CoChat
Sign Up
Cited by 28

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Sirtuins, a key regulator of ageing and age-related neurodegenerative diseases

Bhatt, Vidhi, Tiwari, Anand Krishna·2023·International Journal of Neuroscience
DOI 10.1080/00207454.2022.2057849
Open this paper in CoChat — free account

Abstract

Sirtuins are Nicotinamide Adenine Dinucleotide (NAD + ) dependent class ІΙΙ histone deacetylases enzymes (HDACs) present from lower to higher organisms such as bacteria ( Sulfolobus solfataricus L. major), yeasts ( Saccharomyces cerevisiae ), nematodes ( Caenorhabditis elegans ), fruit flies ( Drosophila melanogaster ), humans ( Homo sapiens sapiens ), even in plants such as rice ( Oryza sativa ), thale cress ( Arabidopsis thaliana ), vine ( Vitis vinifera L.) tomato ( Solanum lycopersicum ). Sirtuins play an important role in the regulation of various vital cellular functions during metabolism and ageing. It also plays a neuroprotective role by modulating several biological pathways such as apoptosis, DNA repair, protein aggregation, and inflammatory processes associated with ageing and neurodegenerative diseases. In this review, we have presented an updated Sirtuins and its role in ageing and age-related neurodegenerative diseases (NDDs). Further, this review also describes the therapeutic potential of Sirtuins and the use of Sirtuins inhibitor/activator for altering the NDDs disease pathology.

Overview

Integrity signals

Registry

Crossref · 10.1080/00207454.2022.2057849

Cites

34 of 34 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Flagged first, then by citations

