SIRT6 in Regulation of Mitochondrial Damage and Associated Cardiac Dysfunctions: A Possible Therapeutic Target for CVDs.

Deaton, C., Froelicher, E. S., Wu, L. H., Ho, C., Shishani, K., & Jaarsma, T. (2011). The Global burden of cardiovascular disease. European Journal of Cardiovascular Nursing, 10(2_Suppl), S5-13.

pubmed: 21762852 doi: 10.1016/S1474-5151(11)00111-3

World Health Organization. Regional Office for Europe. Global atlas on cardiovascular disease prevention and control: published by the World Health Organization in collaboration with the World Heart Federation and the World Stroke Organization [Internet]. Copenhagen: World Health Organization. Regional Office for Europe; 2011. 155 p. https://iris.who.int/handle/10665/329516 . Accessed 20 Nov 2011.

Zhu, L., Chen, Z., Han, K., Zhao, Y., Li, Y., Li, D., et al. (2020). Correlation between mitochondrial dysfunction, cardiovascular diseases, and traditional chinese medicine. Evidence-Based Complementary and Alternative Medicine, 2020, 2902136.

pubmed: 33101442 pmcid: 7568168 doi: 10.1155/2020/2902136

Ruan, L., Wang, Y., Zhang, X., Tomaszewski, A., McNamara, J. T., & Li, R. (2020). Mitochondria-associated proteostasis. Annual Review of Biophysics, 6(49), 41–67.

doi: 10.1146/annurev-biophys-121219-081604

Siasos, G., Tsigkou, V., Kosmopoulos, M., Theodosiadis, D., Simantiris, S., Tagkou, N. M., et al. (2018). Mitochondria and cardiovascular diseases-from pathophysiology to treatment. Annals of Translational Medicine, 6(12), 256.

pubmed: 30069458 pmcid: 6046286 doi: 10.21037/atm.2018.06.21

Gorman, G. S., Chinnery, P. F., DiMauro, S., Hirano, M., Koga, Y., McFarland, R., et al. (2016). Mitochondrial diseases. Nature Reviews Disease Primers, 2(1), 16080.

pubmed: 27775730 doi: 10.1038/nrdp.2016.80

Qiao, X., Jia, S., Ye, J., Fang, X., Zhang, C., Cao, Y., et al. (2017). PTPIP51 regulates mouse cardiac ischemia/reperfusion through mediating the mitochondria-SR junction. Science and Reports, 7(1), 45379.

doi: 10.1038/srep45379

Hao, Y., Lu, Q., Yang, G., & Ma, A. (2016). Lin28a protects against postinfarction myocardial remodeling and dysfunction through Sirt1 activation and autophagy enhancement. Biochemical and Biophysical Research Communications, 479(4), 833–840.

pubmed: 27693787 doi: 10.1016/j.bbrc.2016.09.122

Kennedy, B. K., Gotta, M., Sinclair, D. A., Mills, K., McNabb, D. S., Murthy, M., et al. (1997). Redistribution of silencing proteins from telomeres to the nucleolus Is associated with extension of life span in S. cerevisiae. Cell, 89(3), 381–391.

pubmed: 9150138 doi: 10.1016/S0092-8674(00)80219-6

Kaeberlein, M., McVey, M., & Guarente, L. (1999). The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes & Development, 13(19), 2570–2580.

doi: 10.1101/gad.13.19.2570

Imai, S. I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000). Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature, 403(6771), 795–800.

pubmed: 10693811 doi: 10.1038/35001622

Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., et al. (2000). The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proceedings of the National Academy of Sciences, 97(11), 5807–5811.

doi: 10.1073/pnas.110148297

Kumari, P., Tarighi, S., Braun, T., & Ianni, A. (2021). SIRT7 acts as a guardian of cellular integrity by controlling nucleolar and extra-nucleolar functions. Genes, 12(9), 1361.

pubmed: 34573343 pmcid: 8467518 doi: 10.3390/genes12091361

Ford, E., Voit, R., Liszt, G., Magin, C., Grummt, I., & Guarente, L. (2006). Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes & Development, 20(9), 1075–1080.

doi: 10.1101/gad.1399706

Banks, A. S., Kon, N., Knight, C., Matsumoto, M., Gutiérrez-Juárez, R., Rossetti, L., et al. (2008). SirT1 gain of function increases energy efficiency and prevents diabetes in mice. Cell Metabolism, 8(4), 333–341.

pubmed: 18840364 pmcid: 3222897 doi: 10.1016/j.cmet.2008.08.014

Bonkowski, M. S., & Sinclair, D. A. (2016). Slowing ageing by design: The rise of NAD+ and sirtuin-activating compounds. Nature Reviews Molecular Cell Biology, 17(11), 679–690.

pubmed: 27552971 pmcid: 5107309 doi: 10.1038/nrm.2016.93

Haigis, M. C., & Guarente, L. P. (2006). Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction. Genes & Development, 20(21), 2913–2921.

doi: 10.1101/gad.1467506

Hubbard, B. P., & Sinclair, D. A. (2014). Small molecule SIRT1 activators for the treatment of aging and age-related diseases. Trends in Pharmacological Sciences, 35(3), 146–154.

pubmed: 24439680 pmcid: 3970218 doi: 10.1016/j.tips.2013.12.004

Imai, S. I., & Guarente, L. (2014). NAD+ and sirtuins in aging and disease. Trends in Cell Biology, 24(8), 464–471.

pubmed: 24786309 pmcid: 4112140 doi: 10.1016/j.tcb.2014.04.002

Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., et al. (2012). The sirtuin SIRT6 regulates lifespan in male mice. Nature, 483(7388), 218–221.

pubmed: 22367546 doi: 10.1038/nature10815

Kanfi, Y., Peshti, V., Gil, R., Naiman, S., Nahum, L., Levin, E., et al. (2010). SIRT6 protects against pathological damage caused by diet-induced obesity. Aging Cell, 9(2), 162–173.

pubmed: 20047575 doi: 10.1111/j.1474-9726.2009.00544.x

Kugel, S., Sebastián, C., Fitamant, J., Ross, K. N., Saha, S. K., Jain, E., et al. (2016). SIRT6 suppresses pancreatic cancer through control of Lin28b. Cell, 165(6), 1401–1415.

pubmed: 27180906 pmcid: 4892983 doi: 10.1016/j.cell.2016.04.033

Mitchell, S. J., Martin-Montalvo, A., Mercken, E. M., Palacios, H. H., Ward, T. M., Abulwerdi, G., et al. (2014). The SIRT1 activator SRT1720 extends lifespan and improves health of mice fed a standard diet. Cell Reports, 6(5), 836–843.

pubmed: 24582957 doi: 10.1016/j.celrep.2014.01.031

Pfluger, P. T., Herranz, D., Velasco-Miguel, S., Serrano, M., & Tschop, M. H. (2008). Sirt1 protects against high-fat diet-induced metabolic damage. Proceedings of the National Academy of Sciences, 105(28), 9793–9798.

doi: 10.1073/pnas.0802917105

Satoh, A., Brace, C. S., Rensing, N., Cliften, P., Wozniak, D. F., Herzog, E. D., et al. (2013). Sirt1 extends life span and delays aging in mice through the regulation of Nk2 homeobox 1 in the DMH and LH. Cell Metabolism, 18(3), 416–430.

pubmed: 24011076 pmcid: 3794712 doi: 10.1016/j.cmet.2013.07.013

Borradaile, N. M., & Pickering, J. G. (2009). Nicotinamide phosphoribosyltransferase imparts human endothelial cells with extended replicative lifespan and enhanced angiogenic capacity in a high glucose environment. Aging Cell, 8(2), 100–112.

pubmed: 19302375 doi: 10.1111/j.1474-9726.2009.00453.x

Kane, A. E., & Sinclair, D. A. (2018). Sirtuins and NAD

pubmed: 30355082 pmcid: 6206880 doi: 10.1161/CIRCRESAHA.118.312498

Hou, T., Cao, Z., Zhang, J., Tang, M., Tian, Y., Li, Y., et al. (2020). SIRT6 coordinates with CHD4 to promote chromatin relaxation and DNA repair. Nucleic Acids Research, 48(6), 2982–3000.

pubmed: 31970415 pmcid: 7102973 doi: 10.1093/nar/gkaa006

Mao, Z., Hine, C., Tian, X., Van Meter, M., Au, M., Vaidya, A., et al. (2011). SIRT6 promotes DNA repair under stress by activating PARP1. Science, 332(6036), 1443–1446.

