Inhibition of Histone Deacetylase Activity by Butyrate

Davie, James R.

doi:10.1093/jn/133.7.2485s

Cited by 1,515Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

Inhibition of Histone Deacetylase Activity by Butyrate

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Davie, James R.·2003·The Journal of Nutrition

DOI 10.1093/jn/133.7.2485s

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Abstract

This article reviews the effects of the short-chain fatty acid butyrate on histone deacetylase (HDAC) activity. Sodium butyrate has multiple effects on cultured mammalian cells that include inhibition of proliferation, induction of differentiation and induction or repression of gene expression. The observation that butyrate treatment of cells results in histone hyperacetylation initiated a flurry of activity that led to the discovery that butyrate inhibits HDAC activity. Butyrate has been an essential agent for determining the role of histone acetylation in chromatin structure and function. Interestingly, inhibition of HDAC activity affects the expression of only 2% of mammalian genes. Promoters of butyrate-responsive genes have butyrate response elements, and the action of butyrate is often mediated through Sp1/Sp3 binding sites (e.g., p21(Waf1/Cip1)). We demonstrated that Sp1 and Sp3 recruit HDAC1 and HDAC2, with the latter being phosphorylated by protein kinase CK2. A model is proposed in which inhibition of Sp1/Sp3-associated HDAC activity leads to histone hyperacetylation and transcriptional activation of the p21(Waf1/Cip1) gene; p21(Waf1/Cip1) inhibits cyclin-dependent kinase 2 activity and thereby arrests cell cycling. Pending the cell background, the nonproliferating cells may enter differentiation or apoptotic pathways. The potential of butyrate and HDAC inhibitors in the prevention and treatment of cancer is presented.

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All SCFAs induce histone deacetylase (HDAC) inhibitory effects, with butyrate being the most potent inhibitor of class I and IIa HDACs.
“All SCFAs induce histone deacetylase (HDAC) inhibitory effects, with butyrate being the most potent inhibitor of class I and IIa HDACs”
From The Microbiota-Gut-Brain Axis (2019) · cites this paper as Davie, 2003
Butyrate is the most potent HDAC inhibitor among SCFAs and generally inhibits class I HDACs (HDAC1, -2, -3, and -8) and class IIa HDACs (HDAC4, -5, -7, and -9), but not class IIb HDACs (HDAC6 and HDAC10) and class III HDACs (sirtuins).
“Among the SCFAs, butyrate is the most potent HDAC inhibitor that is generally thought to inhibit the activity of class I HDACs (HDAC1, −2, −3, and −8) and class IIa HDACs (HDAC4, −5, −7, and −9), but not class IIb HDACs (HDAC6 and HDAC10) and class III HDACs (sirtuins).288”
From Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases (2024) · cites this paper as [288]

Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466 · see citing works
Acetylation of Histones and Transcription-Related Factors
Sterner, D. E., & Berger, S. L. (2000) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.64.2.435-459.2000 · Cited by 1,766 · see citing works
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714 · see citing works
Cofactor Dynamics and Sufficiency in Estrogen Receptor–Regulated Transcription
Shang, Y., Hu, X., DiRenzo, J., Lazar, M. A., & Brown, M. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00188-4 · Cited by 1,647 · see citing works
Histone Deacetylase Inhibitors: Inducers of Differentiation or Apoptosis of Transformed Cells
Marks, P. A., Richon, V. M., & Rifkind, R. A. (2000) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/92.15.1210 · Cited by 1,152 · see citing works
The p21Cip1 and p27Kip1 CDK ‘inhibitors’ are essential activators of cyclin D‐dependent kinases in murine fibroblasts
Cheng, M., Olivier, P., Diehl, J. A., Fero, M., Roussel, M. F., Roberts, J. M., & Sherr, C. J. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1571 · Cited by 1,142 · see citing works
The Sp-family of transcription factors
Suske, G. (1999) · Gene · doi:10.1016/s0378-1119(99)00357-1 · Cited by 1,112 · see citing works
Histone deacetylase inhibitor selectively induces p21 <sup>WAF1</sup> expression and gene-associated histone acetylation
Richon, V. M., Sandhoff, T. W., Rifkind, R. A., & Marks, P. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.180316197 · Cited by 1,090 · see citing works
Sodium butyrate inhibits histone deacetylation in cultured cells
Candido, E. (1978) · Cell · doi:10.1016/0092-8674(78)90305-7 · Cited by 1,036 · see citing works
The Phosphorylation Status of Nuclear NF-ΚB Determines Its Association with CBP/p300 or HDAC-1
Zhong, H., May, M. J., Jimi, E., & Ghosh, S. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00477-x · Cited by 930 · see citing works
Effects of sodium butyrate, a new pharmacological agent, on cells in culture
Kruh, J. (1981) · Molecular and Cellular Biochemistry · doi:10.1007/bf00222695 · Cited by 803 · see citing works
n-Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
Riggs, M. G., WHITTAKER, R. G., Neumann, J. R., & Ingram, V. M. (1977) · Nature · doi:10.1038/268462a0 · Cited by 777 · see citing works
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770 · see citing works
The effect of sodium butyrate on histone modification
Sealy, L. J. (1978) · Cell · doi:10.1016/0092-8674(78)90306-9 · Cited by 691 · see citing works
The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation.
