Functional genetic variants within the SIRT2 gene promoter in type 2 diabetes mellitus

Diabetes Research and Clinical Practice

Volumn 137, Issue , 2018, Pages 200-207

  Liu, Tingting ^a   Yang, Wentao ^b   Pang, Shuchao ^a   Yu, Shipeng ^a   Yan, Bo ^a  

^a JINING MEDICAL UNIVERSITY   (China)

^b SHANDONG UNIVERSITY SCHOOL OF MEDICINE   (China)

Author keywords

DNA sequence variants; Promoter; SIRT2; SNP; Type 2 diabetes mellitus

Indexed keywords

SIRTUIN 2; SIRT2 PROTEIN, HUMAN;

ADULT; AGED; ARTICLE; CELL CULTURE; COHORT ANALYSIS; CONTROLLED STUDY; DISEASE COURSE; DNA SEQUENCE; ETHNICITY; FEMALE; GENE ACTIVITY; GENE DELETION; GENETIC TRANSCRIPTION; GENETIC VARIABILITY; HUMAN; HUMAN CELL; MAJOR CLINICAL STUDY; MALE; NON INSULIN DEPENDENT DIABETES MELLITUS; PANCREAS ISLET BETA CELL; PATHOPHYSIOLOGY; PROMOTER REGION; RISK FACTOR; SINGLE NUCLEOTIDE POLYMORPHISM; SIRT2 GENE; CASE CONTROL STUDY; GENETIC VARIATION; GENETICS; METABOLISM; MIDDLE AGED; NUCLEOTIDE SEQUENCE; VERY ELDERLY;

ADULT; AGED; AGED, 80 AND OVER; BASE SEQUENCE; CASE-CONTROL STUDIES; DIABETES MELLITUS, TYPE 2; FEMALE; GENETIC VARIATION; HUMANS; MALE; MIDDLE AGED; POLYMORPHISM, SINGLE NUCLEOTIDE; PROMOTER REGIONS, GENETIC; RISK FACTORS; SIRTUIN 2;

EID: 85041604209     PISSN: 01688227     EISSN: 18728227     Source Type: Journal    
DOI: 10.1016/j.diabres.2018.01.012     Document Type: Article

References (58)

