Kumiss Supplementation Reduces Oxidative Stress and Activates Sirtuin Deacetylases by Regulating Antioxidant System

References

• Danova S, Petrov K, Pavlov P, and Petrova P: Isolation and characterization of Lactobacillus strains involved in koumiss fermentation. Int J Dairy Techol 2, 100–105, 2005.
   Web of Science ®Google Scholar
• Kurmann JA, Rasic JLj, and Kroger M: Encylopedia of Fermented Fresh Milk Products. New York: AVI Books Van Nostrand Reinhold, 1982.
   Google Scholar
• Mendes KL, Lelis DF, and Santos S: Nuclear sirtuins and inflammatory signaling pathways. Cytokine Growth Factor Rev 38, 98–105, 2017.
   PubMed Web of Science ®Google Scholar
• Park SH, Ozden O, Jiang H, Cha YI, Pennington JD, et al. Sirt3, mitochondrial ROS, ageing, and carcinogenesis. Int J Mol Sci 12, 6226–6239, 2011.
   PubMed Web of Science ®Google Scholar
• Pozharisski KM, Kapustin YM, Likhachev AJ, and Shaposhnikov JD: The mechanism of carcinogenic action of 1,2-dimethylhydrazine (SDMH) in rats. Int J Cancer 15, 673–683, 1975.
   PubMed Web of Science ®Google Scholar
• Sosa V, Moliné T, Somoza R, Paciucci R, Kondoh H, and LLeonart ME: Oxidative stress and cancer: an overview. Ageing Res Rev 12, 376–390, 2013.
   PubMed Web of Science ®Google Scholar
• Beutler E, Duron O, and Kelly BM: Improved method for the determination of blood glutathione. J Lab Clin Med 61, 882–888, 1963.
   PubMed Web of Science ®Google Scholar
• Leblanc AM, and Perdigon G: Yogurt feeding inhibits promotion and progression of experimental colorectal cancer. Med Sci Monit 10, 96–104, 2004.
   Web of Science ®Google Scholar
• Newell LE, and Heddle JA: The potent colon carcinogen, 1,2-dimethylhydrazine induces mutations primarily in the colon. Mutat Res 564, 1–7, 2004.
   PubMed Web of Science ®Google Scholar
• Liboredo JC, Anastácio LR, Pelúzio MCG, Valente FX, Penido LCP, et al. Effect of probiotics on the development of dimethylhydrazine-induced preneoplastic lesions in the mice colon. Acta Cir Bras 28, 367–372, 2013.
   PubMed Web of Science ®Google Scholar
• Lee NK, Park JS, Park E, and Paik HD: Adherence and anticarcinogenic effects of Bacillus polyfermenticus SCD in the large intestine. Lett Appl Microbiol 44, 274–278, 2007.
   PubMed Web of Science ®Google Scholar
• Kumar A, Singh NK, and Sinha PR: Inhibition of 1,2-dimethylhydrazine induced colon genotoxicity in rats by the administration of probiotic curd. Mol Biol Rep 37, 1373–1376, 2010.
   PubMed Web of Science ®Google Scholar
• Appleyard CB, Cruz ML, Isidro AA, Arthur JC, Jobin C, et al. Pretreatment with the probiotic VSL#3 delays transition from inflammation to dysplasia in a rat model of colitis-associated cancer. Am J Physiol Gastrointest Liver Physiol 301, 1004–1013, 2011.
   PubMed Web of Science ®Google Scholar
• Rangarajan P, Karthikeyan A, Lu J, Ling EA, and Dheen ST: Sirtuin 3 regulates Foxo3a-mediated antioxidant pathway in microglia. Neuroscience 311, 398–414, 2015.
   PubMed Web of Science ®Google Scholar
• Papa L, and Germain D: Sirt3 regulates the mitochondrial unfolded protein response. Mol Cell Biol 34, 699–710, 2014.
   PubMed Web of Science ®Google Scholar
• Nakamura Y, Ogura M, Tanaka D, and Inagaki N: Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5. Biochem Biophys Res Commun 366, 174–179, 2008.
