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Sirtuins in kidney health and disease – Nature Reviews Nephrology

  • Guarente, L. & Franklin, H. Epstein lecture: sirtuins, aging, and medicine. N. Engl. J. Med. 364, 2235–2244 (2011).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

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

    Article 
    CAS 
    PubMed 
    ADS 

    Google Scholar
     

  • Tissenbaum, H. A. & Guarente, L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227–230 (2001).

    Article 
    CAS 
    PubMed 
    ADS 

    Google Scholar
     

  • Rogina, B. & Helfand, S. L. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl Acad. Sci. USA 101, 15998–16003 (2004).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Kanfi, Y. et al. The sirtuin SIRT6 regulates lifespan in male mice. Nature 483, 218–221 (2012).

    Article 
    CAS 
    PubMed 
    ADS 

    Google Scholar
     

  • Burnett, C. et al. Absence of effects of Sir2 overexpression on lifespan in C. elegans and Drosophila. Nature 477, 482–485 (2011).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Satoh, A. et al. Sirt1 extends life span and delays aging in mice through the regulation of Nk2 homeobox 1 in the DMH and LH. Cell Metab. 18, 416–430 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Benigni, A. et al. Sirt3 deficiency shortens life span and impairs cardiac mitochondrial function rescued by Opa1 gene transfer. Antioxid. Redox Signal. 31, 1255–1271 (2019).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Mostoslavsky, R. et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124, 315–329 (2006).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Yuan, H. & Marmorstein, R. Structural basis for sirtuin activity and inhibition. J. Biol. Chem. 287, 42428–42435 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kiran, S. et al. Intracellular distribution of human SIRT7 and mapping of the nuclear/nucleolar localization signal. FEBS J. 280, 3451–3466 (2013).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Tanner, K. G., Landry, J., Sternglanz, R. & Denu, J. M. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose. Proc. Natl Acad. Sci. USA 97, 14178–14182 (2000).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Vaquero, A. et al. Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin. Mol. Cell 16, 93–105 (2004).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Jin, Q. et al. Cytoplasm-localized SIRT1 enhances apoptosis. J. Cell Physiol. 213, 88–97 (2007).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Tanno, M., Sakamoto, J., Miura, T., Shimamoto, K. & Horio, Y. Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J. Biol. Chem. 282, 6823–6832 (2007).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Li, Y., Xu, W., McBurney, M. W. & Longo, V. D. SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neurons. Cell Metab. 8, 38–48 (2008).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Hisahara, S. et al. Histone deacetylase SIRT1 modulates neuronal differentiation by its nuclear translocation. Proc. Natl Acad. Sci. USA 105, 15599–15604 (2008).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Tennen, R. I. & Chua, K. F. Chromatin regulation and genome maintenance by mammalian SIRT6. Trends Biochem. Sci. 36, 39–46 (2011).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Tsai, Y.-C., Greco, T. M., Boonmee, A., Miteva, Y. & Cristea, I. M. Functional proteomics establishes the interaction of SIRT7 with chromatin remodeling complexes and expands its role in regulation of RNA polymerase I transcription. Mol. Cell. Proteom. 11, 60–76 (2012).

    Article 
    CAS 

    Google Scholar
     

  • Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A.-S. & Tainsky, M. A. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 23, 3173–3185 (2003).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Nekooki-Machida, Y. & Hagiwara, H. Role of tubulin acetylation in cellular functions and diseases. Med. Mol. Morphol. 53, 191–197 (2020).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Serrano, L. et al. The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes. Dev. 27, 639–653 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • North, B. J. et al. SIRT2 induces the checkpoint kinase BubR1 to increase lifespan. EMBO J. 33, 1438–1453 (2014).

    Article 
    MathSciNet 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Baeza, J., Smallegan, M. J. & Denu, J. M. Mechanisms and dynamics of protein acetylation in mitochondria. Trends Biochem. Sci. 41, 231–244 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lombard, D. B. et al. Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation. Mol. Cell. Biol. 27, 8807–8814 (2007).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Iwahara, T., Bonasio, R., Narendra, V. & Reinberg, D. SIRT3 functions in the nucleus in the control of stress-related gene expression. Mol. Cell. Biol. 32, 5022–5034 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, X. et al. Molecular basis for hierarchical histone de-β-hydroxybutyrylation by SIRT3. Cell Discov. 5, 35 (2019).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Scher, M. B., Vaquero, A. & Reinberg, D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes. Dev. 21, 920–928 (2007).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Guarente, L. Calorie restriction and sirtuins revisited. Genes. Dev. 27, 2072–2085 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Nakagawa, T., Lomb, D. J., Haigis, M. C. & Guarente, L. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137, 560–570 (2009).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Du, J. et al. Sirt5 is an NAD-dependent protein lysine demalonylase and desuccinylase. Science 334, 806–809 (2011).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Houtkooper, R. H., Pirinen, E. & Auwerx, J. Sirtuins as regulators of metabolism and healthspan. Nat. Rev. Mol. Cell Biol. 13, 225–238 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ahn, B.-H. et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc. Natl Acad. Sci. USA 105, 14447–14452 (2008).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Finley, L. W. S. et al. Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase activity. PLoS One 6, e23295 (2011).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Rahman, M. et al. Drosophila Sirt2/mammalian SIRT3 deacetylates ATP synthase β and regulates complex V activity. J. Cell Biol. 206, 289–305 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Yang, Y. et al. NAD+-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10. J. Biol. Chem. 285, 7417–7429 (2010).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Dittenhafer-Reed, K. E. et al. SIRT3 mediates multi-tissue coupling for metabolic fuel switching. Cell Metab. 21, 637–646 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Hirschey, M. D. et al. SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464, 121–125 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Shimazu, T. et al. SIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body production. Cell Metab. 12, 654–661 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Picard, F. et al. Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ. Nature 429, 771–776 (2004).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Rodgers, J. T. et al. Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1. Nature 434, 113–118 (2005).

