Physiological effects of Type 2 diabetes on mRNA processing and gene expression

References

• Devaraj S, Dasu MR, Jialal I. Diabetes is a proinflammatory state: a translational perspective. Expert Rev. Endocrinol. Metab.5(1), 19–28 (2010).
   PubMedGoogle Scholar
• Stumvoll M, Goldstein BJ, van Haeften TW. Type 2 diabetes: principles of pathogenesis and therapy. Lancet365(9467), 1333–1346 (2005).
   PubMed Web of Science ®Google Scholar
• Chang-Chen KJ, Mullur R, Bernal-Mizrachi E. β-cell failure as a complication of diabetes. Rev. Endocr. Metab. Disord.9(4), 329–343 (2008).
   PubMed Web of Science ®Google Scholar
• Poitout V, Robertson RP. Glucolipotoxicity: fuel excess and β-cell dysfunction. Endocr. Rev.29(3), 351–366 (2008).
   PubMed Web of Science ®Google Scholar
• Del Prato S. Role of glucotoxicity and lipotoxicity in the pathophysiology of Type 2 diabetes mellitus and emerging treatment strategies. Diabet. Med.26(12), 1185–1192 (2009).
   PubMed Web of Science ®Google Scholar
• Poitout V, Amyot J, Semache M, Zarrouki B, Hagman D, Fontes G. Glucolipotoxicity of the pancreatic β cell. Biochim. Biophys. Acta1801(3), 289–298 (2010).
   PubMed Web of Science ®Google Scholar
• El-Assaad W, Buteau J, Peyot ML et al. Saturated fatty acids synergize with elevated glucose to cause pancreatic β-cell death. Endocrinology144(9), 4154–4163 (2003).
   PubMed Web of Science ®Google Scholar
• Jacqueminet S, Briaud I, Rouault C, Reach G, Poitout V. Inhibition of insulin gene expression by long-term exposure of pancreatic β cells to palmitate is dependent on the presence of a stimulatory glucose concentration. Metabolism49(4), 532–536 (2000).
   PubMedGoogle Scholar
• Briaud I, Kelpe CL, Johnson LM, Tran PO, Poitout V. Differential effects of hyperlipidemia on insulin secretion in islets of langerhans from hyperglycemic versus normoglycemic rats. Diabetes51(3), 662–668 (2002).
   Google Scholar
• Cnop M. Fatty acids and glucolipotoxicity in the pathogenesis of Type 2 diabetes. Biochem. Soc. Trans.36(Pt 3), 348–352 (2008).
   PubMed Web of Science ®Google Scholar
• Briaud I, Harmon JS, Kelpe CL, Segu VB, Poitout V. Lipotoxicity of the pancreatic β-cell is associated with glucose-dependent esterification of fatty acids into neutral lipids. Diabetes50(2), 315–321 (2001).
   PubMed Web of Science ®Google Scholar
• Prentki M, Joly E, El-Assaad W, Roduit R. Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: role in β-cell adaptation and failure in the etiology of diabetes. Diabetes51(Suppl. 3), S405–S413 (2002).
   PubMed Web of Science ®Google Scholar
• Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature414(6865), 813–820 (2001).
   PubMed Web of Science ®Google Scholar
• Albu JB, Heilbronn LK, Kelley DE et al. Metabolic changes following a 1-year diet and exercise intervention in patients with Type 2 diabetes. Diabetes59(3), 627–633 (2010).
   Web of Science ®Google Scholar
• Nadeau DA. Partnering with patients to improve therapeutic outcomes: incretin-based therapy for Type 2 diabetes. Postgrad. Med.122(3), 7–15 (2010).
   PubMed Web of Science ®Google Scholar
• Ghanaat-Pour H, Huang Z, Lehtihet M, Sjoholm A. Global expression profiling of glucose-regulated genes in pancreatic islets of spontaneously diabetic Goto-Kakizaki rats. J. Mol. Endocrinol.39(2), 135–150 (2007).
   Google Scholar
• Ghanaat-Pour H, Sjoholm A. Gene expression regulated by pioglitazone and exenatide in normal and diabetic rat islets exposed to lipotoxicity. Diabetes Metab. Res. Rev.25(2), 163–184 (2009).
   PubMed Web of Science ®Google Scholar
• Patti ME, Butte AJ, Crunkhorn S et al. Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: potential role of PGC1 and NRF1. Proc. Natl Acad. Sci. USA100(14), 8466–8471 (2003).
