Mecanismos celulares en respuesta al estrés: sirtuinas

Publicado

2010-07-01

Cellular mechanisms in response to stress: sirtuin

Palabras clave:

abastecimiento de energía, restricción calórica, senescencia, longevidad, sirtuinas, telómero, telomerasa. (es)
energy supply, caloric restriction, aging, longevity, sirtuins, telomere, telomerase. (en)

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Autores/as

Nancy Paola Echeverri-Ruiz Departamento de Zoología, Miami University, Oxford- Ohio, USA.
Ismena Mockus-Sivickas Profesora Titular, Departamento Ciencias Fisiológicas, Facultad de Medicina, Universidad Nacional de Colombia.

Resumen (es)
Resumen (en)

Desde hace algún tiempo se conoce el papel de la restricción calórica sobre la longevidad y la prevención de enfermedades crónicas, pero hasta hace poco los mecanismos celulares involucrados comienzan a ser elucidados. El estrés celular se podría definir como el estado en el que la célula no presenta las condiciones óptimas de supervivencia, siendo el oxidativo un tipo de estrés en el que se generan radicales libres nocivos para las estructuras celulares. La restricción calórica podría incrementar la resistencia celular a diferentes formas de estrés. Las sirtuinas, proteínas deacetilasas de histonas tipo III, están involucradas en la relación entre balance energético y transcripción génica, permitiendo que la célula responda a la restricción calórica y sobreviva a situaciones de estrés oxidativo. En esta relación las sirtuinas regulan genes de la familia FOXO, cMYC, hTERT, p53, entre otros. La activación o silenciamiento de estos genes es importante en los procesos de apoptosis, reparación y muerte celular.

The role of caloric restriction on longevity and prevention of chronic diseases has been known for some time; recently, cellular mechanisms involved are beginning to be elucidated. Cellular stress could be defined as the state in which the cell does not present optimal survival conditions; oxidative stress is a type of stress in which free radicals harmful cell structures. Caloric restriction might increase cellular resistance to various forms of stress. Sirtuins, histone deacetylases type III proteins are involved in the relationship between energy balance and gene transcription, allowing cell to respond to caloric restriction and to survive to oxidative stress.

In this relationship, sirtuins regulate FOXO family genes, cMYC, hTERT, p53, among others. Activation or silencing of those genes is important in the process of apoptosis, repair and cell death.

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Cerni C. Telomeres, telomerase, and myc. An update. Mutat Res. 2000; 462: 31-47.

Bayne S, Liu JP. At the cutting edge. Hormones and growth factors regulate telomerase activity in ageing and cancer. Mol Cell Endocrinol. 2005; 240: 11-22.

Lithgow GJ. Why aging isn’t regulated: a lamentation on the use of language in aging literature. Exp Gerontol. 2006; 10:890-893.

Lithgow GJ. Hormesis–a new hope for ageing studies or a poor second to genetics? Hum Exp Toxicol. 2001; 20: 301-303.

Maynard S. Prolongation of the life of Drosophila subobscura by brief exposure of adults to a high temperature. Nature. 1958; 181: 496-497.

Lithgow GJ, White TM, Melov S, Johnson TE. Thermotolerance and extended life span conferred by single- gene mutations and induced by thermal stress. Proc Natl Acad Sci USA. 1995; 92: 7540-7544.

Masoro EJ, Austad SN. The evolution of the antiaging action of dietary restriction: a hypothesis. J Gerontol A Biol Sci Med Sci. 1996; 51: B387-B391.

Sinclair DA. Toward a unified theory of caloric restriction and longevity regulation. Mech Ageing Dev. 2005; 126: 987-1002.

Wood JG, Rogina B, Lavu S, Howitz K, Helfand SL, Tatar M, et al. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature. 2004; 430: 686-689.

Poli G, Leonarduzzi G, Biasi F, Chiarpotto E. Oxidative stress and cell signalling. Curr Med Chem. 2004;11: 1163-1182.