(1996) · Europe PMC (PubMed Central) · Cited by 659 · see citing works
Butyric acid, a potent inducer of erythroid differentiation in cultured erythroleukemic cells
Leder, A., & Leder, P. (1975) · Cell · doi:10.1016/0092-8674(75)90107-5 · Cited by 659 · see citing works
A tale of three fingers: the family of mammalian Sp/XKLF transcription factors
Philipsen, S., & Suske, G. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.15.2991 · Cited by 595 · see citing works
Disruption of Higher-Order Folding by Core Histone Acetylation Dramatically Enhances Transcription of Nucleosomal Arrays by RNA Polymerase III
Tse, C., Sera, T., Wolffe, A. P., & Hansen, J. C. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.8.4629 · Cited by 574 · see citing works
The Effects of Short-Chain Fatty Acids on Human Colon Cancer Cell Phenotype Are Associated with Histone Hyperacetylation
Hinnebusch, B. F., Meng, S., Wu, J. T., Archer, S. Y., & Hodin, R. A. (2002) · Journal of Nutrition · doi:10.1093/jn/132.5.1012 · Cited by 546 · see citing works
Deacetylase Enzymes
Grozinger, C. M., & Schreiber, S. L. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00092-3 · Cited by 537 · see citing works
The histone tails of the nucleosome
Luger, K., & Richmond, T. J. (1998) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(98)80134-2 · Cited by 525 · see citing works
Therapeutic targeting of transcription in acute promyelocytic leukemia by use of an inhibitor of histone deacetylase.
Warrell, R. P., He, L.-Z., Richon, V., Calleja, E., & Pandolfi, P. P. (1998) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/90.21.1621 · Cited by 502 · see citing works
Suppression of histone deacetylation in vivo and in vitro by sodium butyrate.
Boffa, L. C., Vidali, G., Mann, R. S., & Allfrey, V. G. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34804-4 · Cited by 478 · see citing works
Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences.
Vidali, G., Boffa, L. C., Bradbury, E. M., & Allfrey, V. G. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.5.2239 · Cited by 464 · see citing works
RNA synthesis and histone acetylation during the course of gene activation in lymphocytes.
Pogo, B. G. T., Allfrey, V. G., & Mirsky, A. E. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.55.4.805 · Cited by 452 · see citing works
Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme
Niefind, K., Guerra, B., Ermakowa, I., & Issinger, O. (2001) · The EMBO Journal · doi:10.1093/emboj/20.19.5320 · Cited by 448 · see citing works
Different activation domains of Sp1 govern formation of multimers and mediate transcriptional synergism.Preprint
Pascal, E., & Tjian, R. (1991) · Genes & Development · doi:10.1101/gad.5.9.1646 · Cited by 441 · see citing works
Functional Synergy between the Transcription Factor Sp1 and the Estrogen Receptor
Porter, W. W., Saville, B., Hoivik, D. J., & Safe, S. H. (1997) · Molecular Endocrinology · doi:10.1210/mend.11.11.9916 · Cited by 430 · see citing works
Histone Deacetylase 1 Can Repress Transcription by Binding to Sp1
Doetzlhofer, A., Rotheneder, H., Egger, G., Koranda, M., Kurtev, V., Brosch, G., Wintersberger, E., & Seiser, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5504 · Cited by 396 · see citing works
Butyrate Activates the WAF1/Cip1 Gene Promoter through Sp1 Sites in a p53-negative Human Colon Cancer Cell Line
Nakano, K., Mizuno, T., Sowa, Y., Orita, T., Yoshino, T., Okuyama, Y., Fujita, T., Ohtani‐Fujita, N., Matsukawa, Y., Tokino, T., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22199 · Cited by 395 · see citing works
Anchorage-dependent Cell Cycle Progression
Assoian, R. K. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.1.1 · Cited by 377 · see citing works
Genetic reprogramming in pathways of colonic cell maturation induced by short chain fatty acids: comparison with trichostatin A, sulindac, and curcumin and implications for chemoprevention of colon cancer.
Mariadason, J. M., Corner, G. A., & Augenlicht, L. H. (2000) · PubMed · Cited by 375 · see citing works
Sin Meets NuRD and Other Tails of Repression
Knoepfler, P. S., & Eisenman, R. N. (1999) · Cell · doi:10.1016/s0092-8674(00)81531-7 · Cited by 356 · see citing works
The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1
Ryu, S., Zhou, S., Ladurner, A. G., & Tjian, R. (1999) · Nature · doi:10.1038/17141 · Cited by 351 · see citing works
Different accessibilities in chromatin to histone acetylase.
