| Peer-Reviewed

Hydrogen Sulfide and SIRT3 Gene, the Strong Preventive and Therapeutic Agent in Aging and Age Related Diseases

Received: 23 October 2014    Accepted: 6 November 2014    Published: 18 December 2014
Views:       Downloads:
Abstract

There are seven SIRT isoforms in mammals, with different biological activities including gene regulation, metabolism and apoptosis. Despite recent controversy about sirtuins function in some organisms, among them SIRT3 is the only sirtuin whose increased expression has been shown to correlate with an extended life span in humans. SIRT3 is a member of the sirtuin family of NAD+ dependent deacetylases, which is localized to the mitochondria and is enriched in kidney, brown adipose tissue, heart, and other metabolically active tissues. It is an endogenous negative regulator of cardiac hypertrophy, which protects hearts by suppressing cellular levels of ROS and modulates mitochondrial intermediary metabolism and fatty acid utilization during fasting. Another one, Hydrogen sulfide is produced within the human body, and relaxes the vascular endothelium and smooth muscle cells, which is important to maintaining clean arteries as one age. It functions as an antioxidant and inhibits expression of pro-inflammatory factors, all of which imply an important role in aging and age-associated diseases. The aim of this review is to find out the anti aging properties of SIRT3 and H2S that can be used to extend the life span of human as a preventive and therapeutic agent.

Published in American Journal of BioScience (Volume 2, Issue 6)
DOI 10.11648/j.ajbio.20140206.16
Page(s) 222-232
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