   PubMed Web of Science ®Google Scholar
• Mootha VK, Lindgren CM, Eriksson KF et al. PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes. Nat. Genet.34(3), 267–273 (2003).
   PubMed Web of Science ®Google Scholar
• Szyf M. Epigenetics, DNA methylation, and chromatin modifying drugs. Annu. Rev. Pharmacol. Toxicol.49, 243–263 (2009).
   PubMed Web of Science ®Google Scholar
• Gunton JE, Kulkarni RN, Yim S et al. Loss of ARNT/HIF1β mediates altered gene expression and pancreatic-islet dysfunction in human Type 2 diabetes. Cell122(3), 337–349 (2005).
   PubMed Web of Science ®Google Scholar
• Marselli L, Thorne J, Dahiya S et al. Gene expression profiles of β-cell enriched tissue obtained by laser capture microdissection from subjects with Type 2 diabetes. PLoS One.5(7), e11499 (2010).
   PubMed Web of Science ®Google Scholar
• Tomita M, Mukae S, Geshi E, Umetsu K, Nakatani M, Katagiri T. Mitochondrial respiratory impairment in streptozotocin-induced diabetic rat heart. Jpn. Circ. J.60(9), 673–682 (1996).
   Google Scholar
• Kelley DE, He J, Menshikova EV, Ritov VB. Dysfunction of mitochondria in human skeletal muscle in Type 2 diabetes. Diabetes51(10), 2944–2950 (2002).
   PubMed Web of Science ®Google Scholar
• Yu T, Robotham JL, Yoon Y. Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology. Proc. Natl Acad. Sci. USA103(8), 2653–2658 (2006).
   PubMed Web of Science ®Google Scholar
• Yang YL, Xiang RL, Yang C et al. Gene expression profile of human skeletal muscle and adipose tissue of Chinese Han patients with Type 2 diabetes mellitus. Biomed. Environ. Sci.22(5), 359–368 (2009).
   Google Scholar
• Meugnier E, Faraj M, Rome S et al. Acute hyperglycemia induces a global downregulation of gene expression in adipose tissue and skeletal muscle of healthy subjects. Diabetes56(4), 992–999 (2007).
   Google Scholar
• Calnan DR, Brunet A. The FoxO code. Oncogene27(16), 2276–2288 (2008).
   PubMed Web of Science ®Google Scholar
• Buteau J, Accili D. Regulation of pancreatic β-cell function by the forkhead protein FoxO1. Diabetes Obes. Metab.9(Suppl. 2), 140–146 (2007).
   PubMed Web of Science ®Google Scholar
• Andrews GK. Regulation of metallothionein gene expression by oxidative stress and metal ions. Biochem. Pharmacol.59(1), 95–104 (2000).
   PubMed Web of Science ®Google Scholar
• Chiaverini N, De Ley M. Protective effect of metallothionein on oxidative stress-induced DNA damage. Free Radic. Res.44(6), 605–613 (2010).
   PubMed Web of Science ®Google Scholar
• Keller MP, Choi Y, Wang P et al. A gene expression network model of Type 2 diabetes links cell cycle regulation in islets with diabetes susceptibility. Genome Res.18(5), 706–716 (2008).
   PubMed Web of Science ®Google Scholar
• Nishikawa T, Edelstein D, Du XL et al. Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature404(6779), 787–790 (2000).
   PubMed Web of Science ®Google Scholar
• Du XL, Edelstein D, Rossetti L et al. Hyperglycemia-induced mitochondrial superoxide overproduction activates the hexosamine pathway and induces plasminogen activator inhibitor-1 expression by increasing Sp1 glycosylation. Proc. Natl Acad. Sci. USA97(22), 12222–12226 (2000).
   PubMed Web of Science ®Google Scholar
• Li N, Brun T, Cnop M, Cunha DA, Eizirik DL, Maechler P. Transient oxidative stress damages mitochondrial machinery inducing persistent β-cell dysfunction. J. Biol. Chem.284(35), 23602–23612 (2009).
   PubMedGoogle Scholar
• Lambert AJ, Brand MD. Reactive oxygen species production by mitochondria. Methods Mol. Biol.554, 165–181 (2009).
   PubMedGoogle Scholar
• Covarrubias L, Hernandez-Garcia D, Schnabel D, Salas-Vidal E, Castro-Obregon S. Function of reactive oxygen species during animal development: passive or active? Dev. Biol.320(1), 1–11 (2008).
   PubMed Web of Science ®Google Scholar
• Pinheiro CH, Silveira LR, Nachbar RT, Vitzel KF, Curi R. Regulation of glycolysis and expression of glucose metabolism-related genes by reactive oxygen species in contracting skeletal muscle cells. Free Radic. Biol. Med.48(7), 953–960 (2010).