pubmed: 21680843 pmcid: 5472447 doi: 10.1126/science.1202723

Zhong, L., D’Urso, A., Toiber, D., Sebastian, C., Henry, R. E., Vadysirisack, D. D., et al. (2010). The histone deacetylase SIRT6 regulates glucose homeostasis via Hif1α. Cell, 140(2), 280–293.

pubmed: 20141841 pmcid: 2821045 doi: 10.1016/j.cell.2009.12.041

Guarente, L. (2011). Sirtuins, aging, and medicine. New England Journal of Medicine, 364(23), 2235–2244.

pubmed: 21651395 doi: 10.1056/NEJMra1100831

Winnik, S., Auwerx, J., Sinclair, D. A., & Matter, C. M. (2015). Protective effects of sirtuins in cardiovascular diseases: From bench to bedside. European Heart Journal, 36(48), 3404–3412.

pubmed: 26112889 pmcid: 4685177 doi: 10.1093/eurheartj/ehv290

Jiang, H., Khan, S., Wang, Y., Charron, G., He, B., Sebastian, C., et al. (2013). SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature, 496(7443), 110–113.

pubmed: 23552949 pmcid: 3635073 doi: 10.1038/nature12038

Ardestani, P. M., & Liang, F. (2012). Sub-cellular localization, expression and functions of SIRT6 during the cell cycle in HeLa cells. Nucleus, 3(5), 442–451.

pubmed: 22743824 pmcid: 3474665 doi: 10.4161/nucl.21134

Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., et al. (2008). SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature, 452(7186), 492–496.

pubmed: 18337721 pmcid: 2646112 doi: 10.1038/nature06736

Xu, F., Zhang, Q., Zhang, K., Xie, W., & Grunstein, M. (2007). Sir2 deacetylates histone H3 lysine 56 to regulate telomeric heterochromatin structure in yeast. Molecular Cell, 27(6), 890–900.

pubmed: 17889663 pmcid: 2048486 doi: 10.1016/j.molcel.2007.07.021

Dang, W., Steffen, K. K., Perry, R., Dorsey, J. A., Johnson, F. B., Shilatifard, A., et al. (2009). Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature, 459(7248), 802–807.

pubmed: 19516333 pmcid: 2702157 doi: 10.1038/nature08085

Dong, X. C. (2023). Sirtuin 6—a key regulator of hepatic lipid metabolism and liver health. Cells, 12(4), 663.

pubmed: 36831330 pmcid: 9954390 doi: 10.3390/cells12040663

Rezazadeh, S., Yang, D., Biashad, S. A., Firsanov, D., Takasugi, M., Gilbert, M., et al. (2020). SIRT6 mono-ADP ribosylates KDM2A to locally increase H3K36me2 at DNA damage sites to inhibit transcription and promote repair. Aging, 12(12), 11165–11184.

pubmed: 32584788 pmcid: 7343504 doi: 10.18632/aging.103567

Lombard, D. B., Schwer, B., Alt, F. W., & Mostoslavsky, R. (2008). SIRT6 in DNA repair, metabolism and ageing. Journal of Internal Medicine, 263(2), 128–141.

pubmed: 18226091 pmcid: 2486832 doi: 10.1111/j.1365-2796.2007.01902.x

McCord, R. A., Michishita, E., Hong, T., Berber, E., Boxer, L. D., Kusumoto, R., et al. (2009). SIRT6 stabilizes DNA-dependent protein kinase at chromatin for DNA double-strand break repair. Aging, 1(1), 109–121.

pubmed: 20157594 pmcid: 2815768 doi: 10.18632/aging.100011

Klein, M. A., & Denu, J. M. (2020). Biological and catalytic functions of sirtuin 6 as targets for small-molecule modulators. Journal of Biological Chemistry, 295(32), 11021–11041.

pubmed: 32518153 pmcid: 7415977 doi: 10.1074/jbc.REV120.011438

Pan, P. W., Feldman, J. L., Devries, M. K., Dong, A., Edwards, A. M., & Denu, J. M. (2011). Structure and biochemical functions of SIRT6. Journal of Biological Chemistry, 286(16), 14575–14587.

pubmed: 21362626 pmcid: 3077655 doi: 10.1074/jbc.M111.218990

Onn, L., Portillo, M., Ilic, S., Cleitman, G., Stein, D., Kaluski, S., et al. (2020). SIRT6 is a DNA double-strand break sensor. eLife, 29(9), e51636.

doi: 10.7554/eLife.51636

Raghu, S., Prabhashankar, A. B., Shivanaiah, B., Tripathi, E., & Sundaresan, N. R. (2022). Sirtuin 6 Is a Critical Epigenetic Regulator of Cancer. In T. K. Kundu & C. Das (Eds.), Metabolism and Epigenetic Regulation: Implications in Cancer (Vol. 100, pp. 337–360). Springer International Publishing. https://doi.org/10.1007/978-3-031-07634-3_10

doi: 10.1007/978-3-031-07634-3_10

Michishita, E., Park, J. Y., Burneskis, J. M., Barrett, J. C., & Horikawa, I. (2005). Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. MBoC, 16(10), 4623–4635.

pubmed: 16079181 pmcid: 1237069 doi: 10.1091/mbc.e05-01-0033

Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H. L., Alt, F. W., et al. (2006). SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes & Development, 20(10), 1256–1261.

doi: 10.1101/gad.1412706

Huang, J. Y., Hirschey, M. D., Shimazu, T., Ho, L., & Verdin, E. (2010). Mitochondrial sirtuins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1804(8), 1645–1651.

pubmed: 20060508 doi: 10.1016/j.bbapap.2009.12.021

Kawahara, T. L. A., Michishita, E., Adler, A. S., Damian, M., Berber, E., Lin, M., et al. (2009). SIRT6 links histone H3 lysine 9 deacetylation to NF-κB-dependent gene expression and organismal life span. Cell, 136(1), 62–74.

pubmed: 19135889 pmcid: 2757125 doi: 10.1016/j.cell.2008.10.052

Barber, M. F., Michishita-Kioi, E., Xi, Y., Tasselli, L., Kioi, M., Moqtaderi, Z., et al. (2012). SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation. Nature, 487(7405), 114–118.

pubmed: 22722849 pmcid: 3412143 doi: 10.1038/nature11043

Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., et al. (2016). SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability. Nature Communications, 7(1), 12235.

pubmed: 27436229 pmcid: 4961794 doi: 10.1038/ncomms12235

Wang, M., Zhang, Y., Komaniecki, G. P., Lu, X., Cao, J., Zhang, M., et al. (2022). Golgi stress induces SIRT2 to counteract Shigella infection via defatty-acylation. Nature Communications, 13(1), 4494.

pubmed: 35918380 pmcid: 9345896 doi: 10.1038/s41467-022-32227-x

Yu, A. Q., Wang, J., Jiang, S. T., Yuan, L. Q., Ma, H. Y., Hu, Y. M., et al. (2021). SIRT7-induced PHF5A decrotonylation regulates aging progress through alternative splicing-mediated downregulation of CDK2. Frontiers in Cell and Developmental Biology, 17(9), 710479.

Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012). Sirtuins as regulators of metabolism and healthspan. Nature Reviews Molecular Cell Biology, 13(4), 225–238.

pubmed: 22395773 pmcid: 4872805 doi: 10.1038/nrm3293

Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., & Villarroya, F. (2009). SIRT1 controls the transcription of the peroxisome proliferator-activated receptor-γ co-activator-1α (PGC-1α) gene in skeletal muscle through the PGC-1α autoregulatory loop and interaction with MyoD. Journal of Biological Chemistry, 284(33), 21872–21880.

pubmed: 19553684 pmcid: 2755911 doi: 10.1074/jbc.M109.022749

Olmos, Y., Sánchez-Gómez, F. J., Wild, B., García-Quintans, N., Cabezudo, S., Lamas, S., et al. (2013). SirT1 regulation of antioxidant genes is dependent on the formation of a FoxO3a/PGC-1α complex. Antioxidants & Redox Signaling, 19(13), 1507–1521.

doi: 10.1089/ars.2012.4713

Lagouge, M., Argmann, C., Gerhart-Hines, Z., Meziane, H., Lerin, C., Daussin, F., et al. (2006). Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1α. Cell, 127(6), 1109–1122.

pubmed: 17112576 doi: 10.1016/j.cell.2006.11.013

Lee, I. H., Cao, L., Mostoslavsky, R., Lombard, D. B., Liu, J., Bruns, N. E., et al. (2008). A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proceedings of the National academy of Sciences of the United States of America, 105(9), 3374–3379.