Dröge W. Free radicals in the physiological control of cell function. Physiol Rev. 2002; 82: 47-95.

Beckman KB, Ames B. Oxidative decay of DNA. J Biol Chem. 1997; 272: 19633-19636.

Dizdaroglu M, Jaruga P, Birincioglu M, Rodriguez H. Free radical-induced damage to DNA: mechanisms and measurement. Free Radic Biol Med. 2002; 32: 1102-1115.

Marnett LJ. Oxyradicals and DNA damage. Carcinogenesis. 2000; 21: 361-370.

Penta JS , Johnson FM, Wachsman JT, Copeland WC. Mitochondrial DNA in human malignancy. Mutat Res. 2001; 488: 119-133.

Esterbauer H, Schaur RJ, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Rad Biol Med. 1991; 11: 81- 128.

Marnett LJ. Lipid peroxidation-DNA damage by malondialdehyde. Mutat Res. 1999; 424: 83-95.

Dröge W. Oxidative stress and aging. Adv Exp Med Biol. 2003; 543: 191-200.

Cheng KC, Preston BD, Cahill DS, Dosanjh MK, Singer B, Loeb L. The vinyl-chloride DNA derivative N2,3- ethenoguanine produces G–A transitions in Escherichia coli. Proc Natl Acad Sci USA. 1991; 88: 9974- 9978.

Toussaint O, Medrano EE, von Zglinicki T. Cellular and molecular mechanisms of stress-induced premature senescence (SIPS) of human diploid fibroblasts and melanocytes. Exp Geronto. 2000; 35: 927-945.

Sastre-Serra JJ, Valle AA, Company MM, Garau II, Oliver JJ, Roca PP. Estrogen down-regulates uncoupling proteins and increases oxidative stress in breast cancer. Free Radic Biol Med. 2009. http://www.sciencedirect.com [Consultado el 22 de diciembre de 2009].

Heydari AR, Unnikrishnan A, Lucente LV, Richardson A. Caloric restriction and genomic stability. Nucleic Acids Res. 2007; 35: 7485-7496.

Stuart J, Karahalil B, Hogue BA, Souza-Pinto NC, Bohr VA. Mitochondrial and nuclear DNA base excision repair are affected differently by caloric restriction. FASEB J. 2004; 18: 595-597.

Swindell WR. Genes and gene expression modules associated with caloric restriction and aging in the laboratory mouse. BMC Genomics. 2009 ;10: 585-612.

Sherlock M, Toogood A. Aging and the growth hormone/ insulin like growth factor-I axis. Pituitary. 2007; 10: 189-203.

Lamberts SW, van den Beld AW, van der Lely AJ. The endocrinology of aging. Science. 1997; 278: 419-424.

Yang J, Anzo M, Cohen P. Control of aging and longevity by IGF-I signaling. Exp Gerontol. 2005; 40: 867-872.

Barbieri M, Bonafe M, Franceschi C, Paolisso G. Insulin/IGF-I signaling pathway: an evolutionarily conserved mechanism of longevity from yeast to humans. Am J Physiol Endocrinol Metab. 2003; 285: E1064- E1071.

Suh Y, Atzmon G, Cho M, Hwang D, Liu B, Leahy D, et al. Functionally significant insulin-like growth factor I receptor mutations in centenarians. Proc Natl Acad Sci USA. 2008; 105: 3438-3442.

Kenyon C, Chang J, Gensch E, Rudner A, Tabtiang R. A C. elegans mutant that lives twice as long as wild type. Nature. 1993; 366: 461-464.

Tatar M, Kopelman A, Epstein D, Tu MP, Yin CM, Garofalo R. A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function. Science. 2001; 292: 107-110.

Blüher M, Kahn BB, Kahn CR. Extended longevity in mice lacking the insulin receptor in adipose tissue. Science. 2003; 299: 572–574.

Flachsbart F, Caliebe A, Kleindorp R, Blanché H, von Eller-Eberstein H, Nikolaus S, et al. Associa tion of FOXO3A variation with human longevity confirmed in German centenarians. Proc Natl Acad Sci USA. 2009; 106: 2700-2705.