   Google Scholar
• Lenzen S, Drinkgern J, Tiedge M. Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues. Free Radic. Biol. Med.20(3), 463–466 (1996).
   PubMed Web of Science ®Google Scholar
• Tiedge M, Lortz S, Drinkgern J, Lenzen S. Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells. Diabetes46(11), 1733–1742 (1997).
   PubMed Web of Science ®Google Scholar
• Prentki M, Nolan CJ. Islet β cell failure in Type 2 diabetes. J. Clin. Invest.116(7), 1802–1812 (2006).
   PubMed Web of Science ®Google Scholar
• Tanaka Y, Tran PO, Harmon J, Robertson RP. A role for glutathione peroxidase in protecting pancreatic β cells against oxidative stress in a model of glucose toxicity. Proc. Natl Acad. Sci. USA99(19), 12363–12368 (2002).
   PubMed Web of Science ®Google Scholar
• Schulze PC, Yoshioka J, Takahashi T, He Z, King GL, Lee RT. Hyperglycemia promotes oxidative stress through inhibition of thioredoxin function by thioredoxin-interacting protein. J. Biol. Chem.279(29), 30369–30374 (2004).
   PubMed Web of Science ®Google Scholar
• Robertson R, Zhou H, Zhang T, Harmon JS. Chronic oxidative stress as a mechanism for glucose toxicity of the β cell in Type 2 diabetes. Cell Biochem. Biophys.48(2–3), 139–146 (2007).
   PubMed Web of Science ®Google Scholar
• Del Guerra S, Lupi R, Marselli L et al. Functional and molecular defects of pancreatic islets in human Type 2 diabetes. Diabetes54(3), 727–735 (2005).
   PubMed Web of Science ®Google Scholar
• Yang RL, Li W, Shi YH, Le GW. Lipoic acid prevents high-fat diet-induced dyslipidemia and oxidative stress: a microarray analysis. Nutrition24(6), 582–588 (2008).
   PubMed Web of Science ®Google Scholar
• Cui J, Le G, Yang R, Shi Y. Lipoic acid attenuates high fat diet-induced chronic oxidative stress and immunosuppression in mice jejunum: a microarray analysis. Cell Immunol.260(1), 44–50 (2009).
   PubMed Web of Science ®Google Scholar
• Dalle-Donne I, Aldini G, Carini M, Colombo R, Rossi R, Milzani A. Protein carbonylation, cellular dysfunction, and disease progression. J. Cell Mol. Med.10(2), 389–406 (2006).
   PubMed Web of Science ®Google Scholar
• Nair U, Bartsch H, Nair J. Lipid peroxidation-induced DNA damage in cancer-prone inflammatory diseases: a review of published adduct types and levels in humans. Free Radic. Biol. Med.43(8), 1109–1120 (2007).
   PubMed Web of Science ®Google Scholar
• Kong Q, Lin CL. Oxidative damage to RNA: mechanisms, consequences, and diseases. Cell Mol. Life Sci.67(11), 1817–1829 (2010).
   PubMed Web of Science ®Google Scholar
• Disher K, Skandalis A. Evidence of the modulation of mRNA splicing fidelity in humans by oxidative stress and p53. Genome50(10), 946–953 (2007).
   Google Scholar
• Takeo K, Kawai T, Nishida K et al. Oxidative stress-induced alternative splicing of transformer 2β (SFRS10) and CD44 pre-mRNAs in gastric epithelial cells. Am. J. Physiol. Cell Physiol.297(2), C330–C338 (2009).
   PubMedGoogle Scholar
• Luna C, Li G, Qiu J, Epstein DL, Gonzalez P. Role of miR-29b on the regulation of the extracellular matrix in human trabecular meshwork cells under chronic oxidative stress. Mol. Vis.15, 2488–2497 (2009).
   PubMed Web of Science ®Google Scholar
• Simone NL, Soule BP, Ly D et al. Ionizing radiation-induced oxidative stress alters miRNA expression. PLoS One4(7), e6377 (2009).
   PubMed Web of Science ®Google Scholar
• Takanabe R, Ono K, Abe Y et al. Up-regulated expression of microRNA-143 in association with obesity in adipose tissue of mice fed high-fat diet. Biochem. Biophys. Res. Commun.376(4), 728–732 (2008).