Cousens, L. S., Gallwitz, D., & Alberts, B. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37831-6 · Cited by 340 · see citing works
Effect of sodium butyrate on mammalian cells in culture: A review
Prasad, K. N., & Sinha, P. K. (1976) · In Vitro Cellular & Developmental Biology - Plant · doi:10.1007/bf02796360 · Cited by 331 · see citing works
Acetylation of HMG I(Y) by CBP Turns off IFNβ Expression by Disrupting the Enhanceosome
Munshi, N., Merika, M., Yie, J., Senger, K., Chen, G., & Thanos, D. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80145-8 · Cited by 321 · see citing works
Modulation of Chromatin Folding by Histone Acetylation
García‐Ramírez, M., Rocchini, C., & Ausió, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.30.17923 · Cited by 317 · see citing works
Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia
He, L.-Z., Tolentino, T., Grayson, P. C., Zhong, S., Warrell, R. P., Rifkind, R. A., Marks, P. A., Richon, V. M., & Pandolfi, P. P. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200111537 · Cited by 303 · see citing works
Role of covalent modifications of histones in regulating gene expression
Spencer, V. A., & Davie, J. (1999) · Gene · doi:10.1016/s0378-1119(99)00405-9 · Cited by 302 · see citing works
Self-citation
Acetylation and chromosomal functions
Cheung, W. L., Briggs, S. D., & Allis, C. D. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00096-x · Cited by 290 · see citing works
Protein kinase CK2 in mammary gland tumorigenesis
Landesman‐Bollag, E., Romieu, R., Song, D. H., Sonenshein, G. E., Cardiff, R. D., & Seldin, D. C. (2001) · Oncogene · doi:10.1038/sj.onc.1204411 · Cited by 290 · see citing works
Butyrate and trichostatin A effects on the proliferation/differentiation of human intestinal epithelial cells: induction of cyclin D3 and p21 expression
Siavoshian, S., Segain, J.-P., Kornprobst, M., Bonnet, C., Cherbut, C., Galmiche, J.-P., & Blottière, H. M. (2000) · Gut · doi:10.1136/gut.46.4.507 · Cited by 277 · see citing works
Histone deacetylases: transcriptional repression with SINers and NuRDs
Ayer, D. E. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01536-6 · Cited by 274 · see citing works
Protein kinase CK2 signal in neoplasia.
Tawfic, S. H., Yu, S., Wang, H., et al. (2001) · PubMed · doi:10.14670/hh-16.573 · Cited by 260 · see citing works
DNA looping and Sp1 multimer links: a mechanism for transcriptional synergism and enhancement.
Mastrangelo, I. A., Courey, A. J., Wall, J. S., Jackson, S. P., & Hough, P. V. C. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.13.5670 · Cited by 257 · see citing works
Histones and Their Modification
Wu, R. S., Panusz, H., Hatch, C. L., & Bonner, W. M. (1986) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238609083735 · Cited by 255 · see citing works
Molecular Cloning and Characterization of a Novel Histone Deacetylase HDAC10
Guardiola, A. R., & Yao, T.-P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109861200 · Cited by 253 · see citing works
Histone Deacetylase 1 Phosphorylation Promotes Enzymatic Activity and Complex Formation
Pflum, M. K. H., Tong, J. K., Lane, W. S., & Schreiber, S. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105590200 · Cited by 253 · see citing works
Structure and Function of the Core Histone N-Termini: More Than Meets the Eye
Hansen, J. C., Tse, C., & Wolffe, A. P. (1998) · Biochemistry · doi:10.1021/bi982409v · Cited by 247 · see citing works
Sp3 encodes multiple proteins that differ in their capacity to stimulate or repress transcription
Kennett, S. B. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.15.3110 · Cited by 247 · see citing works
A New Family of Human Histone Deacetylases Related toSaccharomyces cerevisiae HDA1p
Fischle, W., Emiliani, S., Hendzel, M. J., Nagase, T., Nomura, N., Voelter, W., & Verdin, E. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.17.11713 · Cited by 225 · see citing works
Regulation of histone deacetylase 2 by protein kinase CK2
Tsai, S.-C., & Seto, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204149200 · Cited by 196 · see citing works
Isolation and Characterization of Mammalian HDAC10, a Novel Histone Deacetylase
Kao, H.-Y., Lee, C.-H., Komarov, A., Han, C. C., & Evans, R. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108931200 · Cited by 193 · see citing works
The emerging role of class II histone deacetylases
Fischle, W., Kiermer, V., Dequiedt, F., & Verdin, E. M. (2001) · Biochemistry and Cell Biology · doi:10.1139/bcb-79-3-337 · Cited by 182 · see citing works
p300 Collaborates with Sp1 and Sp3 in p21 / Promoter Activation Induced by Histone Deacetylase Inhibitor
Xiao, H., Hasegawa, T., & Isobe, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1371 · Cited by 171 · see citing works
Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1.