Show all 34 references

Research works printed but not linked: 278

  1. Anekonda TS, Reddy PH. Neuronal protection by sirtuins in Alzheimer’s disease. J Neurochem. 2006;96(2):305–313. · DOI
  2. Donmez G, Guarente L. Aging and disease: connections to sirtuins. Aging Cell. 2010;9(2):285–290. · DOI
  3. Donmez G, Outeiro TF. SIRT1 and SIRT2: emerging targets in neurodegeneration. EMBO Mol Med. 2013;5(3):344–352. · DOI
  4. Dong Y, Zou S. Sirtuins and aging. In Epigenetics of aging. New York, NY: Springer; 2010:51–75. · DOI
  5. Longo VD, Kennedy BK. Sirtuins in aging and age-related disease. Cell. 2006;126(2):257–268. · DOI · Paper page
  6. Mahlknecht U, Voelter-Mahlknecht S. Chromosomal characterization and localization of the NAD+-dependent histone deacetylase gene sirtuin 1 in the mouse. Int J Mol Med. 2009;23(2):245–252.
  7. Potente M, Ghaeni L, Baldessari D, et al. SIRT1 controls endothelial angiogenic functions during vascular growth. Genes Dev. 2007;21(20):2644–2658. · DOI · Paper page
  8. Voelter-Mahlknecht S, Mahlknecht U. Cloning, chromosomal characterization and mapping of the NAD-dependent histone deacetylases gene sirtuin 1. Int J Mol Med. 2006;17(1):59–67.
  9. Li H, Wang R. Blocking SIRT1 inhibits cell proliferation and promotes aging through the PI3K/AKT pathway. Life Sci. 2017;190:84–90. · DOI
  10. Li W, Zhang B,Tang J, et al. Sirtuin 2, a mammalian homolog of yeast silent information regulator-2 longevity regulator, is an oligodendroglial protein that decelerates cell differentiation through deacetylating α-tubulin. J Neurosci. 2007;27(10):2606–2616. · DOI
  11. Liu X, Wei W, Zhu W, et al. Histone deacetylase AtSRT1 links metabolic flux and stress response in Arabidopsis. Mol Plant. 2017;10(12):1510–1522. · DOI
  12. Donmez G, Arun A, Chung C-Y, et al. SIRT1 protects against α-synuclein aggregation by activating molecular chaperones. J Neurosci. 2012;32(1):124–132. · DOI
  13. Horio Y, Hayashi T, Kuno A, et al. Cellular and molecular effects of sirtuins in health and disease. Clin Sci (Lond). 2011;121(5):191–203. · DOI
  14. Lalla R, Donmez G. The role of sirtuins in Alzheimer’s disease. Front Aging Neurosci. 2013;5:16. · DOI
  15. Szućko I. Sirtuins: not only animal proteins. Acta Physiologiae Plantarum. 2016;38(10):237. · DOI
  16. Karagiannis TC, Ververis K. Potential of chromatin modifying compounds for the treatment of Alzheimer’s disease. Pathobiol Aging Age Relat Dis. 2012;2(1):14980. · DOI
  17. Michan S, Sinclair D. Sirtuins in mammals: insights into their biological function. Biochem J. 2007;404(1):1–13. · DOI
  18. Vassilopoulos A, Fritz K, Petersen D, et al. The human sirtuin family: evolutionary divergences and functions. Hum Genomics. 2011;5(5):485–496. · DOI
  19. Frye RA. 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. 1999;260(1):273–279. · DOI
  20. Lombard D, Alt F, Cheng H-L, et al. Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol Cell Biol. 2007;27(24):8807–8814. · DOI · Paper page
  21. Wang H, Li J, Huang R, et al. SIRT4 and SIRT6 serve as novel prognostic biomarkers with competitive functions in serous ovarian cancer. Front Genet. 2021;2021:1208.
  22. Jiao F, Gong Z. The beneficial roles of SIRT1 in neuroinflammation-related diseases. Oxid Med Cell Longevity. 2020;2020:6782872. · DOI
  23. Donmez G. The neurobiology of sirtuins and their role in neurodegeneration. Trends Pharmacol Sci. 2012;33(9):494–501. · DOI
  24. Shoba B, Lwin ZM, Ling LS, et al. Function of sirtuins in biological tissues. Anat Record. 2009;292(4):536–543. · DOI
  25. North BJ, Verdin E. Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol. 2004;5(5):224. · DOI
  26. Tang BL. Sirtuins as modifiers of Parkinson’s disease pathology. J Neurosci Res. 2017;95(4):930–942. · DOI
  27. Jęśko H, Wencel P, Strosznajder R, et al. Sirtuins and their roles in brain aging and neurodegenerative disorders. Neurochem Res. 2017;42(3):876–890. · DOI
  28. Moynihan K, Grimm A, Plueger M, et al . Increased dosage of mammalian Sir2 in pancreatic beta cells enhances glucose-stimulated insulin secretion in mice. Cell Metab. 2005;2(2):105–117. · DOI
  29. Stünkel W, Peh BK, Tan YC, et al. Function of the SIRT1 protein deacetylase in cancer. Biotechnol J. 2007;2(11):1360–1368. · DOI
  30. Jin Q, Yan T, Ge X, et al. Cytoplasm-localized SIRT1 enhances apoptosis. J Cell Physiol. 2007;213(1):88–97. · DOI
  31. Yanagisawa S, Baker J, Vuppusetty C, et al. The dynamic shuttling of SIRT1 between cytoplasm and nuclei in bronchial epithelial cells by single and repeated cigarette smoke exposure. PLoS One. 2018;13(3):e0193921. · DOI
  32. Outeiro TF, Kontopoulos E, Altmann S, et al . Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson’s disease. Science. 2007;317(5837):516–519. · DOI