SIRT3, H2S, ROS, Aging

References
[1] Polito L., Kehoe PG., Forloni G., Albani D. (2010) The molecular genetics of sirtuins: association with humanlongevity and age-related diseases. Int J Mol Epidemiol Genet 1(3):214-225.
[2] Scher MB., Vaquero A., Reinberg D. (2007) SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev. 21:920–928.
[3] Sundaresan NR., Samant SA., Pillai VB., Rajamohan SB., Gupta MP. (2008) SIRT3 Is a Stress-Responsive Deacetylase in Cardiomyocytes That Protects Cells from Stress-Mediated Cell Death by Deacetylation of Ku70. Molecular and Cellular Biology. 28(20):6384–6401.
[4] Jacobs KM., Pennington JD., Bisht KS., Aykin-Burns N., Kim HS., Mishra M., Sun L., Nguyen P., Ahn BH., Leclerc J., Deng CX., Spitz DR., Gius D. (2008) SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression. Int J Biol Sci. 4:291–299.
[5] Cimen H., Han MJ., Yang Y., Tong Q., Koc H., Koc EC. (2009) Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria. Biochemistry. 49:304–311.
[6] Onyango P., Celic I., McCaffery JM., Boeke JD., Feinberg AP. (2002) SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria. Proc Natl Acad Sci USA. 99:13653–13658.
[7] Schwer B., North BJ., Frye RA., Ott M., Verdin E. (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol. 158:647–657.
[8] Hallows WC., Lee S., Denu JM. (2006) Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc Natl Acad Sci USA. 103:10230–10235.
[9] Kenyon CJ. (2010) The genetics of ageing. Nature 464:504–512.
[10] Sahin E., Depinho RA. (2010) Linking functional decline of telomeres, mitochondria and stem cells during ageing. Nature 464:520–528.
[11] Ito K., Hirao A., Arai F., Takubo K., Matsuoka S., Miyamoto K., Ohmura M., Naka K., Hosokawa K., Ikeda Y., Suda T. (2006) Reactive oxygenspecies act through p38 MAPK to limit the lifespan of hematopoietic stem cells. Nat. Med. 12:446–451.
[12] Paik JH., Ding Z., Narurkar R., Ramkissoon S., Muller F., Kamoun WS., Chae SS., Zheng H., Ying H., Mahoney J., Hiller D., Jiang S., Protopopov A., Wong WH., Chin L., Ligon KL., DePinho RA. (2009) FoxOs cooperatively regulate diverse pathways governing neural stem cell homeostasis. Cell Stem Cell. 5:540–553.
[13] Bellizzi D., Rose G., Cavalcante P., Covello G., Dato S., De Rango F., Greco V., Maggiolini M., Feraco E., Mari V., Franceschi C., Passarino G., De Benedictis G. (2005) A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages. Genomics. 85:258–263.
[14] Zhang Y., Tang ZH., Ren Z., Qu SL., Liu MH., Liu LS., Jiang ZS. (2013) Hydrogen sulfide: the next potent preventive and therapeutic agent in aging and age-associated diseases. Mol. Cell. Bio. 33(6):1104-13.
[15] Palacios OM., Carmona JJ., Michan S., Chen KY., Manabe Y., Ward JL., Goodyear LJ., Tong Q.(2009) Diet and exercise signals regulate SIRT3 and activate AMPK and PGC‐1α in skeletal muscle. Aging. 1(9):771-783.
[16] Guarente L., Picard F. (2005) Calorie restriction the SIR2 connection. Cell. 120:473-482.
[17] Kim SC., Sprung, R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L.,Grishin N. V., White M., Yang XJ., Zhao Y. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.Mol. Cell. 23:607–618.
[18] Gerhart-Hines Z., Rodgers JT., Bare O., Lerin C., Kim SH., Mostoslavsky R., Alt FW., Wu Z., Puigserver P. (2007) Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1alpha.EMBO J. 26:1913–1923.
[19] Schwer B., Bunkenborg J., Verdin RO., Andersen JS., Verdin E. (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc Natl Acad Sci U S A. 103:10224-10229.
[20] O'Brien TW., O'Brien BJ., Norman RA. (2005) Nuclear MRP genes and mitochondrial disease. Gene. 354:147–151.
[21] Miller JL., Koc, H., and Koc, E. C. (2008).Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3.Protein Sci. 17, 251–260.
[22] Yang Y., Cimen H., Han M-J., Shi T., Deng J-H., Koc H., Palacios OM., Montier L., Bai Y., Tong Q., Koc EC. (2010) NAD-dependent Deacetylase SIRT3 Regulates Mitochondrial Protein Synthesis by Deacetylation of the Ribosomal Protein MRPL10. Journal of Biological Chemistry. 285 (10):7417–7429.