Sterner, R., Vidali, G., & Allfrey, V. G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86524-9 · Cited by 156 · see citing works
Acetylation Increases the α-Helical Content of the Histone Tails of the Nucleosome
Wang, X., Moore, S. C., Laszckzak, M., & Ausió, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004998200 · Cited by 156 · see citing works
The emerging role of class II histone deacetylases
Fischle, W., Kiermer, V., Dequiedt, S., et al. (2001) · Biochemistry and Cell Biology · doi:10.1139/o01-116 · Cited by 152 · see citing works
Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation.
Perry, M., & Chalkley, R. G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34382-5 · Cited by 150 · see citing works
Gene activation by histone and factor acetyltransferases
Berger, S. L. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80046-5 · Cited by 149 · see citing works
Transcription factor Sp3 is regulated by acetylation
Braun, H. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.24.4994 · Cited by 148 · see citing works
Sp3, but not Sp1, mediates the transcriptional activation of the p21/WAF1/Cip1 gene promoter by histone deacetylase inhibitor.
Sowa, Y., Orita, T., Minamikawa, S., Mizuno, T., Nomura, H., & Sakai, T. (1999) · PubMed · Cited by 148 · see citing works
Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin
Nightingale, K. P., Wellinger, R. E., Sogo, J. M., & Becker, P. B. (1998) · The EMBO Journal · doi:10.1093/emboj/17.10.2865 · Cited by 140 · see citing works
Regulation of P21cip1 Expression by Growth Factors and the Extracellular Matrix Reveals a Role for Transient ERK Activity in G1 Phase
Bottazzi, M. E., Zhu, X., Böhmer, R. M., & Assoian, R. K. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.6.1255 · Cited by 136 · see citing works
Regulation of inducible gene expression by the transcription factor NF-κB
Ghosh, S. (1999) · Immunologic Research · doi:10.1007/bf02786486 · Cited by 126 · see citing works
The identification of distinct populations of acetylated histone.
Covault, J., & Chalkley, R. G. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70534-1 · Cited by 121 · see citing works
Inhibition of transformed cell growth and induction of cellular differentiation by pyroxamide, an inhibitor of histone deacetylase.
Butler, L. M., Webb, Y., Agus, D. B., et al. (2001) · PubMed · Cited by 121 · see citing works
Inhibitors of histone deacetylase are potentially effective anticancer agents.
Marks, P. A., Rifkind, R. A., Richon, V. M., et al. (2001) · PubMed · Cited by 118 · see citing works
Transcription Factor ZBP-89 Cooperates with Histone Acetyltransferase p300 during Butyrate Activation of p21 Transcription in Human Cells
Bai, L., & Merchant, J. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004249200 · Cited by 114 · see citing works
Protein kinase CK2: signaling and tumorigenesis in the mammary gland.
Landesman‐Bollag, E., Song, D. H., Romieu, R., Sussman, D. J., Cardiff, R. D., Sonenshein, G. E., & Seldin, D. C. (2001) · PubMed · Cited by 111 · see citing works
Histone deacetylase is a component of the internal nuclear matrix.
Hendzel, M. J., Delcuve, G. P., & Davie, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54727-x · Cited by 109 · see citing works
Self-citation
Short-Chain Fatty Acids Inhibit Invasive Human Colon Cancer by Modulating uPA, TIMP-1, TIMP-2, Mutant p53, Bcl-2, Bax, p21 and PCNA Protein Expression in an In Vitro Cell Culture Model
Emenaker, N. J., Calaf, G. M., Cox, D., Basson, M. D., & Qureshi, N. (2001) · Journal of Nutrition · doi:10.1093/jn/131.11.3041s · Cited by 99 · see citing works
Effects of Histone Acetylation on the Solubility and Folding of the Chromatin Fiber
Wang, X., He, C., Moore, S. C., & Ausió, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100501200 · Cited by 98 · see citing works
Butyrate, a Histone Deacetylase Inhibitor, Activates the Human IGF Binding Protein-3 Promoter in Breast Cancer Cells: Molecular Mechanism Involves an Sp1/Sp3 Multiprotein Complex
Walker, G. E., Wilson, E. M., Powell, D. R., et al. (2001) · Endocrinology · doi:10.1210/endo.142.9.8380 · Cited by 96 · see citing works
Histone Deacetylase Inhibitors: Development of Suberoylanilide Hydroxamic Acid (SAHA) for the Treatment of Cancers
Richon, V. M., Zhou, X., Rifkind, R. A., & Marks, P. A. (2001) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2000.0376 · Cited by 93 · see citing works
Protein kinase CK2: Signaling and tumorigenesis in the mammary gland
Landesman‐Bollag, E., Song, D. H., Romieu, R., Sussman, D. J., Cardiff, R. D., Sonenshein, G. E., & Seldin, D. C. (2001) · Molecular and Cellular Biochemistry · doi:10.1023/a:1013108822847 · Cited by 93 · see citing works
Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin
Davie, J. (1997) · Molecular Biology Reports · doi:10.1023/a:1006811817247 · Cited by 92 · see citing works
Self-citation
Specific Acetylation of Chromosomal Protein HMG-17 by PCAF Alters Its Interaction with Nucleosomes
Herrera, J. E., Sakaguchi, K., Bergel, M., Trieschmann, L., Nakatani, Y., & Bustin, M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3466 · Cited by 91 · see citing works
The Transcriptional Repressor Sp3 Is Associated with CK2-phosphorylated Histone Deacetylase 2
Sun, J.-M., Chen, H. Y., Moniwa, M., Litchfield, D. W., Seto, E., & Davie, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200378200 · Cited by 89 · see citing works
Self-citation
Sodium Butyrate Induces Transcription from the Gαi2Gene Promoter through Multiple Sp1 Sites in the Promoter and by Activating the MEK-ERK Signal Transduction Pathway
Yang, J., Kawai, Y., Hanson, R. W., & Arinze, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102821200 · Cited by 88 · see citing works
Histone Acetylation / Deacetylation and Cancer: An “Open” and “Shut” Case?
