Heterocycle-containing tranylcypromine derivatives endowed with high anti-LSD1 activity

References

• Bhat KP, Umit Kaniskan H, Jin J, Gozani O. Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease. Nat Rev Drug Discov 2021;20:265–86.
   PubMed Web of Science ®Google Scholar
• Sterling J, Menezes SV, Abbassi RH, Munoz L. Histone lysine demethylases and their functions in cancer. Int J Cancer 2021;148:2375–2388.
   Web of Science ®Google Scholar
• Laurent B, Ruitu L, Murn J, et al. A specific LSD1/KDM1A isoform regulates neuronal differentiation through H3K9 demethylation. Mol Cell 2015;57:957–70.
   PubMed Web of Science ®Google Scholar
• Metzger E, Wissmann M, Yin N, et al. LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 2005;437:436–9.
   PubMed Web of Science ®Google Scholar
• Shi Y, Lan F, Matson C, et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 2004;119:941–53.
   PubMed Web of Science ®Google Scholar
• Shi YJ, Matson C, Lan F, et al. Regulation of LSD1 histone demethylase activity by its associated factors. Mol Cell 2005;19:857–64.
   PubMed Web of Science ®Google Scholar
• Wada T, Koyama D, Kikuchi J, et al. Overexpression of the shortest isoform of histone demethylase LSD1 primes hematopoietic stem cells for malignant transformation. Blood 2015;125:3731–46.
   PubMed Web of Science ®Google Scholar
• Karytinos A, Forneris F, Profumo A, et al. A novel mammalian flavin-dependent histone demethylase. J Biol Chem 2009;284:17775–82.
   PubMed Web of Science ®Google Scholar
• Yang GJ, Lei PM, Wong SY, et al. Pharmacological Inhibition of LSD1 for Cancer Treatment. Molecules 2018;23:3194.
   PubMed Web of Science ®Google Scholar
• Wang Y, Zhang H, Chen Y, et al. LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. Cell 2009;138:660–72.
   PubMed Web of Science ®Google Scholar
• Wang M, Liu X, Jiang G, et al. Relationship between LSD1 expression and E-cadherin expression in prostate cancer. Int Urol Nephrol 2015;47:485–90.
   PubMed Web of Science ®Google Scholar
• Chen L, Xu Y, Xu B, et al. Over-expression of lysine-specific demethylase 1 predicts tumor progression and poor prognosis in human esophageal cancer. Int J Clin Exp Pathol 2014;7:8929–34.
   PubMed Web of Science ®Google Scholar
• Forneris F, Binda C, Battaglioli E, Mattevi A. LSD1: oxidative chemistry for multifaceted functions in chromatin regulation. Trends Biochem Sci 2008;33:181–9.
   PubMed Web of Science ®Google Scholar
• Edmondson DE, Binda C, Wang J, et al. Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases. Biochemistry 2009;48:4220–30.
   PubMed Web of Science ®Google Scholar
• Yang M, Culhane JC, Szewczuk LM, et al. Structural basis of histone demethylation by LSD1 revealed by suicide inactivation. Nat Struct Mol Biol 2007;14:535–9.
   PubMed Web of Science ®Google Scholar
• Dai XJ, Liu Y, Xiong XP, et al. Tranylcypromine based lysine-specific demethylase 1 inhibitor: summary and perspective. J Med Chem 2020;63:14197–215.
   PubMed Web of Science ®Google Scholar
• Binda C, Valente S, Romanenghi M, et al. Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2. J Am Chem Soc 2010;132:6827–33.
   PubMed Web of Science ®Google Scholar
• Valente S, Rodriguez V, Mercurio C, et al. Pure enantiomers of benzoylamino-tranylcypromine: LSD1 inhibition, gene modulation in human leukemia cells and effects on clonogenic potential of murine promyelocytic blasts. Eur J Med Chem 2015;94:163–74.
   PubMed Web of Science ®Google Scholar
• Valente S, Rodriguez V, Mercurio C, et al. Pure diastereomers of a tranylcypromine-based LSD1 inhibitor: enzyme selectivity and in-cell studies. ACS Med Chem Lett 2015;6:173–7.