[23] Frey N., Katus HA., Olson EN., Hill JA. (2004) Hypertrophy of the heart: a new therapeutic target? Circulation. 109:1580–1589.
[24] Sundaresan NR., Gupta M., Kim G., Rajamohan SB., Isbatan A., Gupta MP. (2009) Sirt3 blocks the cardiac hypertrophic response by augmenting Foxo3a-dependent antioxidant defense mechanisms in mice. J. Clin. Invest. 119:2758–2771.
[25] Guarente L. (2006) Sirtuins as potential targets for metabolic syndrome. Nature. 444:868–874.
[26] Hirschey MD., Shimazu T., Goetzman E., Jing E., Schwer B., Lombard DB., Grueter CA., Harris C., Biddinger S., Ilkayeva OR., Stevens RD., Li Y., Saha AK., Ruderman NB., Bain JR., Newgard CB., Farese Jr RV., Alt FW., Kahn CR., Verdin E. (2010) SIRT3 regulates fatty acid oxidation via reversible enzyme Deacetylation. Nature. 464(7285):121–125.
[27] Oberley LW., Oberley TD. (1988) Role of antioxidant enzymes in cell immortalization and transformation. Mol Cell Biochem. 84:147-153.
[28] Lanza IR., Short DK., Short KR., Raghavakaimal S., Basu R., Joyner MJ., McConnell JP., Nair KS. (2008) Endurance exercise as a countermeasure for aging. Diabetes. 57:2933-2942.
[29] Henderson JR., Swalwell H., Boulton S., Manning P., McNeil CJ., Birch-Machin MA. (2009) Direct, real-time monitoring of superoxide generation in isolated mitochondria. Free Radic Res. 43:796-802.
[30] Spitz DR., Adams DT., Sherman CM., Roberts RJ. (1992) Mechanisms of cellular resistance to hydrogen peroxide, hyperoxia, and 4hydroxy 2 nonenal toxicity: the significance of increased catalase activity in H2O2 resistant fibroblasts. Arch Biochem Biophys. 292:221-227.
[31] Sies H. (1991) Oxidative stress: from basic research to clinical application. Am J Med. 91:31S-38S.
[32] Ozden O., Park S-H., Kim H-S., Jiang H., Coleman MC., Spitz DR., Gius D. (2011) Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress. Aging. 3:2
[33] Bao J., Scott I., Lu Z., Pang L., Dimond CC., Gius D., Sack MN. (2010) SIRT3 is regulated by nutrient excess and modulates hepatic susceptibility to lipotoxicity. Free Radic Biol Med. 49(7): 1230–1237.
[34] McGarry JD., Foster DW. (1980) Regulation of hepatic fatty acid oxidation and ketone body production. Annu. Rev. Biochem. 49:395–420.
[35] Laffel L. (1999) Ketone bodies: a review of physiology, pathophysiology and application of monitoring to diabetes. Diabetes Metab. Res. Rev.15:412–426.
[36] Shimazu T., Hirschey MD., Hua L., Dittenhafer-Reed KE., Schwer B., Lombard DB., Li Y., Bunkenborg J., Alt FW., Denu JM., Jacobson MP., Verdin E. (2010) SIRT3 Deacetylates Mitochondrial 3-Hydroxy-3 Methylglutaryl CoA Synthase 2 and Regulates Ketone Body Production. Cell Metab. 12(6): 654–661.
[37] Warburg O. (1956) On the origin of cancer cells. Science.123:309–314.
[38] Tong X., Zhao F., Thompson CB. (2009) The molecular determinants of de novo nucleotide biosynthesis in cancer cells. Curr Opin Genet Dev.19:32–37.
[39] Gatenby RA., Gillies RJ. (2004) Why do cancers have high aerobic glycolysis? Nat Rev Cancer. 4:891-899.
[40] Kaelin WG Jr., Ratcliffe PJ. (2008) Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol Cell. 30:393–402.
[41] Semenza GL. (2010) HIF-1: upstream and downstream of cancer metabolism. Curr Opin Genet Dev. 20:51–56.
[42] Tennant DA., Duran RV., Gottlieb E. (2010) Targeting metabolic transformation for cancer therapy. Nat Rev Cancer.10:267–277.
[43] Gottlieb E., Tomlinson IP. (2005) Mitochondrial tumour suppressors: a genetic and biochemical update. Nat Rev Cancer. 5:857–866.
[44] Zhao S., Lin Y., Xu W., Jiang W., Zha Z., Wang P., Yu W., Li Z., Gong L., Peng Y. (2009) Glioma-derived mutations in IDH1 dominantly inhibits IDH1 catalytic activity and induces HIF-1alpha. Science. 324:261–265.
[45] Finley LWS., Carracedo A., Lee J., Souza A., Egia A., Zhang J., Teruya-Feldstein J., Moreira PI., Cardoso SM., Clish CB., Pandolfi PP., Haigis MC. (2011) SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization. Cancer Cell. 19(3): 416–428.
[46] Schumacker PT. (2011) SIRT3 Controls Cancer Metabolic Reprogramming by Regulating ROS and HIF. Cancer Cell. 19(3): 299–300.