  33. Motta MC, Divecha N, Lemieux M, et al. Mammalian SIRT1 represses forkhead transcription factors. Cell. 2004;116(4):551–563. · DOI
  34. Picard F, Kurtev M, Chung N, et al . Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. Nature. 2004;429(6993):771–776. · DOI
  35. Rodgers J, Lerin C, Haas W, et al . Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature. 2005;434(7029):113–118. · DOI · Paper page
  36. Li K, Casta A, Wang R, et al. Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation. J Biol Chem. 2008;283(12):7590–7598. · DOI
  37. North B, Marshall B, Borra M, et al. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell. 2003;11(2):437–444. · DOI
  38. Vergnes B, Vanhille L, Ouaissi A, et al. Stage-specific antileishmanial activity of an inhibitor of SIR2 histone deacetylase. Acta Trop. 2005;94(2):107–115. · DOI
  39. Inoue T, Hiratsuka M, Osaki M, et al. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress. Oncogene. 2007;26(7):945–957. · DOI
  40. Pillai VB, Sundaresan NR, Gupta MP. Regulation of Akt signaling by sirtuins: its implication in cardiac hypertrophy and aging. Circ Res. 2014;114(2):368–378. · DOI
  41. de Oliveira RM, Vicente Miranda H, Francelle L, et al . The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease. PLoS Biol. 2017;15(3):e2000374. · DOI
  42. Machado De Oliveira R, Sarkander J, Kazantsev AG, et al. SIRT2 as a therapeutic target for age-related disorders. Front Pharmacol. 2012;3:82.
  43. Wei W, Xu X, Li H, et al. The SIRT2 polymorphism rs10410544 and risk of Alzheimer’s disease: a meta-analysis. Neuromolecular Med. 2014;16(2):448–456. · DOI
  44. North BJ, Verdin E. Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis. PLoS One. 2007;2(8):e784. · DOI
  45. Ahn B-H, Kim H-S, Song S, et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci USA. 2008;105(38):14447–14452. · DOI · Paper page
  46. Ansari A, Rahman MS, Saha S, et al . Function of the SIRT3 mitochondrial deacetylase in cellular physiology, cancer, and neurodegenerative disease. Aging Cell. 2017;16(1):4–16. · DOI
  47. Samant S, Zhang H, Hong Z, et al. SIRT3 deacetylates and activates OPA1 to regulate mitochondrial dynamics during stress. Mol Cell Biol. 2014;34(5):807–819. · DOI · Paper page
  48. Papa L, Germain D. Correction for papa and germain,“SirT3 regulates a novel arm of the mitochondrial unfolded protein response”. Mol Cell Biol. 2017;37(13):e00191-17. · DOI
  49. Zhang H, Lu Y, Zhao Y, et al. OsSRT1 is involved in rice seed development through regulation of starch metabolism gene expression. Plant Sci. 2016;248:28–36. · DOI
  50. Pannek M, Simic Z, Fuszard M, et al. Crystal structures of the mitochondrial deacylase Sirtuin 4 reveal isoform-specific acyl recognition and regulation features. Nat Commun. 2017;8(1):1513. · DOI
  51. Wood JG, Schwer B, Wickremesinghe PC, et al. Sirt4 is a mitochondrial regulator of metabolism and lifespan in Drosophila melanogaster. Proc Natl Acad Sci USA. 2018;115(7):1564–1569. · DOI
  52. Tomaselli D, Steegborn C, Mai A, et al. Sirt4: a multifaceted enzyme at the crossroads of mitochondrial metabolism and cancer. Front Oncol. 2020;10:474. · DOI
  53. Herskovits AZ, Guarente L. Sirtuin deacetylases in neurodegenerative diseases of aging. Cell Res. 2013;23(6):746. · DOI
  54. Huang G, Cheng J, Yu F, et al. Clinical and therapeutic significance of sirtuin-4 expression in colorectal cancer. Oncol Rep. 2016;35(5):2801–2810. · DOI
  55. Min S-W, Sohn PD, Li Y, et al. SIRT1 deacetylates tau and reduces pathogenic tau spread in a mouse model of tauopathy. J Neurosci. 2018;38(15):3680–3688. · DOI
  56. Schirmer H, Pereira TCB, Rico EP, et al . Modulatory effect of resveratrol on SIRT1, SIRT3, SIRT4, PGC1α and NAMPT gene expression profiles in wild-type adult zebrafish type adult zebrafish liver. Mol Biol Rep. 2012;39(3):3281–3289. · DOI
  57. Schlicker C, Gertz M, Papatheodorou P, et al. Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol. 2008;382(3):790–801. · DOI · Paper page
  58. Matsushita N, Yonashiro R, Ogata Y, et al. Distinct regulation of mitochondrial localization and stability of two human Sirt5 isoforms. Genes Cells. 2011;16(2):190–202. · DOI · Paper page
  59. Jia G, Su L, Singhal S, et al. Emerging roles of SIRT6 on telomere maintenance, DNA repair, metabolism and mammalian aging. Mol Cell Biochem. 2012;364(1-2):345–350. · DOI
  60. Outeiro TF, Marques O, Kazantsev A. Therapeutic role of sirtuins in neurodegenerative disease. Biochim Biophys Acta. 2008;1782(6):363–369. · DOI
  61. Kugel S, Mostoslavsky R. Chromatin and beyond: the multitasking roles for SIRT6. Trends Biochem Sci. 2014;39(2):72–81. · DOI
