Nörodejeneratif Hastalıklarda Sirtuinler ve Mitokondriyal Aktivite

Finkel T, Deng C-X, Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature. 2009; 460: 587–91.

Huang J-Y, Hirschey MD, Shimazu T, et al. Mitochondrial sirtuins. Biochimica et Biophysica Acta (BBA)- Proteins and Proteomics. 2010; 1804: 1645–51.

Vaquero A, Scher MB, Lee DH, et al. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev. 2006; 20: 1256–61.

Yıldırım S, Demirel R, İçen M, et al. Sirtuin1-3 Deasetilazlar: Biyolojik Fonksiyonları ve Kanserde Terapötik Potansiyelleri. Iğdır Üniversitesi FBED, 2022; 12(2): 1055-1069.

Du J, Jiang H, Lin H. Investigating the ADP-ribosyltransferase Activity of Sirtuins with NAD Analogues and 32 P-NAD. Biochemistry. 2009; 48: 2878–90.

Roessler C, Nowak T, Pannek M et al. Chemical Probing of the Human Sirtuin 5 Active Site Reveals Its Substrate Acyl Specificity and Peptide‐Based Inhibitors. Angewandte Chemie International Edition. 2014; 53: 10728–32.

Bordone L, Cohen D, Robinson A, et al. SIRT1 transgenic mice show phenotypes resembling calorie restriction. Aging Cell. 2007; 6: 759–67.

Rogina B, Helfand SL. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. PNAS. 2004; 101: 15998–6003.

Frye RA. Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity. Biochem Biophys Res Commun. 1999; 260: 273–9.

Frye RA. Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like Proteins. Biochem Biophys Res Commun. 2000; 273: 793–8.

Haigis MC, Guarente LP. Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006; 20: 2913–21.

Jin Q, Yan T, Ge X, et al. Cytoplasm‐localized SIRT1 enhances apoptosis. J Cell Physiol. 2007; 213: 88–97.

Dryden SC, Nahhas FA, Nowak JE, et al. Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle. Mol Cell Biol. 2003; 23: 3173–85.

Serrano L, Martínez-Redondo P, Marazuela-Duque A, et al. The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes Dev. 2013; 27: 639–53.

Chang H-C, Guarente L. SIRT1 and other sirtuins in metabolism. Trends Endocrinol. Metab. 2014; 25: 138–45.

Mahlknecht U, Voelter-Mahlknecht S. Fluorescence in situ hybridization and chromosomal organization of the sirtuin 4 gene (Sirt4) in the mouse. Biochem Biophys Res Commun. 2009; 382: 685–90.

Anderson KA, Huynh FK, Fisher-Wellman K, et al. SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion. Cell Metab. 2017; 25: 838-855.e15.

Mathias RA, Greco TM, Oberstein A, et al. Sirtuin 4 Is a Lipoamidase Regulating Pyruvate Dehydrogenase Complex Activity. Cell. 2014; 159: 1615–25.

Rardin MJ, He W, Nishida Y, et al. SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell Metab. 2013;18(6):920-933.

Kumar S, Lombard DB. Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology. Crit Rev Biochem Mol Biol. 2018; 53: 311–34.

Korotkov A, Seluanov A, Gorbunova V. Sirtuin 6: linking longevity with genome and epigenome stability. Trends Cell Biol. 2021; 31: 994–1006.

Zhang M, Tang Z. Therapeutic potential of natural molecules against Alzheimer’s disease via SIRT1 modulation. Biomed. Pharmacother. 2023; 161: 114474.

Jiang H, Khan S, Wang Y, et al. SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature. 2013; 496: 110–3.

Meng H, Yan W-Y, Lei Y-H, et al. SIRT3 Regulation of Mitochondrial Quality Control in Neurodegenerative Diseases. Front Aging Neurosci. 2019; 11.

Scarpulla RC. Transcriptional activators and coactivators in the nuclear control of mitochondrial function in mammalian cells. Gene. 2002; 286: 81–9.

Chuang YC, Chen SD, Jou SB, et al. Sirtuin 1 Regulates Mitochondrial Biogenesis and Provides an Endogenous Neuroprotective Mechanism Against Seizure-Induced Neuronal Cell Death in the Hippocampus Following Status Epilepticus. Int J Mol Sci. 2019;20(14):3588.

Bernier M, Paul RK, Martin-Montalvo A, et al. Negative regulation of STAT3 protein-mediated cellular respiration by SIRT1 protein. J Biol Chem. 2011;286(22):19270-19279.

