Role of nutraceutical SIRT1 modulators in AMPK and mTOR pathway: Evidence of a synergistic effect

Nutrition

Volumn 34, Issue , 2017, Pages 82-96

  Giovannini, Luca ^a   Bianchi, Sara ^a  

^a UNIVERSITY OF PISA   (Italy)

Author keywords

AMPK; mTOR; Nutraceutical modulators; SIRT1; Synergistic effect

Indexed keywords

BERBERINE; CATECHIN; CURCUMIN; FERULIC ACID; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; MALVIDIN CHLORIDE; MAMMALIAN TARGET OF RAPAMYCIN; NICLOSAMIDE; QUERCETIN; RESVERATROL; SIRTUIN 1; TYROSOL; 4-HYDROXYPHENYLETHANOL; ANTHOCYANIN; COUMARIC ACID; MTOR PROTEIN, HUMAN; PHENETHYL ALCOHOL; SIRT1 PROTEIN, HUMAN; STILBENE DERIVATIVE; TARGET OF RAPAMYCIN KINASE;

ARTICLE; CARCINOMA CELL; CELL VIABILITY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; CYTOTOXICITY TEST; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; HUMAN; HUMAN CELL; IMMUNOBLOTTING; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; UTERINE CERVIX CARCINOMA; WESTERN BLOTTING; ANALOGS AND DERIVATIVES; CELL SURVIVAL; DIETARY SUPPLEMENT; DRUG EFFECTS; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; PHOSPHORYLATION; TUMOR CELL LINE;

AMP-ACTIVATED PROTEIN KINASES; ANTHOCYANINS; BERBERINE; CATECHIN; CELL LINE, TUMOR; CELL SURVIVAL; COUMARIC ACIDS; CURCUMIN; DIETARY SUPPLEMENTS; GENE EXPRESSION REGULATION; HUMANS; NICLOSAMIDE; PHENYLETHYL ALCOHOL; PHOSPHORYLATION; QUERCETIN; SIRTUIN 1; STILBENES; TOR SERINE-THREONINE KINASES;

EID: 85009075027     PISSN: 08999007     EISSN: 18731244     Source Type: Journal    
DOI: 10.1016/j.nut.2016.09.008     Document Type: Article

References (99)