pubmed: 18296641 pmcid: 2265142 doi: 10.1073/pnas.0712145105

Liu, T., Yang, Q., Zhang, X., Qin, R., Shan, W., Zhang, H., et al. (2020). Quercetin alleviates kidney fibrosis by reducing renal tubular epithelial cell senescence through the SIRT1/PINK1/mitophagy axis. Life Sciences, 257, 118116.

pubmed: 32702447 doi: 10.1016/j.lfs.2020.118116

Oanh, N. T. K., Park, Y. Y., & Cho, H. (2017). Mitochondria elongation is mediated through SIRT1-mediated MFN1 stabilization. Cellular Signalling, 38, 67–75.

pubmed: 28669827 doi: 10.1016/j.cellsig.2017.06.019

Song, S. B., Park, J. S., Jang, S. Y., & Hwang, E. S. (2021). Nicotinamide treatment facilitates mitochondrial fission through Drp1 activation mediated by SIRT1-induced changes in cellular levels of cAMP and Ca2+. Cells, 10(3), 612.

pubmed: 33802063 pmcid: 7999186 doi: 10.3390/cells10030612

Lemos, V., De Oliveira, R. M., Naia, L., Szegö, É., Ramos, E., Pinho, S., et al. (2017). The NAD+-dependent deacetylase SIRT2 attenuates oxidative stress and mitochondrial dysfunction and improves insulin sensitivity in hepatocytes. Human Molecular Genetics, 26(21), 4105–4117.

pubmed: 28973648 doi: 10.1093/hmg/ddx298

Fourcade, S., Morató, L., Parameswaran, J., Ruiz, M., Ruiz-Cortés, T., Jové, M., et al. (2017). Loss of SIRT 2 leads to axonal degeneration and locomotor disability associated with redox and energy imbalance. Aging Cell, 16(6), 1404–1413.

pubmed: 28984064 pmcid: 5676070 doi: 10.1111/acel.12682

Cha, Y., Kim, T., Jeon, J., Jang, Y., Kim, P. B., Lopes, C., et al. (2021). SIRT2 regulates mitochondrial dynamics and reprogramming via MEK1-ERK-DRP1 and AKT1-DRP1 axes. Cell Reports, 37(13), 110155.

pubmed: 34965411 doi: 10.1016/j.celrep.2021.110155

Xin, T., & Lu, C. (2020). SirT3 activates AMPK-related mitochondrial biogenesis and ameliorates sepsis-induced myocardial injury. Aging, 12(16), 16224–16237.

pubmed: 32721927 pmcid: 7485737 doi: 10.18632/aging.103644

Tseng, A. H. H., Shieh, S. S., & Wang, D. L. (2013). SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage. Free Radical Biology and Medicine, 63, 222–234.

pubmed: 23665396 doi: 10.1016/j.freeradbiomed.2013.05.002

Zhou, Z. D., & Tan, E. K. (2020). Oxidized nicotinamide adenine dinucleotide-dependent mitochondrial deacetylase sirtuin-3 as a potential therapeutic target of Parkinson’s disease. Ageing Research Reviews, 62, 101107.

pubmed: 32535274 doi: 10.1016/j.arr.2020.101107

Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., et al. (2014). SIRT3 deacetylates and activates OPA1 to regulate mitochondrial dynamics during stress. Molecular and Cellular Biology, 34(5), 807–819.

pubmed: 24344202 pmcid: 4023816 doi: 10.1128/MCB.01483-13

Lang, A., Anand, R., Altinoluk-Hambüchen, S., Ezzahoini, H., Stefanski, A., Iram, A., et al. (2018). Correction: SIRT4 interacts with OPA1 and regulates mitochondrial quality control and mitophagy. Aging (Albany NY), 10(9), 2536c.

pubmed: 30300139 doi: 10.18632/aging.101570

Buler, M., Aatsinki, S., Izzi, V., Uusimaa, J., & Hakkola, A. J. (2014). SIRT5 is under the control of PGC-1α and AMPK and is involved in regulation of mitochondrial energy metabolism. The FASEB Journal, 28(7), 3225–3237.

pubmed: 24687991 doi: 10.1096/fj.13-245241

Haschler, T. N., Horsley, H., Balys, M., Anderson, G., Taanman, J. W., Unwin, R. J., et al. (2021). Sirtuin 5 depletion impairs mitochondrial function in human proximal tubular epithelial cells. Science and Reports, 11(1), 15510.

doi: 10.1038/s41598-021-94185-6

Zhang, M., Wu, J., Sun, R., Tao, X., Wang, X., Kang, Q., et al. (2019). SIRT5 deficiency suppresses mitochondrial ATP production and promotes AMPK activation in response to energy stress. PLoS ONE, 14(2), e0211796.

pubmed: 30759120 pmcid: 6373945 doi: 10.1371/journal.pone.0211796

Guedouari, H., Daigle, T., Scorrano, L., & Hebert-Chatelain, E. (2017). Sirtuin 5 protects mitochondria from fragmentation and degradation during starvation. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1864(1), 169–176.

pubmed: 28340937 doi: 10.1016/j.bbamcr.2016.10.015

Yu, L., Dong, X., Xue, X., Xu, S., Zhang, X., Xu, Y., et al. (2021). Melatonin attenuates diabetic cardiomyopathy and reduces myocardial vulnerability to ischemia-reperfusion injury by improving mitochondrial quality control: Role of SIRT6. Journal of Pineal Research, 70(1), e12698.

pubmed: 33016468 doi: 10.1111/jpi.12698

Hong, Y. X., Wu, W. Y., Song, F., Wu, C., Li, G. R., & Wang, Y. (2021). Cardiac senescence is alleviated by the natural flavone acacetin via enhancing mitophagy. Aging, 13(12), 16381–16403.

pubmed: 34175838 pmcid: 8266317 doi: 10.18632/aging.203163

Chen, Z., Liang, W., Hu, J., Zhu, Z., Feng, J., Ma, Y., et al. (2022). SIRT6 deficiency contributes to mitochondrial fission and oxidative damage in podocytes via ROCK1-DRP1 signalling pathway. Cell Proliferation, 55(10), e13296.

pubmed: 35842903 pmcid: 9528772 doi: 10.1111/cpr.13296

Smirnov, D., Eremenko, E., Stein, D., Kaluski, S., Jasinska, W., Cosentino, C., et al. (2023). SIRT6 is a key regulator of mitochondrial function in the brain. Cell Death & Disease, 14(1), 35.

doi: 10.1038/s41419-022-05542-w

Yan, W., Liang, Y., Zhang, Q., Wang, D., Lei, M., Qu, J., et al. (2018). Arginine methylation of SIRT 7 couples glucose sensing with mitochondria biogenesis. EMBO Reports, 19(12), e46377.

pubmed: 30420520 pmcid: 6280788 doi: 10.15252/embr.201846377

Vakhrusheva, O., Smolka, C., Gajawada, P., Kostin, S., Boettger, T., Kubin, T., et al. (2008). Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice. Circulation Research, 102(6), 703–710.

pubmed: 18239138 doi: 10.1161/CIRCRESAHA.107.164558

Mohrin, M., Shin, J., Liu, Y., Brown, K., Luo, H., Xi, Y., et al. (2015). A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging. Science, 347(6228), 1374–1377.

pubmed: 25792330 pmcid: 4447312 doi: 10.1126/science.aaa2361

Dominy, J. E., Lee, Y., Jedrychowski, M. P., Chim, H., Jurczak, M. J., Camporez, J. P., et al. (2012). The deacetylase SIRT6 activates the acetyltransferase GCN5 and suppresses hepatic gluconeogenesis. Molecular Cell, 48(6), 900–913.

pubmed: 23142079 pmcid: 3534905 doi: 10.1016/j.molcel.2012.09.030

Zhang, P., Tu, B., Wang, H., Cao, Z., Tang, M., Zhang, C., et al. (2014). Tumor suppressor p53 cooperates with SIRT6 to regulate gluconeogenesis by promoting FoxO1 nuclear exclusion. Proceedings of the National academy of Sciences of the United States of America, 111(29), 10684–10689.

pubmed: 25009184 pmcid: 4115576 doi: 10.1073/pnas.1411026111

Qin, K., Zhang, N., Zhang, Z., Nipper, M., Zhu, Z., Leighton, J., et al. (2018). SIRT6-mediated transcriptional suppression of Txnip is critical for pancreatic beta cell function and survival in mice. Diabetologia, 61(4), 906–918.

pubmed: 29322219 pmcid: 6203439 doi: 10.1007/s00125-017-4542-6

van Heemst, D. (2010). Insulin, IGF-1 and longevity. Aging & Disease, 1(2), 147–157.

