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      Sirtuins and renal diseases: relationship with aging and diabetic nephropathy

      review-article
      Author(s): * , † , * , * , *
      Publication date (Electronic):
      Journal: Clinical Science (London, England : 1979)
      Publisher: Portland Press Ltd.
      Keywords: aging, diabetic nephropathy, sirtuin, SIRT1 (sirtuin 1), AGE, advanced glycation end-product, AMPK, AMP-activated protein kinase, AngII, angiotensin II, AT1R, angiotensin type 1 receptor, Atg, autophagy-related gene, BMAL1, brain and muscle ARNT (aryl hydrocarbon receptor nuclear translocator)-like 1 , Bnip3, BCL2/adenovirus E1V 19-kDa interacting protein 3, CKD, chronic kidney disease, CR, calorie restriction, CRP, C-reactive protein, COX2, cyclo-oxygenase 2, α-ENaC, epithelial Na+ channel α-subunit, eNOS, endothelial NO synthase, ER, endoplasmic reticulum, FOXO, forkhead box O, FXR, farnesoid X receptor, H3K9, histone H3 Lys9, H3K9me3, H3K9 trimethylation, HIF, hypoxia-inducible factor, ICAM-1, intercellular adhesion molecule 1, Idh2, isocitrate dehydrogenase 2, IGF, insulin-like growth factor, IRS, insulin receptor substrate, LC3, light chain 3, LXR, liver X receptor, MCP-1, monocyte chemotactic protein-1, Mn-SOD, manganese superoxide dismutase, mTOR, mammalian target of rapamycin, NF-κB, nuclear factor-κB, PARP, poly(ADP-ribose) polymerase, PER2, Period 2, PGC-1α, PPAR-γ co-activator-1α, PKC, protein kinase C, PPAR, peroxisome-proliferator-activated receptor, PTP1B, protein tyrosine phosphatase 1B, RAS, renin–angiotensin system, ROS, reactive oxygen species, Sir2, silent information regulator 2, SIRT1 etc., sirtuin 1 etc., SNP, single nucleotide polymorphism, SREBP, sterol-regulatory-element-binding protein, TGF, transforming growth factor, TNF-α, tumour necrosis factor α, UUO, unilateral ureteral obstruction, VCAM-1, vascular cell adhesion protein 1, WFR, Wistar fatty diabetic rat

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          Abstract

          Sirtuins are members of the Sir2 (silent information regulator 2) family, a group of class III deacetylases. Mammals have seven different sirtuins, SIRT1–SIRT7. Among them, SIRT1, SIRT3 and SIRT6 are induced by calorie restriction conditions and are considered anti-aging molecules. SIRT1 has been the most extensively studied. SIRT1 deacetylates target proteins using the coenzyme NAD + and is therefore linked to cellular energy metabolism and the redox state through multiple signalling and survival pathways. SIRT1 deficiency under various stress conditions, such as metabolic or oxidative stress or hypoxia, is implicated in the pathophysiologies of age-related diseases including diabetes, cardiovascular diseases, neurodegenerative disorders and renal diseases. In the kidneys, SIRT1 may inhibit renal cell apoptosis, inflammation and fibrosis, and may regulate lipid metabolism, autophagy, blood pressure and sodium balance. Therefore the activation of SIRT1 in the kidney may be a new therapeutic target to increase resistance to many causal factors in the development of renal diseases, including diabetic nephropathy. In addition, SIRT3 and SIRT6 are implicated in age-related disorders or longevity. In the present review, we discuss the protective functions of sirtuins and the association of sirtuins with the pathophysiology of renal diseases, including diabetic nephropathy.

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          Sirtuins in mammals: insights into their biological function.

          Shaday Michan, David. Sinclair (2007)
          Sirtuins are a conserved family of proteins found in all domains of life. The first known sirtuin, Sir2 (silent information regulator 2) of Saccharomyces cerevisiae, from which the family derives its name, regulates ribosomal DNA recombination, gene silencing, DNA repair, chromosomal stability and longevity. Sir2 homologues also modulate lifespan in worms and flies, and may underlie the beneficial effects of caloric restriction, the only regimen that slows aging and extends lifespan of most classes of organism, including mammals. Sirtuins have gained considerable attention for their impact on mammalian physiology, since they may provide novel targets for treating diseases associated with aging and perhaps extend human lifespan. In this review we describe our current understanding of the biological function of the seven mammalian sirtuins, SIRT1-7, and we will also discuss their potential as mediators of caloric restriction and as pharmacological targets to delay and treat human age-related diseases.
          Article 0 comments Cited 500 times – based on 0 reviews     Review now
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            SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent gene expression and organismal life span.