1. [1] Naiman, S., Cohen, H.Y., The contentious history of sirtuin debates. Rambam Maimonides Med J, 3, 2012, e0022.
2. [2] Sinclair, D.A., Guarente, L., Unlocking the secrets of longevity genes. Sci Am 294 (2006), 48–57.
3. [3] Wierman, M.B., Smith, J.S., Yeast sirtuins and the regulation of aging. FEMS Yeast Res 14 (2014), 73–88.
4. [4] Houtkooper, R.H., Pirinen, E., Auwerx, J., Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol 13 (2012), 225–238.
5. [5] Chang, H.C., Guarente, L., SIRT1 and other sirtuins in metabolism. Trends Endocrinol Metab 25 (2014), 138–145.
6. [6] Fiorino, E., Giudici, M., Ferrari, A., Mitro, N., Caruso, D., De Fabiani, E., et al. The sirtuin class of histone deacetylases: Regulation and roles in lipid metabolism. IUBMB Life 66 (2014), 89–99.
7. [7] Davenport, A.M., Huber, F.M., Hoelz, A., Structural and functional analysis of human SIRT1. J Mol Biol 426 (2014), 526–541.
8. [8] Kelly, G., A review of the Sirtuin system, its clinical implications, and the potential role of dietary activators: Part 1. Altern Med Rev 15 (2010), 245–263.
9. [9] Kucińska, M., Piotrowska, H., Murias, M., Sirtuins-modulation of their activity as a novel therapeutic target. Pol Merkur Lekarski 28 (2010), 231–235.
10. [10] Sauve, A.A., Wolberger, C., Schramm, V.L., Boeke, J.D., The biochemistry of sirtuins. Annu Rev Biochem 75 (2006), 435–465.
11. [11] Yakamoto, H., Schoonjans, L., Auwerx, J., Sirtuin functions in health and disease. Mol Endocrinol 21 (2007), 1745–1755.
12. [12] Rahman, S., Islam, R., Mammalian Sirt1: insights on its biological function. Cell Commun Signal, 9, 2011, 11.
13. [13] Michishita, E., Park, J.Y., Burneskis, J.M., Barrett, J.C., Horikawa, I., Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 16 (2005), 4623–4635.
14. [14] Schmeisser, K., Mansfeld, J., Kuhlow, D., Weimer, S., Priebe, S., Heiland, I., et al. Role of sirtuins in lifespan regulation is linked to methylation of nicotinamide. Nat Chem Biol 9 (2013), 693–700.
15. [15] Hubbard, B.P., Sinclair, D.A., Measurement of sirtuin enzyme activity using a substrate-agnostic fluorometric nicotinamide assay. Methods Mol Biol 1077 (2013), 167–177.
16. [16] Nogueiras, R., Habegger, K.M., Chaudhary, N., Finan, B., Banks, A.S., Dietrich, M.O., et al. Sirtuin 1 and sirtuin 3: Physiological modulators of metabolism. Physiol Rev 92 (2012), 1479–1514.
17. [17] Haigis, M.C., Sinclair, D.A., Mammalian sirtuins: Biological insights and disease relevance. Annu Rev Pathol 5 (2010), 253–295.
18. [18] Michan, S., Sinclair, D., Sirtuins in mammals: Insights into their biological function. Biochem J 404 (2007), 1–13.
19. [19] North, B.J., Verdin, E., Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol, 5, 2004, 224.
20. [20] Peck, B., Chen, C.Y., Ho, K.K., Di Fruscia, P., Myatt, S.S., Coombes, R., et al. SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2. Mol Cancer Ther 9 (2010), 844–855.
21. [21] Gonfloni, S., Iannizzotto, V., Maiani, E., Bellusci, G., Ciccone, S., Diederich, M., P53 and Sirt1: Routes of metabolism and genome stability. Biochem Pharmacol 92 (2014), 149–156.
22. [22] Hori, Y.S., Kuno, A., Hosoda, R., Horio, Y., Regulation of FOXOs and p53 by SIRT1 modulators under oxidative stress. PLoS One, 8, 2013, e73875.
23. [23] 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.
