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The Epigenetic Drug 5-Azacytidine Interferes with Cholesterol and Lipid Metabolism

Poirier, Steve, Samami, Samaneh, Mamarbachi, Maya, Demers, Annie, Chang, Ta Yuan, Vance, Dennis E., Hatch, Grant M., Mayer, Gaétan·2014·Journal of Biological Chemistry

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Crossref · 10.1074/jbc.m114.563650

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  • Several compounds known to increase LDLR mRNA stability directly have also been reported to decrease expression of SREBP-regulated genes, including PCSK9, exhibiting a dual effect.

    “Interestingly, while these compounds are known to increase LDLR mRNA stability directly, several have also been reported to decrease the expression of SREBP-regulated genes, including PCSK9, thus exhibiting a dual effect that could have significant implications for cholesterol management [19,35,42].”
  • Triciribine shares with berberine and 5-AzaC the traits of inhibition of DNA synthesis, induction of ERK activity, stabilization of LDLR mRNA, and inhibition of PCSK9 expression.

    “Interestingly, triciribine shares a number of similar traits with berberine and 5-AzaC: 1) inhibition of DNA synthesis, 2) induction of ERK activity, 3) stabilization of LDLR mRNA and 4) inhibition of PCSK9 expression11,34,35,49–51.”
  • The effects of triciribine on LDLR mRNA stability and PCSK9 levels were reminiscent of those elicited by berberine and 5-Azacytidine (5-AzaC).

    “The effects of triciribine on LDLR mRNA stability and PCSK9 levels were reminiscent of those elicited by berberine and 5-Azacytidine (5-AzaC)11,34,35.”

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Research works printed but not linked: 53