Gray, S. G., & Teh, B. T. (2001) · Current Molecular Medicine · doi:10.2174/1566524013363537 · Cited by 86 · see citing works
Histone acetylation in chicken erythrocytes. Rates of acetylation and evidence that histones in both active and potentially active chromatin are rapidly modified
Zhang, D., & Nelson, D. A. (1988) · Biochemical Journal · doi:10.1042/bj2500233 · Cited by 73 · see citing works
Effect of Estradiol on Histone Acetylation Dynamics in Human Breast Cancer Cells
Sun, J., Chen, H. Y., & Davie, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108364200 · Cited by 65 · see citing works
Self-citation
Short-chain fatty acids inhibit intestinal trefoil factor gene expression in colon cancer cells
Tran, C. P., Familari, M., Parker, L. M., Whitehead, R. H., & Giraud, A. S. (1998) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1998.275.1.g85 · Cited by 59 · see citing works
Butyrate as a model for “Gene‐regulating chemoprevention and chemotherapy”
Sowa, Y., & Sakai, T. (2000) · BioFactors · doi:10.1002/biof.5520120142 · Cited by 57 · see citing works
The estrogen receptor: more than the average transcription factor
Hart, L. L., & Davie, J. (2002) · Biochemistry and Cell Biology · doi:10.1139/o02-038 · Cited by 50 · see citing works
Self-citation
Transcriptional regulation by butyrate of mouse galectin-1 gene in embryonal carcinoma cells
Lu, Y. W., & Lotan, R. (1999) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(98)00257-7 · Cited by 43 · see citing works
Control of Chromatin Remodeling
Davie, J., & Moniwa, M. (2000) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v10.i3-4.70 · Cited by 35 · see citing works
Self-citation
Dynamically Acetylated Histone Association with Transcriptionally Active and Competent Genes in the Avian Adult β-Globin Gene Domain
Spencer, V. A., & Davie, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104886200 · Cited by 35 · see citing works
Self-citation
Transcriptional regulation: a new dominion for inositol phosphate signaling?
Shears, S. B. (2000) · BioEssays · doi:10.1002/1521-1878(200009)22:9 · Cited by 28 · see citing works

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Commensal microbe-derived butyrate induces the differentiation of colonic regulatory T cells
Furusawa, Y., Obata, Y., Fukuda, S., Endo, T. A., Nakato, G., Takahashi, D., Nakanishi, Y., Uetake, C., Kato, K., Kato, T., et al. (2013) · Nature · doi:10.1038/nature12721 · Cited by 5,549 · see citing works
Role of the microbiota in immunity and inflammation.
Belkaid, Y., & Hand, T. W. (2014) · Cell · doi:10.1016/j.cell.2014.03.011 · Cited by 5,385 · see citing works
The Microbiota-Gut-Brain Axis
Cryan, J. F., O'Riordan, K. J., Cowan, C. S. M., Sandhu, K. V., Bastiaanssen, T. F. S., Boehme, M., Codagnone, M. G., Cussotto, S., Fulling, C., Golubeva, A. V., et al. (2019) · Physiological Reviews · doi:10.1152/physrev.00018.2018 · Cited by 5,286 · see citing works
Functional interactions between the gut microbiota and host metabolism
Tremaroli, V., & Bäckhed, F. (2012) · Nature · doi:10.1038/nature11552 · Cited by 4,387 · see citing works
Short Chain Fatty Acids (SCFAs)-Mediated Gut Epithelial and Immune Regulation and Its Relevance for Inflammatory Bowel Diseases
Parada Venegas, D., De la Fuente, M. K., Landskron, G., González, M. J., Quera, R., Dijkstra, G., Harmsen, H. J. M., Faber, K. N., & Hermoso, M. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00277 · Cited by 3,820 · see citing works
Review article: the role of butyrate on colonic function
HAMER, H. M., JONKERS, D., VENEMA, K., VANHOUTVIN, S., TROOST, F. J., & BRUMMER, R. ‐. (2008) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2007.03562.x · Cited by 2,721 · see citing works
The role of short chain fatty acids in health and disease
Tan, J., McKenzie, C., Potamitis, M., Thorburn, A. N., Mackay, C. R., & Macia, L. (2014) · Advances in immunology · doi:10.1016/b978-0-12-800100-4.00003-9 · Cited by 2,425 · see citing works
Diet–microbiota interactions as moderators of human metabolism
Sonnenburg, J. L., & Bäckhed, F. (2016) · Nature · doi:10.1038/nature18846 · Cited by 2,257 · see citing works
Butyrate improves insulin sensitivity and increases energy expenditure in mice
Gao, Z., Yin, J., Zhang, J., Ward, R. E., Martin, R. J., Lefevre, M., Cefalu, W. T., & Ye, J. (2009) · Diabetes · doi:10.2337/db08-1637 · Cited by 2,204 · see citing works
The microbial metabolite butyrate regulates intestinal macrophage function via histone deacetylase inhibition.