Schartner E, Sabbir MG, Saleh A, et al. High glucose concentration suppresses a SIRT2 regulated pathway that enhances neurite outgrowth in cultured adult sensory neurons. Exp Neurol. 2018; 309: 134–47.

Fourcade S, Morató L, Parameswaran J, et al. Loss of SIRT2 leads to axonal degeneration and locomotor disability associated with redox and energy imbalance. Aging Cell. 2017;16(6):1404-1413.

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

Cantó C, Gerhart-Hines Z, Feige JN et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature. 2009; 458: 1056–60.

Hasan-Olive MM, Lauritzen KH, Ali M, et al. A Ketogenic Diet Improves Mitochondrial Biogenesis and Bioenergetics via the PGC1α-SIRT3-UCP2 Axis. Neurochem Res. 2019; 44: 22–37.

Tseng AHH, Shieh S-S, Wang DL. SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage. Free Radic Biol Med. 2013; 63: 222–34.

Sun Q, Kang R, Chen K, et al. Sirtuin 3 is required for the protective effect of Resveratrol on Manganese‐induced disruption of mitochondrial biogenesis in primary cultured neurons. J Neurochem. 2021; 156: 121–35.

Ho L, Titus AS, Banerjee KK, et al. SIRT4 regulates ATP homeostasis and mediates a retrograde signaling via AMPK. Aging. 2013; 5: 835–49.

Buler M, Aatsinki S, Izzi V, et al. SIRT5 is under the control of PGC‐1α and AMPK and is involved in regulation of mitochondrial energy metabolism. The FASEB Journal. 2014; 28: 3225–37.

Ding W-X, Yin X-M. Mitophagy: mechanisms, pathophysiological roles, and analysis. bchm. 2012; 393: 547–64.

Wang H, Dou S, Zhu J, et al. Ghrelin protects against rotenone-induced cytotoxicity: Involvement of mitophagy and the AMPK/SIRT1/PGC1α pathway. Neuropeptides. 2021; 87: 102134.

Huang S, Hong Z, Zhang L, et al. CERKL alleviates ischemia reperfusion-induced nervous system injury through modulating the SIRT1/PINK1/Parkin pathway and mitophagy induction. Biol Chem. 2022; 403: 691–701.

Zhao N, Xia J, Xu B. Physical exercise may exert its therapeutic influence on Alzheimer’s disease through the reversal of mitochondrial dysfunction via SIRT1–FOXO1/3–PINK1–Parkin-mediated mitophagy. J Sport Health Sci. 2021; 10: 1–3.

Chang C-C, Tsou S-H, Chen W-J, et al. miR-302 Attenuates Mutant Huntingtin-Induced Cytotoxicity through Restoration of Autophagy and Insulin Sensitivity. Int J Mol Sci. 2021; 22: 8424.

Silva DF, Esteves AR, Oliveira CR, Cardoso SM. Mitochondrial Metabolism Power SIRT2-Dependent Deficient Traffic Causing Alzheimer’s-Disease Related Pathology. Mol Neurobiol. 2017; 54: 4021–40.

Sampaio-Marques B, Felgueiras C, Silva A, et al. Autophagy. 2012; 8: 1494–509.

Zhou ZD, Tan EK. Oxidized nicotinamide adenine dinucleotide-dependent mitochondrial deacetylase sirtuin-3 as a potential therapeutic target of Parkinson’s disease. Ageing Res Rev. 2020; 62: 101107.

Lang A, Anand R, Altinoluk-Hambüchen S, et al. SIRT4 interacts with OPA1 and regulates mitochondrial quality control and mitophagy. Aging. 2017; 9: 2163–89.

Polletta L, Vernucci E, Carnevale I, et al. SIRT5 regulation of ammonia-induced autophagy and mitophagy. Autophagy. 2015;11(2):253-270.

Hong Y-X, Wu W-Y, Song F, et al. Cardiac senescence is alleviated by the natural flavone acacetin via enhancing mitophagy. Aging. 2021; 13: 16381–403.

Chang AL, Doering TL. Maintenance of Mitochondrial Morphology in Cryptococcus neoformans Is Critical for Stress Resistance and Virulence. mBio. 2018;9(6):e01375-18.

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Shi H, Deng H-X, Gius D, et al. Sirt3 protects dopaminergic neurons from mitochondrial oxidative stress. Hum Mol Genet. 2017; 26: 1915–26.