    Article 
    CAS 
    PubMed 
    ADS 

    Google Scholar
     

  • Frescas, D., Valenti, L. & Accili, D. Nuclear trapping of the forkhead transcription factor FoxO1 via Sirt-dependent deacetylation promotes expression of glucogenetic genes. J. Biol. Chem. 280, 20589–20595 (2005).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zhong, L. et al. The histone deacetylase Sirt6 regulates glucose homeostasis via Hif1α. Cell 140, 280–293 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lee, Y. et al. Myeloid sirtuin 6 deficiency causes insulin resistance in high-fat diet-fed mice by eliciting macrophage polarization toward an M1 phenotype. Diabetes 66, 2659–2668 (2017).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zhan, M., Brooks, C., Liu, F., Sun, L. & Dong, Z. Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology. Kidney Int. 83, 568–581 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, Q. et al. Resveratrol activation of SIRT1/MFN2 can improve mitochondria function, alleviating doxorubicin-induced myocardial injury. Cancer Innov. 2, 253–264 (2023).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Samant, S. A. et al. SIRT3 deacetylates and activates OPA1 to regulate mitochondrial dynamics during stress. Mol. Cell. Biol. 34, 807–819 (2014).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Morigi, M. et al. Sirtuin 3-dependent mitochondrial dynamic improvements protect against acute kidney injury. J. Clin. Invest. 125, 715–726 (2015).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chen, Z. et al. Sirt6 deficiency contributes to mitochondrial fission and oxidative damage in podocytes via ROCK1-Drp1 signalling pathway. Cell Prolif. 55, e13296 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Wu, Z. et al. Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1. Cell 98, 115–124 (1999).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Dominy, J. E. et al. The deacetylase Sirt6 activates the acetyltransferase GCN5 and suppresses hepatic gluconeogenesis. Mol. Cell 48, 900–913 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

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

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Wan, W. et al. Regulation of mitophagy by sirtuin family proteins: a vital role in aging and age-related diseases. Front. Aging Neurosci. 14, 845330 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Forrester, S. J., Kikuchi, D. S., Hernandes, M. S., Xu, Q. & Griendling, K. K. Reactive oxygen species in metabolic and inflammatory signaling. Circ. Res. 122, 877–902 (2018).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ogura, Y., Kitada, M. & Koya, D. Sirtuins and renal oxidative stress. Antioxidants 10, 1198 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Wu, Q.-J. et al. The sirtuin family in health and disease. Signal. Transduct. Target. Ther. 7, 402 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • He, F., Ru, X. & Wen, T. NRF2, a transcription factor for stress response and beyond. Int. J. Mol. Sci. 21, 4777 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chen, Y. et al. Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep. 12, 534–541 (2011).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Xu, Y. et al. Studies on the regulatory mechanism of isocitrate dehydrogenase 2 using acetylation mimics. Sci. Rep. 7, 9785 (2017).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Alves-Fernandes, D. K. & Jasiulionis, M. G. The role of SIRT1 on DNA damage response and epigenetic alterations in cancer. Int. J. Mol. Sci. 20, 3153 (2019).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Meng, F. et al. Synergy between SIRT1 and SIRT6 helps recognize DNA breaks and potentiates the DNA damage response and repair in humans and mice. eLife 9, e55828 (2020).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Jeong, J. et al. SIRT1 promotes DNA repair activity and deacetylation of Ku70. Exp. Mol. Med. 39, 8–13 (2007).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Kume, S. et al. Silent information regulator 2 (SIRT1) attenuates oxidative stress-induced mesangial cell apoptosis via p53 deacetylation. Free. Radic. Biol. Med. 40, 2175–2182 (2006).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Kume, S. et al. SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation. J. Biol. Chem. 282, 151–158 (2007).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Chuang, P. Y. et al. Alteration of forkhead box O (foxo4) acetylation mediates apoptosis of podocytes in diabetes mellitus. PLoS One 6, e23566 (2011).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Jiao, X., Li, Y., Zhang, T., Liu, M. & Chi, Y. Role of Sirtuin3 in high glucose-induced apoptosis in renal tubular epithelial cells. Biochem. Biophys. Res. Commun. 480, 387–393 (2016).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Liu, M. et al. Sirt6 deficiency exacerbates podocyte injury and proteinuria through targeting Notch signaling. Nat. Commun. 8, 413 (2017).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Guo, H. & Bechtel-Walz, W. The interplay of autophagy and oxidative stress in the kidney: what do we know? Nephron 147, 627–642 (2023).

