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SirT1 gain of function increases energy efficiency and prevents diabetes in mice. J Biol Chem. doi: 10.1111/j.1474-9726.2007.00355.x, 66. Biochim Biophys Acta (2012) 1821:117785. doi: 10.1074/jbc.M501485200, 36. Contrary to some previous studies (98, 99), the SIRT1 level significantly decreased approaching to control values in the CVD patients receiving statin therapy (100). In this previous study, we also found a significant increase in the oxidative stress parameters which may be an inducer for SIRT1 expression. Circulation (2010) 122:217082. Ann Thorac Surg. For example, 2.5- to 7.5-fold increase in the SIRT1 expression attenuated apoptosis, the symptoms of cardiac dysfunction, age-related cardiac hypertrophy and expression of senescence markers. Tissenbaum HA, Guarente L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Inhibition of Poly(ADP-ribose) polymerase-1 enhances gene expression of selected sirtuins and app cleaving enzymes in amyloid beta cytotoxicity. 9:614. doi: 10.3389/fendo.2018.00614. (2010) 30:1022032. Specific alterations in the circulating levels of the SIRT1, TLR4, and IL7 proteins in patients with dementia. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Sirtuins in aging and age-related disease. Epigenetic switching by the metabolism-sensing factors in the generation of orexin neurons from mouse embryonic stem cells. doi: 10.1007/s11064-016-2110-y, 10. Ann Rheum Dis. Int J Obes (Lond) (2011) 35:22635. Cordeira JW, Felsted JA, Teillon S, Daftary S, Panessiti M, Wirth J, et al. In addition, increase in the SIRT1 activity had a protective effect against osteoarthritis in animal models (53, 54). Res. doi: 10.1007/s00296-010-1720-y, 54. Nemoto S, Fergusson MM, Finkel T. SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. By the help of this pathway, cardiac infarct volume is reduced to ameliorate and recover cardiac function after ischemia/reperfusion in mice (92). Cell Metab. Am J Respir Crit Care Med. (2007) 21:174555. (2004) 23:236980. It was demonstrated that ROS inhibited JNK phosphatases which activated the JNK1 to phosphorylate SIRT1 (95, 96). However, they demonstrated a significant increase in the SIRT1 expression in the fructose-induced inflammation suggesting compensatory rise in the level of SIRT1 to decline the inflammation-related metabolic reactions (40). Sirtuins in cognitive ageing and Alzheimer's disease. SIRT1 transcription is decreased in visceral adipose tissue of morbidly obese patients with severe hepatic steatosis. Froy O, Sherman H, Bhargava G, Chapnik N, Cohen R, Gutman R, et al. Pedersen SB, lholm J, Paulsen SK, Bennetzen MF, Richelsen B. Besides its role being a target for histone and non-histone proteins, SIRT1 functions as a transcription factor for many different physiological processes (2). doi: 10.1038/ijo.2010.125, 43. doi: 10.1126/science.1072994, 77. Li W, Cai L, Zhang Y, Cui L, Shen G. Intra-articular resveratrol injection prevents osteoarthritis progression in a mouse model by activating SIRT1 and thereby silencing HIF-2. doi: 10.1093/jb/mvh134, 97. Whereas an increase in the expression of the SIRT1 protein was observed in cancer (12, 13), reductions in the SIRT1 level was more common in other diseases such as Alzheimer's Diseases (AD), Parkinson Disease (PD), obesity, diabetes, and cardiovascular diseases (1418). doi: 10.1523/JNEUROSCI.3442-11.2012, 82. SIRT1 deacetylase protects against neurodegeneration in models for Alzheimer's disease and amyotrophic lateral sclerosis. The decline in the activity of SIRT1 may not be related directly with SIRT1 protein but also its downstream or upstream molecules such as a decline in NAD+ levels with aging (65). (2011) 43:198211. Kim D, Nguyen MD, Dobbin MM, Fischer A, Sananbenesi F, Rodgers JT, et al. Neuroscience (2008) 154:138897. J Neurosci Off J Soc Neurosci. doi: 10.1136/annrheumdis-2012-202620, 53. doi: 10.1016/j.pnpbp.2018.05.017. Science (2004) 305:10103. doi: 10.1111/1440-1681.12362, 101. The neuroprotection against to PD occurred by the mechanism of decreasing in the expression of NF-B and cleaved PARP-1. Ungvari Z, Parrado-Fernandez C, Csiszar A, de Cabo R. Mechanisms underlying caloric restriction and lifespan regulation: implications for vascular aging. (2018) 7:25262.