24. [24] Lai, C.S., Tsai, M.L., Badmaev, V., Jimenez, M., Ho, C.T., Pan, M.H., Xanthigen suppresses preadipocyte differentiation and adipogenesis through down-regulation of PPARγ and C/EBPs and modulation of SIRT-1, AMPK, and FoxO pathways. J Agric Food Chem 60 (2012), 1094–1101.
25. [25] Richard, D., Picard, F., Brown fat biology and thermogenesis. Front Biosci 16 (2011), 1233–1260.
26. [26] Wang, S.J., Zhao, X.H., Chen, W., Bo, N., Wang, X.J., Chi, Z.F., et al. Sirtuin 1 activation enhances the PGC-1 α/mitochondrial antioxidant system pathway in status epilepticus. Mol Med Rep 11 (2015), 521–526.
27. [27] Kauppinen, A., Suuronen, T., Ojala, J., Kaarniranta, K., Salminen, A., Antagonistic crosstalk between NF-κB and SIRT1 in the regulation of inflammation and metabolic disorders. Cell Signal 25 (2013), 1939–1948.
28. [28] Xie, J., Zhang, X., Zhang, L., Negative regulation of inflammation by SIRT1. Pharmacol Res 67 (2013), 60–67.
29. [29] Bellet, M.M., Nakahata, Y., Boudjelal, M., Watts, E., Mossakowska, D.E., Edwards, K.A., et al. Pharmacological modulation of circadian rhythms by synthetic activators of the deacetylase SIRT1. Proc Natl Acad Sci U S A 110 (2013), 3333–3338.
30. [30] Imai, S., Yoshino, J., The importance of NAMPT/NAD/SIRT1 in the systemic regulation of metabolism and ageing. Diabetes Obes Metab 3 (2013), 26–33.
31. [31] Suchankova, G., Nelson, L.E., Gerhart-Hines, Z., Kelly, M., Gauthier, M.S., Saha, A.K., et al. Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells. Biochem Biophys Res Commun 378 (2009), 836–841.
32. [32] Cantó, C., Gerhart-Hines, Z., Feige, J.N., Lagouge, M., Noriega, L., Milne, J.C., et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature 458 (2009), 1050–1060.
33. [33] Narala, S.R., Allsopp, R.C., Wells, T.B., Zhang, G., Prasad, P., Coussens, M.J., et al. SIRT1 acts as a nutrient-sensitive growth suppressor and its loss is associated with increased AMPK and telomerase activity. Mol Biol Cell 19 (2008), 1210–1219.
34. [34] Lan, F., Cacicedo, J.M., Ruderman, N., Ido, Y., SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation. J Biol Chem 283 (2008), 27628–27635.
35. [35] Hardie, D.G., AMPK: Positive and negative regulation, and its role in whole-body energy homeostasis. Curr Opin Cell Biol 33 (2015), 1–7.
36. [36] Shirwany, N.A., Zou, M.H., AMPK: A cellular metabolic and redox sensor. A minireview. Front Biosci 19 (2014), 447–474.
37. [37] Sun, Y., Li, J., Xiao, N., Wang, M., Kou, J., Qi, L., et al. Pharmacological activation of AMPK ameliorates perivascular adipose/endothelial dysfunction in a manner interdependent on AMPK and SIRT1. Pharmacol Res 89 (2014), 19–28.
38. [38] Jeong, H.W., Cho, S.Y., Kim, S.Y., Shin, E.S., Kim, J.M., Song, M.J., et al. Chitooligosaccharide induces mitochondrial biogenesis and increases exercise endurance through the activation of Sirt1 and AMPK in rats. PLoS One, 7, 2012, e40073.
39. [39] Zarogoulidis, P., Lampaki, S., Turner, J.F., Huang, H., Kakolyris, S., Syrigos, K., et al. mTOR pathway: A current, up-to-date mini-review. Oncol Lett 8 (2014), 2367–2370.
40. [40] Ghosh, H.S., McBurney, M., Robbins, P.D., SIRT1 negatively regulates the mammalian target of rapamycin. PLoS One, 5, 2010, e9199.
41. [41] Zhuo, L., Fu, B., Bai, X., Zhang, B., Wu, L., Cui, J., et al. NAD blocks high glucose induced mesangial hypertrophy via activation of the sirtuins-AMPK-mTOR pathway. Cell Physiol Biochem 27 (2011), 681–690.
