- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Recently Accepted Articles ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
Volume 2011 (2011), Article ID 869647, 8 pages
Histone Deacetylase Inhibition and Dietary Short-Chain Fatty Acids
1Allergy and Immune Disorders, Murdoch Childrens Research Institute, Royal Children's Hospital, Flemington Road, Parkville, VIC 3052, Australia
2Department of Paediatrics, The University of Melbourne, Parkville, VIC 3010, Australia
3Epigenomic Medicine, Baker IDI Heart and Diabetes Institute, The Alfred Medical Research and Education Precinct, 75 Commercial Road, Melbourne, VIC 3004, Australia
4Department of Pathology, The University of Melbourne, Parkville, VIC 3010, Australia
Received 12 November 2011; Accepted 5 December 2011
Academic Editors: V. Calder, C. I. Ezeamuzie, E. A. García-Zepeda, and R. Paganelli
Copyright © 2011 Paul V. Licciardi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- P. A. Marks and R. Breslow, “Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug,” Nature Biotechnology, vol. 25, no. 1, pp. 84–90, 2007.
- C. Campàs-Moya, “Romidepsin for the treatment of cutaneous T-cell lymphoma,” Drugs of Today, vol. 45, no. 11, pp. 787–795, 2009.
- F. A.A. Kwa, A. Balcerczyk, P. Licciardi, A. El-Osta, and T. C. Karagiannis, “Chromatin modifying agents—the cutting edge of anticancer therapy,” Drug Discovery Today, vol. 16, no. 13-14, pp. 543–547, 2011.
- P. A. Marks, “Histone deacetylase inhibitors: a chemical genetics approach to understanding cellular functions,” Biochimica et Biophysica Acta, vol. 1799, no. 10-12, pp. 717–725, 2010.
- P. A. Marks and W. S. Xu, “Histone deacetylase inhibitors: potential in cancer therapy,” Journal of Cellular Biochemistry, vol. 107, no. 4, pp. 600–608, 2009.
- M. Dokmanovic, C. Clarke, and P. A. Marks, “Histone deacetylase inhibitors: overview and perspectives,” Molecular Cancer Research, vol. 5, no. 10, pp. 981–989, 2007.
- R. A. Blaheta and J. Cinatl Jr., “Anti-tumor mechanisms of valproate: a novel role for an old drug,” Medicinal Research Reviews, vol. 22, no. 5, pp. 492–511, 2002.
- G. Rosenberg, “The mechanisms of action of valproate in neuropsychiatric disorders: can we see the forest for the trees?” Cellular and Molecular Life Sciences, vol. 64, no. 16, pp. 2090–2103, 2007.
- C. U. Johannessen, “Mechanisms of action of valproate: a commentatory,” Neurochemistry International, vol. 37, no. 2-3, pp. 103–110, 2000.
- M. Gottlicher, S. Minucci, P. Zhu et al., “Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells,” The EMBO Journal, vol. 20, no. 24, pp. 6969–6978, 2001.
- C. J. Phiel, F. Zhang, E. Y. Huang, M. G. Guenther, M. A. Lazar, and P. S. Klein, “Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen,” The Journal of Biological Chemistry, vol. 276, no. 39, pp. 36734–36741, 2001.
- O. H. Kramer, P. Zhu, H. P. Ostendorff et al., “The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2,” The EMBO Journal, vol. 22, no. 13, pp. 3411–3420, 2003.
- J. E. Shabason, P. J. Tofilon, and K. Camphausen, “Grand rounds at the National Institutes of Health: HDAC inhibitors as radiation modifiers, from bench to clinic,” Journal of Cellular and Molecular Medicine, vol. 15, no. 12, pp. 2735–2744, 2011.
- T. Kouzarides, “Chromatin modifications and their function,” Cell, vol. 128, no. 4, pp. 693–705, 2007.
- A. R. Cyr and F. E. Domann, “The redox basis of epigenetic modifications: from mechanisms to functional consequences,” Antioxidants & Redox Signaling, vol. 15, no. 2, pp. 551–589, 2011.