  62. Li X, Liu L, Li T, et al. SIRT6 in senescence and aging-related cardiovascular diseases. Front Cell Dev Biol. 2021;9:739.
  63. Gallagher EJ, LeRoith D. Obesity and diabetes: the increased risk of cancer and cancer-related mortality. Physiol Rev. 2015;95(3):727–748. · DOI · Paper page
  64. Larsen MO, Rolin B. Use of the Göttingen minipig as a model of diabetes, with special focus on type 1 diabetes research. ILAR J. 2004;45(3):303–313. · DOI
  65. Michishita E, McCord R, Boxer L, et al. Cell cycle-dependent deacetylation of telomeric histone H3 lysine K56 by human SIRT6. Cell Cycle. 2009;8(16):2664–2666. · DOI
  66. Haigis M, Mostoslavsky R, Haigis K, et al . SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell. 2006;126(5):941–954. · DOI · Paper page
  67. Tang M, Tang H, Tu B, et al. SIRT7: a sentinel of genome stability. Open Biol. 2021;11(6):210047. · DOI
  68. Axsom JE, Schmidt HD, Matura LA, et al. The influence of epigenetic modifications on metabolic changes in white adipose tissue and liver and their potential impact in exercise. Front Physiol. 2021;12:686270. · DOI
  69. Bendixen E, Danielsen M, Larsen K, et al . Advances in porcine genomics and proteomics—a toolbox for developing the pig as a model organism for molecular biomedical research. Brief Funct Genomics. 2010;9(3):208–219. · DOI
  70. Bellinger DA, Merricks EP, Nichols TC. Swine models of type 2 diabetes mellitus: insulin resistance, glucose tolerance, and cardiovascular complications. ILAR J. 2006;47(3):243–258. · DOI
  71. Bai P, Cantó C, Oudart H, et al. PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation. Cell Metab. 2011;13(4):461–468. · DOI · Paper page
  72. Gabisonia K, Prosdocimo G, Aquaro GD, et al. MicroRNA therapy stimulates uncontrolled cardiac repair after myocardial infarction in pigs. Nature. 2019;569(7756):418–422. · DOI · Paper page
  73. Almond GW. Research applications using pigs. Vet Clin North Am Food Anim Pract. 1996;12(3):707–716. · DOI
  74. Bai L, Pang W-J, Yang Y-J, et al. Modulation of Sirt1 by resveratrol and nicotinamide alters proliferation and differentiation of pig preadipocytes. Mol Cell Biochem. 2008;307(1-2):129–140.
  75. Vodička P, Smetana K Jr, Dvoránková B, et al. The miniature pig as an animal model in biomedical research. Ann NY Acad Sci. 2005;1049(1):161–171. · DOI
  76. Ghinis-Hozumi Y, Antaramian A, Villarroya F, et al. Potential role of sirtuins in livestock production. Animal. 2013;7(1):101–108. · DOI
  77. Ren Y, Shan TZ, Zhu LN, et al. Effect of breed on the expression of Sirtuins (Sirt1-7) and antioxidant capacity in porcine brain. Animal. 2013;7(12):1994–1998. · DOI
  78. Shan T, Wang Y, Wu T, et al. Porcine sirtuin 1 gene clone, expression pattern, and regulation by resveratrol. J Anim Sci. 2009;87(3):895–904. · DOI
  79. Ma R, Zhang Y, Zhang L, et al. Sirt1 protects pig oocyte against in vitro aging. Anim Sci J. 2015;86(9):826–832. · DOI
  80. Luo H, Zhou M, Ji K, et al. Expression of sirtuins in the retinal neurons of mice, rats, and humans. Front Aging Neurosci. 2017;9:366. · DOI
  81. Nakamura Y, Ogura M, Tanaka D, et al. Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5. Biochem Biophys Res Commun. 2008;366(1):174–179. · DOI
  82. Wang C, Dawes L, Liu Y, et al. Dexamethasone influences FGF-induced responses in lens epithelial explants and promotes the posterior capsule coverage that is a feature of glucocorticoid-induced cataract. Exp Eye Res. 2013;111:79–87. · DOI
  83. Peng C-H, Chang YL, Kao CL, et al. SirT1—a sensor for monitoring self-renewal and aging process in retinal stem cells. Sensors. 2010;10(6):6172–6194. · DOI
  84. Sasaki M, Yuki K, Kurihara T, et al. Biological role of lutein in the light-induced retinal degeneration. J Nutr Biochem. 2012;23(5):423–429. · DOI
  85. Osborne B, Bentley N, Montgomery M, et al. The role of mitochondrial sirtuins in health and disease. Free Radic Biol Med. 2016;100:164–174. · DOI
  86. Silberman DM, Ross K, Sande PH, et al. SIRT6 is required for normal retinal function. PLoS One. 2014;9(6):e98831. · DOI
  87. Kim H-S, Xiao C, Wang R-H, 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. · DOI
  88. Nimmagadda V, Bever C, Vattikunta N, et al. Overexpression of SIRT1 protein in neurons protects against experimental autoimmune encephalomyelitis through activation of multiple SIRT1 targets. J Immunol. 2013;190(9):4595–4607. · DOI
  89. Liu Q, Zhu D, Jiang P, et al. Resveratrol synergizes with low doses of L-DOPA to improve MPTP-induced Parkinson disease in mice. Behav Brain Res. 2019;367:10–18. · DOI
  90. Pallos J, Bodai L, Lukacsovich T, et al. Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington’s disease. Human Mol Genet. 2008;17(23):3767–3775. · DOI