            Tiara Kawahara, Eriko Michishita, Adam Adler … (2009)
            Members of the sirtuin (SIRT) family of NAD-dependent deacetylases promote longevity in multiple organisms. Deficiency of mammalian SIRT6 leads to shortened life span and an aging-like phenotype in mice, but the underlying molecular mechanisms are unclear. Here we show that SIRT6 functions at chromatin to attenuate NF-kappaB signaling. SIRT6 interacts with the NF-kappaB RELA subunit and deacetylates histone H3 lysine 9 (H3K9) at NF-kappaB target gene promoters. In SIRT6-deficient cells, hyperacetylation of H3K9 at these target promoters is associated with increased RELA promoter occupancy and enhanced NF-kappaB-dependent modulation of gene expression, apoptosis, and cellular senescence. Computational genomics analyses revealed increased activity of NF-kappaB-driven gene expression programs in multiple Sirt6-deficient tissues in vivo. Moreover, haploinsufficiency of RelA rescues the early lethality and degenerative syndrome of Sirt6-deficient mice. We propose that SIRT6 attenuates NF-kappaB signaling via H3K9 deacetylation at chromatin, and hyperactive NF-kappaB signaling may contribute to premature and normal aging.
            Article 0 comments Cited 390 times – based on 0 reviews     Review now
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              Inflammatory molecules and pathways in the pathogenesis of diabetic nephropathy.

              Juan F. Navarro-González, Carmen Mora-Fernández, Mercedes Muros de Fuentes … (2011)
              Many lines of evidence, ranging from in vitro experiments and pathological examinations to epidemiological studies, show that inflammation is a cardinal pathogenetic mechanism in diabetic nephropathy. Thus, modulation of inflammatory processes in the setting of diabetes mellitus is a matter of great interest for researchers today. The relationships between inflammation and the development and progression of diabetic nephropathy involve complex molecular networks and processes. This Review, therefore, focuses on key proinflammatory molecules and pathways implicated in the development and progression of diabetic nephropathy: the chemokines CCL2, CX3CL1 and CCL5 (also known as MCP-1, fractalkine and RANTES, respectively); the adhesion molecules intercellular adhesion molecule 1, vascular cell adhesion protein 1, endothelial cell-selective adhesion molecule, E-selectin and α-actinin 4; the transcription factor nuclear factor κB; and the inflammatory cytokines IL-1, IL-6, IL-18 and tumor necrosis factor. Advances in the understanding of the roles that these inflammatory pathways have in the context of diabetic nephropathy will facilitate the discovery of new therapeutic targets. In the next few years, promising new therapeutic strategies based on anti-inflammatory effects could be successfully translated into clinical treatments for diabetic complications, including diabetic nephropathy.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Clin Sci (Lond)
                Journal ID (iso-abbrev): Clin. Sci
                Journal ID (pmc): cls
                Journal ID (publisher-id): CS
                Title: Clinical Science (London, England : 1979)
                Publisher: Portland Press Ltd.
                ISSN (Print): 0143-5221
                ISSN (Electronic): 1470-8736
                Publication date (Electronic): 5 October 2012
                Publication date (Print): 1 February 2013
                Volume: 124
                Issue: Pt 3
                Pages: 153-164
                Affiliations
                *Diabetology and Endocrinology, Kanazawa Medical University, 1-1 Daigaku, Uchinada, Ishikawa, Japan
                †Diabetes, Nephrology and Neurology, Shiga University of Medical Science, Setatsukinowa, Otsu, Shiga, Japan
                Author notes
                Correspondence: Professor Daisuke Koya (email koya0516@ 123456kanazawa-med.ac.jp ).
                Article
                Publisher ID: CS20120190
                DOI: 10.1042/CS20120190
                PMC ID: 3466784
                PubMed ID: 23075334
                SO-VID: 17996b6d-28c6-409c-aa9f-fdd90be940b6
                Copyright © © 2013 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 17 April 2012
                Date revision received : 3 August 2012
                Date accepted : 28 August 2012
                Page count
                Figures: 4, Tables: 2, References: 110, Pages: 12
                Categories
                Subject: Review Article
                Subject: S6
                Subject: S4