doi: 10.3390/ijms14023834, PubMed Abstract | CrossRef Full Text | Google Scholar, 2. Int J Obes. However, as seen in the AD, the activity of the SIRT1 protein also decreased in the PD patients producing neurodegeneration in correlation with possible higher oxidative stress, synaptic and cell loss, and neuroinflammation (16). In one of our studies, we found a significant increase in the SIRT1 level of dementia patients (80). doi: 10.1016/j.yexmp.2018.07.008, 89. Induction of manganese superoxide dismutase by nuclear translocation and activation of SIRT1 promotes cell survival in chronic heart failure. Therefore, the investigators suggested that the increase both in the activity and expression of SIRT1 might be a protective strategy for progression of osteoarthritis via the modulation of the NF-B pathway (55). Guarente L. Mitochondriaa nexus for aging, calorie restriction, and sirtuins? Int J Mol Sci. Cell (2005) 123:43748. Olmos Y, Brosens JJ, Lam EW. Alterations of the level of SIRT1 expression were determined in several diseases including metabolic diseases, neurodegenerative diseases, cancer and aging. Alageel A, Tomasi J, Tersigni C, Brietzke E, Zuckerman H, Subramaniapillai M, et al. For example, in one of our previous study, it was noted higher level of SIRT1 protein in older people compared with the SIRT1 level in the younger people (62). doi: 10.1126/science.1099196, 60. Low Sirt1 expression, which is upregulated by fasting, in human adipose tissue from obese women. doi: 10.1161/01.RES.0000268411.49545.9c, 102. Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. In cardiomyocytes, myoblast gains resistance against to oxidative stress by increasing expression of nuclear SIRT1 protein. Lutz MI, Milenkovic I, Regelsberger G, Kovacs GG. Nat Cell Biol. SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus. Sirt1 activator induces proangiogenic genes in preadipocytes to rescue insulin resistance in diet-induced obese mice. SIRT1 gene variants are related to risk of childhood obesity. doi: 10.1002/jor.21284, 52. Aging Cell (2008) 7:7888. doi: 10.1016/j.cell.2005.08.011, 13. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Kilic U, Elibol B, Uysal O, Kilic E, Yulug B, Sakul AS, et al. (2013) 67:607. J Neurosci. In this type of disease, the action mechanism of SIRT1 acted through the modulation of PPAR activity and fatty acid oxidation (48). (2018) 111:2039. Tanno M, Kuno A, Yano T, Miura T, Hisahara S, Ishikawa S, et al.
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Phosphorylated SIRT1 as a biomarker of relapse and response to treatment with glatiramer acetate in multiple sclerosis. Curr Pharm Des. In addition, we found a polymorphism in the promoter region of SIRT1 gene in obese children drawing attention to the association between altered SIRT1 activity and the risk of obesity (50).
doi: 10.1073/pnas.0802917105, 42. In a previous study, investigators observed that increase in the expression level of SIRT1 cannot protect the brain from neurodegeneration without increasing the activity level of SIRT1. In one of the recent study, after feeding with high dietary fructose, the liver of rats were investigated in response to SIRT1 expression as a main energy sensing protein (40). (2010) 21:299313. The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. (2010) 20:6339. PARP inhibition protects against alcoholic and non-alcoholic steatohepatitis. doi: 10.1371/journal.pone.0090428, 62. SIRT1 but not its increased expression is essential for lifespan extension in caloric-restricted mice. Koltai E, Szabo Z, Atalay M, Bolodogh I, Naito H, Goto S, et al. Genes Dev. doi: 10.1371/journal.pone.0008414, 98. doi: 10.1038/sj.emboj.7601758, 90. Matsukawa J, Matsuzawa A, Takeda K, Ichijo H. The ASK1-MAP kinase cascades in mammalian stress response. doi: 10.1016/S0003-4975(99)01033-4, 95.