  91. Pichler F, Laurenson S, Williams L, et al. Chemical discovery and global gene expression analysis in zebrafish. Nat Biotechnol. 2003;21(8):879–883. · DOI
  92. Barbazuk WB, Korf I, Kadavi C, et al. The syntenic relationship of the zebrafish and human genomes. Genome Res. 2000;10(9):1351–1358. · DOI
  93. Pereira TCB, Rico EP, Rosemberg DB, et al. Zebrafish as a model organism to evaluate drugs potentially able to modulate sirtuin expression. Zebrafish. 2011;8(1):9–16. · DOI
  94. Do Hee Kim IHJ, Kim DH, Park SW. Knockout of longevity gene Sirt1 in zebrafish leads to oxidative injury, chronic inflammation, and reduced life span. PLoS One. 2019;14(8):e0220581. · DOI
  95. Rahman M, Nirala N, Singh A, et al. Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity. J Cell Biol. 2014;206(2):289–305. · DOI · Paper page
  96. Rosenberg MI, Parkhurst SM . Drosophila Sir2 is required for heterochromatic silencing and by euchromatic Hairy/E(Spl) bHLH repressors in segmentation and sex determination. Cell. 2002;109(4):447–458. · DOI
  97. Frankel S, Ziafazeli T, Rogina B. dSir2 and longevity in Drosophila. Exp Gerontol. 2011;46(5):391–396. · DOI
  98. Tanny JC, Moazed D. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product Proc Natl Acad Sci USA. 2001;98(2):415–420. · DOI
  99. Banerjee KK, Ayyub C, Ali SZ, et al. dSir2 in the adult fat body, but not in muscles, regulates life span in a diet-dependent manner. Cell Rep. 2012;2(6):1485–1491. · DOI
  100. Griswold AJ, Chang KT, Runko AP, et al. Sir2 mediates apoptosis through JNK-dependent pathways in Drosophila. Proc Natl Acad Sci USA. 2008;105(25):8673–8678. · DOI
  101. Åström SU, Cline TW, Rine J. The Drosophila melanogaster sir2+ gene is nonessential and has only minor effects on position-effect variegation. Genetics. 2003;163(3):931–937. · DOI
  102. Feller C, Forné I, Imhof A, et al. Global and specific responses of the histone acetylome to systematic perturbation. Mol Cell. 2015;57(3):559–571. · DOI
  103. Taylor J, Wood J,Chang C, et al. Regulation of lifespan by dsirt6 in DROSOPHILA MELANOGASTER. Innovat Aging. 2018;2(Suppl 1):90. · DOI
  104. Wierman MB, Smith JS. Yeast sirtuins and the regulation of aging. FEMS Yeast Res. 2014;14(1):73–88. · DOI
  105. Derbyshire MK, Weinstock KG, Strathern JN. HST1, a new member of the SIR2 family of genes. Yeast. 1996;12(7):631–640. · DOI
  106. Brachmann CB, Sherman JM, Devine SE, et al. The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev. 1995;9(23):2888–2902. · DOI
  107. Imai S, Armstrong CM, Kaeberlein M, et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. 2000;403(6771):795–800. · DOI · Paper page
  108. Viswanathan M, Tissenbaum HA. C. elegans sirtuins. In Sirtuins. New York, NY: Springer; 2013:39–56. · DOI
  109. Cantó C, Houtkooper RH. Sirtuins and aging. In Sirtuins. New York, NY: Springer; 2016:213–227. · DOI
  110. Chang SM, McReynolds MR, Hanna-Rose W. Mitochondrial sirtuins sir-2.2 and sir-2.3 regulate lifespan in C. elegans. bioRxiv. 2017;2017:181727.
  111. Dang W. The controversial world of sirtuins. Drug Discovery Today Technol. 2014;12:e9–e17. · DOI
  112. Zheng W. The plant sirtuins. Plant Sci. 2020;2020:110434. · DOI
  113. Zhang H, Zhao Y, Zhou D-X. Rice NAD+-dependent histone deacetylase OsSRT1 represses glycolysis and regulates the moonlighting function of GAPDH as a transcriptional activator of glycolytic genes. Nucleic Acids Res. 2017;45(21):12241–12255. · DOI
  114. Chung PJ, Kim YS, Park S-H, et al. Subcellular localization of rice histone deacetylases in organelles. FEBS Lett. 2009;583(13):2249–2254. · DOI
  115. Lu Y, Xu Q, Liu Y, et al. Dynamics and functional interplay of histone lysine butyrylation, crotonylation, and acetylation in rice under starvation and submergence. Genome Biol. 2018;19(1):1–14.
  116. Chen Z, Luo L, Chen R, et al. Acetylome profiling reveals extensive lysine acetylation of the fatty acid metabolism pathway in the diatom Phaeodactylum tricornutum. Mol Cell Proteomics. 2018;17(3):399–412. · DOI
  117. Yang C, Shen W, Chen H, et al. Characterization and subcellular localization of histone deacetylases and their roles in response to abiotic stresses in soybean. BMC Plant Biol. 2018;18(1):1–13. · DOI
  118. Cucurachi M, Busconi M, Morreale G, et al. Characterization and differential expression analysis of complete coding sequences of Vitis vinifera L. sirtuin genes. Plant Physiol Biochem. 2012;54:123–132. · DOI
  119. Zhao L, Lu J, Zhang J, et al. Identification and characterization of histone deacetylases in tomato (Solanum lycopersicum). Front Plant Sci. 2014;5:760.