Sundaresan, N. R., Vasudevan, P., Zhong, L., Kim, G., Samant, S., Parekh, V., et al. (2012). The sirtuin SIRT6 blocks IGF-Akt signaling and development of cardiac hypertrophy by targeting c-Jun. Nature Medicine, 18(11), 1643–1650.

pubmed: 23086477 pmcid: 4401084 doi: 10.1038/nm.2961

Xiao, C., Kim, H. S., Lahusen, T., Wang, R. H., Xu, X., Gavrilova, O., et al. (2010). SIRT6 deficiency results in severe hypoglycemia by enhancing both basal and insulin-stimulated glucose uptake in mice. Journal of Biological Chemistry, 285(47), 36776–36784.

pubmed: 20847051 pmcid: 2978606 doi: 10.1074/jbc.M110.168039

Wu, M., Seto, E., & Zhang, J. (2015). E2F1 enhances glycolysis through suppressing SIRT6 transcription in cancer cells. Oncotarget, 6(13), 11252–11263.

pubmed: 25816777 pmcid: 4484454 doi: 10.18632/oncotarget.3594

Santos-Barriopedro, I., Bosch-Presegué, L., Marazuela-Duque, A., De La Torre, C., Colomer, C., Vazquez, B. N., et al. (2018). SIRT6-dependent cysteine monoubiquitination in the PRE-SET domain of Suv39h1 regulates the NF-κB pathway. Nature Communications, 9(1), 101.

pubmed: 29317652 pmcid: 5760577 doi: 10.1038/s41467-017-02586-x

Cui, X., Yao, L., Yang, X., Gao, Y., Fang, F., Zhang, J., et al. (2017). SIRT6 regulates metabolic homeostasis in skeletal muscle through activation of AMPK. American Journal of Physiology-Endocrinology and Metabolism, 313(4), E493-505.

pubmed: 28765271 doi: 10.1152/ajpendo.00122.2017

Tao, R., Xiong, X., DePinho, R. A., Deng, C. X., & Dong, X. C. (2013). FoxO3 transcription factor and SIRT6 deacetylase regulate low density lipoprotein (LDL)-cholesterol homeostasis via control of the proprotein convertase subtilisin/kexin type 9 (Pcsk9) gene expression. Journal of Biological Chemistry, 288(41), 29252–29259.

pubmed: 23974119 pmcid: 3795227 doi: 10.1074/jbc.M113.481473

Kuang, J., Zhang, Y., Liu, Q., Shen, J., Pu, S., Cheng, S., et al. (2017). Fat-specific Sirt6 ablation sensitizes mice to high-fat diet-induced obesity and insulin resistance by inhibiting lipolysis. Diabetes, 66(5), 1159–1171.

pubmed: 28250020 doi: 10.2337/db16-1225

Chen, Q., Hao, W., Xiao, C., Wang, R., Xu, X., Lu, H., et al. (2017). SIRT6 is essential for adipocyte differentiation by regulating mitotic clonal expansion. Cell Reports, 18(13), 3155–3166.

pubmed: 28355567 doi: 10.1016/j.celrep.2017.03.006

Fan, Y., Yang, Q., Yang, Y., Gao, Z., Ma, Y., Zhang, L., et al. (2019). SIRT6 suppresses high glucose-induced mitochondrial dysfunction and apoptosis in podocytes through AMPK activation. International Journal of Biological Sciences, 15(3), 701–713.

pubmed: 30745856 pmcid: 6367578 doi: 10.7150/ijbs.29323

Wang, R., Wang, J., Zhang, Z., Ma, B., Sun, S., Gao, L., et al. (2023). FGF21 alleviates endothelial mitochondrial damage and prevents BBB from disruption after intracranial hemorrhage through a mechanism involving SIRT6. Molecular Medicine, 29(1), 165.

pubmed: 38049769 pmcid: 10696847 doi: 10.1186/s10020-023-00755-x

Lu, J., Sun, D., Liu, Z., Li, M., Hong, H., Liu, C., et al. (2016). SIRT6 suppresses isoproterenol-induced cardiac hypertrophy through activation of autophagy. Translational Research, 172, 96-112.e6.

pubmed: 27016702 doi: 10.1016/j.trsl.2016.03.002

Cheng, M. Y., Cheng, Y. W., Yan, J., Hu, X. Q., Zhang, H., Wang, Z. R., et al. (2016). SIRT6 suppresses mitochondrial defects and cell death via the NF-κB pathway in myocardial hypoxia/reoxygenation induced injury. American Journal of Translational Research, 8(11), 5005–5015.

pubmed: 27904701 pmcid: 5126343

Maksin-Matveev, A., Kanfi, Y., Hochhauser, E., Isak, A., Cohen, H. Y., & Shainberg, A. (2015). Sirtuin 6 protects the heart from hypoxic damage. Experimental Cell Research, 330(1), 81–90.

pubmed: 25066211 doi: 10.1016/j.yexcr.2014.07.013

Wang, T., Sun, C., Hu, L., Gao, E., Li, C., Wang, H., et al. (2020). SIRT6 stabilizes atherosclerosis plaques by promoting macrophage autophagy and reducing contact with endothelial cells. Biochemistry and Cell Biology, 98(2), 120–129.

pubmed: 31063699 doi: 10.1139/bcb-2019-0057

Pillai, V. B., Samant, S., Hund, S., Gupta, M., & Gupta, M. P. (2021). The nuclear sirtuin SIRT6 protects the heart from developing aging-associated myocyte senescence and cardiac hypertrophy. Aging, 13(9), 12334–12358.

pubmed: 33934090 pmcid: 8148452 doi: 10.18632/aging.203027

Tian, K., Liu, Z., Wang, J., Xu, S., You, T., & Liu, P. (2015). Sirtuin-6 inhibits cardiac fibroblasts differentiation into myofibroblasts via inactivation of nuclear factor κB signaling. Translational Research, 165(3), 374–386.

pubmed: 25475987 doi: 10.1016/j.trsl.2014.08.008

Maity, S., Muhamed, J., Sarikhani, M., Kumar, S., Ahamed, F., Spurthi, K. M., et al. (2020). Sirtuin 6 deficiency transcriptionally up-regulates TGF-β signaling and induces fibrosis in mice. Journal of Biological Chemistry, 295(2), 415–434.

pubmed: 31744885 doi: 10.1074/jbc.RA118.007212

Li, X., Liu, L., Li, T., Liu, M., Wang, Y., Ma, H., et al. (2021). SIRT6 in senescence and aging-related cardiovascular diseases. Frontiers in Cell and Developmental Biology, 29(9), 641315.

doi: 10.3389/fcell.2021.641315

Cardus, A., Uryga, A. K., Walters, G., & Erusalimsky, J. D. (2013). SIRT6 protects human endothelial cells from DNA damage, telomere dysfunction, and senescence. Cardiovascular Research, 97(3), 571–579.

pubmed: 23201774 doi: 10.1093/cvr/cvs352

Wallace, D. C. (2005). A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: A dawn for evolutionary medicine. Annual Review of Genetics, 39(1), 359–407.

pubmed: 16285865 pmcid: 2821041 doi: 10.1146/annurev.genet.39.110304.095751

Finkel, T., & Holbrook, N. J. (2000). Oxidants, oxidative stress and the biology of ageing. Nature, 408(6809), 239–247.

pubmed: 11089981 doi: 10.1038/35041687

Ryan, M. T., & Hoogenraad, N. J. (2007). Mitochondrial-nuclear communications. Annual Review of Biochemistry, 76(1), 701–722.

pubmed: 17227225 doi: 10.1146/annurev.biochem.76.052305.091720

Hall, A. R., Burke, N., Dongworth, R. K., & Hausenloy, D. J. (2014). Mitochondrial fusion and fission proteins: Novel therapeutic targets for combating cardiovascular disease. British Journsl of Pharmacology, 171(8), 1890–1906.

doi: 10.1111/bph.12516

Ott, M., Amunts, A., & Brown, A. (2016). Organization and regulation of mitochondrial protein synthesis. Annual Review of Biochemistry, 2(85), 77–101.

doi: 10.1146/annurev-biochem-060815-014334

Scarpulla, R. C. (2002). Nuclear activators and coactivators in mammalian mitochondrial biogenesis. Biochimica et Biophysica Acta (BBA) - Structure and Expression, 1576(1–2), 1–14.

