Sirtuins as therapeutic targets for improving delayed wound healing in diabetes

References

• American Diabetes Association. Diagnosis and classification of diabetes mellitus. Diabetes Care. 2009;32(Suppl. 1):S62–S67.
   PubMed Web of Science ®Google Scholar
• Saeedi P, Petersohn I, Salpea P, et al. Global and regional diabetes prevalence estimates for 2019 and projections for 2030 and 2045: results from the International Diabetes Federation Diabetes Atlas, 9th edition. Diabetes Res Clin Pract. 2019;157:107843.
   PubMed Web of Science ®Google Scholar
• Cade WT. Diabetes-related microvascular and macrovascular diseases in the physical therapy setting. Phys Ther. 2008;88(11):1322–1335.
   PubMed Web of Science ®Google Scholar
• Wu SC, Driver VR, Wrobel JS, et al. Foot ulcers in the diabetic patient, prevention and treatment. Vasc Health Risk Manag. 2007;3(1):65–76.
   PubMedGoogle Scholar
• Zhang P, Lu J, Jing Y, et al. Global epidemiology of diabetic foot ulceration: a systematic review and meta-analysis. Ann Med. 2017;49(2):106–116.
   PubMed Web of Science ®Google Scholar
• Gonzalez AdO, Costa TF, Andrade ZdA, et al. Wound healing – a literature review. An Bras Dermatol. 2016;91(5):614–620.
   PubMed Web of Science ®Google Scholar
• Mittal M, Siddiqui MR, Tran K, et al. Reactive oxygen species in inflammation and tissue injury. Antioxid Redox Signal. 2014;20(7):1126–1167.
   PubMed Web of Science ®Google Scholar
• Selders GS, Fetz AE, Radic MZ, et al. An overview of the role of neutrophils in innate immunity, inflammation and host–biomaterial integration. Regen Biomater. 2017;4(1):55–68.
   PubMed Web of Science ®Google Scholar
• Ellis S, Lin EJ, Tartar D. Immunology of wound healing. Curr Dermatol Rep. 2018;7(4):350–358.
   PubMed Web of Science ®Google Scholar
• Parisi L, Gini E, Baci D, et al. Macrophage polarization in chronic inflammatory diseases: killers or builders? J Immunol Res. 2018;2018:8917804.
   PubMed Web of Science ®Google Scholar
• Ogle ME, Segar CE, Sridhar S, et al. Monocytes and macrophages in tissue repair: implications for immunoregenerative biomaterial design. Exp Biol Med. 2016;241(10):1084–1097.
   Web of Science ®Google Scholar
• Hirayama D, Iida T, Nakase H. The phagocytic function of macrophage-enforcing innate immunity and tissue homeostasis. Int J Mol Sci. 2017;19(1):92.
   PubMed Web of Science ®Google Scholar
• Pastar I, Stojadinovic O, Yin NC, et al. Epithelialization in wound healing: a comprehensive review. Adv Wound Care. 2014;3(7):445–464.
   PubMedGoogle Scholar
• Xue M, Jackson CJ. Extracellular matrix reorganization during wound healing and its impact on abnormal scarring. Adv Wound Care. 2015;4(3):119–136.
   PubMed Web of Science ®Google Scholar
• Wojtowicz AM, Oliveira S, Carlson MW, et al. The importance of both fibroblasts and keratinocytes in a bilayered living cellular construct used in wound healing. Wound Repair Regen. 2014;22(2):246–255.
   PubMed Web of Science ®Google Scholar
• Kumar P, Kumar S, Udupa EP, et al. Role of angiogenesis and angiogenic factors in acute and chronic wound healing. Plast Aesthet Res. 2015;2(5):243.
   Google Scholar
• Darby IA, Laverdet B, Bonté F, et al. Fibroblasts and myofibroblasts in wound healing. Clin Cosmet Investig Dermatol. 2014;7:301–311.
   PubMedGoogle Scholar
• Kalluri R, Weinberg RA. The basics of epithelial–mesenchymal transition. J Clin Invest. 2009;119(6):1420–1428.
   PubMed Web of Science ®Google Scholar
• Stone RC, Pastar I, Ojeh N, et al. Epithelial–mesenchymal transition in tissue repair and fibrosis. Cell Tissue Res. 2016;365(3):495–506.
   PubMed Web of Science ®Google Scholar
• Guo S, DiPietro LA. Factors affecting wound healing. J Dent Res. 2010;89(3):219–229.