Chang, P. V., Hao, L., Offermanns, S., & Medzhitov, R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322269111 · Cited by 2,175 · see citing works
Potential beneficial effects of butyrate in intestinal and extraintestinal diseases
Canani, R. B. (2011) · World Journal of Gastroenterology · doi:10.3748/wjg.v17.i12.1519 · Cited by 1,381 · see citing works
Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases
Loh, J. S., Mak, W. Q., Tan, L. K. S., Ng, C. X., Chan, H. H., Yeow, S. H., Foo, J. B., Ong, Y. S., How, C. W., & Khaw, K. Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01743-1 · Cited by 1,193 · see citing works
Short chain fatty acids in human gut and metabolic health
Blaak, E. E., Canfora, E. E., Theis, S., Frost, G., Groen, A. K., Mithieux, G., Nauta, A., Scott, K., Stahl, B., van Harsselaar, J., et al. (2020) · Beneficial Microbes · doi:10.3920/bm2020.0057 · Cited by 1,103 · see citing works
The Short Chain Fatty Acid Butyrate Imprints an Antimicrobial Program in Macrophages
Schulthess, J., Pandey, S., Capitani, M., Rue-Albrecht, K. C., Arnold, I., Franchini, F., Chomka, A., Ilott, N. E., Johnston, D. G. W., Pires, E., et al. (2019) · Immunity · doi:10.1016/j.immuni.2018.12.018 · Cited by 1,037 · see citing works
The Warburg Effect Dictates the Mechanism of Butyrate-Mediated Histone Acetylation and Cell Proliferation
Donohoe, D. R., Collins, L. B., Wali, A., Bigler, R., Sun, W., & Bultman, S. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.033 · Cited by 993 · see citing works
Gut Microbial Metabolites Fuel Host Antibody Responses
Kim, M., Qie, Y., Park, J., & Kim, C. H. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.07.001 · Cited by 893 · see citing works
“SCFAs are HDAC inhibitors and, therefore, have the potential to regulate gene expression and cell signaling through regulation of protein acetylation (Davie, 2003).”
Background
The neuropharmacology of butyrate: the bread and butter of the microbiota-gut-brain axis
Stilling, R. M., van de Wouw, M., Clarke, G., Stanton, C., Dinan, T. G., & Cryan, J. F. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.06.011 · Cited by 891 · see citing works
Insights into the role of the microbiome in obesity and type 2 diabetes
Hartstra, A. V., Bouter, K. E. C., Bäckhed, F., & Nieuwdorp, M. (2015) · Diabetes Care · doi:10.2337/dc14-0769 · Cited by 641 · see citing works
Microbial genes, brain & behaviour – epigenetic regulation of the gut–brain axis
Stilling, R. M., Dinan, T. G., & Cryan, J. F. (2014) · Genes, Brain and Behavior · doi:10.1111/gbb.12109 · Cited by 637 · see citing works
Lactic acid bacteria contribution to gut microbiota complexity: lights and shadows.
Pessione, E. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00086 · Cited by 592 · see citing works
Antidepressant-Like Effects of the Histone Deacetylase Inhibitor, Sodium Butyrate, in the Mouse
Schroeder, F. A., Lin, C. L., Crusio, W. E., & Akbarian, S. (2007) · Biological Psychiatry · doi:10.1016/j.biopsych.2006.06.036 · Cited by 541 · see citing works
Short-Chain Fatty Acids Regulate the Enteric Neurons and Control Gastrointestinal Motility in Rats
Soret, R., Chevalier, J., De Coppet, P., Poupeau, G., Derkinderen, P., Segain, J. P., & Neunlist, M. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.01.053 · Cited by 530 · see citing works
Nondigestible carbohydrates, butyrate, and butyrate-producing bacteria
Fu, X., Liu, Z., Zhu, C., Mou, H., & Kong, Q. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1542587 · Cited by 497 · see citing works
Feeding the microbiota–gut–brain axis: Diet, microbiome, and neuropsychiatry
Sandhu, K. V., Sherwin, E., Schellekens, H., Stanton, C., Dinan, T. G., & Cryan, J. F. (2017) · Translational Research · doi:10.1016/j.trsl.2016.10.002 · Cited by 491 · see citing works
Microbiota-gut-brain axis: Modulator of host metabolism and appetite
van de Wouw, M., Schellekens, H., Dinan, T. G., & Cryan, J. F. (2017) · The Journal of Nutrition · doi:10.3945/jn.116.240481 · Cited by 461 · see citing works
Short-chain fatty acids: ready for prime time?