Arany, Z., Novikov, M., Chin, S., Ma, Y., Rosenzweig, A., & Spiegelman, B. M. (2006). Transverse aortic constriction leads to accelerated heart failure in mice lacking PPAR-γ coactivator 1α. Proceedings of the National academy of Sciences of the United States of America, 103(26), 10086–10091.

pubmed: 16775082 pmcid: 1502510 doi: 10.1073/pnas.0603615103

Garnier, A., Fortin, D., Deloménie, C., Momken, I., Veksler, V., & Ventura-Clapier, R. (2003). Depressed mitochondrial transcription factors and oxidative capacity in rat failing cardiac and skeletal muscles. The Journal of Physiology, 551(2), 491–501.

pubmed: 12824444 pmcid: 2343221 doi: 10.1113/jphysiol.2003.045104

Wang, L., Zhang, Q., Yuan, K., & Yuan, J. (2021). mtDNA in the pathogenesis of cardiovascular diseases. Disease Markers, 2021, 1–8.

doi: 10.1155/2021/6407528

Chen, Y., Liu, Y., & Dorn, G. W. (2011). Mitochondrial fusion is essential for organelle function and cardiac homeostasis. Circulation Research, 109(12), 1327–1331.

pubmed: 22052916 pmcid: 3237902 doi: 10.1161/CIRCRESAHA.111.258723

Papanicolaou, K. N., Kikuchi, R., Ngoh, G. A., Coughlan, K. A., Dominguez, I., Stanley, W. C., et al. (2012). Mitofusins 1 and 2 Are essential for postnatal metabolic remodeling in heart. Circulation Research, 111(8), 1012–1026.

pubmed: 22904094 pmcid: 3518037 doi: 10.1161/CIRCRESAHA.112.274142

Manczak, M., Sesaki, H., Kageyama, Y., & Reddy, P. H. (2012). Dynamin-related protein 1 heterozygote knockout mice do not have synaptic and mitochondrial deficiencies. Biochimica et Biophysica (BBA) - Molecular Basis of Disease, 1822(6), 862–874.

doi: 10.1016/j.bbadis.2012.02.017

Kubli, D. A., Zhang, X., Lee, Y., Hanna, R. A., Quinsay, M. N., Nguyen, C. K., et al. (2013). Parkin protein deficiency exacerbates cardiac injury and reduces survival following myocardial infarction. Journal of Biological Chemistry, 288(2), 915–926.

pubmed: 23152496 doi: 10.1074/jbc.M112.411363

Kattoor, A. J., Pothineni, N. V. K., Palagiri, D., & Mehta, J. L. (2017). Oxidative stress in atherosclerosis. Current Atherosclerosis Reports, 19(11), 42.

pubmed: 28921056 doi: 10.1007/s11883-017-0678-6

Sovari, A. A., Rutledge, C. A., Jeong, E. M., Dolmatova, E., Arasu, D., Liu, H., et al. (2013). Mitochondria oxidative stress, Connexin43 remodeling, and sudden arrhythmic death. Circulation Arrhythmia and Electrophysiology, 6(3), 623–631.

pubmed: 23559673 pmcid: 3716298 doi: 10.1161/CIRCEP.112.976787

Rutledge, C., & Dudley, S. (2013). Mitochondria and arrhythmias. Expert Review of Cardiovascular Therapy, 11(7), 799–801.

pubmed: 23895021 pmcid: 4211874 doi: 10.1586/14779072.2013.811969

Karamanlidis, G., Nascimben, L., Couper, G. S., Shekar, P. S., del Monte, F., & Tian, R. (2010). Defective DNA replication impairs mitochondrial biogenesis in human failing hearts. Circulation Research, 106(9), 1541–1548.

pubmed: 20339121 pmcid: 2880225 doi: 10.1161/CIRCRESAHA.109.212753

Borchi, E., Bargelli, V., Stillitano, F., Giordano, C., Sebastiani, M., Nassi, P. A., et al. (2010). Enhanced ROS production by NADPH oxidase is correlated to changes in antioxidant enzyme activity in human heart failure. Biochimica et Biophysica (BBA) - Molecular Basis of Disease, 1802(3), 331–338.

doi: 10.1016/j.bbadis.2009.10.014

Sam, F., Kerstetter, D. L., Pimental, D. R., Mulukutla, S., Tabaee, A., Bristow, M. R., et al. (2005). Increased reactive oxygen species production and functional alterations in antioxidant enzymes in human failing myocardium. Journal of Cardiac Failure, 11(6), 473–480.

pubmed: 16105639 doi: 10.1016/j.cardfail.2005.01.007

Ahuja, P., Wanagat, J., Wang, Z., Wang, Y., Liem, D. A., Ping, P., et al. (2013). Divergent mitochondrial biogenesis responses in human cardiomyopathy. Circulation, 127(19), 1957–1967.

pubmed: 23589024 pmcid: 4236313 doi: 10.1161/CIRCULATIONAHA.112.001219

Garnier, A., Zoll, J., Fortin, D., N’Guessan, B., Lefebvre, F., Geny, B., et al. (2009). Control by circulating factors of mitochondrial function and transcription cascade in heart failure: A role for endothelin-1 and angiotensin II. Circulation Heart Failure, 2(4), 342–350.

pubmed: 19808358 doi: 10.1161/CIRCHEARTFAILURE.108.812099

Maejima, Y., Kuroda, J., Matsushima, S., Ago, T., & Sadoshima, J. (2011). Regulation of myocardial growth and death by NADPH oxidase. Journal of Molecular and Cellular Cardiology, 50(3), 408–416.

pubmed: 21215757 pmcid: 3257581 doi: 10.1016/j.yjmcc.2010.12.018

Neubauer, S. (2007). The failing heart—an engine out of fuel. New England Journal of Medicine, 356(11), 1140–1151.

pubmed: 17360992 doi: 10.1056/NEJMra063052

Peng, W., Cai, G., Xia, Y., Chen, J., Wu, P., Wang, Z., et al. (2019). Mitochondrial dysfunction in atherosclerosis. DNA and Cell Biology, 38(7), 597–606.

pubmed: 31095428 doi: 10.1089/dna.2018.4552

Hulsmans, M., Van Dooren, E., & Holvoet, P. (2012). Mitochondrial reactive oxygen species and risk of atherosclerosis. Current Atherosclerosis Reports, 14(3), 264–276.

pubmed: 22350585 doi: 10.1007/s11883-012-0237-0

Huss, J. M., & Kelly, D. P. (2005). Mitochondrial energy metabolism in heart failure: A question of balance. The Journal of Clinical Investigation, 115(3), 547–555.

pubmed: 15765136 pmcid: 1052011 doi: 10.1172/JCI24405

Finsterer, J. (2009). Cardiogenetics, neurogenetics, and pathogenetics of left ventricular hypertrabeculation/noncompaction. Pediatric Cardiology, 30(5), 659–681.

pubmed: 19184181 doi: 10.1007/s00246-008-9359-0

Rouslin, W. (1983). Mitochondrial complexes I, II, III, IV, and V in myocardial ischemia and autolysis. American Journal of Physiology-Heart and Circulatory Physiology, 244(6), H743–H748.

doi: 10.1152/ajpheart.1983.244.6.H743

Asimakis, G., & Conti, V. (1984). Myocardial ischemia: Correlation of mitochondrial adenine nucleotide and respiratory function. Journal of Molecular and Cellular Cardiology, 16(5), 439–447.

pubmed: 6737484 doi: 10.1016/S0022-2828(84)80615-X

Borutaite, V., Mildaziene, V., Brown, G. C., & Brand, M. D. (1995). Control and kinetic analysis of ischemia-damaged heart mitochondria: which parts of the oxidative phosphorylation system are affected by ischemia? Biochimica et Biophysica (BBA) - Molecular Basis of Disease, 1272(3), 154–158.

doi: 10.1016/0925-4439(95)00080-1

Paradies, G., Petrosillo, G., Pistolese, M., Di Venosa, N., Serena, D., & Ruggiero, F. M. (1999). Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion. Free Radical Biology and Medicine, 27(1–2), 42–50.

pubmed: 10443918 doi: 10.1016/S0891-5849(99)00032-5

Turrens, J. F., Beconi, M., Barilla, J., Chavez, U. B., & McCord, J. M. (1991). Mitochondrial generation of oxygen radicals during reoxygenation of ischemic tissues. Free Radical Research Communications, 13(1), 681–689.

doi: 10.3109/10715769109145847

Griffiths, E. J., & Halestrap, A. P. (1995). Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion. Biochemical Journal, 307(1), 93–98.

pubmed: 7717999 pmcid: 1136749 doi: 10.1042/bj3070093

Di Lisa, F., Menabò, R., Canton, M., Barile, M., & Bernardi, P. (2001). Opening of the mitochondrial permeability transition pore causes depletion of mitochondrial and cytosolic NAD

pubmed: 11073947 doi: 10.1074/jbc.M006825200

Stone, D., Darley-Usmar, V., Smith, D. R., & O’Leary, V. (1989). Hypoxia-reoxygenation induced increase in cellular Ca2+ in myocytes and perfused hearts: The role of mitochondria. Journal of Molecular and Cellular Cardiology, 21(10), 963–973.