   PubMed Web of Science ®Google Scholar
• Okonkwo U, DiPietro L. Diabetes and wound angiogenesis. Int J Mol Sci. 2017;18(7):1419.
   PubMed Web of Science ®Google Scholar
• Singh VP, Bali A, Singh N, et al. Advanced glycation end products and diabetic complications. Korean J Physiol Pharmacol. 2014;18(1):1–14.
   PubMed Web of Science ®Google Scholar
• Gkogkolou P, Böhm M. Advanced glycation end products: key players in skin aging? Dermatoendocrinology. 2012;4(3):259–270.
   PubMedGoogle Scholar
• Atalay M, Oksala N, Lappalainen J, et al. Heat shock proteins in diabetes and wound healing. Curr Protein Pept Sci. 2009;10(1):85–95.
   PubMed Web of Science ®Google Scholar
• Tsourdi E, Barthel A, Rietzsch H, et al. Current aspects in the pathophysiology and treatment of chronic wounds in diabetes mellitus. Biomed Res Int. 2013;2013:385641.
   PubMed Web of Science ®Google Scholar
• Shi GJ, Shi GR, Zhou JY, et al. Involvement of growth factors in diabetes mellitus and its complications: a general review. Biomed Pharmacother. 2018;101:510–527.
   PubMed Web of Science ®Google Scholar
• Sofer Y, Nash Y, Osher E, et al. Insulin-degrading enzyme higher in subjects with metabolic syndrome. Endocrine. 2021;71(2):357–364.
   PubMed Web of Science ®Google Scholar
• Caley MP, Martins VLC, O'Toole EA. Metalloproteinases and wound healing. Adv Wound Care. 2015;4(4):225–234.
   PubMed Web of Science ®Google Scholar
• Muller M, Trocme C, Lardy B, et al. Matrix metalloproteinases and diabetic foot ulcers: the ratio of MMP-1 to TIMP-1 is a predictor of wound healing. Diabet Med. 2008;25(4):419–426.
   PubMed Web of Science ®Google Scholar
• Michan S, Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem J. 2007;404(1):1–13.
   PubMed Web of Science ®Google Scholar
• Vassilopoulos A, Fritz KS, Petersen DR, et al. The human sirtuin family: evolutionary divergences and functions. Hum Genomics. 2011;5(5):485–496.
   PubMedGoogle Scholar
• Ropero S, Esteller M. The role of histone deacetylases (HDACs) in human cancer. Mol Oncol. 2007;1(1):19–25.
   PubMed Web of Science ®Google Scholar
• Sauve AA. Sirtuin chemical mechanisms. Biochim Biophys Acta. 2010;1804(8):1591–1603.
   PubMed Web of Science ®Google Scholar
• Dang W. The controversial world of sirtuins. Drug Discov Today Technol. 2014;12:e9–e17.
   PubMedGoogle Scholar
• Hwang ES, Song SB. Nicotinamide is an inhibitor of SIRT1 in vitro, but can be a stimulator in cells. Cell Mol Life Sci. 2017;74(18):3347–3362.
   PubMed Web of Science ®Google Scholar
• Hershberger KA, Martin AS, Hirschey MD. Role of NAD+ and mitochondrial sirtuins in cardiac and renal diseases. Nat Rev Nephrol. 2017;13(4):213–225.
   PubMed Web of Science ®Google Scholar
• Kupis W, Pałyga J, Tomal E, et al. The role of sirtuins in cellular homeostasis. J Physiol Biochem. 2016;72(3):371–380.
   PubMed Web of Science ®Google Scholar
• Greiss S, Gartner A. Sirtuin/Sir2 phylogeny, evolutionary considerations and structural conservation. Mol Cells. 2009;28(5):407–415.
   PubMed Web of Science ®Google Scholar
• Sudhakar M, Silambanan S, Ramakrishnan R. Sirtuins in adipose tissue metabolism. In: Szablewski L, editor. Adipose tissue. InTech; 2018.
   Google Scholar
• Rifaï K, Judes G, Idrissou M, et al. SIRT1-dependent epigenetic regulation of H3 and H4 histone acetylation in human breast cancer. Oncotarget. 2018;9(55):30661–30678.
   PubMedGoogle Scholar
• Dimauro T, David G. Chromatin modifications: the driving force of senescence and aging? Aging. 2009;1(2):182–190.
   PubMedGoogle Scholar
• Kumari P, Popescu D, Yue S, et al. Sirt7 inhibits Sirt1-mediated activation of Suv39h1. Cell Cycle. 2018;17(12):1403–1412.