   PubMed Web of Science ®Google Scholar
• Herrera BM, Lockstone HE, Taylor JM et al. MicroRNA-125a is over-expressed in insulin target tissues in a spontaneous rat model of Type 2 diabetes. BMC Med. Genomics2, 54 (2009).
   PubMed Web of Science ®Google Scholar
• Sundar IK, Caito S, Yao H, Rahman I. Oxidative stress, thiol redox signaling methods in epigenetics. Methods Enzymol.474, 213–244 (2010).
   Google Scholar
• Noh H, Oh EY, Seo JY et al. Histone deacetylase-2 is a key regulator of diabetes- and transforming growth factor-β1-induced renal injury. Am. J. Physiol. Renal. Physiol.297(3), F729–F739 (2009).
   PubMed Web of Science ®Google Scholar
• Pan Q, Shai O, Lee LJ, Frey BJ, Blencowe BJ. Addendum: deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat. Genet.41(6), 762 (2009).
   Web of Science ®Google Scholar
• Spellman CW. Pathophysiology of Type 2 diabetes: targeting islet cell dysfunction. J. Am. Osteopath. Assoc.110(3 Suppl. 2), S2–S7 (2010).
   Google Scholar
• Tazi J, Bakkour N, Stamm S. Alternative splicing and disease. Biochim. Biophys. Acta.1792(1), 14–26 (2009).
   PubMed Web of Science ®Google Scholar
• Cartegni L, Chew SL, Krainer AR. Listening to silence and understanding nonsense: exonic mutations that affect splicing. Nat. Rev. Genet.3(4), 285–298 (2002).
   PubMed Web of Science ®Google Scholar
• Minn AH, Lan H, Rabaglia ME et al. Increased insulin translation from an insulin splice-variant overexpressed in diabetes, obesity, and insulin resistance. Mol. Endocrinol.19(3), 794–803 (2005).
   Google Scholar
• Fred RG, Bang-Berthelsen CH, Mandrup-Poulsen T, Grunnet LG, Welsh N. High glucose suppresses human islet insulin biosynthesis by inducing miR-133a leading to decreased polypyrimidine tract binding protein-expression. PLoS One5(5), e10843 (2010).
   PubMedGoogle Scholar
• Tillmar L, Carlsson C, Welsh N. Control of insulin mRNA stability in rat pancreatic islets. Regulatory role of a 3´-untranslated region pyrimidine-rich sequence. J. Biol. Chem.277(2), 1099–1106 (2002).
   PubMedGoogle Scholar
• Spellman R, Rideau A, Matlin A et al. Regulation of alternative splicing by PTB and associated factors. Biochem. Soc. Trans.33(Pt 3), 457–460 (2005).
   PubMedGoogle Scholar
• Wang W, Lai MD. [Alternative splicing of insulin receptor mRNA in cancer and Type 2 diabetes mellitus: a review]. Yi Chuan.28(2), 226–230 (2006).
   Google Scholar
• Keembiyehetty C, Augustin R, Carayannopoulos MO et al. Mouse glucose transporter 9 splice variants are expressed in adult liver and kidney and are up-regulated in diabetes. Mol. Endocrinol.20(3), 686–697 (2006).
   PubMed Web of Science ®Google Scholar
• Harada N, Yamada Y, Tsukiyama K et al. A novel GIP receptor splice variant influences GIP sensitivity of pancreatic β-cells in obese mice. Am. J. Physiol. Endocrinol. Metab.294(1), E61–E68 (2008).
   Google Scholar
• Oram JF. ATP-binding cassette transporter A1 and cholesterol trafficking. Curr. Opin. Lipidol.13(4), 373–381 (2002).
   PubMed Web of Science ®Google Scholar
• Singaraja RR, James ER, Crim J, Visscher H, Chatterjee A, Hayden MR. Alternate transcripts expressed in response to diet reflect tissue-specific regulation of ABCA1. J. Lipid Res.46(10), 2061–2071 (2005).
   PubMed Web of Science ®Google Scholar
• Wellington CL, Walker EK, Suarez A et al. ABCA1 mRNA and protein distribution patterns predict multiple different roles and levels of regulation. Lab. Invest.82(3), 273–283 (2002).
   PubMed Web of Science ®Google Scholar
• Singaraja RR, Bocher V, James ER et al. Human ABCA1 BAC transgenic mice show increased high density lipoprotein cholesterol and ApoAI-dependent efflux stimulated by an internal promoter containing liver X receptor response elements in intron 1. J. Biol. Chem.276(36), 33969–33979 (2001).