  120. Ho Y-S, So K-F, Chang RC-C. Anti-aging herbal medicine—how and why can they be used in aging-associated neurodegenerative diseases? Ageing Res Rev. 2010;9(3):354–362. · DOI
  121. Albers DS, Beal MF. Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative disease. In Advances in dementia research. New York, NY: Springer; 2000. p. 133–154. · DOI
  122. Braidy N, Poljak A, Grant R, et al. Differential expression of sirtuins in the aging rat brain. Front Cell Neurosci. 2015;9:167. · DOI
  123. Pallàs M, Verdaguer E, Tajes M, et al. Modulation of sirtuins: new targets for antiageing. Recent Pat CNS Drug Discov. 2008;3(1):61–69. · DOI
  124. Schwer B, Bunkenborg J, Verdin RO, et al. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci USA. 2006;103(27):10224–10229. · DOI · Paper page
  125. Smith BC, Denu JM. Sirtuins caught in the act. Structure. 2006;14(8):1207–1208. · DOI
  126. Kennedy BK, Austriaco Jr NR, Zhang J, et al. Mutation in the silencing gene S/R4 can delay aging in S. cerevisiae. Cell. 1995;80(3):485–496. · DOI
  127. Poulose N, Raju R. Sirtuin regulation in aging and injury. Biochim Biophys Acta. 2015;1852(11):2442–2455. · DOI · Paper page
  128. Sacks FM. The crucial roles of apolipoproteins E and C-III in apoB lipoprotein metabolism in normolipidemia and hypertriglyceridemia. Curr Opin Lipidol. 2015;26(1):56–63. · DOI · Paper page
  129. Kaeberlein M, McVey M, Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 1999;13(19):2570–2580. · DOI · Paper page
  130. Lin S-J, Defossez P-A, Guarente L. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science. 2000;289(5487):2126–2128. · DOI · Paper page
  131. Lin K, Hsin H, Libina N, et al. Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling. Nat Genet. 2001;28(2):139–145. · DOI
  132. Baohua Y, Li L. Effects of SIRT6 silencing on collagen metabolism in human dermal fibroblasts. Cell Biol Int. 2012;36(1):105–108. · DOI
  133. Wang Q-L, Guo S-J. Sirtuins function as the modulators in aging-related diseases in common or respectively. Chin Med J (Engl). 2015;128(12):1671–1678. · DOI
  134. Finley LW, Haigis MC. Metabolic regulation by SIRT3: implications for tumorigenesis. Trends Mol Med. 2012;18(9):516–523. · DOI
  135. Giralt A, Villarroya F. SIRT3, a pivotal actor in mitochondrial functions: metabolism, cell death and aging. Biochem J. 2012;444(1):1–10. · DOI
  136. Werner CT, Williams CJ, Fermelia MR, et al. Circuit mechanisms of neurodegenerative diseases: a new frontier with miniature fluorescence microscopy. Front Neurosci. 2019;13:1174. · DOI
  137. Sheikh S, Haque E, Mir SS. Neurodegenerative diseases: multifactorial conformational diseases and their therapeutic interventions. J Neurodegener Dis. 2013;2013:563481.
  138. Wood LB, Winslow AR, Strasser SD. Systems biology of neurodegenerative diseases. Integr Biol (Camb). 2015;7(7):758–775. · DOI
  139. Beal MF, Lang AE, Ludolph AC. Neurodegenerative diseases: neurobiology, pathogenesis and therapeutics. Cambridge, UK: Cambridge University Press; 2005. · DOI
  140. Hirth F. Drosophila melanogaster in the study of human neurodegeneration. CNS Neurol Disord Drug Target. 2010;9(4):504–523. · DOI
  141. Hung C-W, Chen Y-C, Hsieh W-L, et al. Ageing and neurodegenerative diseases. Ageing Res Rev. 2010;9:S36–S46. · DOI
  142. Guo J, Cheng J, North BJ, et al. Functional analyses of major cancer-related signaling pathways in Alzheimer’s disease etiology. Biochim Biophys Acta. 2017;1868(2):341–358.
  143. Hippius H, Neundörfer G. The discovery of Alzheimer’s disease. Dialogues Clin Neurosci. 2003;5(1):101–108. · DOI
  144. Hoekstra JG, Montine KS, Zhang J, et al. Mitochondrial therapeutics in Alzheimer’s disease and Parkinson’s disease. Alzheimers Res Therapy. 2011;3(3):21. · DOI
  145. O’Brien RJ, Wong PC. Amyloid precursor protein processing and Alzheimer’s disease. Annu Rev Neurosci. 2011;34:185–204. · DOI · Paper page
  146. Galasko DR, Shaw LM. Alzheimer disease: CSF biomarkers for Alzheimer disease—approaching consensus. Nat Rev Neurol. 2017;13(3):131. · DOI
  147. Biella G, Fusco F, Nardo E, et al . Sirtuin 2 inhibition improves cognitive performance and acts on amyloid-β protein precursor processing in two Alzheimer’s disease mouse models. J Alzheimers Dis. 2016;53(3):1193–1207. · DOI
  148. Jeibmann A, Paulus W. Drosophila melanogaster as a model organism of brain diseases. Int J Mol Sci. 2009;10(2):407–440. · DOI
  149. Rajasekhar K, Chakrabarti M, Govindaraju T. Function and toxicity of amyloid beta and recent therapeutic interventions targeting amyloid beta in Alzheimer’s disease. Chem Commun (Camb). 2015;51(70):13434–13450. · DOI
  150. Yin J, Han P, Song M, et al. Amyloid-β increases tau by mediating sirtuin 3 in Alzheimer’s disease. Mol Neurobiol. 2018;55:8592–8601. · DOI