- M. H. Kuo and C. D. Allis, “Roles of histone acetyltransferases and deacetylases in gene regulation,” BioEssays, vol. 20, no. 8, pp. 615–626, 1998.
- P. A. Wade, D. Pruss, and A. P. Wolffe, “Histone acetylation: chromatin in action,” Trends in Biochemical Sciences, vol. 22, no. 4, pp. 128–132, 1997.
- S. Y. Roth, J. M. Denu, and C. D. Allis, “Histone acetyltransferases,” Annual Review of Biochemistry, vol. 70, pp. 81–120, 2001.
- B. C. Smith and J. M. Denu, “Chemical mechanisms of histone lysine and arginine modifications,” Biochimica et Biophysica Acta, vol. 1789, no. 1, pp. 45–57, 2009.
- M. C. Haigis and L. P. Guarente, “Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction,” Genes & Development, vol. 20, no. 21, pp. 2913–2921, 2006.
- J. Landry, J. T. Slama, and R. Sternglanz, “Role of NAD+ in the deacetylase activity of the SIR2-like proteins,” Biochemical and Biophysical Research Communications, vol. 278, no. 3, pp. 685–690, 2000.
- J. Landry, A. Sutton, S. T. Tafrov et al., “The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 11, pp. 5807–5811, 2000.
- Y. Horio, T. Hayashi, A. Kuno, and R. Kunimoto, “Cellular and molecular effects of sirtuins in health and disease,” Clinical Science, vol. 121, no. 5, pp. 191–203, 2011.
- G. S. Kelly, “A review of the sirtuin system, its clinical implications, and the potential role of dietary activators like resveratrol: part 2,” Alternative Medicine Review, vol. 15, pp. 313–328, 2010.
- A. J. M. de Ruijter, A. H. van Gennip, H. N. Caron, S. Kemp, and A. B. P. van Kuilenburg, “Histone deacetylases (HDACs): characterization of the classical HDAC family,” Biochemical Journal, vol. 370, no. 3, pp. 737–749, 2003.
- I. V. Gregoretti, Y. M. Lee, and H. V. Goodson, “Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis,” Journal of Molecular Biology, vol. 338, no. 1, pp. 17–31, 2004.
- J. E. Bolden, M. J. Peart, and R. W. Johnstone, “Anticancer activities of histone deacetylase inhibitors,” Nature Reviews Drug Discovery, vol. 5, no. 9, pp. 769–784, 2006.
- P. A. Marks, R. A. Rifkind, V. M. Richon, R. Breslow, T. Miller, and W. K. Kelly, “Histone deacetylases and cancer: causes and therapies,” Nature Reviews Cancer, vol. 1, no. 3, pp. 194–202, 2001.
- X. J. Yang and E. Seto, “Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression,” Current Opinion in Genetics & Development, vol. 13, no. 2, pp. 143–153, 2003.
- M. Martin, R. Kettmann, and F. Dequiedt, “Class IIa histone deacetylases: regulating the regulators,” Oncogene, vol. 26, no. 37, pp. 5450–5467, 2007.
- O. Witt, H. E. Deubzer, T. Milde, and I. Oehme, “HDAC family: what are the cancer relevant targets?” Cancer Letters, vol. 277, no. 1, pp. 8–21, 2009.
- A. Mai, D. Rotili, S. Valente, and A. G. Kazantsev, “Histone deacetylase inhibitors and neurodegenerative disorders: holding the promise,” Current Pharmaceutical Design, vol. 15, no. 34, pp. 3940–3957, 2009.
- S. Minucci and P. G. Pelicci, “Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer,” Nature Reviews Cancer, vol. 6, no. 1, pp. 38–51, 2006.
- W. S. Xu, R. B. Parmigiani, and P. A. Marks, “Histone deacetylase inhibitors: molecular mechanisms of action,” Oncogene, vol. 26, no. 37, pp. 5541–5552, 2007.
- A. Villagra, F. Cheng, H. W. Wang et al., “The histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance,” Nature Immunology, vol. 10, no. 1, pp. 92–100, 2009.