[47] Hirschey MD., Shimazu T., Jing E., Grueter CA., Collins AM., Aouizerat B., Stančáková A., Goetzman E., Lam MM., Schwer B., Stevens RD., Muehlbauer MJ., Kakar S., Bass NM., Kuusisto J., Laakso M., Alt FW., Newgard CB., Farese Jr RV., Kahn CR., Verdin E. (2011) SIRT3 Deficiency and Mitochondrial Protein Hyperacetylation Accelerate the Development of the Metabolic Syndrome. Mol Cell. 44(2): 177–190.
[48] Wang GL., Jiang BH., Rue EA., Semenza GL. (1995) Hypoxiainducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci U S A. 92(12):5510-5514.
[49] Webb J., Coleman M., Pugh C. (2009) Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing. Cell Mol Life Sci. 66:3539–3554.
[50] Semenza GL. (2003) Targeting HIF-1 for cancer therapy. Nat Rev Cancer. 3:721–732.
[51] Bell EL., Emerling BM., SJH Ricoult SJH., Guarente L.( 2011) SirT3 suppresses hypoxia inducible factor 1a and tumor growth by inhibiting mitochondrial ROS production. Oncogene. 30:2986–2996.
[52] Mattson MP., Liu D. (2002) Energetics and oxidative stress in synaptic plasticity and neurodegenerative disorders. Neuromolecular Med. 2: 215–231.
[53] Zeng J., Yang GY., Ying W., Kelly M., Hirai K., James TL., Swanson RA., Litt L. (2007) Pyruvate improves recovery after PARP-1-associated energy failure induced by oxidative stress in neonatal rat cerebrocortical slices. J Cereb Blood Flow Metab. 27:304–315.
[54] Liu D., Pitta M., Mattson MP. (2008) Preventing NAD(+) depletion protects neurons against excitotoxicity: bioenergetic effects of mild mitochondrial uncoupling and caloric restriction. Ann N Y Acad Sci. 1147:275–282.
[55] Wang S., Xing Z., Vosler PS., Yin H., Li W., Zhang F., Signore AP., Stetler RA., Gao Y., Chen J. (2008) Cellular NAD replenishment confers marked neuroprotection against ischemic cell death: role of enhanced DNA repair. Stroke. 39:2587–2595.
[56] Yu SW., Andrabi SA., Wang H., Kim NS., Poirier GG., Dawson TM., Dawson VL. (2006) Apoptosisinducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death.Proc Natl Acad Sci USA. 103(48):18314–18319.
[57] Liu D., Gharavi R., Pitta M., Gleichmann M., Mattson MP. (2009) Nicotinamide prevents NAD+ depletion and protects neurons against excitotoxicity and cerebral ischemia: NAD+ consumption by SIRT1 may endanger energetically compromised neurons. Neuromolecular Med. 11: 28–42.
[58] Ying W., Sevigny MB., Chen Y., Swanson RA. (2001) Poly (ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death. Proc Natl Acad Sci USA. 98:12227–12232.
[59] Yu SW., Wang H., Poitras MF., Coombs C., Bowers WJ., Federoff HJ., Poirier GG., Dawson TM., Dawson VL. (2002) Mediation of poly (ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science. 297:259–263
[60] Alano CC., Ying W., Swanson RA. (2004) Poly(ADP-ribose) polymerase-1- mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition. J Biol Chem. 279:18895–18902.
[61] Alano CC., Tran A., Tao R., Ying W., Karliner JS., Swanson RA. (2007) Differences among cell types in NAD(+) compartmentalization: a comparison of neurons, astrocytes, and cardiac myocytes. J Neurosci Res. 85:3378–3385.
[62] Kim SH., Lu HF., Alano CC. (2011) Neuronal Sirt3 Protects against Excitotoxic Injury in Mouse Cortical Neuron Culture. PLoS ONE. 6(3): e14731.
[63] Ballatori N., Krance SM., Notenboom S., Shi S., Tieu K., Hammond CL. (2009) Glutathione dysregulation and the etiology and progression of human diseases. Biol Chem. 390:191–214.
[64] Ishigami M., Hiraki K., Umemura K., Ogasawara Y., Ishii K., Kimura H. (2009) A source of hydrogen sulfide and a mechanism of its release in the brain. Antioxid Redox Signal. 11:205–214,
[65] Tang G., Wu L., Wang R. (2010) Interaction of hydrogen sulfide with ion channels. Clin Exp Pharmacol Physiol. 37:753– 763.
[66] Wallace JL. (2010) Physiological and pathophysiological roles of hydrogen sulfide in the gastrointestinal tract. Antioxid Redox Signal. 12: 1125–1133.
[67] Aggarwal BB., Gehlot P. (2009) Inflammation and cancer: How friendly is the relationship for cancer patients? Curr Opin Pharmacol. 9:351–369.