  151. Manjula R, Anuja K, Alcain FJ. SIRT1 and SIRT2 activity control in neurodegenerative diseases. Front Pharmacol. 2021;11:1899. · DOI
  152. Bonda D, Lee H-G, Camins A, et al. The sirtuin pathway in ageing and Alzheimer disease: mechanistic and therapeutic considerations. Lancet Neurol. 2011;10(3):275–279. · DOI
  153. Sundaresan N, Pillai V, Wolfgeher D, et al. The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy. Sci Signal. 2011;4(182):ra46–ra46. · DOI
  154. Yang W, Zou Y, Zhang M, et al. Mitochondrial Sirt3 expression is decreased in APP/PS1 double transgenic mouse model of Alzheimer’s disease. Neurochem Res. 2015;40(8):1576–1582. · DOI
  155. Motyl J, Wencel PL, Cieślik M, et al. Alpha-synuclein alters differently gene expression of Sirts, PARPs and other stress response proteins: implications for neurodegenerative disorders. Mol Neurobiol. 2018;55(1):727–740. · DOI
  156. Salvatori I, Valle C, Ferri A, et al. SIRT3 and mitochondrial metabolism in neurodegenerative diseases. Neurochem Int. 2017;109:184–192. · DOI
  157. Mattson MP, Magnus T. Ageing and neuronal vulnerability. Nat Rev Neurosci. 2006;7(4):278–294. · DOI · Paper page
  158. Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature. 2006;443(7113):787–795. · DOI · Paper page
  159. Mäkelä J, Tselykh T, Kukkonen J, et al. Peroxisome proliferator-activated receptor-γ (PPARγ) agonist is neuroprotective and stimulates PGC-1α expression and CREB phosphorylation in human dopaminergic neurons. Neuropharmacology. 2016;102:266–275. · DOI
  160. Rugarli EI, Langer T. Mitochondrial quality control: a matter of life and death for neurons. EMBO J. 2012;31(6):1336–1349. · DOI
  161. Henchcliffe C, Beal MF. Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis. Nat Clin Pract Neurol. 2008;4(11):600–609. · DOI
  162. Hasegawa K, Yasuda T, Shiraishi C, et al. Promotion of mitochondrial biogenesis by necdin protects neurons against mitochondrial insults. Nat Commun. 2016;7(1):1–15. · DOI
  163. Eschbach J, von Einem B, Müller K, et al . Mutual exacerbation of peroxisome proliferator-activated receptor γ coactivator 1α deregulation and α-synuclein oligomerization. Ann Neurol. 2015;77(1):15–32. · DOI
  164. Khanna A, Acharjee P, Acharjee A, et al. Mitochondrial SIRT3 and neurodegenerative brain disorders. J Chem Neuroanat. 2017;95:43–53.
  165. Signorile A, Santeramo A, Tamma G, et al. Mitochondrial cAMP prevents apoptosis modulating Sirt3 protein level and OPA1 processing in cardiac myoblast cells. Biochim Biophys Acta. 2017;1864(2):355–366. · DOI
  166. Duan W. Targeting sirtuin-1 in Huntington’s disease: rationale and current status. CNS Drugs. 2013;27(5):345–352. · DOI
  167. Proenca CC, Stoehr N, Bernhard M, et al. Atg4b-dependent autophagic flux alleviates Huntington’s disease progression. PLoS One. 2013;8(7):e68357. · DOI
  168. Schulte J, Littleton JT. The biological function of the Huntingtin protein and its relevance to Huntington’s disease pathology. Curr Trends Neurol. 2011;5:65.
  169. Quarrell OW, Rigby AJ, Barron L, et al. Reduced penetrance alleles for Huntington’s disease: a multi-centre direct observational study. J Med Genet. 2007;44(3):e68–e68. · DOI
  170. Imarisio S, Carmichael J, Korolchuk V, et al. Huntington’s disease: from pathology and genetics to potential therapies. Biochem J. 2008;412(2):191–209. · DOI · Paper page
  171. Cui L, Jeong H, Borovecki F, et al . Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration. Cell. 2006;127(1):59–69. · DOI · Paper page
  172. Weydt P, Pineda VV, Torrence AE, et al. Thermoregulatory and metabolic defects in Huntington’s disease transgenic mice implicate PGC-1α in Huntington’s disease neurodegeneration. Cell Metab. 2006;4(5):349–362. · DOI · Paper page
  173. Parker A, Arango M, Abderrahmane S, et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat Genet. 2005;37(4):349–350. · DOI
  174. Ho DJ, Calingasan NY, Wille E, et al. Resveratrol protects against peripheral deficits in a mouse model of Huntington’s disease. Exp Neurol. 2010;225(1):74–84. · DOI
  175. Giralt A, Carretón O, Lao-Peregrin C, et al. Conditional BDNF release under pathological conditions improves Huntington’s disease pathology by delaying neuronal dysfunction. Mol Neurodegener. 2011;6(1):71. · DOI
  176. Xie Y, Hayden MR, Xu B. BDNF overexpression in the forebrain rescues Huntington’s disease phenotypes in YAC128 mice. J Neurosci. 2010;30(44):14708–14718. · DOI · Paper page
  177. Luthi-Carter R, Taylor DM, Pallos J, et al. SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis. Proc Natl Acad Sci USA. 2010;107(17):7927–7932. · DOI