    Article 
    PubMed 

    Google Scholar
     

  • Lee, I. H. Mechanisms and disease implications of sirtuin-mediated autophagic regulation. Exp. Mol. Med. 51, 1–11 (2019).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lee, I. H. et al. A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc. Natl Acad. Sci. USA 105, 3374–3379 (2008).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Chun, S. K. et al. Loss of sirtuin 1 and mitofusin 2 contributes to enhanced ischemia/reperfusion injury in aged livers. Aging Cell 17, e12761 (2018).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Wang, Y., Chang, J., Wang, Z.-Q. & Li, Y. Sirt3 promotes the autophagy of HK-2 human proximal tubular epithelial cells via the inhibition of Notch-1/Hes-1 signaling. Mol. Med. Rep. 24, 634 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Li, R. et al. Therapeutic effect of Sirtuin 3 on ameliorating nonalcoholic fatty liver disease: The role of the ERK-CREB pathway and Bnip3-mediated mitophagy. Redox Biol. 18, 229–243 (2018).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Takasaka, N. et al. Autophagy induction by SIRT6 through attenuation of insulin-like growth factor signaling is involved in the regulation of human bronchial epithelial cell senescence. J. Immunol. 192, 958–968 (2014).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Xu, C. et al. SIRT1 is downregulated by autophagy in senescence and ageing. Nat. Cell Biol. 22, 1170–1179 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lee, S.-H., Lee, J.-H., Lee, H.-Y. & Min, K.-J. Sirtuin signaling in cellular senescence and aging. BMB Rep. 52, 24–34 (2019).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Hayakawa, T. et al. SIRT1 suppresses the senescence-associated secretory phenotype through epigenetic gene regulation. PLoS One 10, e0116480 (2015).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Huang, J. et al. SIRT1 overexpression antagonizes cellular senescence with activated ERK/S6k1 signaling in human diploid fibroblasts. PLoS One 3, e1710 (2008).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Zu, Y. et al. SIRT1 promotes proliferation and prevents senescence through targeting LKB1 in primary porcine aortic endothelial cells. Circ. Res. 106, 1384–1393 (2010).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Grootaert, M. O. J., Finigan, A., Figg, N. L., Uryga, A. K. & Bennett, M. R. SIRT6 protects smooth muscle cells from senescence and reduces atherosclerosis. Circ. Res. 128, 474–491 (2021).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zhao, G. et al. SIRT6 delays cellular senescence by promoting p27Kip1 ubiquitin-proteasome degradation. Aging 8, 2308–2323 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Diao, Z. et al. SIRT3 consolidates heterochromatin and counteracts senescence. Nucleic Acids Res. 49, 4203–4219 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ma, C. et al. Sirt3 attenuates oxidative stress damage and rescues cellular senescence in rat bone marrow mesenchymal stem cells by targeting superoxide dismutase 2. Front. Cell Dev. Biol. 8, 599376 (2020).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Fan, X. et al. Sirt3 activates autophagy to prevent DOX-induced senescence by inactivating PI3K/AKT/mTOR pathway in A549 cells. Biochim. Biophys. Acta Mol. Cell Res. 1870, 119411 (2023).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Gómez, H. Reprogramming metabolism to enhance kidney tolerance during sepsis: the role of fatty acid oxidation, aerobic glycolysis, and epithelial de-differentiation. Nephron 147, 31–34 (2023).

    Article 
    PubMed 

    Google Scholar
     

  • Vachharajani, V. T. et al. Sirtuins link inflammation and metabolism. J. Immunol. Res. 2016, 8167273 (2016).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kauppinen, A., Suuronen, T., Ojala, J., Kaarniranta, K. & Salminen, A. Antagonistic crosstalk between NF-κB and SIRT1 in the regulation of inflammation and metabolic disorders. Cell. Signal. 25, 1939–1948 (2013).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Rabadi, M. M. et al. High-mobility group box 1 is a novel deacetylation target of Sirtuin1. Kidney Int. 87, 95–108 (2015).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Labiner, H. E., Sas, K. M., Baur, J. A. & Sims, C. A. Sirtuin 1 deletion increases inflammation and mortality in sepsis. J. Trauma. Acute Care Surg. 93, 672–678 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhao, W.-Y., Zhang, L., Sui, M.-X., Zhu, Y.-H. & Zeng, L. Protective effects of sirtuin 3 in a murine model of sepsis-induced acute kidney injury. Sci. Rep. 6, 33201 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Zhang, W. et al. An immune atlas of nephrolithiasis: single-cell mass cytometry on SIRT3 knockout and calcium oxalate-induced renal injury. J. Immunol. Res. 2021, 1260140 (2021).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Doke, T. et al. NAD+ precursor supplementation prevents mtRNA/RIG-I-dependent inflammation during kidney injury. Nat. Metab. 5, 414–430 (2023).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Pantaleon, M. & Kaye, P. L. Glucose transporters in preimplantation development. Rev. Reprod. 3, 77–81 (1998).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Ochocki, J. D. & Simon, M. C. Nutrient-sensing pathways and metabolic regulation in stem cells. J. Cell Biol. 203, 23–33 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chevalier, R. L. Bioenergetic evolution explains prevalence of low nephron number at birth: risk factor for CKD. Kidney360 1, 863–879 (2020).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Mandal, S., Lindgren, A. G., Srivastava, A. S., Clark, A. T. & Banerjee, U. Mitochondrial function controls proliferation and early differentiation potential of embryonic stem cells. Stem Cell 29, 486–495 (2011).