   PubMed Web of Science ®Google Scholar
• Kersten S, Desvergne B, Wahli W. Roles of PPARs in health and disease. Nature405(6785), 421–424 (2000).
   PubMed Web of Science ®Google Scholar
• Vozarova B, Stefan N, Lindsay RS et al. High alanine aminotransferase is associated with decreased hepatic insulin sensitivity and predicts the development of Type 2 diabetes. Diabetes51(6), 1889–1895 (2002).
   PubMed Web of Science ®Google Scholar
• West J, Brousil J, Gazis A et al. Elevated serum alanine transaminase in patients with Type 1 or Type 2 diabetes mellitus. QJM99(12), 871–876 (2006).
   PubMed Web of Science ®Google Scholar
• Anemaet IG, Meton I, Salgado MC, Fernandez F, Baanante IV. A novel alternatively spliced transcript of cytosolic alanine aminotransferase gene associated with enhanced gluconeogenesis in liver of Sparus aurata.Int. J. Biochem. Cell Biol.40(12), 2833–2844 (2008).
   Google Scholar
• Davies KP, Zhao W, Tar M et al. Diabetes-induced changes in the alternative splicing of the Slo gene in corporal tissue. Eur. Urol.52(4), 1229–1237 (2007).
   PubMedGoogle Scholar
• Zygalaki E, Kaklamanis L, Nikolaou NI et al. Expression profile of total VEGF, VEGF splice variants and VEGF receptors in the myocardium and arterial vasculature of diabetic and non-diabetic patients with coronary artery disease. Clin. Biochem.41(1–2), 82–87 (2008).
   Google Scholar
• Bird A. Perceptions of epigenetics. Nature447(7143), 396–398 (2007).
   PubMed Web of Science ®Google Scholar
• Hales CN, Barker DJ. The thrifty phenotype hypothesis. Br. Med. Bull.60, 5–20 (2001).
   PubMed Web of Science ®Google Scholar
• Liu L, Li Y, Tollefsbol TO. Gene-environment interactions and epigenetic basis of human diseases. Curr. Issues. Mol. Biol.10(1–2), 25–36 (2008).
   PubMed Web of Science ®Google Scholar
• Nathan DM, Cleary PA, Backlund JY et al. Intensive diabetes treatment and cardiovascular disease in patients with Type 1 diabetes. N. Engl. J. Med.353(25), 2643–2653 (2005).
   PubMed Web of Science ®Google Scholar
• Miao F, Gonzalo IG, Lanting L, Natarajan R. In vivo chromatin remodeling events leading to inflammatory gene transcription under diabetic conditions. J. Biol. Chem.279(17), 18091–18097 (2004).
   PubMed Web of Science ®Google Scholar
• Miao F, Wu X, Zhang L, Yuan YC, Riggs AD, Natarajan R. Genome-wide analysis of histone lysine methylation variations caused by diabetic conditions in human monocytes. J. Biol. Chem.282(18), 13854–13863 (2007).
   PubMed Web of Science ®Google Scholar
• Tateishi K, Okada Y, Kallin EM, Zhang Y. Role of Jhdm2a in regulating metabolic gene expression and obesity resistance. Nature458(7239), 757–761 (2009).
   PubMed Web of Science ®Google Scholar
• El-Osta A, Brasacchio D, Yao D et al. Transient high glucose causes persistent epigenetic changes and altered gene expression during subsequent normoglycemia. J. Exp. Med.205(10), 2409–2417 (2008).
   PubMed Web of Science ®Google Scholar
• Brasacchio D, Okabe J, Tikellis C et al. Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with gene-activating epigenetic marks that coexist on the lysine tail. Diabetes58(5), 1229–1236 (2009).
   PubMed Web of Science ®Google Scholar
• Reddy MA, Villeneuve LM, Wang M, Lanting L, Natarajan R. Role of the lysine-specific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice. Circ. Res.103(6), 615–623 (2008).
   PubMed Web of Science ®Google Scholar
• Shi Y, Lan F, Matson C et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell119(7), 941–953 (2004).
   PubMed Web of Science ®Google Scholar
• Villeneuve LM, Reddy MA, Lanting LL, Wang M, Meng L, Natarajan R. Epigenetic histone H3 lysine 9 methylation in metabolic memory and inflammatory phenotype of vascular smooth muscle cells in diabetes. Proc. Natl Acad. Sci. USA105(26), 9047–9052 (2008).
   PubMed Web of Science ®Google Scholar
• Ling C, Del Guerra S, Lupi R et al. Epigenetic regulation of PPARGC1A in human Type 2 diabetic islets and effect on insulin secretion. Diabetologia51(4), 615–622 (2008).