   PubMed Web of Science ®Google Scholar
• Zhang T, Kraus WL. SIRT1-dependent regulation of chromatin and transcription: linking NAD(+) metabolism and signaling to the control of cellular functions. Biochim Biophys Acta. 2010;1804(8):1666–1675.
   PubMed Web of Science ®Google Scholar
• McBurney MW, Clark-Knowles KV, Caron AZ, et al. SIRT1 is a highly networked protein that mediates the adaptation to chronic physiological stress. Genes Cancer. 2013;4(3–4):125–134.
   PubMedGoogle Scholar
• Erion DM, Yonemitsu S, Nie Y, et al. SirT1 knockdown in liver decreases basal hepatic glucose production and increases hepatic insulin responsiveness in diabetic rats. Proc Natl Acad Sci U S A. 2009;106(27):11288–11293.
   PubMed Web of Science ®Google Scholar
• Liu Y, Dentin R, Chen D, et al. A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange. Nature. 2008;456(7219):269–273.
   PubMed Web of Science ®Google Scholar
• Cantó C, Auwerx J. PGC-1alpha, SIRT1 and AMPK, an energy sensing network that controls energy expenditure. Curr Opin Lipidol. 2009;20(2):98–105.
   PubMed Web of Science ®Google Scholar
• Pfluger PT, Herranz D, Velasco-Miguel S, et al. Sirt1 protects against high-fat diet-induced metabolic damage. Proc Natl Acad Sci U S A. 2008;105(28):9793–9798.
   PubMed Web of Science ®Google Scholar
• Raynes R, Brunquell J, Westerheide SD. Stress inducibility of SIRT1 and its role in cytoprotection and cancer. Genes Cancer. 2013;4(3–4):172–182.
   PubMedGoogle Scholar
• Kauppinen A, Suuronen T, Ojala J, et al. Antagonistic crosstalk between NF-κB and SIRT1 in the regulation of inflammation and metabolic disorders. Cell Signal. 2013;25(10):1939–1948.
   PubMed Web of Science ®Google Scholar
• Yoon H, Shin SH, Shin DH, et al. Differential roles of Sirt1 in HIF-1α and HIF-2α mediated hypoxic responses. Biochem Biophys Res Commun. 2014;444(1):36–43.
   PubMed Web of Science ®Google Scholar
• Lim JH, Lee YM, Chun YS, et al. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol Cell. 2010;38(6):864–878.
   PubMed Web of Science ®Google Scholar
• Pecher SJ, Potthast AB, von Versen-Höynck F, et al. Impact of short-term hypoxia on sirtuins as regulatory elements in HUVECs. J Clin Med. 2020;9(8):2604.
   Web of Science ®Google Scholar
• Westerheide SD, Anckar J, Stevens SM, et al. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science. 2009;323(5917):1063–1066.
   PubMed Web of Science ®Google Scholar
• Nakagawa T, Guarente L. Sirtuins at a glance. J Cell Sci. 2011;124(Pt 6):833–838.
   PubMed Web of Science ®Google Scholar
• Zhu X, Liu Q, Wang M, et al. Activation of Sirt1 by resveratrol inhibits TNF-α induced inflammation in fibroblasts. PLOS One. 2011;6(11):e27081.
   PubMed Web of Science ®Google Scholar
• Matsushima S, Sadoshima J. The role of sirtuins in cardiac disease. Am J Physiol Heart Circ Physiol. 2015;309(9):H1375–H1389.
   PubMed Web of Science ®Google Scholar
• Hsu CP, Zhai P, Yamamoto T, et al. Silent information regulator 1 protects the heart from ischemia/reperfusion. Circulation. 2010;122(21):2170–2182.
   PubMed Web of Science ®Google Scholar
• Mattagajasingh I, Kim CS, Naqvi A, et al. SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase. Proc Natl Acad Sci U S A. 2007;104(37):14855–14860.
   PubMed Web of Science ®Google Scholar
• Chong ZZ, Wang S, Shang YC, et al. Targeting cardiovascular disease with novel SIRT1 pathways. Future Cardiol. 2012;8(1):89–100.
   PubMedGoogle Scholar
• Sundaresan NR, Pillai VB, Gupta MP. Emerging roles of SIRT1 deacetylase in regulating cardiomyocyte survival and hypertrophy. J Mol Cell Cardiol. 2011;51(4):614–618.