42. [42] Tillu, D.V., Melemedjian, O.K., Asiedu, M.N., Qu, N., De Felice, M., Dussor, G., et al. Resveratrol engages AMPK to attenuate ERK and mTOR signaling in sensory neurons and inhibits incision-induced acute and chronic pain. Mol Pain, 8, 2012, 5.
43. [43] Krishan, S., Richardson, D.R., Sahni, S., Adenosine monophosphate activated kinase and its key role in catabolism: Structure, regulation, biological activity and pharmacological activation. Mol Pharmacol 87 (2015), 363–377.
44. [44] Kimura, N., Tokunaga, C., Dalal, S., Richardson, C., Yoshino, K., Hara, K., et al. A possible linkage between AMP-activated protein kinase and mammalian target of rapamycin signaling pathway. Genes Cells 8 (2003), 65–79.
45. [45] Borra, M.T., Smith, B.C., Denu, J.M., Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 280 (2005), 17187–17195.
46. [46] Kwon, H.S., Ott, M., The ups and downs of SIRT1. Trends Biochem Sci 33 (2008), 517–525.
47. [47] Ferrara, N., Rinaldi, B., Corbi, G., Conti, V., Stiuso, P., Boccuti, S., et al. Exercise training promotes SIRT1 activity in aged rats. Rejuvenation Res 11 (2008), 139–150.
48. [48] Lappalainen, Z., Sirtuins: A family of proteins with implications for human performance and exercise physiology. Res Sports Med 19 (2011), 53–65.
49. [49] Revollo, J.R., Grimm, A.A., Imai, S., The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J Biol Chem 279 (2004), 50754–50763.
50. [50] Guarente, L., Picard, F., Calorie restriction–the SIR2 connection. Cell 120 (2005), 473–482.
51. [51] Imai, S., Guarente, L., NAD+ and sirtuins in aging and disease. Trends Cell Biol 24 (2014), 464–471.
52. [52] Baretić, D., Williams, R.L., The structural basis for mTOR function. Semin Cell Dev Biol 36 (2014), 91–101.
53. [53] Neuhaus, P., Klupp, J., Langrehr, J.M., mTOR inhibitors: An overview. Liver Transpl 7 (2001), 473–484.
54. [54] Tan, H.K., Moad, A.I., Tan, M.L., The mTOR signalling pathway in cancer and the potential mTOR inhibitory activities of natural phytochemicals. Asian Pac J Cancer Prev 15 (2014), 6463–6475.
55. [55] Milne, J.C., Lambert, P.D., Schenk, S., Carney, D.P., Smith, J.J., Gagne, D.J., et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450 (2007), 712–716.
56. [56] Mukherjee, S., Lekli, I., Gurusamy, N., Bertelli, A.A., Das, D.K., Expression of the longevity proteins by both red and white wines and their cardioprotective components, resveratrol, tyrosol, and hydroxytyrosol. Free Radic Biol Med 46 (2009), 573–578.
57. [57] Bruckbauer, A., Zemel, M.B., Synergistic effects of polyphenols and methylxanthines with Leucine on AMPK/Sirtuin-mediated metabolism in muscle cells and adipocytes. PLoS One, 9, 2014, e89166.
58. [58] Wang, S., Moustaid-Moussa, N., Chen, L., Mo, H., Shastri, A., Su, R., et al. Novel insights of dietary polyphenols and obesity. J Nutr Biochem 25 (2014), 1–18.
59. [59] Howitz, K.T., Bitterman, K.J., Cohen, H.Y., Lamming, D.W., Lavu, S., Wood, J.G., et al. Small molecule activators of sirtuins extend saccharomyces cerevisiae lifespan. Nature 425 (2003), 191–196.
60. [60] Chi, L., Peng, L., Pan, N., Hu, X., Zhang, Y., The anti-atherogenic effects of berberine on foam cell formation are mediated through the upregulation of sirtuin 1. Int J Mol Med 34 (2014), 1087–1093.
61. [61] Zhu, X., Guo, X., Mao, G., Gao, Z., Wang, H., He, Q., et al. Hepatoprotection of berberine against hydrogen peroxide-induced apoptosis by upregulation of Sirtuin 1. Phytother Res 27 (2013), 417–421.