   PubMed Web of Science ®Google Scholar
• Vianello P, Botrugno OA, Cappa A, et al. Synthesis, biological activity and mechanistic insights of 1-substituted cyclopropylamine derivatives: a novel class of irreversible inhibitors of histone demethylase KDM1A. Eur J Med Chem 2014;86:352–63.
   PubMed Web of Science ®Google Scholar
• Vianello P, Botrugno OA, Cappa A, et al. Discovery of a novel inhibitor of histone lysine-specific demethylase 1A (KDM1A/LSD1) as orally active antitumor agent. J Med Chem 2016;59:1501–17.
   PubMedGoogle Scholar
• Rodriguez V, Valente S, Rovida S, et al. Pyrrole- and indole-containing tranylcypromine derivatives as novel lysine-specific demethylase 1 inhibitors active on cancer cells. MedChemComm 2015;6:665–70.
   Web of Science ®Google Scholar
• Rotili D, Tomassi S, Conte M, et al. Pan-histone demethylase inhibitors simultaneously targeting Jumonji C and lysine-specific demethylases display high anticancer activities. J Med Chem 2014;57:42–55.
   PubMed Web of Science ®Google Scholar
• Kalin JH, Wu M, Gomez AV, et al. Targeting the CoREST complex with dual histone deacetylase and demethylase inhibitors. Nat Commun 2018;9:53.
   PubMed Web of Science ®Google Scholar
• Fioravanti R, Romanelli A, Mautone N, et al. Tranylcypromine-based LSD1 inhibitors: structure-activity relationships, antiproliferative effects in leukemia, and gene target modulation. ChemMedChem 2020;15:643–58.
   PubMed Web of Science ®Google Scholar
• Ravasio R, Ceccacci E, Nicosia L, et al. Targeting the scaffolding role of LSD1 (KDM1A) poises acute myeloid leukemia cells for retinoic acid-induced differentiation. Sci Adv 2020;6:eaax2746.
   PubMed Web of Science ®Google Scholar
• Nicosia L, Boffo FL, Ceccacci E, et al. Pharmacological inhibition of LSD1 triggers myeloid differentiation by targeting GSE1 oncogenic functions in AML. Oncogene 2022;41:878–894.
   PubMed Web of Science ®Google Scholar
• Forneris F, Orru R, Bonivento D, et al. ThermoFAD, a thermofluor-adapted flavin ad hoc detection system for protein folding and ligand binding. Febs J 2009;276:2833–40.
   PubMed Web of Science ®Google Scholar
• Forneris F, Binda C, Adamo A, et al. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J Biol Chem 2007;282:20070–4.
   PubMed Web of Science ®Google Scholar
• Gaur S, Gross ME, Liao CP, et al. Effect of monoamine oxidase A (MAOA) inhibitors on androgen-sensitive and castration-resistant prostate cancer cells. Prostate 2019;79:667–77.
   PubMed Web of Science ®Google Scholar
• Wu JB, Shao C, Li X, et al. Monoamine oxidase A mediates prostate tumorigenesis and cancer metastasis. J Clin Invest 2014;124:2891–908.
   PubMed Web of Science ®Google Scholar
• Wu JB, Lin TP, Gallagher JD, et al. Monoamine oxidase A inhibitor-near-infrared dye conjugate reduces prostate tumor growth. J Am Chem Soc 2015;137:2366–74.
   PubMed Web of Science ®Google Scholar
• Wang K, Luo J, Yeh S, et al. The MAO inhibitors phenelzine and clorgyline revert enzalutamide resistance in castration resistant prostate cancer. Nat Commun 2020;11:2689.
   PubMed Web of Science ®Google Scholar
• Wissmann M, Yin N, Muller JM, et al. Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression. Nat Cell Biol 2007;9:347–53.
   PubMed Web of Science ®Google Scholar
• Maes T, Mascaro C, Tirapu I, et al. ORY-1001, a potent and selective covalent KDM1A inhibitor, for the treatment of acute leukemia. Cancer Cell 2018;33:495–511 e12.
   PubMed Web of Science ®Google Scholar