    Article 
    CAS 

    Google Scholar
     

  • Chung, S. et al. Mitochondrial oxidative metabolism is required for the cardiac differentiation of stem cells. Nat. Clin. Pract. Cardiovasc. Med. 4, S60–S67 (2007).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Folmes, C. D. L. & Terzic, A. Metabolic determinants of embryonic development and stem cell fate. Reprod. Fertil. Dev. 27, 82–88 (2014).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Liu, J. et al. Regulation of nephron progenitor cell self-renewal by intermediary metabolism. J. Am. Soc. Nephrol. 28, 3323–3335 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Perico, L. et al. Post-translational modifications by SIRT3 de-2-hydroxyisobutyrylase activity regulate glycolysis and enable nephrogenesis. Sci. Rep. 11, 23580 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Pezzotta, A. et al. Low nephron number induced by maternal protein restriction is prevented by nicotinamide riboside supplementation depending on sirtuin 3 activation. Cells 11, 3316 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Luyckx, V. A. & Brenner, B. M. Birth weight, malnutrition and kidney-associated outcomes — a global concern. Nat. Rev. Nephrol. 11, 135–149 (2015).

    Article 
    PubMed 

    Google Scholar
     

  • Erichsen, L. & Adjaye, J. Crosstalk between age accumulated DNA-damage and the SIRT1-AKT-GSK3ß axis in urine derived renal progenitor cells. Aging 14, 8179–8204 (2022).

    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Bhargava, P. & Schnellmann, R. G. Mitochondrial energetics in the kidney. Nat. Rev. Nephrol. 3, 629–646 (2017).

    Article 

    Google Scholar
     

  • Haschler, T. N. et al. Sirtuin 5 depletion impairs mitochondrial function in human proximal tubular epithelial cells. Sci. Rep. 11, 15510 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chiba, T. et al. Sirtuin 5 regulates proximal tubule fatty acid oxidation to protect against AKI. J. Am. Soc. Nephrol. 30, 2384–2398 (2019).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ozawa, S. et al. Glycolysis, but not mitochondria, responsible for intracellular ATP distribution in cortical area of podocytes. Sci. Rep. 5, 18575 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Perico, L., Conti, S., Benigni, A. & Remuzzi, G. Podocyte-actin dynamics in health and disease. Nat. Rev. Nephrol. 12, 692–710 (2016).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Tsai, Y.-C. et al. Upregulating sirtuin 6 ameliorates glycolysis, EMT and distant metastasis of pancreatic adenocarcinoma with krüppel-like factor 10 deficiency. Exp. Mol. Med. 53, 1623–1635 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Huang, W. et al. Sirt6 deficiency results in progression of glomerular injury in the kidney. Aging 9, 1069–1083 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, D., Li, S., Cruz, P. & Kone, B. C. Sirtuin 1 functionally and physically interacts with disruptor of telomeric silencing-1 to regulate alpha-ENaC transcription collecting duct. J. Biol. Chem. 284, 20917–20926 (2009).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Yang, S.-Y. et al. A low-salt diet increases the expression of renal sirtuin 1 through activation of the ghrelin receptor in rats. Sci. Rep. 6, 32787 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Noriega, L. G. et al. SIRT7 modulates the stability and activity of the renal K-Cl cotransporter KCC4 through deacetylation. EMBO Rep. 22, e50766 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Mercado, A. et al. The K+:Cl cotransporter KCC4 is activated by deacetylation induced by the sirtuin7 (SIRT7). FASEB J. 29, 666.24 (2015).

    Article 

    Google Scholar
     

  • Mattagajasingh, I. et al. SIRT1 promotes endothelium-dependent vascular relaxation by activating endothelial nitric oxide synthase. Proc. Natl Acad. Sci. USA 104, 14855–14860 (2007).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Dioum, E. M. et al. Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science 324, 1289–1293 (2009).