62. [62] Gomes, A.P., Duarte, F.V., Nunes, P., Hubbard, B.P., Teodoro, J.S., Varela, A.T., et al. Berberine protects against high fat diet-induced dysfunction in muscle mitochondria by inducing SIRT1-dependent mitochondrial biogenesis. Biochim Biophys Acta 1822 (2012), 185–195.
63. [63] Gambini, J., Inglés, M., Olaso, G., Lopez-Grueso, R., Bonet-Costa, V., Gimeno-Mallench, L., et al. Properties of resveratrol: In vitro and in vivo studies about metabolism, bioavailability, and biological effects in animal models and humans. Oxid Med Cell Longev, 2015, 2015, 837042.
64. [64] Samuel, S.M., Thirunavukkarasu, M., Penumathsa, S.V., Paul, D., Maulik, N., Akt/FOXO3 a/SIRT1-mediated cardioprotection by n-tyrosol against ischemic stress in rat in vivo model of myocardial infarction: Switching gears toward survival and longevity. J Agric Food Chem 56 (2008), 9692–9698.
65. [65] Chao, H.M., Lin, D.E., Chang, Y., Hsu, W.M., Lee, S.M., Lee, F.L., et al. Ferulic acid, but not tetramethylpyrazine, significantly attenuates retinal ischemia/reperfusion-induced alterations by acting as a hydroxyl radical scavenger. J Ocul Pharmacol Ther 24 (2008), 461–472.
66. [66] Chao, H.M., Chen, Y.H., Liu, J.H., Hsu, W.M., Lee, S.M., Lee, F.L., et al. Iron-generated hydroxyl radicals kill retinal cells in vivo: Effect of ferulic acid. Hum Exp Toxicol 27 (2008), 327–339.
67. [67] Li, G.L., Wang, J.J., Wang, J.Z., Liu, Y.Y., Jin, Y., Effect of ferulic acid on the proliferation of nerve cells of retinas in vitro. Zhonghua Yan Ke Za Zhi 39 (2003), 650–654.
68. [68] Jiménez-Flores, L.M., López-Briones, S., Macías-Cervantes, M.H., Ramírez-Emiliano, J., Pérez-Vázquez, V., A PPARγ, NF-κB and AMPK-dependent mechanism may be involved in the beneficial effects of curcumin in the diabetic db/db mice liver. Molecules 19 (2014), 8289–8302.
69. [69] Sun, Q., Jia, N., Wang, W., Jin, H., Xu, J., Hu, H., Activation of SIRT1 by curcumin blocks the neurotoxicity of amyloid-β25-35 in rat cortical neurons. Biochem Biophys Res Commun 448 (2014), 89–94.
70. [70] Liu, P., Zou, D., Yi, L., Chen, M., Chen, M., Gao, Y., et al. Quercetin ameliorates hypobaric hypoxia-induced memory impairment through mitochondrial and neuron function adaptation via the PGC-1 α pathway. Restor Neurol Neurosci 33 (2015), 143–157.
71. [71] Dong, J., Zhang, X., Zhang, L., Bian, H.X., Xu, N., Bao, B., et al. Quercetin reduces obesity-associated ATM infiltration and inflammation in mice: A mechanism including AMPKα1/SIRT1. J Lipid Res 55 (2014), 363–374.
72. [72] Park, D., Jeong, H., Lee, M.N., Koh, A., Kwon, O., Yang, Y.R., et al. Resveratrol induces autophagy by directly inhibiting mTOR through ATP competition. Sci Rep, 6, 2016, 21772.
73. [73] Hasima, N., Ozpolat, B., Regulation of autophagy by polyphenolic compounds as a potential therapeutic strategy for cancer. Cell Death Dis, 5, 2014, e1509.
74. [74] Aubert, G., Telomere dynamics and aging. Prog Mol Biol Transl Sci 125 (2014), 89–111.
75. [75] Zhang, W., Hui, R., Yang, S., Telomeres, cardiovascular aging, and potential intervention for cellular senescence. Sci China Life Sci 57 (2014), 858–862.
76. [76] Tzanetakou, I.P., Nzietchueng, R., Perrea, D.N., Benetos, A., Telomeres and their role in aging and longevity. Curr Vasc Pharmacol 12 (2014), 726–734.