1. Kahn, S.E., Cooper, M.E., Del Prato, S., Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future. Lancet 383 (2014), 1068–1083.
2. Stančáková, A., Laakso, M., Genetics of Type 2 diabetes. Endocr Dev 31 (2016), 203–220.
3. Grarup, N., Sandholt, C.H., Hansen, T., Pedersen, O., Genetic susceptibility to type 2 diabetes and obesity: from genome-wide association studies to rare variants and beyond. Diabetologia 57 (2014), 1528–1541.
4. Hashimoto, N., Tanaka, T., Role of miRNAs in the pathogenesis and susceptibility of diabetes mellitus. J Hum Genet 62 (2017), 141–150.
5. Kwak, S.H., Park, K.S., Recent progress in genetic and epigenetic research on type 2 diabetes. Exp Mol Med, 48, 2016, e220.
6. Choi, J.E., Mostoslavsky, R., Sirtuins, metabolism, and DNA repair. Curr Opin Genet Dev 26 (2014), 24–32.
7. Houtkooper, R.H., Pirinen, E., Auwerx, J., Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol 13 (2012), 225–238.
8. Hall, J.A., Dominy, J.E., Lee, Y., Puigserver, P., The sirtuin family's role in aging and age-associated pathologies. J Clin Invest 123 (2013), 973–979.
9. Dryden, S.C., Nahhas, F.A., Nowak, J.E., Goustin, A.S., Tainsky, M.A., Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol Cell Biol 23 (2003), 3173–3185.
10. Gomes, P., Outeiro, T.F., Cavadas, C., Emerging role of Sirtuin 2 in the regulation of mammalian metabolism. Trends Pharmacol Sci 36 (2015), 756–768.
11. Inoue, T., Hiratsuka, M., Osaki, M., Oshimura, M., The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation. Cell Cycle 6 (2007), 1011–1018.
12. Jing, E., Gesta, S., Kahn, C.R., SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab 6 (2007), 105–114.
13. Kim, H.S., Vassilopoulos, A., Wang, R.H., Lahusen, T., Xiao, Z., Xu, X., et al. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell 20 (2011), 487–499.
14. North, B.J., Marshall, B.L., Borra, M.T., Denu, J.M., Verdin, E., The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11 (2003), 437–444.
15. Vaquero, A., Scher, M.B., Lee, D.H., Sutton, A., Cheng, H.L., Alt, F.W., et al. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev 20 (2006), 1256–1261.
16. Wang, F., Tong, Q., SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma. Mol Biol Cell 20 (2009), 801–808.
17. Donmez, G., Outeiro, T.F., SIRT1 and SIRT2: emerging targets in neurodegeneration. EMBO Mol Med 5 (2013), 344–352.
18. Matsushima, S., Sadoshima, J., The role of sirtuins in cardiac disease. Am J Physiol Heart Circ Physiol 309 (2015), H1375–H1389.
19. German, N.J., Haigis, M.C., Sirtuins and the metabolic hurdles in cancer. Curr Biol 25 (2015), R569–R583.
20. Krishnan, J., Danzer, C., Simka, T., Ukropec, J., Walter, K.M., Kumpf, S., et al. Dietary obesity-associated Hif1α activation in adipocytes restricts fatty acid oxidation and energy expenditure via suppression of the Sirt2-NAD+ system. Genes Dev 26 (2012), 259–270.
21. Arora, A., Dey, C.S., SIRT2 negatively regulates insulin resistance in C2C12 skeletal muscle cells. Biochim Biophys Acta 1842 (2014), 1372–1378.
22. Arora, A., Dey, C.S., SIRT2 regulates insulin sensitivity in insulin resistant neuronal cells. Biochem Biophys Res Commun 474 (2016), 747–752.
23. Chen, J., Chan, A.W., To, K.F., Chen, W., Zhang, Z., Ren, J., et al. SIRT2 overexpression in hepatocellular carcinoma mediates epithelial to mesenchymal transition by protein kinase B/glycogen synthase kinase-3β/β-catenin signaling. Hepatology 57 (2013), 2287–2298.
24. Ramakrishnan, G., Davaakhuu, G., Kaplun, L., Chung, W.C., Rana, A., Atfi, A., et al. Sirt2 deacetylase is a novel AKT binding partner critical for AKT activation by insulin. J Biol Chem 289 (2014), 6054–6066.
25. Belman, J.P., Bian, R.R., Habtemichael, E.N., Li, D.T., Jurczak, M.J., Alcázar-Román, A., et al. Acetylation of TUG protein promotes the accumulation of GLUT4 glucose transporters in an insulin-responsive intracellular compartment. J Biol Chem 290 (2015), 4447–4463.
26. Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., et al. Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol Cell 43 (2011), 33–44.
27. Rothgiesser, K.M., Erener, S., Waibel, S., Lüscher, B., Hottiger, M.O., SIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310. J Cell Sci 123 (2010), 4251–4258.
28. Xu, S.N., Wang, T.S., Li, X., Wang, Y.P., SIRT2 activates G6PD to enhance NADPH production and promote leukaemia cell proliferation. Sci Rep, 6, 2016, 32734.
29. Xu, Y., Li, F., Lv, L., Li, T., Zhou, X., Deng, C.X., et al. Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase. Cancer Res 74 (2014), 3630–3642.
30. Wang, Y.P., Zhou, L.S., Zhao, Y.Z., Wang, S.W., Chen, L.L., Liu, L.X., et al. Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress. EMBO J 33 (2014), 1304–1320.