Roy, C. C., Kien, C. L., Bouthillier, L., & Levy, E. (2006) · Nutrition in Clinical Practice · doi:10.1177/0115426506021004351 · Cited by 443 · see citing works
Butyrate and other short-chain fatty acids as modulators of immunity: What relevance for health?
Meijer, K., de Vos, P., & Priebe, M. G. (2010) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/mco.0b013e32833eebe5 · Cited by 443 · see citing works
Role of the Microbiome in Energy Regulation and Metabolism
Nieuwdorp, M., Gilijamse, P. W., Pai, N., & Kaplan, L. M. (2014) · Gastroenterology · doi:10.1053/j.gastro.2014.02.008 · Cited by 421 · see citing works
Control of lymphocyte functions by gut microbiota-derived short-chain fatty acids
Kim, C. H. (2021) · Cellular & Molecular Immunology · doi:10.1038/s41423-020-00625-0 · Cited by 404 · see citing works
Microbiota-derived short chain fatty acids modulate microglia and promote Aβ plaque deposition
Colombo, A. V., Sadler, R. K., Llovera, G., Singh, V., Roth, S., Heindl, S., Sebastian Monasor, L., Verhoeven, A., Peters, F., Parhizkar, S., et al. (2021) · eLife · doi:10.7554/elife.59826 · Cited by 354 · see citing works
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331 · see citing works
Microbiota-derived butyrate dynamically regulates intestinal homeostasis through regulation of actin-associated protein synaptopodin
Wang, R. X., Lee, J. S., Campbell, E. L., & Colgan, S. P. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917597117 · Cited by 318 · see citing works
Microbial metabolite butyrate facilitates M2 macrophage polarization and function
Ji, J., Shu, D., Zheng, M., Wang, J., Luo, C., Wang, Y., Guo, F., Zou, X., Lv, X., Li, Y., et al. (2016) · Scientific Reports · doi:10.1038/srep24838 · Cited by 334 · see citing works
Autism spectrum disorders and intestinal microbiota
De Angelis, M., Francavilla, R., Piccolo, M., De Giacomo, A., & Gobbetti, M. (2015) · Gut Microbes · doi:10.1080/19490976.2015.1035855 · Cited by 311 · see citing works
Gut Microbiota, Immune System, and Bone
D’Amelio, P., & Sassi, F. (2018) · Calcified Tissue International · doi:10.1007/s00223-017-0331-y · Cited by 315 · see citing works
Target intestinal microbiota to alleviate disease progression in amyotrophic lateral sclerosis
Zhang, Y.-G., Wu, S., Yi, J., Xia, Y., Jin, D., Zhou, J., & Sun, J. (2017) · Clinical Therapeutics · doi:10.1016/j.clinthera.2016.12.014 · Cited by 287 · see citing works
Influences of diet and the gut microbiome on epigenetic modulation in cancer and other diseases
Paul, B., Barnes, S., Demark-Wahnefried, W., Morrow, C., Salvador, C., Skibola, C., & Tollefsbol, T. O. (2015) · Clinical Epigenetics · doi:10.1186/s13148-015-0144-7 · Cited by 306 · see citing works
Anti-inflammatory effects of short chain fatty acids in IFN-γ-stimulated RAW 264.7 murine macrophage cells: Involvement of NF-κB and ERK signaling pathways
Park, J.-S., Lee, E.-J., Lee, J.-C., Kim, W.-K., & Kim, H.-S. (2007) · International Immunopharmacology · doi:10.1016/j.intimp.2006.08.015 · Cited by 278 · see citing works
Microbial modulation of insulin sensitivity
Khan, M. T., Nieuwdorp, M., & Bäckhed, F. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.07.006 · Cited by 260 · see citing works
HDAC inhibitor sodium butyrate-mediated epigenetic regulation enhances neuroprotective function of microglia during ischemic stroke
Patnala, R., Arumugam, T. V., Gupta, N., & Dheen, S. T. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-0149-z · Cited by 278 · see citing works
Emerging roles of the microbiome in cancer
Bultman, S. J. (2014) · Carcinogenesis · doi:10.1093/carcin/bgt392 · Cited by 239 · see citing works
Microbiome disturbances and autism spectrum disorders
Rosenfeld, C. S. (2015) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.063826 · Cited by 229 · see citing works
Epigenetic mechanisms in anti-cancer actions of bioactive food components—the implications in cancer prevention
Stefanska, B., Karlic, H., Varga, F., Fabianowska‐Majewska, K., & Haslberger, A. (2012) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2012.02002.x · Cited by 200 · see citing works
The role of gut microbiota in bone homeostasis
Behera, J., Ison, J., Tyagi, S. C., & Tyagi, N. (2020) · Bone · doi:10.1016/j.bone.2020.115317 · Cited by 162 · see citing works