[68] Lee S., Park Y., Zuidema MY., Hannink M., Zhang C. (2011) Effects of interventions on oxidative stress and inflammation of cardiovascular diseases. World J Cardiol. 3:18–24.
[69] Pan LL., Liu XH., Gong QH., Wu D., Zhu YZ. (2011) Hydrogen sulfide attenuated tumor necrosis factor alpha-induced inflammatory signaling and dysfunction in vascular endothelial cells. PLoS One. 6: e19766.
[70] Kida K., Yamada M., Tokuda K., Marutani E., Kakinohana M., Kaneki M., Ichinose F. (2011) Inhaled hydrogen sulfide prevents neurodegeneration and movement disorder in a mouse model of Parkinson’s disease. Antioxid Redox Signal. 15:343–352.
[71] Fiorucci S., Distrutti E., Cirino G., Wallace JL. (2006) The emerging roles of hydrogen sulfide in the gastrointestinal tract and liver. Gastroenterology 131: 259–271.
[72] Aminzadeh MA., Vaziri ND. (2012) Downregulation of the renal and hepatic hydrogen sulfide (H2S)-producing enzymes and capacity in chronic kidney disease. Nephrol Dial Transplant. 27:498–504.
[73] Lin CC., Yin MC. (2008) Antiglycative and anti-VEGF effects of S-ethyl cysteine and S-propyl cysteine in kidney of diabetic mice. Mol Nutr Food Res. 52:1358–1364.
[74] Sen U., Basu P., Abe OA., Givvimani S., Tyagi N., Metreveli N., Shah KS., Passmore JC., Tyagi SC. (2009) Hydrogen sulfide ameliorates hyperhomocysteinemia-associated chronic renal failure. Am J Physiol Renal Physiol. 297:F410–419.
[75] Morsy MA., Ibrahim SA., Abdelwahab SA., Zedan MZ., Elbitar HI. (2010) Curative effects of hydrogen sulfide against acetaminophen-induced hepatotoxicity in mice. Life Sci. 87:692–698.
[76] Olson KR. (2009) Is hydrogen sulfide a circulating ‘‘gasotransmitter’’ in vertebrate blood? Biochim Biophys Acta. 1787:856–863.
[77] Nagy P., Winterbourn CC. (2010) Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides. Chem Res Toxicol. 23:1541– 1543.
[78] Kimura Y., Goto Y., Kimura H. (2010) Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria. Antioxid Redox Signal. 12: 1–13.
[79] Stasko A., Brezova V., Zalibera M., Biskupic S., Ondrias K. (2009) Electron transfer: A primary step in the reactions of sodium hydrosulphide, an H2S/HS(-) donor. Free Radic Res. 43:581–593.
[80] Olson KR., Whitfield NL. (2010) Hydrogen sulfide and oxygen sensing in the cardiovascular system. Antioxid Redox Signal. 12:1219–1234.
[81] Osborne NN., Ji D., Abdul Majid AS., Fawcett RJ., Sparatore A., Del Soldato P. (2010) ACS67, a hydrogen sulfide-releasing derivative of latanoprost acid, attenuates retinal ischemia and oxidative stress to RGC-5 cells in culture. Invest Ophthalmol Vis Sci. 51: 284–294.
[82] Bass SE., Sienkiewicz P., Macdonald CJ., Cheng RY., Sparatore A., Del Soldato P., Roberts DD., Moody TW.., Wink DA., Yeh GC. (2009) Novel dithiolethione-modified nonsteroidal anti-inflammatory drugs in human hepatoma HepG2 and colon LS180 cells. Clin Cancer Res. 15:1964–1972.
[83] Mantovani G., Madeddu C., Maccio A., Gramignano G., Lusso MR., Massa E., Astara G., Serpe R. (2004) Cancer-related anorexia/cachexia syndrome and oxidative stress: An innovative approach beyond current treatment. Cancer Epidemiol Biomarkers Prev. 13:1651–1659.
[84] Nian H., Delage B., Ho E., Dashwood RH. (2009) Modulation of histone deacetylase activity by dietary isothiocyanates and allyl sulfides: Studies with sulforaphane and garlic organosulfur compounds. Environ Mol Mutagen. 50:213–221.
[85] Droge W., Kinscherf R. (2008) Aberrant insulin receptor signaling and amino acid homeostasis as a major cause of oxidative stress in aging. Antioxid Redox Signal. 10:661– 678.
[86] Nimni ME., Han B., Cordoba F. (2007) Are we getting enough sulfur in our diet? Nutr Metab (Lond). 4: 24.
[87] Howard EW., Ling MT., Chua CW., Cheung HW., Wang X., Wong YC. (2007) Garlic-derived S-allylmercaptocysteine is a novel in vivo antimetastatic agent for androgen-independent prostate cancer. Clin Cancer Res. 13:1847–1856.
[88] Ma K., Liu Y., Zhu Q., Liu CH., Duan JL., Tan BK., Zhu YZ. (2011) H2S donor, S-propargyl-cysteine, increases CSE in SGC-7901 and cancer-induced mice: Evidence for a novel anti-cancer effect of endogenous H2S? PLoS One 6:e20525.
Cite This Article
  • APA Style