doi: 10.1016/j.bbalip.2012.05.006, 79. Int J Mol Sci. doi: 10.1161/CIRCULATIONAHA.110.958033, 93. In a postmortem study, the levels of SIRT1 showed a slight increase in the dementia patients with Lewy bodies (16, 83). doi: 10.1016/j.phrs.2012.10.010, 76. Previously, we found that the level of the SIRT1 expression was significantly higher in the CVD patients compared to the levels of SIRT1 in healthy subjects pointing the cross-talk between SIRT1 protein expression and reactive oxygen species (61). In literature, it was reported that the activity of SIRT1 protein is directly or indirectly controlled via the JNK1-SIRT1 link by accumulated oxidative stress which is caused by an increase in the ROS level due to aging or age-related diseases enzyme (1). doi: 10.1038/cr.2013.70, 68. doi: 10.1371/journal.pone.0019194, 64. In the light of this information, we reviewed recent findings related to the association of the increasing level of SIRT1 protein rather than reduction of the SIRT1 expression and regulation of some disease related conditions such as obesity, cardiovascular diseases and neurodegeneration. (2018). It is also thought that transcriptional activity of NF-B protein, a preconditioner in cardiac ischemia, is inhibited by SIRT1 protein to promote cell protection (93, 94). In addition, it was observed that brains of AD patients have consistently reduced NAD+ levels and SIRT1 transcription and/or protein levels involved in chronic inflammation that can also be altered by increased levels of the activated proinflammatory transcription factor NF-B (7779). (2018) 105:17580. Specificity for SIRT1 increases in the relevant metabolic pathways in the hypothalamic circuitries which is also associated with altered downstream factors of SIRT1 such as FoxO transcription factors (27, 28). doi: 10.1016/j.cell.2006.07.002, 8. The common underlying mechanisms of neurodegeneration are increase in the neuroinflammation, mitochondrial damages and oxidative stress (66, 67). On the other hand, it was found that increase in the SIRT1 activity upregulates genes-related metabolic functions, promotes insulin sensitivity and reduces inflammatory gene expressions in the adipose tissue of diet-induced obese animals (49). Hypothalamic dysfunction of the thrombospondin receptor alpha2delta-1 underlies the overeating and obesity triggered by brain-derived neurotrophic factor deficiency. Purushotham A, Schug TT, Xu Q, Surapureddi S, Guo X, Li X. Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation. Kilic U, Gok O, Elibol-Can B, Uysal O, Bacaksiz A. Efficacy of statins on sirtuin 1 and endothelial nitric oxide synthase expression: the role of sirtuin 1 gene variants in human coronary atherosclerosis. The positive correlation between age and SIRT1 expression and/or activity may be a compensation against unexpected situations such as oxidative stress (61, 62). These favorable effects of SIRT1 may be related with the activation of the antioxidant enzymes and stimulation of PGC1 to decrease the level of pro-inflammatory cytokines (41). (2016) 438:7788 doi: 10.1016/j.mce.2016.09.002, 27. doi: 10.1164/rccm.200708-1269OC, 24. doi: 10.1523/JNEUROSCI.1385-10.2010, 26. In this context, the current approaches to enhancing the expression of SIRT1 points the importance of epigenetics in several age-related diseases to provide a healthy aging by developing novel therapies which can prevent or damp the progression of some diseases. Rheumatol Int. doi: 10.1016/j.ijbiomac.2018.07.099, 22. Kilic U, Gok O, Elibol-Can B, Ozgen IT, Erenberk U, Uysal O, et al. (2017) 18:46. doi: 10.1186/s12868-017-0364-1, 17. In the in vitro PD model, it was observed that an overexpression of SIRT1 due to application of toxin (rotenone or MPTP) which causes neurodegeneration was rescued cells from oxidative stress (16, 83).
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