pubmed: 2479760 doi: 10.1016/0022-2828(89)90795-5

Schilling, J. D. (2015). The mitochondria in diabetic heart failure: From pathogenesis to therapeutic promise. Antioxidants & Redox Signaling, 22(17), 1515–1526.

doi: 10.1089/ars.2015.6294

Verma, S. K., Garikipati, V. N. S., & Kishore, R. (2017). Mitochondrial dysfunction and its impact on diabetic heart. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1863(5), 1098–1105.

pubmed: 27593695 doi: 10.1016/j.bbadis.2016.08.021

Zhou, B., & Tian, R. (2018). Mitochondrial dysfunction in pathophysiology of heart failure. Journal of Clinical Investigation, 128(9), 3716–3726.

pubmed: 30124471 pmcid: 6118589 doi: 10.1172/JCI120849

Mahalakshmi, A., & Kurian, G. A. (2020). Mitochondrial dysfunction plays a key role in the abrogation of cardioprotection by sodium hydrosulfide post-conditioning in diabetic cardiomyopathy rat heart. Naunyn-Schmiedeberg’s Archives of Pharmacology, 393(3), 339–348.

doi: 10.1007/s00210-019-01733-z

Yao, K., Zhang, W. W., Yao, L., Yang, S., Nie, W., & Huang, F. (2016). Carvedilol promotes mitochondrial biogenesis by regulating the PGC-1/TFAM pathway in human umbilical vein endothelial cells (HUVECs). Biochemical and Biophysical Research Communications, 470(4), 961–966.

pubmed: 26797282 doi: 10.1016/j.bbrc.2016.01.089

Andres, A. M., Hernandez, G., Lee, P., Huang, C., Ratliff, E. P., Sin, J., et al. (2014). Mitophagy is required for acute cardioprotection by simvastatin. Antioxidants & Redox Signaling, 21(14), 1960–1973.

doi: 10.1089/ars.2013.5416

Coronado, M., Fajardo, G., Nguyen, K., Zhao, M., Kooiker, K., Jung, G., et al. (2018). Physiological mitochondrial fragmentation is a normal cardiac adaptation to increased energy demand. Circulation Research, 122(2), 282–295.

pubmed: 29233845 doi: 10.1161/CIRCRESAHA.117.310725

Kong, D., Zhan, Y., Liu, Z., Ding, T., Li, M., Yu, H., et al. (2016). SIRT1-mediated ERβ suppression in the endothelium contributes to vascular aging. Aging Cell, 15(6), 1092–1102.

pubmed: 27470296 pmcid: 6398526 doi: 10.1111/acel.12515

Cea, M., Cagnetta, A., Adamia, S., Acharya, C., Tai, Y. T., Fulciniti, M., et al. (2016). Evidence for a role of the histone deacetylase SIRT6 in DNA damage response of multiple myeloma cells. Blood, 127(9), 1138–1150.

pubmed: 26675349 pmcid: 4778164 doi: 10.1182/blood-2015-06-649970

Feldman, J. L., Baeza, J., & Denu, J. M. (2013). Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. Journal of Biological Chemistry, 288(43), 31350–31356.

pubmed: 24052263 pmcid: 3829447 doi: 10.1074/jbc.C113.511261

Guo, Z., Li, P., Ge, J., & Li, H. (2022). SIRT6 in aging, metabolism, inflammation and cardiovascular diseases. Aging and disease, 13(6), 1787.

pubmed: 36465178 pmcid: 9662279 doi: 10.14336/AD.2022.0413

Kanwal, A., Pillai, V. B., Samant, S., Gupta, M., & Gupta, M. P. (2019). The nuclear and mitochondrial sirtuins, SIRT6 and SIRT3, regulate each other’s activity and protect the heart from developing obesity-mediated diabetic cardiomyopathy. The FASEB Journal, 33(10), 10872–10888.

pubmed: 31318577 pmcid: 6766651 doi: 10.1096/fj.201900767R

Kugel, S., & Mostoslavsky, R. (2014). Chromatin and beyond: The multitasking roles for SIRT6. Trends in Biochemical Sciences, 39(2), 72–81.

pubmed: 24438746 pmcid: 3912268 doi: 10.1016/j.tibs.2013.12.002

Stein, A. B., Giblin, W., Guo, A. H., & Lombard, D. B. (2018). Roles for Sirtuins in Cardiovascular Biology. Introductory Review on Sirtuins in Biology, Aging, and Disease (pp. 155–173). Elsevier.

Kim, J. W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006). HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia. Cell Metabolism, 3(3), 177–185.

pubmed: 16517405 doi: 10.1016/j.cmet.2006.02.002

Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., & Denko, N. C. (2006). HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption. Cell Metabolism, 3(3), 187–197.

pubmed: 16517406 doi: 10.1016/j.cmet.2006.01.012

Kouzarides, T. (2007). Chromatin modifications and their function. Cell, 128(4), 693–705.

pubmed: 17320507 doi: 10.1016/j.cell.2007.02.005

van Loo, G., Saelens, X., van Gurp, M., MacFarlane, M., Martin, S. J., & Vandenabeele, P. (2002). The role of mitochondrial factors in apoptosis: A Russian roulette with more than one bullet. Cell Death and Differentiation, 9(10), 1031–1042.

pubmed: 12232790 doi: 10.1038/sj.cdd.4401088

Song, L., Chen, X., Mi, L., Liu, C., Zhu, S., Yang, T., et al. (2020). Icariin-induced inhibition of SIRT6/NF-κB triggers redox mediated apoptosis and enhances anti-tumor immunity in triple-negative breast cancer. Cancer Science, 111(11), 4242–4256.

pubmed: 32926492 pmcid: 7648025 doi: 10.1111/cas.14648

Balestrieri, M. L., Rizzo, M. R., Barbieri, M., Paolisso, P., D’Onofrio, N., Giovane, A., et al. (2015). Sirtuin 6 expression and inflammatory activity in diabetic atherosclerotic plaques: Effects of incretin treatment. Diabetes, 64(4), 1395–1406.

pubmed: 25325735 doi: 10.2337/db14-1149

Xiong, X., Wang, G., Tao, R., Wu, P., Kono, T., Li, K., et al. (2016). Sirtuin 6 regulates glucose-stimulated insulin secretion in mouse pancreatic beta cells. Diabetologia, 59(1), 151–160.

pubmed: 26471901 pmcid: 4792692 doi: 10.1007/s00125-015-3778-2

Xiong, X., Sun, X., Wang, Q., Qian, X., Zhang, Y., Pan, X., et al. (2016). SIRT6 protects against palmitate-induced pancreatic β-cell dysfunction and apoptosis. Journal of Endocrinology, 231(2), 159–165.

pubmed: 27601447 doi: 10.1530/JOE-16-0317

Feng, J., Yan, P. F., Zhao, H. Y., Zhang, F. C., Zhao, W. H., & Feng, M. (2016). SIRT6 suppresses glioma cell growth via induction of apoptosis, inhibition of oxidative stress and suppression of JAK2/STAT3 signaling pathway activation. Oncology Reports, 35(3), 1395–1402.

pubmed: 26648570 doi: 10.3892/or.2015.4477

Xie, X., Zhang, H., Gao, P., Wang, L., Zhang, A., Xie, S., et al. (2012). Overexpression of SIRT6 in porcine fetal fibroblasts attenuates cytotoxicity and premature senescence caused by D-galactose and tert-butylhydroperoxide. DNA and Cell Biology, 31(5), 745–752.

pubmed: 22149724 doi: 10.1089/dna.2011.1435

Saiyang, X., Deng, W., & Qizhu, T. (2020). Sirtuin 6: A potential therapeutic target for cardiovascular diseases. Pharmacological Research, 163, 105214.

pubmed: 33007414 doi: 10.1016/j.phrs.2020.105214

Xu, S., Yin, M., Koroleva, M., Mastrangelo, M. A., Zhang, W., Bai, P., et al. (2016). SIRT6 protects against endothelial dysfunction and atherosclerosis in mice. Aging, 8(5), 1064–1082.

pubmed: 27249230 pmcid: 4931854 doi: 10.18632/aging.100975

Sosnowska, B., Mazidi, M., Penson, P., Gluba-Brzózka, A., Rysz, J., & Banach, M. (2017). The sirtuin family members SIRT1, SIRT3 and SIRT6: Their role in vascular biology and atherogenesis. Atherosclerosis, 265, 275–282.