    Article 
    CAS 
    PubMed 
    ADS 

    Google Scholar
     

  • Potente, M. et al. SIRT1 controls endothelial angiogenic functions during vascular growth. Genes. Dev. 21, 2644–2658 (2007).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Pezzotta, A. et al. Sirt3 deficiency promotes endothelial dysfunction and aggravates renal injury. PLoS One 18, e0291909 (2023).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ho, K. M. & Morgan, D. J. R. The proximal tubule as the pathogenic and therapeutic target in acute kidney injury. Nephron 146, 494–502 (2022).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Koehler, F. C., Späth, M. R., Hoyer-Allo, K. J. R. & Müller, R.-U. Mechanisms of caloric restriction-mediated stress-resistance in acute kidney injury. Nephron 146, 234–238 (2022).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Hasegawa, K. et al. Kidney-specific overexpression of Sirt1 protects against acute kidney injury by retaining peroxisome function. J. Biol. Chem. 285, 13045–13056 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Funk, J. A. & Schnellmann, R. G. Accelerated recovery of renal mitochondrial and tubule homeostasis with SIRT1/PGC-1α activation following ischemia-reperfusion injury. Toxicol. Appl. Pharmacol. 273, 345–354 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Fan, H. et al. The histone deacetylase, SIRT1, contributes to the resistance of young mice to ischemia/reperfusion-induced acute kidney injury. Kidney Int. 83, 404–413 (2013).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Han, S. et al. miR-132-3p promotes the cisplatin-induced apoptosis and inflammatory response of renal tubular epithelial cells by targeting SIRT1 via the NF-κB pathway. Int. Immunopharmacol. 99, 108022 (2021).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • He, S. et al. NAD+ ameliorates endotoxin-induced acute kidney injury in a sirtuin1-dependent manner via GSK-3β/Nrf2 signalling pathway. J. Cell. Mol. Med. 26, 1979–1993 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, J., Yang, S., Chen, F., Li, H. & Chen, B. Ginkgetin aglycone ameliorates LPS-induced acute kidney injury by activating SIRT1 via inhibiting the NF-κB signaling pathway. Cell Biosci. 7, 44 (2017).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lempiäinen, J., Finckenberg, P., Levijoki, J. & Mervaala, E. AMPK activator AICAR ameliorates ischaemia reperfusion injury in the rat kidney. Br. J. Pharmacol. 166, 1905–1915 (2012).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Gan, Y., Tao, S., Cao, D., Xie, H. & Zeng, Q. Protection of resveratrol on acute kidney injury in septic rats. Hum. Exp. Toxicol. 36, 1015–1022 (2017).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Li, Z. et al. Overexpressed SIRT6 attenuates cisplatin-induced acute kidney injury by inhibiting ERK1/2 signaling. Kidney Int. 93, 881–892 (2018).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Miao, J. et al. Sirtuin 6 is a key contributor to gender differences in acute kidney injury. Cell Death Discov. 9, 134 (2023).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Jian, Y. et al. Sirt3 mitigates LPS-induced mitochondrial damage in renal tubular epithelial cells by deacetylating YME1L1. Cell Prolif. 56, e13362 (2023).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Shen, L., Zhang, Q., Tu, S. & Qin, W. SIRT3 mediates mitofusin 2 ubiquitination and degradation to suppress ischemia reperfusion-induced acute kidney injury. Exp. Cell Res. 408, 112861 (2021).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Brooks, C., Wei, Q., Cho, S.-G. & Dong, Z. Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models. J. Clin. Invest. 119, 1275–1285 (2009).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ugur, S. et al. The renoprotective effect of curcumin in cisplatin-induced nephrotoxicity. Ren. Fail. 37, 332–336 (2015).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zhao, L. et al. Protective effect of the total flavonoids from Rosa laevigata Michx fruit on renal ischemia-reperfusion injury through suppression of oxidative stress and inflammation. Molecules 21, 952 (2016).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Li, Y. et al. Activation of sirtuin 3 by silybin attenuates mitochondrial dysfunction in cisplatin-induced acute kidney injury. Front. Pharmacol. 8, 178 (2017).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • Xu, S. et al. SIRT1/3 activation by resveratrol attenuates acute kidney injury in a septic rat model. Oxid. Med. Cell. Longev. 2016, 7296092 (2016).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Pan, J. S.-C. et al. Stanniocalcin-1 inhibits renal ischemia/reperfusion injury via an AMP-activated protein kinase-dependent pathway. J. Am. Soc. Nephrol. 26, 364–378 (2015).

    Article 
    PubMed 

    Google Scholar
     

  • Perico, L. et al. Human mesenchymal stromal cells transplanted into mice stimulate renal tubular cells and enhance mitochondrial function. Nat. Commun. 8, 983 (2017).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Miyasato, Y. et al. Sirtuin 7 deficiency ameliorates cisplatin-induced acute kidney injury through regulation of the inflammatory response. Sci. Rep. 8, 5927 (2018).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Sánchez-Navarro, A. et al. Sirtuin 7 deficiency reduces inflammation and tubular damage induced by an episode of acute kidney injury. Int. J. Mol. Sci. 23, 2573 (2022).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Poyan Mehr, A. et al. De novo NAD+ biosynthetic impairment in acute kidney injury in humans. Nat. Med. 24, 1351–1359 (2018).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Katsyuba, E. et al. De novo NAD+ synthesis enhances mitochondrial function and improves health. Nature 563, 354–359 (2018).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Cortinovis, M., Perico, N., Ruggenenti, P., Remuzzi, A. & Remuzzi, G. Glomerular hyperfiltration. Nat. Rev. Nephrol. 18, 435–451 (2022).