   PubMed Web of Science ®Google Scholar
• Tang BL, Chua CEL. SIRT2, tubulin deacetylation, and oligodendroglia differentiation. Cell Motil Cytoskeleton. 2008;65(3):179–182.
   PubMed Web of Science ®Google Scholar
• Serrano L, Martinez-Redondo P, Marazuela-Duque A, et al. The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes Dev. 2013;27(6):639–653.
   PubMed Web of Science ®Google Scholar
• Jing E, Gesta S, Kahn CR. SIRT2 regulates adipocyte differentiation through FoxO1 acetylation/deacetylation. Cell Metab. 2007;6(2):105–114.
   PubMed Web of Science ®Google Scholar
• Liu Y, Zhang Y, Zhu K, et al. Emerging role of sirtuin 2 in Parkinson's disease. Front Aging Neurosci. 2019;11:372.
   PubMed Web of Science ®Google Scholar
• Carrico C, Meyer JG, He W, et al. The mitochondrial acylome emerges: proteomics, regulation by sirtuins, and metabolic and disease implications. Cell Metab. 2018;27(3):497–512.
   PubMed Web of Science ®Google Scholar
• Hirschey MD, Shimazu T, Goetzman E, et al. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature. 2010;464(7285):121–125.
   PubMed Web of Science ®Google Scholar
• Min Z, Gao J, Yu Y. The roles of mitochondrial SIRT4 in cellular metabolism. Front Endocrinol. 2018;9:783.
   PubMed Web of Science ®Google Scholar
• Argmann C, Auwerx J. Insulin secretion: SIRT4 gets in on the act. Cell. 2006;126(5):837–839.
   PubMed Web of Science ®Google Scholar
• Nakagawa T, Guarente L. Urea cycle regulation by mitochondrial sirtuin, SIRT5. Aging. 2009;1(6):578–581.
   PubMedGoogle Scholar
• Lombard DB, Tishkoff DX, Bao J. Mitochondrial sirtuins in the regulation of mitochondrial activity and metabolic adaptation. In: Yao TP, Seto E, editors. Histone deacetylases: the biology and clinical implication. Vol. 206. Handbook of experimental pharmacology. Berlin Heidelberg: Springer; 2011. p. 163–188.
   Google Scholar
• Xiao C, Kim HS, Lahusen T, et al. SIRT6 deficiency results in severe hypoglycemia by enhancing both basal and insulin-stimulated glucose uptake in mice. J Biol Chem. 2010;285(47):36776–36784.
   PubMed Web of Science ®Google Scholar
• McCord RA, Michishita E, Hong T, et al. SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair. Aging. 2009;1(1):109–121.
   PubMedGoogle Scholar
• Chang AR, Ferrer CM, Mostoslavsky R. SIRT6, a mammalian deacylase with multitasking abilities. Physiol Rev. 2020;100(1):145–169.
   PubMed Web of Science ®Google Scholar
• Nagai K, Matsushita T, Matsuzaki T, et al. Depletion of SIRT6 causes cellular senescence, DNA damage, and telomere dysfunction in human chondrocytes. Osteoarthritis Cartilage. 2015;23(8):1412–1420.
   PubMed Web of Science ®Google Scholar
• Kawahara TLA, Michishita E, Adler AS, et al. SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span. Cell. 2009;136(1):62–74.
   PubMed Web of Science ®Google Scholar
• Zhong L, D'Urso A, Toiber D, et al. The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1alpha. Cell. 2010;140(2):280–293.
   PubMed Web of Science ®Google Scholar
• Kim HS, Xiao C, Wang RH, et al. Hepatic-specific disruption of SIRT6 in mice results in fatty liver formation due to enhanced glycolysis and triglyceride synthesis. Cell Metab. 2010;12(3):224–236.
   PubMed Web of Science ®Google Scholar
• Zhou S, Tang X, Chen HZ. Sirtuins and insulin resistance. Front Endocrinol. 2018;9:748.
   PubMed Web of Science ®Google Scholar
• Song J, Yang B, Jia X, et al. Distinctive roles of sirtuins on diabetes, protective or detrimental? Front Endocrinol. 2018;9:724.
   PubMed Web of Science ®Google Scholar
• Mussbacher M, Salzmann M, Brostjan C, et al. Cell type-specific roles of NF-κB linking inflammation and thrombosis. Front Immunol. 2019;10:85.
   PubMed Web of Science ®Google Scholar
• Ford E, Voit R, Liszt G, et al. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 2006;20(9):1075–1080.
   PubMed Web of Science ®Google Scholar
• Vakhrusheva O, Smolka C, Gajawada P, et al. Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circ Res. 2008;102(6):703–710.