31. Inoue, T., Nakayama, Y., Li, Y., Matsumori, H., Takahashi, H., Kojima, H., et al. SIRT2 knockdown increases basal autophagy and prevents postslippage death by abnormally prolonging the mitotic arrest that is induced by microtubule inhibitors. FEBS J 281 (2014), 2623–2637.
32. Gal, J., Bang, Y., Choi, H.J., SIRT2 interferes with autophagy-mediated degradation of protein aggregates in neuronal cells under proteasome inhibition. Neurochem Int 61 (2012), 992–1000.
33. Watada, H., Fujitani, Y., Minireview: autophagy in pancreatic β-cells and its implication in diabetes. Mol Endocrinol 29 (2015), 338–348.
34. Coope, A., Torsoni, A.S., Velloso, L.A., Mechanisms in endocrinology: metabolic and inflammatory pathways on the pathogenesis of type 2 diabetes. Eur J Endocrinol 174 (2016), R175–R187.
35. Lumeng, C.N., Saltiel, A.R., Inflammatory links between obesity and metabolic disease. J Clin Invest 121 (2011), 2111–2117.
36. Lee, T.I., Young, R.A., Transcriptional regulation and its misregulation in disease. Cell 152 (2013), 1237–1251.
37. American Diabetes Association, (2) Classification and diagnosis of diabetes. Diabetes Care 38:Suppl (2015), S8–S16.
38. Crocco, P., Montesanto, A., Passarino, G., Rose, G., Polymorphisms falling within putative miRNA target sites in the 3'UTR region of SIRT2 and DRD2 genes are correlated with human longevity. J Gerontol A Biol Sci Med Sci 71 (2016), 586–592.
39. Haketa, A., Soma, M., Nakayama, T., Kosuge, K., Aoi, N., Hishiki, M., et al. Association between SIRT2 gene polymorphism and height in healthy, elderly Japanese subjects. Transl Res 161 (2013), 57–58.
40. Wei, W., Xu, X., Li, H., Zhang, Y., Han, D., Wang, Y., et al. The SIRT2 polymorphism rs10410544 and risk of Alzheimer's disease: a meta-analysis. Neuromol Med 16 (2014), 448–456.
41. Afshar, G., Murnane, J.P., Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2. Gene 234 (1999), 161–168.
42. Frye, R.A., Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260 (1999), 273–279.
43. Voelter-Mahlknecht, S., Ho, A.D., Mahlknecht, U., FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2). Int J Oncol 27 (2005), 1187–1196.
44. Anwar, T., Khosla, S., Ramakrishna, G., Increased expression of SIRT2 is a novel marker of cellular senescence and is dependent on wild type p53 status. Cell Cycle 15 (2016), 1883–1897.
45. Li, S., Lv, X., Zhai, K., Xu, R., Zhang, Y., Zhao, S., et al. MicroRNA-7 inhibits neuronal apoptosis in a cellular Parkinson's disease model by targeting Bax and Sirt2. Am J Transl Res 8 (2016), 993–1004.
46. Crujeiras, A.B., Parra, D., Goyenechea, E., Martínez, J.A., Sirtuin gene expression in human mononuclear cells is modulated by caloric restriction. Eur J Clin Invest 38 (2008), 672–678.
47. Yudoh, K., Karasawa, R., Ishikawa, J., Age-related decrease of Sirtuin 2 protein in human peripheral blood mononuclear cells. Curr Aging Sci 8 (2015), 256–258.
48. Mortuza, R., Chen, S., Feng, B., Sen, S., Chakrabarti, S., High glucose induced alteration of SIRTs in endothelial cells causes rapid aging in a p300 and FOXO regulated pathway. PLoS ONE, 8, 2013, e54514.
49. Sebastián, C., Mostoslavsky, R., The role of mammalian sirtuins in cancer metabolism. Semin Cell Dev Biol 43 (2015), 33–42.
50. Lin, R., Tao, R., Gao, X., Li, T., Zhou, X., Guan, K.L., et al. Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth. Mol Cell 51 (2013), 506–518.
51. Luthi-Carter, R., Taylor, D.M., Pallos, J., Lambert, E., Amore, A., Parker, A., et al. SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis. Proc Natl Acad Sci USA 107 (2010), 7927–7932.
52. Wang, F., Chan, C.H., Chen, K., Guan, X., Lin, H.K., Tong, Q., Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation. Oncogene 31 (2012), 1546–1557.
53. Wang, F., Nguyen, M., Qin, F.X., Tong, Q., SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6 (2007), 505–514.
54. Kitamura, T., The role of FOXO1 in β-cell failure and type 2 diabetes mellitus. Nat Rev Endocrinol 9 (2013), 615–623.
55. Zhao, Y., Yang, J., Liao, W., Liu, X., Zhang, H., Wang, S., et al. Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity. Nat Cell Biol 12 (2010), 665–675.
56. Budayeva, H.G., Cristea, I.M., Human Sirtuin 2 localization, transient interactions, and impact on the proteome point to its role in intracellular trafficking. Mol Cell Proteom 15 (2016), 3107–3125.
57. Armoni, M., Harel, C., Karni, S., Chen, H., Bar-Yoseph, F., Ver, M.R., et al. FOXO1 represses peroxisome proliferator-activated receptor-gamma1 and -gamma2 gene promoters in primary adipocytes. A novel paradigm to increase insulin sensitivity. J Biol Chem 281 (2006), 19881–19891.
58. Armoni, M., Kritz, N., Harel, C., Bar-Yoseph, F., Chen, H., Quon, M.J., et al. Peroxisome proliferator-activated receptor-gamma represses GLUT4 promoter activity in primary adipocytes, and rosiglitazone alleviates this effect. J Biol Chem 278 (2003), 30614–30623.