    Article 
    PubMed 

    Google Scholar
     

  • Kitada, M., Kume, S., Takeda-Watanabe, A., Kanasaki, K. & Koya, D. Sirtuins and renal diseases: relationship with aging and diabetic nephropathy. Clin. Sci. 124, 153–164 (2013).

    Article 
    CAS 

    Google Scholar
     

  • Lagouge, M. et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1α. Cell 127, 1109–1122 (2006).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Baur, J. A. et al. Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444, 337–342 (2006).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Zoja, C., Xinaris, C. & Macconi, D. Diabetic nephropathy: novel molecular mechanisms and therapeutic targets. Front. Pharmacol. 11, 586892 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Yasuda, I. et al. Pre-emptive short-term nicotinamide mononucleotide treatment in a mouse model of diabetic nephropathy. J. Am. Soc. Nephrol. 32, 1355–1370 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Hasegawa, K. et al. Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. Nat. Med. 19, 1496–1504 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Yubero-Serrano, E. M. et al. Effects of sevelamer carbonate on advanced glycation end products and antioxidant/pro-oxidant status in patients with diabetic kidney disease. Clin. J. Am. Soc. Nephrol. 10, 759–766 (2015).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Fan, Y. et al. Sirt6 suppresses high glucose-induced mitochondrial dysfunction and apoptosis in podocytes through AMPK activation. Int. J. Biol. Sci. 15, 701–713 (2019).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Wang, X., Ji, T., Li, X., Qu, X. & Bai, S. FOXO3a protects against kidney injury in type II diabetic nephropathy by promoting Sirt6 expression and inhibiting Smad3 acetylation. Oxid. Med. Cell. Longev. 2021, 5565761 (2021).

    PubMed 
    PubMed Central 

    Google Scholar
     

  • Liu, J. et al. CircRNA circ-ITCH improves renal inflammation and fibrosis in streptozotocin-induced diabetic mice by regulating the miR-33a-5p/SIRT6 axis. Inflamm. Res. 70, 835–846 (2021).

    Article 
    CAS 
    PubMed 
    ADS 

    Google Scholar
     

  • Muraoka, H. et al. Role of Nampt-Sirt6 axis in renal proximal tubules in extracellular matrix deposition in diabetic nephropathy. Cell Rep. 27, 199–212.e5 (2019).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Ji, L. et al. Overexpression of Sirt6 promotes M2 macrophage transformation, alleviating renal injury in diabetic nephropathy. Int. J. Oncol. 55, 103–115 (2019).

    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Locatelli, M. et al. Manipulating Sirtuin 3 pathway ameliorates renal damage in experimental diabetes. Sci. Rep. 10, 8418 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Wang, X. X. et al. G protein-coupled bile acid receptor TGR5 activation inhibits kidney disease in obesity and diabetes. J. Am. Soc. Nephrol. 27, 1362–1378 (2016).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Locatelli, M. et al. Sirtuin 3 deficiency aggravates kidney disease in response to high-fat diet through lipotoxicity-induced mitochondrial damage. Int. J. Mol. Sci. 23, 8345 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhou, Y. et al. Metrnl alleviates lipid accumulation by modulating mitochondrial homeostasis in diabetic nephropathy. Diabetes 72, 611–626 (2023).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Macconi, D., Remuzzi, G. & Benigni, A. Key fibrogenic mediators: old players. Renin-angiotensin system. Kidney Int. Suppl. 4, 58–64 (2014).