   PubMed Web of Science ®Google Scholar
• Satoh A, Stein L, Imai S. The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity. In: Yao TP, Seto E, editors. Histone deacetylases: the biology and clinical implication. Vol. 206. Handbook of experimental pharmacology. Berlin, Heidelberg: Springer; 2011. p. 125–162.
   Google Scholar
• Wu L, Zhou L, Lu Y, et al. Activation of SIRT1 protects pancreatic β-cells against palmitate-induced dysfunction. Biochim Biophys Acta. 2012;1822(11):1815–1825.
   PubMed Web of Science ®Google Scholar
• Bordone L, Motta MC, Picard F, et al. Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic beta cells. PLoS Biol. 2006;4(2):e31.
   PubMed Web of Science ®Google Scholar
• Watanabe H, Inaba Y, Kimura K, et al. Sirt2 facilitates hepatic glucose uptake by deacetylating glucokinase regulatory protein. Nat Commun. 2018;9(1):30.
   PubMedGoogle Scholar
• Kanwal A, Dsouza LA. Sirtuins and diabetes: optimizing the sweetness in the blood. Transl Med Commun. 2019;4(1):3.
   Google Scholar
• Jing E, Emanuelli B, Hirschey MD, et al. Sirtuin-3 (Sirt3) regulates skeletal muscle metabolism and insulin signaling via altered mitochondrial oxidation and reactive oxygen species production. Proc Natl Acad Sci U S A. 2011;108(35):14608–14613.
   PubMed Web of Science ®Google Scholar
• Huang X, Sun J, Chen G, et al. Resveratrol promotes diabetic wound healing via SIRT1-FOXO1-c-Myc signaling pathway-mediated angiogenesis. Front Pharmacol. 2019;10:421.
   PubMed Web of Science ®Google Scholar
• Kuang J, Chen L, Tang Q, et al. The role of Sirt6 in obesity and diabetes. Front Physiol. 2018;9:135.
   PubMed Web of Science ®Google Scholar
• Aioi A. Sirtuins in wound healing. Trends Immunother. 2017;1(3):89–95.
   Google Scholar
• Garcia-Peterson LM, Wilking-Busch MJ, Ndiaye MA, et al. Sirtuins in skin and skin cancers. Skin Pharmacol Physiol. 2017;30(4):216–224.
   PubMed Web of Science ®Google Scholar
• Wahedi H, Chae J, Subedi L, et al. NED416, a novel synthetic Sirt1 activator, promotes cutaneous wound healing via the MAPK/rho pathway. Int J Mol Med. 2020;46(1):149–158.
   PubMed Web of Science ®Google Scholar
• Lee JS, Park KY, Min HG, et al. Negative regulation of stress-induced matrix metalloproteinase-9 by Sirt1 in skin tissue: negative regulation of MMP-9 by SIRT1. Exp Dermatol. 2010;19(12):1060–1066.
   PubMed Web of Science ®Google Scholar
• Strycharz J, Rygielska Z, Swiderska E, et al. SIRT1 as a therapeutic target in diabetic complications. Curr Med Chem. 2018;25(9):1002–1035.
   PubMed Web of Science ®Google Scholar
• Prabhakar PK, Singh K, Kabra D, et al. Natural SIRT1 modifiers as promising therapeutic agents for improving diabetic wound healing. Phytomedicine. 2020;76:153252.
   PubMed Web of Science ®Google Scholar
• Dou YQ, Kong P, Li CL, et al. Smooth muscle SIRT1 reprograms endothelial cells to suppress angiogenesis after ischemia. Theranostics. 2020;10(3):1197–1212.
   PubMed Web of Science ®Google Scholar
• Qiang L, Sample A, Liu H, et al. Epidermal SIRT1 regulates inflammation, cell migration, and wound healing. Sci Rep. 2017;7(1):14110.
   PubMed Web of Science ®Google Scholar
• Wang Y, Zhao X, Shi D, et al. Overexpression of SIRT1 promotes high glucose-attenuated corneal epithelial wound healing via p53 regulation of the IGFBP3/IGF-1R/AKT pathway. Invest Ophthalmol Vis Sci. 2013;54(5):3806–3814.
   PubMed Web of Science ®Google Scholar
• Wendling D, Abbas W, Godfrin-Valnet M, et al. Resveratrol, a sirtuin 1 activator, increases IL-6 production by peripheral blood mononuclear cells of patients with knee osteoarthritis. Clin Epigenetics. 2013;5(1):10.