   PubMed Web of Science ®Google Scholar
• Barrès R, Osler ME, Yan J et al. Non-CpG methylation of the PGC-1α promoter through DNMT3B controls mitochondrial density. Cell Metab.10(3), 189–198 (2009).
   PubMed Web of Science ®Google Scholar
• Feng B, Chen S, Chiu J, George B, Chakrabarti S. Regulation of cardiomyocyte hypertrophy in diabetes at the transcriptional level. Am. J. Physiol. Endocrinol. Metab.294(6), E1119–E1126 (2008).
   PubMedGoogle Scholar
• Kaur H, Chen S, Xin X, Chiu J, Khan ZA, Chakrabarti S. Diabetes-induced extracellular matrix protein expression is mediated by transcription coactivator p300. Diabetes55(11), 3104–3111 (2006).
   PubMedGoogle Scholar
• Xu P, Vernooy SY, Guo M, Hay BA. The drosophila microRNA Mir-14 suppresses cell death and is required for normal fat metabolism. Curr. Biol.13(9), 790–795 (2003).
   PubMed Web of Science ®Google Scholar
• Poy MN, Spranger M, Stoffel M. microRNAs and the regulation of glucose and lipid metabolism. Diabetes Obes. Metab.9(Suppl. 2), 67–73 (2007).
   PubMedGoogle Scholar
• Poy MN, Eliasson L, Krutzfeldt J et al. A pancreatic islet-specific microRNA regulates insulin secretion. Nature432(7014), 226–230 (2004).
   PubMed Web of Science ®Google Scholar
• Lynn FC, Skewes-Cox P, Kosaka Y, McManus MT, Harfe BD, German MS. MicroRNA expression is required for pancreatic islet cell genesis in the mouse. Diabetes56(12), 2938–2945 (2007).
   PubMedGoogle Scholar
• Krol J, Loedige I, Filipowicz W. The widespread regulation of microRNA biogenesis, function and decay. Nat. Rev. Genet.11(9), 597–610 (2010).
   PubMed Web of Science ®Google Scholar
• Guil S, Esteller M. DNA methylomes, histone codes and miRNAs: tying it all together. Int. J. Biochem. Cell Biol.41(1), 87–95 (2009).
   PubMed Web of Science ®Google Scholar
• Guo H, Ingolia NT, Weissman JS, Bartel DP. Mammalian microRNAs predominantly act to decrease target mRNA levels. Nature466(7308), 835–840 (2010).
   PubMed Web of Science ®Google Scholar
• Hutvagner G, Zamore PD. A microRNA in a multiple-turnover RNAi enzyme complex. Science297(5589), 2056–2060 (2002).
   PubMed Web of Science ®Google Scholar
• Li L, Xu J, Yang D, Tan X, Wang H. Computational approaches for microRNA studies: a review. Mamm. Genome21(1–2), 1–12 (2010).
   PubMed Web of Science ®Google Scholar
• Croce CM. Causes and consequences of microRNA dysregulation in cancer. Nat. Rev. Genet.10(10), 704–714 (2009).
   PubMed Web of Science ®Google Scholar
• Kolfschoten IG, Roggli E, Nesca V, Regazzi R. Role and therapeutic potential of microRNAs in diabetes. Diabetes Obes. Metab.11(Suppl. 4), 118–129 (2009).
   Google Scholar
• Esau C, Davis S, Murray SF et al. miR-122 regulation of lipid metabolism revealed by in vivo antisense targeting. Cell Metab.3(2), 87–98 (2006).
   PubMed Web of Science ®Google Scholar
• Krutzfeldt J, Rajewsky N, Braich R et al. Silencing of microRNAs in vivo with ‘antagomirs’. Nature438(7068), 685–689 (2005).
   PubMed Web of Science ®Google Scholar
• Moore KJ, Rayner KJ, Suarez Y, Fernandez-Hernando C. MicroRNAs and cholesterol metabolism. Trends Endocrinol. Metab.21(12), 699–706 (2010).
   PubMed Web of Science ®Google Scholar
• Najafi-Shoushtari SH, Kristo F, Li Y et al. MicroRNA-33 and the SREBP host genes cooperate to control cholesterol homeostasis. Science328(5985), 1566–1569 (2010).
   PubMed Web of Science ®Google Scholar
• Rayner KJ, Suarez Y, Davalos A et al. MiR-33 contributes to the regulation of cholesterol homeostasis. Science328(5985), 1570–1573 (2010).