77. [77] Schug, T.T., Li, X., Sirtuin 1 in lipid metabolism and obesity. Ann Med 43 (2011), 198–211.
78. [78] Metoyer, C.F., The role of sirtuin proteins in obesity. Pathophysiology 15 (2008), 103–108.
79. [79] Pillarisetti, S., A review of Sirt1 and Sirt1 modulators in cardiovascular and metabolic diseases. Recent Pat Cardiovasc Drug Discov 3 (2008), 156–164.
80. [80] Yacoub, R., Lee, K., He, J.C., The role of SIRT1 in diabetic kidney disease. Front Endocrinol (Lausanne), 5, 2014, 166.
81. [81] Baksi, A., Kraydashenko, O., Zalevkaya, A., Stets, R., Elliott, P., Haddad, J., et al. A phase II, randomized, placebo-double-blind, multi-dose study of SRT2104, a SIRT1 activator, in subjects with type 2 diabetes. Br J Clin Pharmacol 78 (2014), 69–77.
82. [82] Kitada, M., Kume, S., Kanasaki, K., Takeda-Watanabe, A., Koya, D., Sirtuins as possible drug targets in type 2 diabetes. Curr Drug Targets 14 (2013), 622–636.
83. [83] De Oliveira, R.M., Pais, T.F., Outeiro, T.F., Sirtuins: Common targets in aging and in neurodegeneration. Curr Drug Targets 10 (2010), 1270–1280.
84. [84] Luo, X.Y., Qu, S.L., Tang, Z.H., Zhang, Y., Liu, M.H., Peng, J., et al. SIRT1 in cardiovascular. Clin Chim Acta 437 (2014), 106–114.
85. [85] Kilic, U., Gok, O., Bacaksiz, A., Izmirli, M., Elibol-Can, B., Uysal, O., SIRT1 gene polymorphisms affect the protein expression in cardiovascular diseases. PLoS One, 9, 2014, e90428.
86. [86] Herskovits, A.Z., Guarente, L., SIRT1 in neurodevelopment and brain senescence. Neuron 81 (2014), 471–483.
87. [87] Mohrin, M., Chen, D., Sirtuins, tissue maintenance, and tumorigenesis. Genes Cancer 4 (2013), 76–81.
88. [88] 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.
89. [89] Maloney, S.C., Antecka, E., Odashiro, A.N., Fernandes, B.F., Doyle, M., Lim, L.A., et al. Expression of SIRT1 and DBC1 in developing and adult retinas. Stem Cells Int, 2012, 2012, 908183.
90. [90] Roth, M., Chen, W.Y., Sorting out functions of sirtuins in cancer. Oncogene 33 (2014), 1609–1620.
91. [91] Kawashima, M., Ozawa, Y., Shinmura, K., Inaba, T., Nakamura, S., Kawakita, T., et al. Calorie restriction (CR) and CR mimetics for the prevention and treatment of age-related eye disorders. Exp Gerontol 48 (2013), 1096–1100.
92. [92] Kalt, W., Hanneken, A., Milbury, P., Tremblay, F., Recent research on polyphenolics in vision and eye health. J Agric Food Chem 58 (2010), 4001–4007.
93. [93] Zschoernig, B., Mahlknecht, U., SIRTUIN 1: Regulating the regulator. Biochem Biophys Res Commun 376 (2008), 251–255.
94. [94] Milner, J., Cellular regulation of SIRT1. Curr Pharm Des 15 (2009), 39–44.
95. [95] Zhang, T., Berrocal, J.G., Frizzell, K.M., Gamble, M.J., DuMond, M.E., Krishnakumar, R., et al. Enzymes in the NAD+ salvage pathway regulate SIRT1 activity at target gene promoters. J Biol Chem 284 (2009), 20408–20417.
96. [96] Alcaín, F.J., Villalba, J.M., Sirtuin inhibitors. Expert Opin Ther Pat 19 (2009), 283–294.
97. [97] Blagosklonny, M.V., Linking calorie restriction to longevity through sirtuins and autophagy: Any role for TOR. Cell Death Dis, 1, 2010, e12.
98. [98] Mimura, T., Kaji, Y., Noma, H., Funatsu, H., Okamoto, S., The role of SIRT1 in ocular aging. Exp Eye Res 116 (2013), 17–26.
99. [99] Ozawa, Y., Kubota, S., Narimatsu, T., Yuki, K., Koto, T., Sasaki, M., et al. Retinal aging and sirtuins. Ophthalmic Res 44 (2010), 199–203.