Kenyon C, Murphy CT. Enrichment of regulatory motifs upstream of predicted. DAF-16 targets. Nat Genet. 2006; 38: 397-398.

Daitoku H, Fukamizu A. FOXO transcription factors in the regulatory networks of longevity. J Biochem. 2007; 141: 769-774.

Essers M. de Vries-Smits LM, Barker N, Polderman PE, Burgering BM, Korswagen H. Functional interaction between beta-catenin and FOXO in oxidative stress signaling. Science. 2005; 308: 1181-1184.

Willcox BJ, Donlon TA, He Q, Chen R, Grove JS, Yano K, et al. FOXO3A genotype is strongly associated with human longevity. Proc Natl Acad Sci USA. 2008; 105: 13987-13992.

Finkel T, Deng CX, Mostoslavsky R. Recent progress in the biology and physiology of sirtuins. Nature. 2009; 460: 587-591.

Saunders LR, Verdin E. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene. 2007; 26: 5489-5504.

Yamamoto H, Schoonjans K, Auwerx J. Sirtuin functions in health and disease. Mol Endocrinol. 2007; 21: 1745-1755.

Liou GG, Tanny JC, Kruger RG, Walz T, Moazed D. Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell. 2005; 121: 515-527.

Blander G, Guarente L. The Sir2 family of protein deacetylases. Annu Rev Biochem. 2004; 73:417-435.

Cohen HY, Miller C, Bitterman KJ, Wall NR, Hekking B, Kessler B, et al. Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science. 2004; 305: 390-392.

Landry J, Sutton A, Tafrov ST, Heller RC, Stebbins J, Pillus L, et al. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci USA. 2000; 97: 5807-5811.

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

Mostoslavsky R, Chua KF, Lombard DB, Pang WW, Fischer MR, Gellon L, et al. Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell. 2006; 124: 315-329.

North BJ, Marshall BL, Borra MT, Denu JM, Verdin E. The human Sir2 ortholog, SIRT2, is an NAD+- dependent tubulin deacetylase. Mol Cell. 2003; 11: 437-444.

Scher MB, Vaquero A, Reinberg D. SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 2007; 21: 920-928.

Haigis MC, Mostoslavsky R, Haigis KM, Fahie K, Christodoulou DC, Murphy AJ, et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic b cells. Cell. 2006; 126: 941-954.

Liszt G, Ford E, Kurtev M, Guarente L. Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J Biol Chem. 2005; 280: 21313-21320.

Shi T, Wang F, Stieren E, Tong Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J Biol Chem. 2005; 280: 13560-13567.

Michishita E, McCord RA, Berber E, Kioi M, Padilla- Nash H, Damian M, et al. SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin. Nature. 2008; 45: 492-496.

Ford E, Voit R, Liszt G, Magin C, Grummt I, Guarente L. Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I transcription. Genes Dev. 2006; 20: 1075-1080.

Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I. Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell. 2005; 16: 4623-4635.

Feige JN, Auwerx J. Transcriptional targets of sirtuins in the coordination of mammalian physiology. Curr Opin Cell Biol. 2008; 20: 303-309.

Salih DA, Brunet A. FoxO transcription factors in the maintenance of cellular homeostasis during aging. Curr Opin Cell Biol. 2008; 20:126-136.

Rodgers JT, Lerin C, Gerhart-Hines Z, Puigserver P. Metabolic adaptations through the PGC-1 alpha and SIRT1 pathways. FEBS Lett. 2008; 582: 46-53.

Cantó C, Auwerx J. Caloric restriction, SIRT1 and longevity. Trends Endocrinol Metab. 2009; 20: 325-331.

Chen D, Bruno J, Easlon E, Lin SJ, Cheng HL, Alt FW, et al. Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev. 2008; 22: 1753-1757.

Wang C, Chen L, Hou X, Li Z, Kabra N, Ma Y, et al. Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat Cell Biol. 2006; 8: 1025-1031.