  1. Jaenisch, 2003, Epigenetic regulation of gene expression: how the genome integrates intrinsic and environmental signals, Nat. Genet, 33, 245, 10.1038/ng1089 · DOI · Paper page
  2. Gnyszka, 2013, DNA methyltransferase inhibitors and their emerging role in epigenetic therapy of cancer, Anticancer Res, 33, 2989
  3. Estey, 2013, Epigenetics in clinical practice: the examples of azacitidine and decitabine in myelodysplasia and acute myeloid leukemia, Leukemia, 27, 1803, 10.1038/leu.2013.173 · DOI
  4. Hollenbach, 2010, A comparison of azacitidine and decitabine activities in acute myeloid leukemia cell lines, PLoS One, 5, e9001, 10.1371/journal.pone.0009001 · DOI
  5. Flotho, 2009, The DNA methyltransferase inhibitors azacitidine, decitabine and zebularine exert differential effects on cancer gene expression in acute myeloid leukemia cells, Leukemia, 23, 1019, 10.1038/leu.2008.397 · DOI
  6. Cihák, 1974, Biological effects of 5-azacytidine in eukaryotes, Oncology, 30, 405, 10.1159/000224981 · DOI
  7. Vigna, 2011, Epigenetic regulation in myelodysplastic syndromes: implications for therapy, Expert Opin. Investig. Drugs, 20, 465, 10.1517/13543784.2011.559164 · DOI
  8. Aimiuwu, 2012, RNA-dependent inhibition of ribonucleotide reductase is a major pathway for 5-azacytidine activity in acute myeloid leukemia, Blood, 119, 5229, 10.1182/blood-2011-11-382226 · DOI
  9. Brown, 2009, Cholesterol feedback: from Schoenheimer's bottle to Scap's MELADL, J. Lipid Res, 50, S15, 10.1194/jlr.R800054-JLR200 · DOI · Paper page
  10. Moon, 2012, The Scap/SREBP pathway is essential for developing diabetic fatty liver and carbohydrate-induced hypertriglyceridemia in animals, Cell Metab, 15, 240, 10.1016/j.cmet.2011.12.017 · DOI · Paper page
  11. Tang, 2011, Inhibition of SREBP by a small molecule, betulin, improves hyperlipidemia and insulin resistance and reduces atherosclerotic plaques, Cell Metab, 13, 44, 10.1016/j.cmet.2010.12.004 · DOI · Paper page
  12. Global Lipids Genetics Consortium, 2013, Discovery and refinement of loci associated with lipid levels, Nat. Genet, 45, 1274, 10.1038/ng.2797 · DOI
  13. Rakyan, 2011, Epigenome-wide association studies for common human diseases, Nat. Rev. Genet, 12, 529, 10.1038/nrg3000 · DOI
  14. Ehara, 2012, Role of DNA methylation in the regulation of lipogenic glycerol-3-phosphate acyltransferase 1 gene expression in the mouse neonatal liver, Diabetes, 61, 2442, 10.2337/db11-1834 · DOI
  15. Mayer, 2008, The regulated cell surface zymogen activation of the proprotein convertase PC5A directs the processing of its secretory substrates, J. Biol. Chem, 283, 2373, 10.1074/jbc.M708763200 · DOI
  16. Horton, 1998, Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2, J. Clin. Invest, 101, 2331, 10.1172/JCI2961 · DOI
  17. Hua, 1996, Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein, Cell, 87, 415, 10.1016/S0092-8674(00)81362-8 · DOI · Paper page
  18. Rawson, 1997, Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs, Mol. Cell, 1, 47, 10.1016/S1097-2765(00)80006-4 · DOI · Paper page
  19. Chang, 1993, Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells, J. Biol. Chem, 268, 20747, 10.1016/S0021-9258(19)36846-2 · DOI
  20. Huang da, 2009, Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources, Nat. Protoc, 4, 44, 10.1038/nprot.2008.211 · DOI · Paper page
  21. Li, 2009, Hepatocyte nuclear factor 1α plays a critical role in PCSK9 gene transcription and regulation by the natural hypocholesterolemic compound berberine, J. Biol. Chem, 284, 28885, 10.1074/jbc.M109.052407 · DOI
  22. Jeong, 2008, Sterol-dependent regulation of proprotein convertase subtilisin/kexin type 9 expression by sterol-regulatory element binding protein-2, J. Lipid Res, 49, 399, 10.1194/jlr.M700443-JLR200 · DOI · Paper page
  23. Seidah, 2012, Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced LDL receptor degradation, PLoS One, 7, e41865, 10.1371/journal.pone.0041865 · DOI · Paper page
  24. Wang, 1994, SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis, Cell, 77, 53, 10.1016/0092-8674(94)90234-8 · DOI
  25. Pelech, 1981, cAMP analogues inhibit phosphatidylcholine biosynthesis in cultured rat hepatocytes, J. Biol. Chem, 256, 8283, 10.1016/S0021-9258(19)68839-3 · DOI
  26. Hatch, 1996, Regulation of cardiolipin biosynthesis in H9c2 cardiac myoblasts by cytidine 5′-triphosphate, J. Biol. Chem, 271, 25810, 10.1074/jbc.271.42.25810 · DOI
  27. Abifadel, 2003, Mutations in PCSK9 cause autosomal dominant hypercholesterolemia, Nat. Genet, 34, 154, 10.1038/ng1161 · DOI · Paper page
  28. Horton, 2003, Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes, Proc. Natl. Acad. Sci. U.S.A, 100, 12027, 10.1073/pnas.1534923100 · DOI · Paper page