   PubMedGoogle Scholar
• Witte MB, Barbul A. Role of nitric oxide in wound repair. Am J Surg. 2002;183(4):406–412.
   PubMed Web of Science ®Google Scholar
• Kowluru RA, Santos JM, Zhong Q. Sirt1, a negative regulator of matrix metalloproteinase-9 in diabetic retinopathy. Invest Ophthalmol Vis Sci. 2014;55(9):5653–5660.
   PubMedGoogle Scholar
• Yang S, Xu M, Meng G, et al. SIRT3 deficiency delays diabetic skin wound healing via oxidative stress and necroptosis enhancement. J Cell Mol Med. 2020;24(8):4415–4427.
   PubMed Web of Science ®Google Scholar
• Petyaev I, Bashmakov YK, Assaad Khalil S. Resveratrol and diabetic foot syndrome. J Int Soc Antioxid Nutr Health. 2016;3(1).
   Google Scholar
• Berce C, Muresan MS, Soritau O, et al. Cutaneous wound healing using polymeric surgical dressings based on chitosan, sodium hyaluronate and resveratrol. A preclinical experimental study. Colloids Surf B Biointerfaces. 2018;163:155–166.
   PubMed Web of Science ®Google Scholar
• Beretta GL, Corno C, Zaffaroni N, et al. Role of FoxO proteins in cellular response to antitumor agents. Cancers. 2019;11(1):90.
   PubMed Web of Science ®Google Scholar
• Boccitto M, Kalb RG. Regulation of foxo-dependent transcription by post-translational modifications. Curr Drug Targets. 2011;12(9):1303–1310.
   PubMed Web of Science ®Google Scholar
• Fu Z, Tindall DJ. FOXOs, cancer and regulation of apoptosis. Oncogene. 2008;27(16):2312–2319.
   PubMed Web of Science ®Google Scholar
• Sergi C, Shen F, Liu SM. Insulin/IGF-1R, SIRT1, and FOXOs pathways—an intriguing interaction platform for bone and osteosarcoma. Front Endocrinol. 2019;10:93.
   PubMed Web of Science ®Google Scholar
• Lee Y, Ka SO, Cha HN, et al. Myeloid sirtuin 6 deficiency causes insulin resistance in high-fat diet-fed mice by eliciting macrophage polarization toward an M1 phenotype. Diabetes. 2017;66(10):2659–2668.
   PubMed Web of Science ®Google Scholar
• Huang L, Cai HA, Zhang MS, et al. Ginsenoside Rg1 promoted the wound healing in diabetic foot ulcers via miR-489-3p/Sirt1 axis. J Pharmacol Sci. 2021;147(3):271–283.
   PubMed Web of Science ®Google Scholar
• Singh CK, Chhabra G, Ndiaye MA, et al. The role of sirtuins in antioxidant and redox signaling. Antioxid Redox Signal. 2018;28(8):643–661.
   PubMed Web of Science ®Google Scholar
• Uchitomi R, Nakai S, Matsuda R, et al. Genistein, daidzein, and resveratrols stimulate PGC-1β-mediated gene expression. Biochem Biophys Rep. 2019;17:51–55.
   PubMedGoogle Scholar
• Gutiérrez M, Andrianasolo EH, Shin WK, et al. Structural and synthetic investigations of tanikolide dimer, a SIRT2 selective inhibitor, and tanikolide seco-acid from the Madagascar marine cyanobacterium Lyngbya majuscula. J Org Chem. 2009;74(15):5267–5275.
   PubMed Web of Science ®Google Scholar
• Thandavarayan RA, Garikipati VNS, Joladarashi D, et al. Sirtuin-6 deficiency exacerbates diabetes-induced impairment of wound healing. Exp Dermatol. 2015;24(10):773–778.
   PubMed Web of Science ®Google Scholar
• Dai H, Sinclair DA, Ellis JL, et al. Sirtuin activators and inhibitors: promises, achievements, and challenges. Pharmacol Ther. 2018;188:140–154.
   PubMed Web of Science ®Google Scholar
• Liu YC, Zou XB, Chai YF, et al. Macrophage polarization in inflammatory diseases. Int J Biol Sci. 2014;10(5):520–529.
   PubMed Web of Science ®Google Scholar
• Lo Sasso G, Menzies KJ, Mottis A, et al. SIRT2 deficiency modulates macrophage polarization and susceptibility to experimental colitis. PLOS One. 2014;9(7):e103573.