Chua KF, Mostoslavsky R, Lombard DB, Pang WW, Saito S, Franco S et al. Mammalian SIRT1 limits replicative life span in response to chronic genotoxic stress. Cell Metab. 2005; 2: 67-76.

Yuan J, Minter-Dykhouse K, Lou Z. A c-Myc–SIRT1 feedback loop regulates cell growth and transformation. J Cell Biol. 2009; 185: 203-211.

Moynihan KA, Grimm AA, Plueger MM, Bernal- Mizrachi E, Ford E, Cras-Méneur C, et al. Increased dosage of mammalian Sir2 in pancreatic b cells enhances glucose-stimulated insulin secretion in mice. Cell Metab. 2005; 2: 105-117.

Nemoto S, Fergusson MM, Finkel T. Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science. 2004; 306: 2105-2108.

Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000; 408: 239-247.

Narala SR, Allsopp RC, Wells TB, Zhang G, Prasad P, Coussens MJ, et al. SIRT1 acts as a nutrientsensitive growth suppressor and its loss is associated with Increased AMPK and telomerase activity. Mol Biol Cell. 2008; 19: 1210-1219.

Inoue T, Hiratsuka M, Osaki M, Yamada H, Kishimoto I, Yamaguchi S et al. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress. Oncogene. 2006; 26: 945-957.

Rowinsky EK, Calvo E. Novel agents that target tubulin and related elements. Semin Oncol. 2006; 33: 421- 435.

De Lange T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 2005; 19: 2100-2110.

Makarov VL, Hirose Y, Langmore JP. Long G tails at both ends of human chromosomes suggest a C strand degradation mechanism for telomere shortening. Cell. 1997; 88: 657-666.

Wong KK, Chang S, Weiler SR, Ganesan S, Chaudhuri J, Zhu C, et al. Telomere dysfunction impairs DNA repair and enhances radiosensitivity to ionizing radiation. Nat Genet. 2000; 26: 85-88.

Bachand F, Autexier C. Functional regions of human telomerase reverse transcriptase and human telomerase RNA required for telomerase activity and RNAprotein interactions. Mol Cell Biol. 2001; 21: 1888- 1897.

Shay JW, Bacchetti S. A survey of telomerase activity in human cancer. Eur J Cancer. 1997; 33: 787-791.

Seimiya H, Sawada H, Muramatsu Y, Shimizu M, Ohko K, Yamane K et al. Involvement of 14-3-3 proteins in nuclear localization of telomerase. EMBO J. 2000; 19: 2652-2661.

Cao Y, Li H, Deb S, Liu JP. TERT regulates cell survival independent of telomerase enzymatic activity. Oncogene. 2002; 21: 3130-3138.

Horikawa I, Cable PL, Afshari C, Barrett JC. Cloning and characterization of the promoter region of human telomerase reverse transcriptase gene. Cancer Res. 1999; 59: 826-830.

Misiti S, Nanni S, Fontemaggi G, Cong YS, Wen J, Hirte HW, et al. Induction of hTERT expression and telomerase activity by estrogens in human ovary epithelium cells. Mol Cell Biol. 2000; 20: 3764-3771.

Lebeau J, Fouchet P, Ory K, Chevillard S. Downregulation of telomerase activity after progesterone treatment of human breast cancer cells: essential role of the cell cycle status. Anticancer Res. 2002; 22: 2161- 2166.

Karlseder J, Hoke K, Mirzoeva OK, Bakkenist C, Kastan MB, Petrini JH, et al. The telomeric protein TRF2 Binds the ATM Kinase and can inhibit the ATMdependent DNA damage response. PLoS Biol. 2004; 2: 1150-1156.

Lorenz M, Saretzki G, Sitte N, Metzkow S, von Zglinicki T. BJ fibroblasts display high antioxidant capacity and slow telomere shortening independent of hTERT transfection. Free Radic Biol Med. 2001; 31: 824-831.

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