- A. Villagra, E. M. Sotomayor, and E. Seto, “Histone deacetylases and the immunological network: implications in cancer and inflammation,” Oncogene, vol. 29, no. 2, pp. 157–173, 2010.
- H. H. Chang, C. P. Chiang, H. C. Hung, C. Y. Lin, Y. T. Deng, and M. Y. P. Kuo, “Histone deacetylase 2 expression predicts poorer prognosis in oral cancer patients,” Oral Oncology, vol. 45, no. 7, pp. 610–614, 2009.
- A. Gloghini, D. Buglio, N. M. Khaskhely et al., “Expression of histone deacetylases in lymphoma: implication for the development of selective inhibitors,” British Journal of Haematology, vol. 147, no. 4, pp. 515–525, 2009.
- M. Dokmanovic and P. A. Marks, “Prospects: histone deacetylase inhibitors,” Journal of Cellular Biochemistry, vol. 96, no. 2, pp. 293–304, 2005.
- J. R. Davie, “Inhibition of histone deacetylase activity by butyrate,” Journal of Nutrition, vol. 133, pp. 2485S–2493S, 2003.
- H.-J. Kim and S.-C. Bae, “Histone deacetylase inhibitors: molecular mechanisms of action and clinical trials as anti-cancer drugs,” American Journal of Translational Research, vol. 3, no. 2, pp. 166–179, 2011.
- M. Yoshida, M. Kijima, M. Akita, and T. Beppu, “Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A,” The Journal of Biological Chemistry, vol. 265, no. 28, pp. 17174–17179, 1990.
- C. M. Arundel, A. S. Glicksman, and J. T. Leith, “Enhancement of radiation injury in human colon tumor cells by the maturational agent sodium butyrate (NaB),” Radiation Research, vol. 104, no. 3, pp. 443–448, 1985.
- J. T. Leith, “Potentiation of X ray sensitivity by combinations of sodium butyrate and buthionine sulfoximine,” International Journal of Radiation Oncology Biology Physics, vol. 15, no. 4, pp. 949–951, 1988.
- Z. Nackerdien, J. Michie, and L. Bohm, “Chromatin decondensed by acetylation shows an elevated radiation response,” Radiation Research, vol. 117, no. 2, pp. 234–244, 1989.
- Y. L. Chung, Y. H. W. Lee, S. H. Yen, and K. H. Chi, “A novel approach for nasopharyngeal carcinoma treatment uses phenylbutyrate as a protein kinase C modulator: implications for radiosensitization and EBV-targeted therapy,” Clinical Cancer Research, vol. 6, no. 4, pp. 1452–1458, 2000.
- G. Musso, R. Gambino, and M. Cassader, “Obesity, diabetes, and gut microbiota: the hygiene hypothesis expanded?” Diabetes Care, vol. 33, no. 10, pp. 2277–2284, 2010.
- J. Amar, C. Chabo, A. Waget et al., “Intestinal mucosal adherence and translocation of commensal bacteria at the early onset of type 2 diabetes: molecular mechanisms and probiotic treatment,” EMBO Molecular Medicine, vol. 3, no. 9, pp. 559–572, 2011.
- F. Backhed, H. Ding, T. Wang et al., “The gut microbiota as an environmental factor that regulates fat storage,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 44, pp. 15718–15723, 2004.
- F. Backhed, J. K. Manchester, C. F. Semenkovich, and J. I. Gordon, “Mechanisms underlying the resistance to diet-induced obesity in germ-free mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 3, pp. 979–984, 2007.
- M. L. K. Tang, “Probiotics and prebiotics: immunological and clinical effects in allergic disease,” Nestle Nutrition Workshop Series: Pediatric Program, vol. 64, pp. 219–238, 2009.
- G. C. Yap, K. K. Chee, P.-Y. Hong et al., “Evaluation of stool microbiota signatures in two cohorts of Asian (Singapore and Indonesia) newborns at risk of atopy,” BMC Microbiology, vol. 11, article 193, 2011.
