticancer Drugs 2013;24:32–42
   PubMed Web of Science ®Google Scholar
• Fuchs BC, Bode BP. Amino acid transporters ASCT2 and LAT1 in cancer: partners in crime? Semin Cancer Biol 2005;15:254–66
   PubMed Web of Science ®Google Scholar
• Delcros JG, Tomasi S, Duhieu S, et al. Effect of polyamine homologation on the transport and biological properties of heterocyclic amidines. J Med Chem 2006;49:232–45
   PubMed Web of Science ®Google Scholar
• Ganapathy V, Thangaraju M, Prasad PD. Nutrient transporters in cancer: relevance to Warburg hypothesis and beyond. Pharmacol Ther 2009;121:29–40
   PubMed Web of Science ®Google Scholar
• Palacín M, Estévez R, Bertran J, Zorzano A. Molecular biology of mammalian plasma membrane amino acid transporters. Physiol Rev 1998;78:969–1054
   PubMed Web of Science ®Google Scholar
• del Amo EM, Urtti A, Yliperttula M. Pharmacokinetic role of L-type amino acid transporters LAT1 and LAT2. Eur J Pharm Sci 2008;35:161–74
   PubMed Web of Science ®Google Scholar
• Shikano N, Ogura M, Okudaira H, et al. Uptake of 3-[125I]iodo-alpha-methyl-L-tyrosine into colon cancer DLD-1 cells: characterization and inhibitory effect of natural amino acids and amino acid-like drugs. Nucl Med Biol 2010;37:197–204
   PubMed Web of Science ®Google Scholar
• Kalliokoski A, Niemi M. Impact of OATP transporters on phamacokinetics. Br J Pharmacol 2009;158:693–705
   PubMed Web of Science ®Google Scholar
• König J. Uptake transporters of the human OATP family: molecular characteristics, substrates, their role in drug-drug interactions, and functional consequences of polymorphisms. In: Fromm MF, Kim RB, eds. Drug transporters. Handbook of experimental pharmacology. Vol. 201. Berlin, Heidelberg: Springer-Verlag; 2011:1–28
   Google Scholar
• Fearn RA, Hirst BH. Predicting oral absorption and hepatobiliary clearance: human intestinal and hepatic in vitro cell models. Environ Toxicol Pharmacol 2006;21:168–78
   PubMed Web of Science ®Google Scholar
• Nies AT, Koepsell H, Damme K, Schwab M. Organic cation transporters (OCTs, MATEs), in vitro and in vivo evidence for the importance in drug therapy. In: Fromm MF, Kim RB, eds. Drug transporters. Handbook of experimental pharmacology. Vol. 201. Berlin, Heidelberg: Springer-Verlag; 2011:105–67
   Google Scholar
• Lozano E, Herraez E, Briz O, et al. Role of the plasma membrane transporter of organic cations OCT1 and its genetic variant in modern liver pharmacology. Biomed Res Int 2013;2013:692071
   PubMed Web of Science ®Google Scholar