    Md. Shamim Hossain, Md. Ashrafuzzaman Sapon, Naim Hassan. (2014). Hydrogen Sulfide and SIRT3 Gene, the Strong Preventive and Therapeutic Agent in Aging and Age Related Diseases. American Journal of BioScience, 2(6), 222-232. https://doi.org/10.11648/j.ajbio.20140206.16

    Copy | Download

    ACS Style

    Md. Shamim Hossain; Md. Ashrafuzzaman Sapon; Naim Hassan. Hydrogen Sulfide and SIRT3 Gene, the Strong Preventive and Therapeutic Agent in Aging and Age Related Diseases. Am. J. BioScience 2014, 2(6), 222-232. doi: 10.11648/j.ajbio.20140206.16

    Copy | Download

    AMA Style

    Md. Shamim Hossain, Md. Ashrafuzzaman Sapon, Naim Hassan. Hydrogen Sulfide and SIRT3 Gene, the Strong Preventive and Therapeutic Agent in Aging and Age Related Diseases. Am J BioScience. 2014;2(6):222-232. doi: 10.11648/j.ajbio.20140206.16

    Copy | Download

  • @article{10.11648/j.ajbio.20140206.16,
      author = {Md. Shamim Hossain and Md. Ashrafuzzaman Sapon and Naim Hassan},
      title = {Hydrogen Sulfide and SIRT3 Gene, the Strong Preventive and Therapeutic Agent in Aging and Age Related Diseases},
      journal = {American Journal of BioScience},
      volume = {2},
      number = {6},
      pages = {222-232},
      doi = {10.11648/j.ajbio.20140206.16},
      url = {https://doi.org/10.11648/j.ajbio.20140206.16},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbio.20140206.16},
      abstract = {There are seven SIRT isoforms in mammals, with different biological activities including gene regulation, metabolism and apoptosis. Despite recent controversy about sirtuins function in some organisms, among them SIRT3 is the only sirtuin whose increased expression has been shown to correlate with an extended life span in humans. SIRT3 is a member of the sirtuin family of NAD+ dependent deacetylases, which is localized to the mitochondria and is enriched in kidney, brown adipose tissue, heart, and other metabolically active tissues. It is an endogenous negative regulator of cardiac hypertrophy, which protects hearts by suppressing cellular levels of ROS and modulates mitochondrial intermediary metabolism and fatty acid utilization during fasting. Another one, Hydrogen sulfide is produced within the human body, and relaxes the vascular endothelium and smooth muscle cells, which is important to maintaining clean arteries as one age. It functions as an antioxidant and inhibits expression of pro-inflammatory factors, all of which imply an important role in aging and age-associated diseases. The aim of this review is to find out the anti aging properties of SIRT3 and H2S that can be used to extend the life span of human as a preventive and therapeutic agent.},
     year = {2014}
    }
    

    Copy | Download

  • TY  - JOUR
    T1  - Hydrogen Sulfide and SIRT3 Gene, the Strong Preventive and Therapeutic Agent in Aging and Age Related Diseases
    AU  - Md. Shamim Hossain
    AU  - Md. Ashrafuzzaman Sapon
    AU  - Naim Hassan
    Y1  - 2014/12/18
    PY  - 2014
    N1  - https://doi.org/10.11648/j.ajbio.20140206.16
    DO  - 10.11648/j.ajbio.20140206.16
    T2  - American Journal of BioScience
    JF  - American Journal of BioScience
    JO  - American Journal of BioScience
    SP  - 222
    EP  - 232
    PB  - Science Publishing Group
    SN  - 2330-0167
    UR  - https://doi.org/10.11648/j.ajbio.20140206.16
    AB  - There are seven SIRT isoforms in mammals, with different biological activities including gene regulation, metabolism and apoptosis. Despite recent controversy about sirtuins function in some organisms, among them SIRT3 is the only sirtuin whose increased expression has been shown to correlate with an extended life span in humans. SIRT3 is a member of the sirtuin family of NAD+ dependent deacetylases, which is localized to the mitochondria and is enriched in kidney, brown adipose tissue, heart, and other metabolically active tissues. It is an endogenous negative regulator of cardiac hypertrophy, which protects hearts by suppressing cellular levels of ROS and modulates mitochondrial intermediary metabolism and fatty acid utilization during fasting. Another one, Hydrogen sulfide is produced within the human body, and relaxes the vascular endothelium and smooth muscle cells, which is important to maintaining clean arteries as one age. It functions as an antioxidant and inhibits expression of pro-inflammatory factors, all of which imply an important role in aging and age-associated diseases. The aim of this review is to find out the anti aging properties of SIRT3 and H2S that can be used to extend the life span of human as a preventive and therapeutic agent.
    VL  - 2
    IS  - 6
    ER  - 

    Copy | Download

Author Information
  • Department of Biotechnology and Genetic Engineering, Faculty of Applied Science and Technology, Islamic University, Kushtia-7003, Bangladesh

  • Department of Biotechnology and Genetic Engineering, Faculty of Applied Science and Technology, Islamic University, Kushtia-7003, Bangladesh; Bioscience Division, Graduate school of Science & Technology, Shizuoka University, Shizuoka, Japan

  • Department of Biotechnology and Genetic Engineering, Faculty of Applied Science and Technology, Islamic University, Kushtia-7003, Bangladesh

  • Sections