    Article 
    CAS 

    Google Scholar
     

  • Liu, X. et al. Impaired nicotinamide adenine dinucleotide biosynthesis in the kidney of chronic kidney disease. Front. Physiol. 12, 723690 (2021).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, Y. et al. Sirtuin 1 activation reduces transforming growth factor-β1-induced fibrogenesis and affords organ protection in a model of progressive, experimental kidney and associated cardiac disease. Am. J. Pathol. 187, 80–90 (2017).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • He, W. et al. Sirt1 activation protects the mouse renal medulla from oxidative injury. J. Clin. Invest. 120, 1056–1068 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Simic, P. et al. SIRT1 suppresses the epithelial-to-mesenchymal transition in cancer metastasis and organ fibrosis. Cell Rep. 3, 1175–1186 (2013).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Huang, X.-Z. et al. Sirt1 activation ameliorates renal fibrosis by inhibiting the TGF-β/Smad3 pathway. J. Cell. Biochem. 115, 996–1005 (2014).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Vasko, R. et al. Endothelial sirtuin 1 deficiency perpetrates nephrosclerosis through downregulation of matrix metalloproteinase-14: relevance to fibrosis of vascular senescence. J. Am. Soc. Nephrol. 25, 276–291 (2014).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Kida, Y., Zullo, J. A. & Goligorsky, M. S. Endothelial sirtuin 1 inactivation enhances capillary rarefaction and fibrosis following kidney injury through Notch activation. Biochem. Biophys. Res. Commun. 478, 1074–1079 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Li, P. et al. SIRT1 attenuates renal fibrosis by repressing HIF-2α. Cell Death Discov. 7, 59 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Lipphardt, M., Dihazi, H., Müller, G. A. & Goligorsky, M. S. Fibrogenic secretome of sirtuin 1-deficient endothelial cells: Wnt, notch and glycocalyx rheostat. Front. Physiol. 9, 1325 (2018).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Cai, J. et al. The deacetylase sirtuin 6 protects against kidney fibrosis by epigenetically blocking β-catenin target gene expression. Kidney Int. 97, 106–118 (2020).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Li, X., Li, W., Zhang, Z., Wang, W. & Huang, H. SIRT6 overexpression retards renal interstitial fibrosis through targeting HIPK2 in chronic kidney disease. Front. Pharmacol. 13, 1007168 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Cai, J. et al. Phosphorylation by GSK-3β increases the stability of SIRT6 to alleviate TGF-β-induced fibrotic response in renal tubular cells. Life Sci. 308, 120914 (2022).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Benigni, A., Perico, L. & Macconi, D. Mitochondrial dynamics is linked to longevity and protects from end-organ injury: the emerging role of sirtuin 3. Antioxid. Redox Signal. 25, 185–199 (2016).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Sundaresan, N. R. et al. SIRT3 blocks aging-associated tissue fibrosis in mice by deacetylating and activating glycogen synthase kinase 3β. Mol. Cell. Biol. 36, 678–692 (2015).

    Article 
    PubMed 

    Google Scholar
     

  • Cheng, L. et al. SIRT3 deficiency exacerbates early-stage fibrosis after ischaemia-reperfusion-induced AKI. Cell. Signal. 93, 110284 (2022).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Zhang, Y. et al. Sirtuin 3 regulates mitochondrial protein acetylation and metabolism in tubular epithelial cells during renal fibrosis. Cell Death Dis. 12, 847 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Quan, Y. et al. Sirtuin 3 activation by honokiol decreases unilateral ureteral obstruction-induced renal inflammation and fibrosis via regulation of mitochondrial dynamics and the renal NF-κB-TGF-β1/Smad signaling pathway. Int. J. Mol. Sci. 21, 402 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Li, N. et al. SIRT3-KLF15 signaling ameliorates kidney injury induced by hypertension. Oncotarget 8, 39592–39604 (2017).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Srivastava, S. P. et al. Endothelial SIRT3 regulates myofibroblast metabolic shifts in diabetic kidneys. iScience 24, 102390 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • The EMPA-KIDNEY Collaborative Group. Empagliflozin in patients with chronic kidney disease. N. Engl. J. Med. 388, 117–127 (2023).

    Article 

    Google Scholar
     

  • Wang, Z. et al. Canagliflozin ameliorates epithelial-mesenchymal transition in high-salt diet-induced hypertensive renal injury through restoration of sirtuin 3 expression and the reduction of oxidative stress. Biochem. Biophys. Res. Commun. 653, 53–61 (2023).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Packer, M. Critical reanalysis of the mechanisms underlying the cardiorenal benefits of SGLT2 inhibitors and reaffirmation of the nutrient deprivation signaling/autophagy hypothesis. Circulation 146, 1383–1405 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Li, W. et al. SIRT6 protects vascular smooth muscle cells from osteogenic transdifferentiation via Runx2 chronic kidney disease. J. Clin. Invest. 132, e150051 (2022).

    Article 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Badi, I. et al. miR-34a promotes vascular smooth muscle cell calcification by downregulating SIRT1 (Sirtuin 1) and Axl (AXL receptor tyrosine kinase). Arterioscler. Thromb. Vasc. Biol. 38, 2079–2090 (2018).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Liu, X. et al. Spermidine inhibits vascular calcification in chronic kidney disease through modulation of SIRT1 signaling pathway. Aging Cell 20, e13377 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Liu, S.-M. et al. Intermedin alleviates vascular calcification in CKD through sirtuin 3-mediated inhibition of mitochondrial oxidative stress. Pharmaceuticals 15, 1224 (2022).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ong, A. C. M., Devuyst, O., Knebelmann, B. & Walz, G. & ERA-EDTA Working Group for Inherited Kidney Diseases. Autosomal dominant polycystic kidney disease: the changing face of clinical management. Lancet 385, 1993–2002 (2015).

    Article 
    PubMed 

    Google Scholar
     

  • Zhou, X. et al. Sirtuin 1 inhibition delays cyst formation in autosomal-dominant polycystic kidney disease. J. Clin. Invest. 123, 3084–3098 (2013).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • El Ters, M. et al. Biological efficacy and safety of niacinamide in patients with ADPKD. Kidney Int. Rep. 5, 1271–1279 (2020).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Shen, P. et al. SIRT1: a potential therapeutic target in autoimmune diseases. Front. Immunol. 12, 779177 (2021).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Olivares, D. et al. Urinary levels of sirtuin-1 associated with disease activity in lupus nephritis. Clin. Sci. 132, 569–579 (2018).