   PubMed Web of Science ®Google Scholar
• Marquart TJ, Allen RM, Ory DS, Baldan A. miR-33 links SREBP-2 induction to repression of sterol transporters. Proc. Natl Acad. Sci. USA107(27), 12228–12232 (2010).
   PubMed Web of Science ®Google Scholar
• Horie T, Ono K, Horiguchi M et al. MicroRNA-33 encoded by an intron of sterol regulatory element-binding protein 2 (Srebp2) regulates HDL in vivo. Proc. Natl Acad. Sci. USA107(40), 17321–17326 (2010).
   PubMed Web of Science ®Google Scholar
• Gerin I, Clerbaux LA, Haumont O et al. Expression of miR-33 from an SREBP2 intron inhibits cholesterol export and fatty acid oxidation. J. Biol. Chem.285(44), 33652–33661 (2010).
   PubMed Web of Science ®Google Scholar
• Foretz M, Pacot C, Dugail I et al. ADD1/SREBP-1c is required in the activation of hepatic lipogenic gene expression by glucose. Mol. Cell Biol.19(5), 3760–3768 (1999).
   PubMed Web of Science ®Google Scholar
• Kim JB, Sarraf P, Wright M et al. Nutritional and insulin regulation of fatty acid synthetase and leptin gene expression through ADD1/SREBP1. J. Clin. Invest.101(1), 1–9 (1998).
   PubMed Web of Science ®Google Scholar
• Poy MN, Hausser J, Trajkovski M et al. miR-375 maintains normal pancreatic α- and β-cell mass. Proc. Natl Acad. Sci. USA106(14), 5813–5818 (2009).
   PubMed Web of Science ®Google Scholar
• Li Y, Xu X, Liang Y et al. miR-375 enhances palmitate-induced lipoapoptosis in insulin-secreting NIT-1 cells by repressing myotrophin (V1) protein expression. Int. J. Clin. Exp. Pathol.3(3), 254–264 (2010).
   PubMedGoogle Scholar
• Lovis P, Roggli E, Laybutt DR et al. Alterations in microRNA expression contribute to fatty acid-induced pancreatic β-cell dysfunction. Diabetes57(10), 2728–2736 (2008).
   PubMed Web of Science ®Google Scholar
• Lovis P, Gattesco S, Regazzi R. Regulation of the expression of components of the exocytotic machinery of insulin-secreting cells by microRNAs. Biol. Chem.389(3), 305–312 (2008).
   PubMed Web of Science ®Google Scholar
• Ling HY, Ou HS, Feng SD et al. Changes in microRNA profile and effects of miR-320 in insulin-resistant 3T3-L1 adipocytes. Clin. Exp. Pharmacol. Physiol. DOI: 10.1111/j.1440-1681.2009.05207.x (2009) (Epub ahead of print).
   Google Scholar
• Esau C, Kang X, Peralta E et al. MicroRNA-143 regulates adipocyte differentiation. J. Biol. Chem.279(50), 52361–52365 (2004).
   PubMed Web of Science ®Google Scholar
• Gallagher IJ, Scheele C, Keller P et al. Integration of microRNA changes in vivo identifies novel molecular features of muscle insulin resistance in Type 2 diabetes. Genome Med.2(2), 9 (2010).
   PubMedGoogle Scholar
• He A, Zhu L, Gupta N, Chang Y, Fang F. Overexpression of micro ribonucleic acid 29, highly up-regulated in diabetic rats, leads to insulin resistance in 3T3-L1 adipocytes. Mol. Endocrinol.21(11), 2785–2794 (2007).
   PubMedGoogle Scholar
• Herrera BM, Lockstone HE, Taylor JM et al. Global microRNA expression profiles in insulin target tissues in a spontaneous rat model of Type 2 diabetes. Diabetologia53(6), 1099–1109 (2010).
   PubMed Web of Science ®Google Scholar
• Sengupta U, Ukil S, Dimitrova N, Agrawal S. Expression-based network biology identifies alteration in key regulatory pathways of Type 2 diabetes and associated risk/complications. PLoS One4(12), e8100 (2009).
   Google Scholar
• Wang Q, Wang Y, Minto AW et al. MicroRNA-377 is up-regulated and can lead to increased fibronectin production in diabetic nephropathy. FASEB J.22(12), 4126–4135 (2008).
   PubMed Web of Science ®Google Scholar
• Du B, Ma LM, Huang MB et al. High glucose down-regulates miR-29a to increase collagen IV production in HK-2 cells. FEBS Lett.584(4), 811–816 (2010).