  178. Fu J, Jin J, Cichewicz RH, et al. trans-(−)-ϵ-Viniferin increases mitochondrial sirtuin 3 (SIRT3), activates AMP-activated protein kinase (AMPK), and protects cells in models of Huntington disease. J Biol Chem. 2012;287(29):24460–24472. · DOI
  179. Butterworth J, Yates CM, Reynolds GP. Distribution of phosphate-activated glutaminase, succinic dehydrogenase, pyruvate dehydrogenase and γ-glutamyl transpeptidase in post-mortem brain from Huntington’s disease and agonal cases. J Neurol Sci. 1985;67(2):161–171. · DOI
  180. Ferreira IL, Cunha-Oliveira T, Nascimento MV, et al. Bioenergetic dysfunction in Huntington’s disease human cybrids. Exp Neurol. 2011;231(1):127–134. · DOI
  181. Naia L, Cunha-Oliveira T, Rodrigues J, et al. Histone deacetylase inhibitors protect against pyruvate dehydrogenase dysfunction in Huntington’s disease. J Neurosci. 2017;37(10):2776–2794. · DOI
  182. Fan J, Shan C, Kang H-B, et al. Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex. Mol Cell. 2014;53(4):534–548. · DOI · Paper page
  183. Cozzolino M, Carrì MT. Mitochondrial dysfunction in ALS. Prog Neurobiol. 2012;97(2):54–66. · DOI
  184. Tan W, Pasinelli P, Trotti D. Role of mitochondria in mutant SOD1 linked amyotrophic lateral sclerosis. Biochim Biophys Acta. 2014;1842(8):1295–1301. · DOI
  185. Rice C, Sun M, Kemp K, et al. Mitochondrial sirtuins–a new therapeutic target for repair and protection in multiple sclerosis. Eur J Neurosci. 2012;35(12):1887–1893. · DOI
  186. Foolad F, Khodagholi F, Javan M. Sirtuins in multiple sclerosis: the crossroad of neurodegeneration, autoimmunity and metabolism. Mult Scler Relat Disord. 2019;34:47–58. · DOI
  187. Baranzini SE, Srinivasan R, Khankhanian P, et al. Genetic variation influences glutamate concentrations in brains of patients with multiple sclerosis. Brain. 2010;133(9):2603–2611. · DOI
  188. Geurts JJG, Wolswijk G, Bö L, et al. Expression patterns of group III metabotropic glutamate receptors mGluR4 and mGluR8 in multiple sclerosis lesions. J Neuroimmunol. 2005;158(1-2):182–190. · DOI
  189. Faghihzadeh F, Adibi P, Rafiei R, et al. Resveratrol supplementation improves inflammatory biomarkers in patients with nonalcoholic fatty liver disease. Nutr Res. 2014;34(10):837–843. · DOI
  190. Witte AV, Kerti L, Margulies DS, et al. Effects of resveratrol on memory performance, hippocampal functional connectivity, and glucose metabolism in healthy older adults. J Neurosci. 2014;34(23):7862–7870. · DOI · Paper page
  191. Moussa C, Hebron M, Huang X, et al. Resveratrol regulates neuro-inflammation and induces adaptive immunity in Alzheimer’s disease. J Neuroinflamm. 2017;14(1):1–10. · DOI
  192. Milne JC, Denu JM. The sirtuin family: therapeutic targets to treat diseases of aging. Curr Opin Chem Biol. 2008;12(1):11–17. · DOI
  193. Singh S, McClung J, Thompson E, et al. Cardioprotective heme oxygenase-1-PGC1α signaling in epicardial fat attenuates cardiovascular risk in humans as in obese mice. Obesity (Silver Spring). 2019;27(10):1634–1643. · DOI
  194. Sidorova-Darmos E, Sommer R, Eubanks JH. The role of SIRT3 in the brain under physiological and pathological conditions. Front Cell Neurosci. 2018;12:196. · DOI
  195. Zhao H-C, Ding T, Ren Y, et al. Role of Sirt3 in mitochondrial biogenesis and developmental competence of human in vitro matured oocytes. Human Reprod. 2016;31(3):607–622. · DOI
  196. Morigi M, Perico L, Rota C, et al . Sirtuin 3-dependent mitochondrial dynamic improvements protect against acute kidney injury. J Clin Invest. 2015;125(2):715–726. · DOI
  197. Miyo M, Yamamoto H, Konno M, et al. Tumour-suppressive function of SIRT4 in human colorectal cancer. Br J Cancer. 2015;113(3):492–499. · DOI
  198. Kumar S, Lombard DB. Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology. Crit Rev Biochem Mol Biol. 2018;53(3):311–334. · DOI
  199. Guedouari H, Daigle T, Scorrano L, et al. Sirtuin 5 protects mitochondria from fragmentation and degradation during starvation. Biochim Biophys Acta. 2017;1864(1):169–176. · DOI
  200. Liu L, Peritore C, Ginsberg J, et al. Protective role of SIRT5 against motor deficit and dopaminergic degeneration in MPTP-induced mice model of Parkinson’s disease. Behav Brain Res. 2015;281:215–221. · DOI

200 of 278 shown

Cited by

Sorted by citations

See all 28

Metadata

Authors
Bhatt, V., & Tiwari, A. K.
Affiliations
Department of Biological Sciences & Biotechnology, Institute of Advanced Research, Koba, Gandhinagar, Gujarat, India
ORCID
Tiwari, Anand Krishna
Venue
International Journal of Neuroscience
Publisher
Informa UK Limited
Published
2022-05-13
Volume
133
Issue
10
Pages
1167-1192
ISSN
  • 0020-7454
  • 1543-5245
DOI
10.1080/00207454.2022.2057849
Cited by
28
References
34
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review