    Article 
    CAS 

    Google Scholar
     

  • Consiglio, C. R. et al. SIRT1 promoter polymorphisms as clinical modifiers on systemic lupus erythematosus. Mol. Biol. Rep. 41, 4233–4239 (2014).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Hu, N., Long, H., Zhao, M., Yin, H. & Lu, Q. Aberrant expression pattern of histone acetylation modifiers and mitigation of lupus by SIRT1-siRNA in MRL/lpr mice. Scand. J. Rheumatol. 38, 464–471 (2009).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Gan, H. et al. B cell Sirt1 deacetylates histone and non-histone proteins for epigenetic modulation of AID expression and the antibody response. Sci. Adv. 6, eaay2793 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 
    ADS 

    Google Scholar
     

  • Guan, Y. et al. Nicotinamide mononucleotide, an NAD+ precursor, rescues age-associated susceptibility to AKI in a sirtuin 1-dependent manner. J. Am. Soc. Nephrol. 28, 2337–2352 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Kume, S. et al. Calorie restriction enhances cell adaptation to hypoxia through Sirt1-dependent mitochondrial autophagy in mouse aged kidney. J. Clin. Invest. 120, 1043–1055 (2010).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chuang, P. Y. et al. Reduction in podocyte SIRT1 accelerates kidney injury in aging mice. Am. J. Physiol. Renal Physiol. 313, F621–F628 (2017).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Chen, J. et al. Cathepsin cleavage of sirtuin 1 in endothelial progenitor cells mediates stress-induced premature senescence. Am. J. Pathol. 180, 973–983 (2012).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Mitchell, S. J. et al. The SIRT1 activator SRT1720 extends lifespan and improves health of mice fed a standard diet. Cell Rep. 6, 836–843 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhang, N. et al. Calorie restriction-induced SIRT6 activation delays aging by suppressing NF-κB signaling. Cell Cycle 15, 1009–1018 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Benigni, A. et al. Disruption of the Ang II type 1 receptor promotes longevity in mice. J. Clin. Invest. 119, 524–530 (2009).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Dai, H., Sinclair, D. A., Ellis, J. L. & Steegborn, C. Sirtuin activators and inhibitors: promises, achievements, and challenges. Pharmacol. Ther. 188, 140–154 (2018).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Dang, W. The controversial world of sirtuins. Drug. Discov. Today Technol. 12, e9–e17 (2014).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • US National Library of Medicine. ClinicalTrials.gov https://clinicaltrials.gov/search?intr=Resveratrol&limit=100&page=1&viewType=Table (accessed 2 February 2024).

  • Baksi, A. et al. A phase II, randomized, placebo-controlled, double-blind, multi-dose study of SRT2104, a SIRT1 activator, in subjects with type 2 diabetes. Br. J. Clin. Pharmacol. 78, 69–77 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Curry, A. M., White, D. S., Donu, D. & Cen, Y. Human sirtuin regulators: the “Success” stories. Front. Physiol. 12, 752117 (2021).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Radenkovic, D. R. & Verdin, E. Clinical evidence for targeting NAD therapeutically. Pharmaceuticals 13, 247 (2020).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Camacho-Pereira, J. et al. CD38 dictates age-related NAD decline and mitochondrial dysfunction through an SIRT3-dependent mechanism. Cell Metab. 23, 1127–1139 (2016).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Ugamraj, H. S. et al. TNB-738, a biparatopic antibody, boosts intracellular NAD+ by inhibiting CD38 ecto-enzyme activity. mAbs 14, 2095949 (2022).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Loboda, A., Sobczak, M., Jozkowicz, A. & Dulak, J. TGF-β1/Smads and miR-21 in renal fibrosis and inflammation. Mediators Inflamm. 2016, 8319283 (2016).

    Article 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Zhuo, L. et al. NAD blocks high glucose induced mesangial hypertrophy via activation of the sirtuins-AMPK-mTOR pathway. Cell. Physiol. Biochem. 27, 681–690 (2011).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Ren, Y. et al. The Sirt1 activator, SRT1720, attenuates renal fibrosis by inhibiting CTGF and oxidative stress. Int. J. Mol. Med. 39, 1317–1324 (2017).

    Article 
    CAS 
    PubMed 

    Google Scholar
     

  • Mercken, E. M. et al. SRT2104 extends survival of male mice on a standard diet and preserves bone and muscle mass. Aging Cell 13, 787–796 (2014).

    Article 
    CAS 
    PubMed 
    PubMed Central 

    Google Scholar
     

  • Davenport, A. M., Huber, F. M. & Hoelz, A. Structural and functional analysis of human SIRT1. J. Mol. Biol. 426, 526–541 (2014).

    Article 
    CAS 
    PubMed 

    Google Scholar