                ScienceOpen disciplines: Medicine
                Keywords: diabetic nephropathy,aging,sirtuin,sirt1 (sirtuin 1),age, advanced glycation end-product,ampk, amp-activated protein kinase,angii, angiotensin ii,at1r, angiotensin type 1 receptor,atg, autophagy-related gene,bmal1, brain and muscle arnt (aryl hydrocarbon receptor nuclear translocator)-like 1,bnip3, bcl2/adenovirus e1v 19-kda interacting protein 3,ckd, chronic kidney disease,cr, calorie restriction,crp, c-reactive protein,cox2, cyclo-oxygenase 2,α-enac, epithelial na+ channel α-subunit,enos, endothelial no synthase,er, endoplasmic reticulum,foxo, forkhead box o,fxr, farnesoid x receptor,h3k9, histone h3 lys9,h3k9me3, h3k9 trimethylation,hif, hypoxia-inducible factor,icam-1, intercellular adhesion molecule 1,idh2, isocitrate dehydrogenase 2,igf, insulin-like growth factor,irs, insulin receptor substrate,lc3, light chain 3,lxr, liver x receptor,mcp-1, monocyte chemotactic protein-1,mn-sod, manganese superoxide dismutase,mtor, mammalian target of rapamycin,nf-κb, nuclear factor-κb,parp, poly(adp-ribose) polymerase,per2, period 2,pgc-1α, ppar-γ co-activator-1α,pkc, protein kinase c,ppar, peroxisome-proliferator-activated receptor,ptp1b, protein tyrosine phosphatase 1b,ras, renin–angiotensin system,ros, reactive oxygen species,sir2, silent information regulator 2,sirt1 etc., sirtuin 1 etc., snp, single nucleotide polymorphism,srebp, sterol-regulatory-element-binding protein,tgf, transforming growth factor,tnf-α, tumour necrosis factor α,uuo, unilateral ureteral obstruction,vcam-1, vascular cell adhesion protein 1,wfr, wistar fatty diabetic rat
                Data availability:
                ScienceOpen disciplines: Medicine
                Keywords: diabetic nephropathy, aging, sirtuin, sirt1 (sirtuin 1), age, advanced glycation end-product, ampk, amp-activated protein kinase, angii, angiotensin ii, at1r, angiotensin type 1 receptor, atg, autophagy-related gene, bmal1, brain and muscle arnt (aryl hydrocarbon receptor nuclear translocator)-like 1, bnip3, bcl2/adenovirus e1v 19-kda interacting protein 3, ckd, chronic kidney disease, cr, calorie restriction, crp, c-reactive protein, cox2, cyclo-oxygenase 2, α-enac, epithelial na+ channel α-subunit, enos, endothelial no synthase, er, endoplasmic reticulum, foxo, forkhead box o, fxr, farnesoid x receptor, h3k9, histone h3 lys9, h3k9me3, h3k9 trimethylation, hif, hypoxia-inducible factor, icam-1, intercellular adhesion molecule 1, idh2, isocitrate dehydrogenase 2, igf, insulin-like growth factor, irs, insulin receptor substrate, lc3, light chain 3, lxr, liver x receptor, mcp-1, monocyte chemotactic protein-1, mn-sod, manganese superoxide dismutase, mtor, mammalian target of rapamycin, nf-κb, nuclear factor-κb, parp, poly(adp-ribose) polymerase, per2, period 2, pgc-1α, ppar-γ co-activator-1α, pkc, protein kinase c, ppar, peroxisome-proliferator-activated receptor, ptp1b, protein tyrosine phosphatase 1b, ras, renin–angiotensin system, ros, reactive oxygen species, sir2, silent information regulator 2, sirt1 etc., sirtuin 1 etc., snp, single nucleotide polymorphism, srebp, sterol-regulatory-element-binding protein, tgf, transforming growth factor, tnf-α, tumour necrosis factor α, uuo, unilateral ureteral obstruction, vcam-1, vascular cell adhesion protein 1, wfr, wistar fatty diabetic rat

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