   PubMed Web of Science ®Google Scholar
• Park SY, Lee SW, Lee SY, et al. SIRT1/adenosine monophosphate-activated protein kinase α signaling enhances macrophage polarization to an anti-inflammatory phenotype in rheumatoid arthritis. Front Immunol. 2017;8:1135.
   PubMed Web of Science ®Google Scholar
• Pandey KB, Rizvi SI. Plant polyphenols as dietary antioxidants in human health and disease. Oxid Med Cell Longev. 2009;2(5):270–278.
   PubMed Web of Science ®Google Scholar
• Karaman Mayack B, Sippl W, Ntie-Kang F. Natural products as modulators of sirtuins. Molecules. 2020;25(14):3287.
   Web of Science ®Google Scholar
• Ito-Nagahata T, Kurihara C, Hasebe M, et al. Stilbene analogs of resveratrol improve insulin resistance through activation of AMPK. Biosci Biotechnol Biochem. 2013;77(6):1229–1235.
   PubMed Web of Science ®Google Scholar
• Lee YE, Kim JW, Lee EM, et al. Chronic resveratrol treatment protects pancreatic islets against oxidative stress in db/db mice. PLOS One. 2012;7(11):e50412.
   PubMed Web of Science ®Google Scholar
• Zhang J, Chen L, Zheng J, et al. The protective effect of resveratrol on islet insulin secretion and morphology in mice on a high-fat diet. Diabetes Res Clin Pract. 2012;97(3):474–482.
   PubMed Web of Science ®Google Scholar
• Xu Y, Nie L, Yin YG, et al. Resveratrol protects against hyperglycemia-induced oxidative damage to mitochondria by activating SIRT1 in rat mesangial cells. Toxicol Appl Pharmacol. 2012;259(3):395–401.
   PubMed Web of Science ®Google Scholar
• Schmatz R, Perreira LB, Stefanello N, et al. Effects of resveratrol on biomarkers of oxidative stress and on the activity of delta aminolevulinic acid dehydratase in liver and kidney of streptozotocin-induced diabetic rats. Biochimie. 2012;94(2):374–383.
   PubMed Web of Science ®Google Scholar
• Chen KH, Hung CC, Hsu HH, et al. Resveratrol ameliorates early diabetic nephropathy associated with suppression of augmented TGF-β/Smad and ERK1/2 signaling in streptozotocin-induced diabetic rats. Chem Biol Interact. 2011;190(1):45–53.
   PubMed Web of Science ®Google Scholar
• Cao D, Wang M, Qiu X, et al. Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol. Genes Dev. 2015;29(12):1316–1325.
   PubMed Web of Science ®Google Scholar
• Popat R, Plesner T, Davies F, et al. A phase 2 study of SRT501 (resveratrol) with bortezomib for patients with relapsed and or refractory multiple myeloma. Br J Haematol. 2013;160(5):714–717.
   PubMed Web of Science ®Google Scholar
• Piotrowska H, Kucinska M, Murias M. Biological activity of piceatannol: leaving the shadow of resveratrol. Mutat Res. 2012;750(1):60–82.
   PubMed Web of Science ®Google Scholar
• Khan K, Najmi AK, Akhtar M. A natural phenolic compound quercetin showed the usefulness by targeting inflammatory, oxidative stress markers and augment 5-HT levels in one of the animal models of depression in mice. Drug Res. 2019;69(7):392–400.
   Web of Science ®Google Scholar
• Oza MJ, Kulkarni YA. Biochanin A improves insulin sensitivity and controls hyperglycemia in type 2 diabetes. Biomed Pharmacother. 2018;107:1119–1127.
   PubMed Web of Science ®Google Scholar
• Zhuang K, Jiang X, Liu R, et al. Formononetin activates the Nrf2/ARE signaling pathway via Sirt1 to improve diabetic renal fibrosis. Front Pharmacol. 2020;11:616378.
   PubMed Web of Science ®Google Scholar
• Oza MJ, Kulkarni YA. Formononetin ameliorates diabetic neuropathy by increasing expression of SIRT1 and NGF. Chem Biodivers. 2020;17(6):e2000162.
   PubMed Web of Science ®Google Scholar
• Oza M, Kulkarni Y. Formononetin alleviates diabetic cardiomyopathy by inhibiting oxidative stress and upregulating SIRT1 in rats. Asian Pac J Trop Biomed. 2020;10(6):254.