Liu L, Peritore C, Ginsberg J, et al. Protective role of SIRT5 against motor deficit and dopaminergic degeneration in MPTP-induced mice model of Parkinson’s disease. Behav. Brain Res. 2015; 281: 215–21.

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Song W, Song Y, Kincaid B, et al. Mutant SOD1G93A triggers mitochondrial fragmentation in spinal cord motor neurons: Neuroprotection by SIRT3 and PGC-1α. Neurobiol Dis. 2013; 51: 72–81.

Finkel T, Deng C-X, Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature. 2009; 460: 587–91.

Huang J-Y, Hirschey MD, Shimazu T, et al. Mitochondrial sirtuins. Biochimica et Biophysica Acta (BBA)- Proteins and Proteomics. 2010; 1804: 1645–51.

Vaquero A, Scher MB, Lee DH, et al. SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev. 2006; 20: 1256–61.

Yıldırım S, Demirel R, İçen M, et al. Sirtuin1-3 Deasetilazlar: Biyolojik Fonksiyonları ve Kanserde Terapötik Potansiyelleri. Iğdır Üniversitesi FBED, 2022; 12(2): 1055-1069.

Du J, Jiang H, Lin H. Investigating the ADP-ribosyltransferase Activity of Sirtuins with NAD Analogues and 32 P-NAD. Biochemistry. 2009; 48: 2878–90.

Roessler C, Nowak T, Pannek M et al. Chemical Probing of the Human Sirtuin 5 Active Site Reveals Its Substrate Acyl Specificity and Peptide‐Based Inhibitors. Angewandte Chemie International Edition. 2014; 53: 10728–32.

Bordone L, Cohen D, Robinson A, et al. SIRT1 transgenic mice show phenotypes resembling calorie restriction. Aging Cell. 2007; 6: 759–67.

Rogina B, Helfand SL. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. PNAS. 2004; 101: 15998–6003.

Frye RA. Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity. Biochem Biophys Res Commun. 1999; 260: 273–9.

Frye RA. Phylogenetic Classification of Prokaryotic and Eukaryotic Sir2-like Proteins. Biochem Biophys Res Commun. 2000; 273: 793–8.

Haigis MC, Guarente LP. Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction. Genes Dev. 2006; 20: 2913–21.

Jin Q, Yan T, Ge X, et al. Cytoplasm‐localized SIRT1 enhances apoptosis. J Cell Physiol. 2007; 213: 88–97.

Dryden SC, Nahhas FA, Nowak JE, et al. Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle. Mol Cell Biol. 2003; 23: 3173–85.

Serrano L, Martínez-Redondo P, Marazuela-Duque A, et al. The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes Dev. 2013; 27: 639–53.

Chang H-C, Guarente L. SIRT1 and other sirtuins in metabolism. Trends Endocrinol. Metab. 2014; 25: 138–45.

Mahlknecht U, Voelter-Mahlknecht S. Fluorescence in situ hybridization and chromosomal organization of the sirtuin 4 gene (Sirt4) in the mouse. Biochem Biophys Res Commun. 2009; 382: 685–90.

Anderson KA, Huynh FK, Fisher-Wellman K, et al. SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion. Cell Metab. 2017; 25: 838-855.e15.

Mathias RA, Greco TM, Oberstein A, et al. Sirtuin 4 Is a Lipoamidase Regulating Pyruvate Dehydrogenase Complex Activity. Cell. 2014; 159: 1615–25.

Rardin MJ, He W, Nishida Y, et al. SIRT5 regulates the mitochondrial lysine succinylome and metabolic networks. Cell Metab. 2013;18(6):920-933.

Kumar S, Lombard DB. Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology. Crit Rev Biochem Mol Biol. 2018; 53: 311–34.

Korotkov A, Seluanov A, Gorbunova V. Sirtuin 6: linking longevity with genome and epigenome stability. Trends Cell Biol. 2021; 31: 994–1006.

Zhang M, Tang Z. Therapeutic potential of natural molecules against Alzheimer’s disease via SIRT1 modulation. Biomed. Pharmacother. 2023; 161: 114474.

Jiang H, Khan S, Wang Y, et al. SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature. 2013; 496: 110–3.

Meng H, Yan W-Y, Lei Y-H, et al. SIRT3 Regulation of Mitochondrial Quality Control in Neurodegenerative Diseases. Front Aging Neurosci. 2019; 11.

Scarpulla RC. Transcriptional activators and coactivators in the nuclear control of mitochondrial function in mammalian cells. Gene. 2002; 286: 81–9.