- S. Mueller, K. Saunier, C. Hanisch et al., “Differences in fecal microbiota in different European study populations in relation to age, gender, and country: a cross-sectional study,” Applied and Environmental Microbiology, vol. 72, no. 2, pp. 1027–1033, 2006.
- V. Mai, Q. M. McCrary, R. Sinha, and M. Glei, “Associations between dietary habits and body mass index with gut microbiota composition and fecal water genotoxicity: an observational study in African American and Caucasian American volunteers,” Nutrition Journal, vol. 8, no. 1, article 49, 2009.
- D. W. Thomas and F. R. Greer, “Probiotics and prebiotics in pediatrics,” Pediatrics, vol. 126, pp. 1217–1231, 2010.
- B. Bjorksten, E. Sepp, K. Julge, T. Voor, and M. Mikelsaar, “Allergy development and the intestinal microflora during the first year of life,” The Journal of Allergy and Clinical Immunology, vol. 108, no. 4, pp. 516–520, 2001.
- S. Watanabe, Y. Narisawa, S. Arase et al., “Differences in fecal microflora between patients with atopic dermatitis and healthy control subjects,” The Journal of Allergy and Clinical Immunology, vol. 111, no. 3, pp. 587–591, 2003.
- M. Wang, C. Karlsson, C. Olsson et al., “Reduced diversity in the early fecal microbiota of infants with atopic eczema,” The Journal of Allergy and Clinical Immunology, vol. 121, no. 1, pp. 129–134, 2008.
- R. E. Ley, P. J. Turnbaugh, S. Klein, and J. I. Gordon, “Microbial ecology: human gut microbes associated with obesity,” Nature, vol. 444, no. 7122, pp. 1022–1023, 2006.
- P. J. Turnbaugh, M. Hamady, T. Yatsunenko et al., “A core gut microbiome in obese and lean twins,” Nature, vol. 457, no. 7228, pp. 480–484, 2009.
- A. Sandin, L. Bråbäck, E. Norin, and B. Bjorksten, “Faecal short chain fatty acid pattern and allergy in early childhood,” Acta Paediatrica, vol. 98, no. 5, pp. 823–827, 2009.
- O. C. Thompson-Chagoyan, M. Fallani, J. Maldonado et al., “Faecal microbiota and short-chain fatty acid levels in faeces from infants with cow's milk protein allergy,” International Archives of Allergy and Immunology, vol. 156, no. 3, pp. 325–332, 2011.
- M. Roberfroid, G. R. Gibson, L. Hoyles et al., “Prebiotic effects: metabolic and health benefits,” British Journal of Nutrition, vol. 104, supplement 2, pp. S1–S63, 1999.
- N. Huda-Faujan, A. S. Abdulamir, A. B. Fatimah, et al., “The impact of the level of the intestinal short chain Fatty acids in inflammatory bowel disease patients versus healthy subjects,” The Open Biochemistry Journal, vol. 4, pp. 53–58, 2010.
- G. D'Argenio and G. Mazzacca, “Short-chain fatty acid in the human colon: relation to inflammatory bowel diseases and colon cancer,” Advances in Experimental Medicine and Biology, vol. 472, pp. 149–158, 2000.
- K. M. Maslowski, A. T. Vieira, A. Ng et al., “Regulation of inflammatory responses by gut microbiota and chemoattractant receptor GPR43,” Nature, vol. 461, no. 7268, pp. 1282–1286, 2009.
- G. Musso, R. Gambino, M. Cassader, et al., “Interactions between gut microbiota and host metabolism predisposing to obesity and diabetes,” Annual Review of Medicine, vol. 62, pp. 361–380, 2011.
- M. Vijay-Kumar, J. D. Aitken, F. A. Carvalho et al., “Metabolie syndrome and altered gut microbiota in mice lacking toll-like receptor 5,” Science, vol. 328, no. 5975, pp. 228–231, 2010.
- R. Stienstra, J. A. van Diepen, C. J. Tack et al., “Inflammasome is a central player in the induction of obesity and insulin resistance,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 37, pp. 15324–15329, 2011.