pubmed: 28870631 doi: 10.1016/j.atherosclerosis.2017.08.027

Bulbulia, R., & Armitage, J. (2012). LDL cholesterol targets – how low to go? Current Opinion in Lipidology, 23(4), 265–270.

pubmed: 22732520 doi: 10.1097/MOL.0b013e3283556c1b

Marais, D. A., Blom, D. J., Petrides, F., Gouëffic, Y., & Lambert, G. (2012). Proprotein convertase subtilisin/kexin type 9 inhibition. Current Opinion in Lipidology, 23(6), 511–517.

pubmed: 22907332 doi: 10.1097/MOL.0b013e3283587563

He, J., Zhang, G., Pang, Q., Yu, C., Xiong, J., Zhu, J., et al. (2017). SIRT 6 reduces macrophage foam cell formation by inducing autophagy and cholesterol efflux under ox- LDL condition. FEBS Journal, 284(9), 1324–1337.

pubmed: 28296196 doi: 10.1111/febs.14055

Tao, R., Xiong, X., DePinho, R. A., Deng, C. X., & Dong, X. C. (2013). Hepatic SREBP-2 and cholesterol biosynthesis are regulated by FoxO3 and Sirt6. Journal of Lipid Research, 54(10), 2745–2753.

pubmed: 23881913 pmcid: 3770087 doi: 10.1194/jlr.M039339

Kim, H. S., Xiao, C., Wang, R. H., Lahusen, T., Xu, X., Vassilopoulos, A., et al. (2010). Hepatic-specific disruption of SIRT6 in mice results in fatty liver formation due to enhanced glycolysis and triglyceride synthesis. Cell Metabolism, 12(3), 224–236.

pubmed: 20816089 pmcid: 2935915 doi: 10.1016/j.cmet.2010.06.009

Takasaka, N., Araya, J., Hara, H., Ito, S., Kobayashi, K., Kurita, Y., et al. (2014). Autophagy induction by SIRT6 through attenuation of insulin-like growth factor signaling is involved in the regulation of human bronchial epithelial cell senescence. The Journal of Immunology, 192(3), 958–968.

pubmed: 24367027 doi: 10.4049/jimmunol.1302341

Zhang, Z. Z., Cheng, Y. W., Jin, H. Y., Chang, Q., Shang, Q. H., Xu, Y. L., et al. (2017). The sirtuin 6 prevents angiotensin II-mediated myocardial fibrosis and injury by targeting AMPK-ACE2 signaling. Oncotarget, 8(42), 72302–72314.

pubmed: 29069788 pmcid: 5641131 doi: 10.18632/oncotarget.20305

Li, Y., Meng, X., Wang, W., Liu, F., Hao, Z., Yang, Y., et al. (2017). Cardioprotective effects of SIRT6 in a mouse model of transverse aortic constriction-induced heart failure. Frontiers in Physiology, 13(8), 394.

doi: 10.3389/fphys.2017.00394

Matsushima, S., & Sadoshima, J. (2015). The role of sirtuins in cardiac disease. American Journal of Physiology-Heart and Circulatory Physiology, 309(9), H1375–H1389.

pubmed: 26232232 pmcid: 4666968 doi: 10.1152/ajpheart.00053.2015

Van Meter, M., Simon, M., Tombline, G., May, A., Morello, T. D., Hubbard, B. P., et al. (2016). JNK phosphorylates SIRT6 to stimulate DNA double-strand break repair in response to oxidative stress by recruiting PARP1 to DNA breaks. Cell Reports, 16(10), 2641–2650.

pubmed: 27568560 doi: 10.1016/j.celrep.2016.08.006

D’Onofrio, N., Servillo, L., & Balestrieri, M. L. (2018). SIRT1 and SIRT6 signaling pathways in cardiovascular disease protection. Antioxidants & Redox Signaling, 28(8), 711–732.

doi: 10.1089/ars.2017.7178

Jung, S. M., Hung, C. M., Hildebrand, S. R., Sanchez-Gurmaches, J., Martinez-Pastor, B., Gengatharan, J. M., et al. (2019). Non-canonical mTORC2 signaling regulates brown adipocyte lipid catabolism through SIRT6-FoxO1. Molecular Cell, 75(4), 807-822.e8.

pubmed: 31442424 pmcid: 7388077 doi: 10.1016/j.molcel.2019.07.023

Khan, D., Sarikhani, M., Dasgupta, S., Maniyadath, B., Pandit, A. S., Mishra, S., et al. (2018). SIRT6 deacetylase transcriptionally regulates glucose metabolism in heart. Journal of Cellular Physiology, 233(7), 5478–5489.

pubmed: 29319170 doi: 10.1002/jcp.26434

Wang, X. X., Wang, X. L., Tong, M. M., Gan, L., Chen, H., Wu, S. S., et al. (2016). SIRT6 protects cardiomyocytes against ischemia/reperfusion injury by augmenting FoxO3α-dependent antioxidant defense mechanisms. Basic Research in Cardiology. https://doi.org/10.1007/s00395-016-0531-z

doi: 10.1007/s00395-016-0531-z pubmed: 27660282 pmcid: 5033992

Naiman, S., Huynh, F. K., Gil, R., Glick, Y., Shahar, Y., Touitou, N., et al. (2019). SIRT6 promotes hepatic beta-oxidation via activation of PPARα. Cell Reports, 29(12), 4127-4143.e8.

pubmed: 31851938 doi: 10.1016/j.celrep.2019.11.067

Guo, J., Wang, Z., Wu, J., Liu, M., Li, M., Sun, Y., et al. (2019). Endothelial SIRT6 is vital to prevent hypertension and associated cardiorenal injury through targeting Nkx3.2-GATA5 signaling. Circulation Research, 124(10), 1448–1461.

pubmed: 30894089 doi: 10.1161/CIRCRESAHA.118.314032

Masri, S., & Sassone-Corsi, P. (2014). Sirtuins and the circadian clock: Bridging chromatin and metabolism. Science Signaling, 7(342), re6.

pubmed: 25205852 doi: 10.1126/scisignal.2005685

Bugger, H., Witt, C. N., & Bode, C. (2016). Mitochondrial sirtuins in the heart. Heart Failure Reviews, 21(5), 519–528.

pubmed: 27295248 doi: 10.1007/s10741-016-9570-7

Chalkiadaki, A., & Guarente, L. (2015). The multifaceted functions of sirtuins in cancer. Nature Reviews Cancer, 15(10), 608–624.

pubmed: 26383140 doi: 10.1038/nrc3985

Madhavi, Y. V., Gaikwad, N., Yerra, V. G., Kalvala, A. K., Nanduri, S., & Kumar, A. (2019). Targeting AMPK in diabetes and diabetic complications: energy homeostasis. Autophagy and Mitochondrial Health CMC, 26(27), 5207–5229.

Palikaras, K., & Tavernarakis, N. (2014). Mitochondrial homeostasis: The interplay between mitophagy and mitochondrial biogenesis. Experimental Gerontology, 56, 182–188.

pubmed: 24486129 doi: 10.1016/j.exger.2014.01.021

Wu, S., & Zou, M. H. (2020). AMPK, mitochondrial function, and cardiovascular disease. International Journal of Molecular Science, 21(14), 4987.

doi: 10.3390/ijms21144987

Myers, R. W., Guan, H. P., Ehrhart, J., Petrov, A., Prahalada, S., Tozzo, E., et al. (2017). Systemic pan-AMPK activator MK-8722 improves glucose homeostasis but induces cardiac hypertrophy. Science, 357(6350), 507–511.

pubmed: 28705990 doi: 10.1126/science.aah5582

Anderson, K. A., Madsen, A. S., Olsen, C. A., & Hirschey, M. D. (2017). Metabolic control by sirtuins and other enzymes that sense NAD+, NADH, or their ratio. Biochimica et Biophysica Acta, Bioenergetics, 1858(12), 991–998.

pubmed: 28947253 doi: 10.1016/j.bbabio.2017.09.005

Cai, Y., Yu, S. S., Chen, S. R., Pi, R. B., Gao, S., Li, H., et al. (2012). Nmnat2 protects cardiomyocytes from hypertrophy via activation of SIRT6. FEBS Letters, 586(6), 866–874.

pubmed: 22449973 doi: 10.1016/j.febslet.2012.02.014

Pillai, V., Samant, S. A., Gupta, M., & Gupta, M. P. (2019). Sirt6 protects the heart from aging-induced cardiac hypertrophy by enhancing mitochondrial fitness. Circulation, 140, A11897.