   PubMed Web of Science ®Google Scholar
• Scher MB, Vaquero A, and Reinberg D: SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress. Genes Dev 21, 920–928, 2007.
   PubMed Web of Science ®Google Scholar
• Iwahara T, Bonasio R, Narendra V, and Reinberg D: SIRT3 functions in the nucleus in the control of stress-related gene expression. Mol Cell Biol 32, 5022–5034, 2012.
   PubMed Web of Science ®Google Scholar
• Palmirotta F, Cives M, Della-Morte D, Capuani B, Lauro D, et al. Sirtuins and cancer: role in the epithelial–mesenchymal transition. Oxid Med Cell Longev 2016, 1–9, 2016.
   Web of Science ®Google Scholar
• Bell EL, Emerling BM, Ricoult SJ, and Guarente L: SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production. Oncogene 30, 2986–2996, 2011.
   PubMed Web of Science ®Google Scholar
• Kim HS, Patel K, Muldoon-Jacobs K, Bisht KS, Aykin-Burns N, et al. SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress. Cancer Cell 17, 41–52, 2010.
   PubMed Web of Science ®Google Scholar
• Kulıć A, Sırotkovıć-Skerlev M, Dedıć Plavetıć N, Belev B, Kralık-Oguıć S, et al. Sirtuins in tumorigenesis. Period Biol 116, 381–386, 2014.
   Web of Science ®Google Scholar
• Ozden O: SIRT2-JAK1 interaction decreases IL-6 induced inflammatory response in cancer cells. Kafkas Uni J Fac Vet Med 21, 813–817, 2015.
   Web of Science ®Google Scholar
• Fiskus W, Coothankandaswamy V, Chen J, Ma H, Ha K, et al. SIRT2 deacetylates and inhibits the peroxidase activity of peroxiredoxin-1 to sensitize breast cancer cells to oxidant stress-inducing agents. Cancer Res 76, 5467–5478, 2016.
   PubMed Web of Science ®Google Scholar
• Liu PY, Xu N, Malyukova A, Scarlett CJ, Sun YT, et al. The histone deacetylase SIRT2 stabilizes Myc oncoproteins. Cell Death Differ 20, 503–505, 2013.
   PubMed Web of Science ®Google Scholar
• Chen J, Chan AW, To KF, Chen W, Zhang Z, et al. SIRT2 overexpression in hepatocellular carcinoma mediates epithelial to mesenchymal transition by protein kinase B/glycogen synthase kinase-3b/β-catenin signaling. Hepatology 57, 2287–2298, 2013.
   PubMed Web of Science ®Google Scholar
• Ma L, Maruwge W, Strambi A, D'Arcy P, Pellegrini P, et al. SIRT1 and SIRT2 inhibition impairs pediatric soft tissue sarcoma growth. Cell Death Dis 5, e1483–11, 2014.
   PubMed Web of Science ®Google Scholar
• Someya S, Yu W, Hallows WC, Xu J, Vann JM, et al. Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction. Cell 143, 802–812, 2010.
   PubMed Web of Science ®Google Scholar
• Anilakumar KR, Nagaraj NS, and Santhanam K: Protective effects of amla on oxidative stress and toxicity in rats challenged with dimethyl hydrazine. Nutr Res 24, 313–319, 2004.
   Web of Science ®Google Scholar
• Jrah-Harzallah H, Ben-Hadj-Khalifa S, Almawi WY, Maaloul A, Houas Z, et al. Effect of thymoquinone on 1,2-dimethyl-hydrazine-induced oxidative stress during initiation and promotion of colon carcinogenesis. Eur J Cancer 49, 1127–1135, 2013.
   PubMed Web of Science ®Google Scholar
• Habib HM, Ibrahim WH, Schneider-Stock R, and Hassan HM: Camel milk lactoferrin reduces the proliferation of colorectal cancer cells and exerts antioxidant and DNA damage inhibitory activities. Food Chem 141, 148–152, 2013.
   PubMed Web of Science ®Google Scholar