- B. Vandanmagsar, Y. H. Youm, A. Ravussin et al., “The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance,” Nature Medicine, vol. 17, pp. 179–188, 2011.
- G. Caramia, “Metchnikoff and the centenary of probiotics: an update of their use in gastroenteric pathology during the age of development,” Minerva Pediatrica, vol. 60, no. 6, pp. 1417–1435, 2008.
- M. G. Gareau, P. M. Sherman, and W. A. Walker, “Probiotics and the gut microbiota in intestinal health and disease,” Nature Reviews Gastroenterology and Hepatology, vol. 7, pp. 503–514, 2010.
- G. Reid, J. A. Younes, H. C. van der Mei, G. B. Gloor, R. Knight, and H. J. Busscher, “Microbiota restoration: natural and supplemented recovery of human microbial communities,” Nature Reviews Microbiology, vol. 9, no. 1, pp. 27–38, 2011.
- M. Kalliomäki, S. Salminen, H. Arvilommi, P. Kero, P. Koskinen, and E. Isolauri, “Probiotics in primary prevention of atopic disease: a randomised placebo-controlled trial,” The Lancet, vol. 357, no. 9262, pp. 1076–1079, 2001.
- H. Sokol, B. Pigneur, L. Watterlot et al., “Faecalibacterium prausnitzii is an anti-inflammatory commensal bacterium identified by gut microbiota analysis of Crohn disease patients,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 43, pp. 16731–16736, 2008.
- T. von der Weid, C. Bulliard, and E. J. Schiffrin, “Induction by a lactic acid bacterium of a population of CD4+ T cells with low proliferative capacity that produce transforming growth factor β and interleukin-10,” Clinical and Diagnostic Laboratory Immunology, vol. 8, no. 4, pp. 695–701, 2001.
- H. Braat, J. van den Brande, E. van Tol, D. Hommes, M. Peppelenbosch, and S. van Deventer, “Lactobacillus rhamnosus induces peripheral hyporesponsiveness in stimulated CD4+ T cells via modulation of dendritic cell function,” American Journal of Clinical Nutrition, vol. 80, no. 6, pp. 1618–1625, 2004.
- C. Di Giacinto, M. Marinaro, M. Sanchez, W. Strober, and M. Boirivant, “Probiotics ameliorate recurrent Th1-mediated murine colitis by inducing IL-10 and IL-10-dependent TGF-β-bearing regulatory cells,” The Journal of Immunology, vol. 174, no. 6, pp. 3237–3246, 2005.
- T. Pessi, Y. Sütas, M. Hurme, and E. Isolauri, “Interleukin-10 generation in atopic children following oral lactobacillus rhamnosus GG,” Clinical & Experimental Allergy, vol. 30, no. 12, pp. 1804–1808, 2000.
- C. Mullié, A. Yazourh, H. Thibault et al., “Increased poliovirus-specific intestinal antibody response coincides with promotion of Bifidobacterium longum-infantis and Bifidobacterium breve in infants: a randomized, double-blind, placebo-controlled trial,” Pediatric Research, vol. 56, no. 5, pp. 791–795, 2004.
- E. Isolauri, J. Joensuu, H. Suomalainen, M. Luomala, and T. Vesikari, “Improved immunogenicity of oral D x RRV reassortant rotavirus vaccine by Lactobacillus casei GG,” Vaccine, vol. 13, no. 3, pp. 310–312, 1995.
- H. Fang, T. Elina, A. Heikki, and S. Seppo, “Modulation of humoral immune response through probiotic intake,” FEMS Immunology & Medical Microbiology, vol. 29, no. 1, pp. 47–52, 2000.
- P. V. Licciardi, S.-S. Wong, M. L. Tang, and T. C. Karagiannis, “Epigenome targeting by probiotic metabolites,” Gut Pathogens, vol. 2, article 24, 2010.
- S. Brand, R. Teich, T. Dicke et al., “Epigenetic regulation in murine offspring as a novel mechanism for transmaternal asthma protection induced by microbes,” The Journal of Allergy and Clinical Immunology, vol. 128, no. 3, pp. 618–625.e7, 2011.