  29. Cameron, 2008, Berberine decreases PCSK9 expression in HepG2 cells, Atherosclerosis, 201, 266, 10.1016/j.atherosclerosis.2008.02.004 · DOI
  30. Poirier, 2013, The biology of PCSK9 from the endoplasmic reticulum to lysosomes: new and emerging therapeutics to control low-density lipoprotein cholesterol, Drug Des. Devel. Ther, 7, 1135
  31. Maxwell, 2003, Novel putative SREBP and LXR target genes identified by microarray analysis in liver of cholesterol-fed mice, J. Lipid Res, 44, 2109, 10.1194/jlr.M300203-JLR200 · DOI · Paper page
  32. Sato, 1996, Sterol-dependent transcriptional regulation of sterol regulatory element-binding protein-2, J. Biol. Chem, 271, 26461, 10.1074/jbc.271.43.26461 · DOI
  33. Cao, 2006, Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis, Proc. Natl. Acad. Sci. U.S.A, 103, 19695, 10.1073/pnas.0609140103 · DOI
  34. Lagace, 2013, The role of phospholipids in the biological activity and structure of the endoplasmic reticulum, Biochim. Biophys. Acta, 1833, 2499, 10.1016/j.bbamcr.2013.05.018 · DOI
  35. Jamal, 1991, Plasma membrane fractions from rat liver contain a phosphatidate phosphohydrolase distinct from that in the endoplasmic reticulum and cytosol, J. Biol. Chem, 266, 2988, 10.1016/S0021-9258(18)49945-0 · DOI
  36. Meza-Avina, 2010, Structural determinants for the inhibitory ligands of orotidine-5′-monophosphate decarboxylase, Bioorg. Med. Chem, 18, 4032, 10.1016/j.bmc.2010.04.017 · DOI
  37. Carter, 1966, Enzymatic synthesis of cytidine diphosphate diglyceride, J. Lipid Res, 7, 678, 10.1016/S0022-2275(20)39250-6 · DOI
  38. Keating, 2012, Azacitidine: a review of its use in the management of myelodysplastic syndromes/acute myeloid leukaemia, Drugs, 72, 1111, 10.2165/11209430-000000000-00000 · DOI
  39. Abidi, 2005, Extracellular signal-regulated kinase-dependent stabilization of hepatic low-density lipoprotein receptor mRNA by herbal medicine berberine, Arterioscler. Thromb. Vasc. Biol, 25, 2170, 10.1161/01.ATV.0000181761.16341.2b · DOI · Paper page
  40. Lehner, 2012, Lumenal lipid metabolism: implications for lipoprotein assembly, Arterioscler. Thromb. Vasc. Biol, 32, 1087, 10.1161/ATVBAHA.111.241497 · DOI
  41. Sokolov, 2010, Accessibility of cholesterol in endoplasmic reticulum membranes and activation of SREBP-2 switch abruptly at a common cholesterol threshold, J. Biol. Chem, 285, 29480, 10.1074/jbc.M110.148254 · DOI · Paper page
  42. Raabe, 1999, Analysis of the role of microsomal triglyceride transfer protein in the liver of tissue-specific knockout mice, J. Clin. Invest, 103, 1287, 10.1172/JCI6576 · DOI · Paper page
  43. Newberry, 2003, Decreased hepatic triglyceride accumulation and altered fatty acid uptake in mice with deletion of the liver fatty acid-binding protein gene, J. Biol. Chem, 278, 51664, 10.1074/jbc.M309377200 · DOI
  44. Sturley, 2012, Lipid droplet formation on opposing sides of the endoplasmic reticulum, J. Lipid Res, 53, 1800, 10.1194/jlr.R028290 · DOI
  45. Shan, 2010, GPAT3 and GPAT4 are regulated by insulin-stimulated phosphorylation and play distinct roles in adipogenesis, J. Lipid Res, 51, 1971, 10.1194/jlr.M006304 · DOI
  46. Schulze, 2012, How cancer metabolism is tuned for proliferation and vulnerable to disruption, Nature, 491, 364, 10.1038/nature11706 · DOI
  47. Shao, 2012, Expanding roles for SREBP in metabolism, Cell Metab, 16, 414, 10.1016/j.cmet.2012.09.002 · DOI
  48. Ellis, 2012, Alteration of lipids and the transcription of lipid-related genes in myelodysplastic syndromes via a TP53-related pathway, Exp. Hematol, 40, 540, 10.1016/j.exphem.2012.02.003 · DOI
  49. Williams, 2013, An essential requirement for the SCAP/SREBP signaling axis to protect cancer cells from lipotoxicity, Cancer Res, 73, 2850, 10.1158/0008-5472.CAN-13-0382-T · DOI
  50. Fozza, 2009, Patients with myelodysplastic syndromes display several T-cell expansions, which are mostly polyclonal in the CD4+ subset and oligoclonal in the CD8+ subset, Exp. Hematol, 37, 947, 10.1016/j.exphem.2009.04.009 · DOI
  51. Santos, 2012, Lipid metabolism in cancer, FEBS J, 279, 2610, 10.1111/j.1742-4658.2012.08644.x · DOI
  52. Abbas, 2012, Survival outcome of veterans with myelodysplastic syndrome (MDS) treated with statins, J. Clin. Oncol, 30, e17018, 10.1200/jco.2012.30.15_suppl.e17018 · DOI
  53. van Besien, 2013, Antileukemic properties of 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors, Leuk. Lymphoma, 54, 2601, 10.3109/10428194.2013.790022 · DOI

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Metadata

Authors
Poirier, S., Samami, S., Mamarbachi, M., Demers, A., Chang, T. Y., Vance, D. E., Hatch, G. M., & Mayer, G.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2014-07
Volume
289
Issue
27
Pages
18736-18751
ISSN
0021-9258
Cited by
47
References
2
Language
en

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