Chuang YC, Chen SD, Jou SB, et al. Sirtuin 1 Regulates Mitochondrial Biogenesis and Provides an Endogenous Neuroprotective Mechanism Against Seizure-Induced Neuronal Cell Death in the Hippocampus Following Status Epilepticus. Int J Mol Sci. 2019;20(14):3588.

Bernier M, Paul RK, Martin-Montalvo A, et al. Negative regulation of STAT3 protein-mediated cellular respiration by SIRT1 protein. J Biol Chem. 2011;286(22):19270-19279.

Schartner E, Sabbir MG, Saleh A, et al. High glucose concentration suppresses a SIRT2 regulated pathway that enhances neurite outgrowth in cultured adult sensory neurons. Exp Neurol. 2018; 309: 134–47.

Fourcade S, Morató L, Parameswaran J, et al. Loss of SIRT2 leads to axonal degeneration and locomotor disability associated with redox and energy imbalance. Aging Cell. 2017;16(6):1404-1413.

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

Cantó C, Gerhart-Hines Z, Feige JN et al. AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity. Nature. 2009; 458: 1056–60.

Hasan-Olive MM, Lauritzen KH, Ali M, et al. A Ketogenic Diet Improves Mitochondrial Biogenesis and Bioenergetics via the PGC1α-SIRT3-UCP2 Axis. Neurochem Res. 2019; 44: 22–37.

Tseng AHH, Shieh S-S, Wang DL. SIRT3 deacetylates FOXO3 to protect mitochondria against oxidative damage. Free Radic Biol Med. 2013; 63: 222–34.

Sun Q, Kang R, Chen K, et al. Sirtuin 3 is required for the protective effect of Resveratrol on Manganese‐induced disruption of mitochondrial biogenesis in primary cultured neurons. J Neurochem. 2021; 156: 121–35.

Ho L, Titus AS, Banerjee KK, et al. SIRT4 regulates ATP homeostasis and mediates a retrograde signaling via AMPK. Aging. 2013; 5: 835–49.

Buler M, Aatsinki S, Izzi V, et al. SIRT5 is under the control of PGC‐1α and AMPK and is involved in regulation of mitochondrial energy metabolism. The FASEB Journal. 2014; 28: 3225–37.

Ding W-X, Yin X-M. Mitophagy: mechanisms, pathophysiological roles, and analysis. bchm. 2012; 393: 547–64.

Wang H, Dou S, Zhu J, et al. Ghrelin protects against rotenone-induced cytotoxicity: Involvement of mitophagy and the AMPK/SIRT1/PGC1α pathway. Neuropeptides. 2021; 87: 102134.

Huang S, Hong Z, Zhang L, et al. CERKL alleviates ischemia reperfusion-induced nervous system injury through modulating the SIRT1/PINK1/Parkin pathway and mitophagy induction. Biol Chem. 2022; 403: 691–701.

Zhao N, Xia J, Xu B. Physical exercise may exert its therapeutic influence on Alzheimer’s disease through the reversal of mitochondrial dysfunction via SIRT1–FOXO1/3–PINK1–Parkin-mediated mitophagy. J Sport Health Sci. 2021; 10: 1–3.

Chang C-C, Tsou S-H, Chen W-J, et al. miR-302 Attenuates Mutant Huntingtin-Induced Cytotoxicity through Restoration of Autophagy and Insulin Sensitivity. Int J Mol Sci. 2021; 22: 8424.

Silva DF, Esteves AR, Oliveira CR, Cardoso SM. Mitochondrial Metabolism Power SIRT2-Dependent Deficient Traffic Causing Alzheimer’s-Disease Related Pathology. Mol Neurobiol. 2017; 54: 4021–40.

Sampaio-Marques B, Felgueiras C, Silva A, et al. Autophagy. 2012; 8: 1494–509.

Zhou ZD, Tan EK. Oxidized nicotinamide adenine dinucleotide-dependent mitochondrial deacetylase sirtuin-3 as a potential therapeutic target of Parkinson’s disease. Ageing Res Rev. 2020; 62: 101107.

Lang A, Anand R, Altinoluk-Hambüchen S, et al. SIRT4 interacts with OPA1 and regulates mitochondrial quality control and mitophagy. Aging. 2017; 9: 2163–89.

Polletta L, Vernucci E, Carnevale I, et al. SIRT5 regulation of ammonia-induced autophagy and mitophagy. Autophagy. 2015;11(2):253-270.

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