   Web of Science ®Google Scholar
• Dihingia A, Ozah D, Ghosh S, et al. Vitamin K1 inversely correlates with glycemia and insulin resistance in patients with type 2 diabetes (T2D) and positively regulates SIRT1/AMPK pathway of glucose metabolism in liver of T2D mice and hepatocytes cultured in high glucose. J Nutr Biochem. 2018;52:103–114.
   PubMed Web of Science ®Google Scholar
• Yerra VG, Kalvala AK, Kumar A. Isoliquiritigenin reduces oxidative damage and alleviates mitochondrial impairment by SIRT1 activation in experimental diabetic neuropathy. J Nutr Biochem. 2017;47:41–52.
   PubMed Web of Science ®Google Scholar
• Ma B, Zhu Z, Zhang J, et al. Aucubin alleviates diabetic nephropathy by inhibiting NF-κB activation and inducing SIRT1/SIRT3-FOXO3a signaling pathway in high-fat diet/streptozotocin-induced diabetic mice. J Funct Foods. 2020;64:103702.
   Web of Science ®Google Scholar
• Kadowaki T, Yamauchi T, Kubota N, et al. Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome. J Clin Invest. 2006;116(7):1784–1792.
   PubMed Web of Science ®Google Scholar
• Pillai VB, Kanwal A, Fang YH, et al. Honokiol, an activator of sirtuin-3 (SIRT3) preserves mitochondria and protects the heart from doxorubicin-induced cardiomyopathy in mice. Oncotarget. 2017;8(21):34082–34098.
   PubMedGoogle Scholar
• Dong J, Zhang X, Zhang L, et al. Quercetin reduces obesity-associated ATM infiltration and inflammation in mice: a mechanism including AMPKα1/SIRT1. J Lipid Res. 2014;55(3):363–374.
   PubMed Web of Science ®Google Scholar
• Smoliga J, Blanchard O. Enhancing the delivery of resveratrol in humans: if low bioavailability is the problem, what is the solution? Molecules. 2014;19(11):17154–17172.
   PubMed Web of Science ®Google Scholar
• Zhang LX, Li CX, Kakar MU, et al. Resveratrol (RV): a pharmacological review and call for further research. Biomed Pharmacother. 2021;143:112164.
   PubMed Web of Science ®Google Scholar
• Jimenez-Gomez Y, Mattison JA, Pearson KJ, et al. Resveratrol improves adipose insulin signaling and reduces the inflammatory response in adipose tissue of rhesus monkeys on high-fat, high-sugar diet. Cell Metab. 2013;18(4):533–545.
   PubMed Web of Science ®Google Scholar
• Zheng X, Zhu S, Chang S, et al. Protective effects of chronic resveratrol treatment on vascular inflammatory injury in streptozotocin-induced type 2 diabetic rats: role of NF-kappa B signaling. Eur J Pharmacol. 2013;720(1–3):147–157.
   PubMed Web of Science ®Google Scholar
• Cheng AS, Cheng YH, Chang TL. Resveratrol protects RINm5F pancreatic cells from methylglyoxal-induced apoptosis. J Funct Foods. 2013;5(4):1774–1783.
   Web of Science ®Google Scholar
• Yücel Ç, Karatoprak GŞ, Aktaş Y. Nanoliposomal resveratrol as a novel approach to treatment of diabetes mellitus. J Nanosci Nanotechnol. 2018;18(6):3856–3864.
   PubMed Web of Science ®Google Scholar
• Mohseni R, ArabSadeghabadi Z, Ziamajidi N, et al. Oral administration of resveratrol-loaded solid lipid nanoparticle improves insulin resistance through targeting expression of SNARE proteins in adipose and muscle tissue in rats with type 2 diabetes. Nanoscale Res Lett. 2019;14(1):227.
   PubMedGoogle Scholar
• Bhatt JK, Thomas S, Nanjan MJ. Resveratrol supplementation improves glycemic control in type 2 diabetes mellitus. Nutr Res. 2012;32(7):537–541.
   PubMed Web of Science ®Google Scholar
• Movahed A, Nabipour I, Lieben Louis X, et al. Antihyperglycemic effects of short term resveratrol supplementation in type 2 diabetic patients. Evid Based Complement Alternat Med. 2013;2013:851267.
   PubMed Web of Science ®Google Scholar
• Brasnyó P, Molnár GA, Mohás M, et al. Resveratrol improves insulin sensitivity, reduces oxidative stress and activates the Akt pathway in type 2 diabetic patients. Br J Nutr. 2011;106(3):383–389.
   PubMed Web of Science ®Google Scholar