Acin-Perez, R., Lechuga-Vieco, A. V., Mar Muñoz, M. D., Nieto-Arellano, R., Torroja, C., Sánchez-Cabo, F., et al. (2018). Ablation of the stress protease OMA1 protects against heart failure in mice. Science Translational Medicine, 10(434), eaan4935.

pubmed: 29593106 doi: 10.1126/scitranslmed.aan4935

Han, J. (2017). Mitochondrial DNA mitochondrial dysfunction and cardiac manifestations. Frontiers in Bioscience, 22(7), 1177–1194.

doi: 10.2741/4541

Yu, S., Cai, Y., Ye, J., Pi, R., Chen, S., Liu, P., et al. (2013). Sirtuin 6 protects cardiomyocytes from hypertrophy in vitro via inhibition of NF-κB-dependent transcriptional activity. British Journal of Pharmacology, 168(1), 117–128.

pubmed: 22335191 pmcid: 3570008 doi: 10.1111/j.1476-5381.2012.01903.x

Brito, V. B., Nascimento, L. V. M., Nunes, R. B., Moura, D. J., Lago, P. D., & Saffi, J. (2016). Exercise during pregnancy decreases doxorubicin-induced cardiotoxic effects on neonatal hearts. Toxicology, 368–369, 46–57.

pubmed: 27565713 doi: 10.1016/j.tox.2016.08.017

Rocha, B., Rodrigues, A. R., Tomada, I., Martins, M. J., Guimarães, J. T., Gouveia, A. M., et al. (2018). Energy restriction, exercise and atorvastatin treatment improve endothelial dysfunction and inhibit miRNA-155 in the erectile tissue of the aged rat. Nutrition & Metabolism (London), 15(1), 28.

doi: 10.1186/s12986-018-0265-z

Koltai, E., Szabo, Z., Atalay, M., Boldogh, I., Naito, H., Goto, S., et al. (2010). Exercise alters SIRT1, SIRT6, NAD and NAMPT levels in skeletal muscle of aged rats. Mechanisms of Ageing and Development., 131(1), 21–28.

pubmed: 19913571 doi: 10.1016/j.mad.2009.11.002

Zhang, N., Li, Z., Mu, W., Li, L., Liang, Y., Lu, M., et al. (2016). Calorie restriction-induced SIRT6 activation delays aging by suppressing NF-κB signaling. Cell Cycle, 15(7), 1009–1018.

pubmed: 26940461 pmcid: 4889297 doi: 10.1080/15384101.2016.1152427

Kitada, M., Ogura, Y., Monno, I., & Koya, D. (2019). Sirtuins and type 2 diabetes: Role in inflammation, oxidative stress, and mitochondrial function. Frontiers in Endocrinology, 10, 1–12.

doi: 10.3389/fendo.2019.00187

Yasuda, M., Wilson, D. R., Fugmann, S. D., & Moaddel, R. (2011). Synthesis and characterization of SIRT6 protein coated magnetic beads: Identification of a novel inhibitor of SIRT6 deacetylase from medicinal plant extracts. Analytical Chemistry, 83(19), 7400–7407.

pubmed: 21854049 pmcid: 3197717 doi: 10.1021/ac201403y

Chang, Y.-L., et al. (2016). An improved fluorogenic assay for SIRT1, SIRT2, and SIRT3. Organic & Biomolecular Chemistry, 14(7), 2186–2190.

doi: 10.1039/C5OB02609A

Gertz, M., Fischer, F., Nguyen, G. T. T., Lakshminarasimhan, M., Schutkowski, M., Weyand, M., et al. (2013). Ex-527 inhibits Sirtuins by exploiting their unique NAD+-dependent deacetylation mechanism. Proceedings of the National Academy of Sciences, 110(30), E2772–E2781.

doi: 10.1073/pnas.1303628110

Kokkonen, P., Rahnasto-Rilla, M., Mellini, P., Jarho, E., Lahtela-Kakkonen, M., & Kokkola, T. (2014). Studying SIRT6 regulation using H3K56 based substrate and small molecules. European Journal of Pharmaceutical Sciences, 63, 71–76.

pubmed: 25004411 doi: 10.1016/j.ejps.2014.06.015

Singh, N., Ravichandran, S., Norton, D. D., Fugmann, S. D., & Moaddel, R. (2013). Synthesis and characterization of a SIRT6 open tubular column: Predicting deacetylation activity using frontal chromatography. Analytical Biochemistry, 436(2), 78–83.

pubmed: 23376017 pmcid: 4167792 doi: 10.1016/j.ab.2013.01.018

Rahnasto-Rilla, M., Kokkola, T., Jarho, E., Lahtela-Kakkonen, M., & Moaddel, R. (2016). N-Acylethanolamines bind to SIRT6. ChemBioChem, 17(1), 77–81.

pubmed: 26607666 doi: 10.1002/cbic.201500482

Sociali, G., Galeno, L., Parenti, M. D., Grozio, A., Bauer, I., Passalacqua, M., et al. (2015). Quinazolinedione SIRT6 inhibitors sensitize cancer cells to chemotherapeutics. European Journal of Medicinal Chemistry., 102, 530–539.

pubmed: 26310895 doi: 10.1016/j.ejmech.2015.08.024

Yang, S. J., Choi, J. M., Chae, S. W., Kim, W. J., Park, S. E., Rhee, E. J., et al. (2011). Activation of peroxisome proliferator-activated receptor gamma by rosiglitazone increases Sirt6 expression and ameliorates hepatic steatosis in rats. PLoS ONE, 6(2), e17057.

pubmed: 21373642 pmcid: 3044155 doi: 10.1371/journal.pone.0017057

Li, Y., Li, X., Cole, A., McLaughlin, S., & Du, W. (2018). Icariin improves Fanconi anemia hematopoietic stem cell function through SIRT6-mediated NF-kappa B inhibition. Cell Cycle, 17(3), 367–376.

pubmed: 29355456 pmcid: 5914729 doi: 10.1080/15384101.2018.1426413

Chen, Y., Sun, T., Wu, J., Kalionis, B., Zhang, C., Yuan, D., et al. (2015). Icariin intervenes in cardiac inflammaging through upregulation of SIRT6 enzyme activity and inhibition of the NF-kappa B pathway. BioMed Research International, 2015, 1–12.

Tang, Y. L., Zhou, Y., Wang, Y. P., Wang, J. W., & Ding, J. C. (2015). SIRT6/NF-κB signaling axis in ginsenoside Rg1-delayed hematopoietic stem/progenitor cell senescence. International Journal of Clinical and Experimental Pathology, 8(5), 5591–5596.

pubmed: 26191269 pmcid: 4503140

D’Onofrio, N., Servillo, L., Giovane, A., Casale, R., Vitiello, M., Marfella, R., et al. (2016). Ergothioneine oxidation in the protection against high-glucose induced endothelial senescence: Involvement of SIRT1 and SIRT6. Free Radical Biology and Medicine, 96, 211–222.

pubmed: 27101740 doi: 10.1016/j.freeradbiomed.2016.04.013

Smeriglio, A., Barreca, D., Bellocco, E., & Trombetta, D. (2016). Chemistry, pharmacology and health benefits of anthocyanins. Phytotherapy Research, 30(8), 1265–1286.

pubmed: 27221033 doi: 10.1002/ptr.5642

Rahnasto-Rilla, M., Tyni, J., Huovinen, M., Jarho, E., Kulikowicz, T., Ravichandran, S., et al. (2018). Natural polyphenols as sirtuin 6 modulators. Scientific Reports, 8(1), 1–11.

doi: 10.1038/s41598-018-22388-5

You, W., & Steegborn, C. (2020). Structural basis for activation of human sirtuin 6 by fluvastatin. ACS Medicinal Chemistry Letters, 11(11), 2285–2289.

pubmed: 33214841 pmcid: 7667847 doi: 10.1021/acsmedchemlett.0c00407

Gertz, M., Fischer, F., Nguyen, G. T. T., Lakshminarasimhan, M., Schutkowski, M., Weyand, M., et al. (2013). Ex-527 inhibits Sirtuins by exploiting their unique NAD

doi: 10.1073/pnas.1303628110

SIRT6 in Regulation of Mitochondrial Damage and Associated Cardiac Dysfunctions: A Possible Therapeutic Target for CVDs.

Journal

Informations de publication

Résumé

Identifiants

Types de publication

Langues

Sous-ensembles de citation

Informations de copyright

Références

Auteurs

K P Divya (KP)

Navjot Kanwar (N)

P V Anuranjana (PV)

Gautam Kumar (G)

Fathima Beegum (F)

Krupa Thankam George (KT)

Nitesh Kumar (N)

K Nandakumar (K)

Abhinav Kanwal (A)

Classifications MeSH