   PubMed Web of Science ®Google Scholar
• Yu XY, Song YH, Geng YJ et al. Glucose induces apoptosis of cardiomyocytes via microRNA-1 and IGF-1. Biochem. Biophys. Res. Commun.376(3), 548–552 (2008).
   Google Scholar
• Xiao J, Luo X, Lin H et al. MicroRNA miR-133 represses HERG K+ channel expression contributing to QT prolongation in diabetic hearts. J. Biol. Chem.282(17), 12363–12367 (2007).
   PubMed Web of Science ®Google Scholar
• Li Y, Song YH, Li F, Yang T, Lu YW, Geng YJ. MicroRNA-221 regulates high glucose-induced endothelial dysfunction. Biochem. Biophys. Res. Commun.381(1), 81–83 (2009).
   PubMed Web of Science ®Google Scholar
• Zampetaki A, Kiechl S, Drozdov I et al. Plasma microRNA profiling reveals loss of endothelial miR-126 and other microRNAs in Type 2 diabetes. Circ. Res.107(6), 810–817 (2010).
   PubMed Web of Science ®Google Scholar
• Moulton HM, Moulton JD. Morpholinos and their peptide conjugates: therapeutic promise and challenge for Duchenne muscular dystrophy. Biochim. Biophys. Acta1798(12), 2296–2303 (2010).
   PubMed Web of Science ®Google Scholar
• Groop LC, Bonadonna RC, DelPrato S et al. Glucose and free fatty acid metabolism in non-insulin-dependent diabetes mellitus. Evidence for multiple sites of insulin resistance. J. Clin. Invest.84(1), 205–213 (1989).
   PubMed Web of Science ®Google Scholar
• Abdul-Ghani MA, DeFronzo RA. Pathophysiology of prediabetes. Curr. Diab. Rep.9(3), 193–199 (2009).
   PubMed Web of Science ®Google Scholar
• Staley JP, Woolford JL Jr. Assembly of ribosomes and spliceosomes: complex ribonucleoprotein machines. Curr. Opin. Cell Biol.21(1), 109–118 (2009).
   PubMedGoogle Scholar
• Warf MB, Berglund JA. Role of RNA structure in regulating pre-mRNA splicing. Trends Biochem. Sci.35(3), 169–178 (2010).
   PubMed Web of Science ®Google Scholar
• Licatalosi DD, Darnell RB. RNA processing and its regulation: global insights into biological networks. Nat. Rev. Genet.11(1), 75–87 (2010).
   PubMed Web of Science ®Google Scholar
• Kouzarides T. Chromatin modifications and their function. Cell128(4), 693–705 (2007).
   PubMed Web of Science ®Google Scholar
• Jenuwein T, Allis CD. Translating the histone code. Science293(5532), 1074–1080 (2001).
   PubMed Web of Science ®Google Scholar
• Burdge GC, Hanson MA, Slater-Jefferies JL, Lillycrop KA. Epigenetic regulation of transcription: a mechanism for inducing variations in phenotype (fetal programming) by differences in nutrition during early life? Br. J. Nutr.97(6), 1036–1046 (2007).
   PubMed Web of Science ®Google Scholar
• Bird A. DNA methylation patterns and epigenetic memory. Genes Dev.16(1), 6–21 (2002).
   PubMed Web of Science ®Google Scholar
• Fabian MR, Sonenberg N, Filipowicz W. Regulation of mRNA translation and stability by microRNAs. Annu. Rev. Biochem.79, 351–379 (2010).
   PubMed Web of Science ®Google Scholar
• Orom UA, Nielsen FC, Lund AH. MicroRNA-10a binds the 5´UTR of ribosomal protein mRNAs and enhances their translation. Mol. Cell30(4), 460–471 (2008).
   PubMed Web of Science ®Google Scholar
• Rigoutsos I. New tricks for animal microRNAs: targeting of amino acid coding regions at conserved and nonconserved sites. Cancer Res.69(8), 3245–3248 (2009).
   PubMed Web of Science ®Google Scholar
• Wu S, Huang S, Ding J et al. Multiple microRNAs modulate p21Cip1/Waf1 expression by directly targeting its 3´ untranslated region. Oncogene.29(15), 2302–2308 (2010).
   PubMed Web of Science ®Google Scholar
• Vasudevan S, Tong Y, Steitz JA. Switching from repression to activation: microRNAs can up-regulate translation. Science318(5858), 1931–1934 (2007).
   PubMed Web of Science ®Google Scholar