Inhibition of HDAC8 and HDAC9 by microbial short-chain fatty acids breaks immune tolerance of the epidermis to TLR ligands
Sanford, J. A., Zhang, L.-J., Williams, M. R., Gangoiti, J. A., Huang, C.-M., & Gallo, R. L. (2016) · Science Immunology · doi:10.1126/sciimmunol.aah4609 · Cited by 166 · see citing works
A mechanism for expansion of regulatory T-cell repertoire and its role in self-tolerance
Feng, Y., van der Veeken, J., Shugay, M., Putintseva, E. V., Osmanbeyoglu, H. U., Dikiy, S., Hoyos, B. E., Moltedo, B., Hemmers, S., Treuting, P., et al. (2015) · Nature · doi:10.1038/nature16141 · Cited by 157 · see citing works
Molecular pathways: gene-environment interactions regulating dietary fiber induction of proliferation and apoptosis via butyrate for cancer prevention
Bultman, S. J. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2483 · Cited by 157 · see citing works
Histone deacetylase inhibitors suppress mutant p53 transcription via histone deacetylase 8
Yan, W., Liu, S., Xu, E., Zhang, J., Zhang, Y., Chen, X., & Chen, X. (2013) · Oncogene · doi:10.1038/onc.2012.81 · Cited by 153 · see citing works
Drug-Induced Activation of Dopamine D1 Receptor Signaling and Inhibition of Class I/II Histone Deacetylase Induce Chromatin Remodeling in Reward Circuitry and Modulate Cocaine-Related Behaviors
Schroeder, F. A., Penta, K. L., Matevossian, A., Jones, S. R., Konradi, C., Tapper, A. R., & Akbarian, S. (2008) · Neuropsychopharmacology · doi:10.1038/npp.2008.15 · Cited by 139 · see citing works
The microbiome and its potential as a cancer preventive intervention
Bultman, S. J. (2016) · Seminars in Oncology · doi:10.1053/j.seminoncol.2015.09.001 · Cited by 134 · see citing works
Stress-induced epigenetic transcriptional memory of acetylcholinesterase by HDAC4
Sailaja, B. S., Cohen-Carmon, D., Zimmerman, G., Soreq, H., & Meshorer, E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209990110 · Cited by 121 · see citing works
Short-chain fatty acids, secondary bile acids and indoles: gut microbial metabolites with effects on enteroendocrine cell function and their potential as therapies for metabolic disease
Masse, K. E., & Lu, V. B. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1169624 · Cited by 120 · see citing works
“This is supported by previous studies suggesting that HDAC inhibition by butyrate induces expression of many genes in various tissues and cell lines (109, 112).”
Result
Sodium butyrate stimulates monoclonal antibody over-expression in CHO cells by improving gene accessibility
Jiang, Z., & Sharfstein, S. T. (2008) · Biotechnology and Bioengineering · doi:10.1002/bit.21726 · Cited by 118 · see citing works
The microbiota and its metabolites in colonic mucosal health and cancer risk
Vipperla, K., & O'Keefe, S. J. (2012) · Nutrition in Clinical Practice · doi:10.1177/0884533612452012 · Cited by 116 · see citing works
Current status and future prospects for epigenetic psychopharmacology
Boks, M. P., de Jong, N. M., Kas, M. J. H., Vinkers, C. H., Fernandes, C., Kahn, R. S., Mill, J., & Ophoff, R. A. (2012) · Epigenetics · doi:10.4161/epi.7.1.18688 · Cited by 89 · see citing works
Butyrate modulates gene and protein expression in human intestinal endothelial cells
Ogawa, H., Rafiee, P., Fisher, P. J., Johnson, N. A., Otterson, M. F., & Binion, D. G. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.026 · Cited by 70 · see citing works
New avenues for Parkinson's disease therapeutics: disease-modifying strategies based on the gut microbiota
Lorente-Picón, M., & Laguna, A. (2021) · Biomolecules · doi:10.3390/biom11030433 · Cited by 69 · see citing works
Gut microbiota-driven neuroinflammation in Alzheimer's disease: from mechanisms to therapeutic opportunities
Lei, W., Cheng, Y., Liu, X., Gao, J., Zhu, Z., Ding, W., Xu, X., Li, Y., Ling, Z., Jiang, R., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1582119 · Cited by 68 · see citing works
Interplay of good bacteria and central nervous system: cognitive aspects and mechanistic considerations
Salami, M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.613120 · Cited by 67 · see citing works
Beyond the Calorie Paradigm: Taking into Account in Practice the Balance of Fat and Carbohydrate Oxidation during Exercise?
Brun, J.-F., Myzia, J., Varlet-Marie, E., Raynaud de Mauverger, E., & Mercier, J. (2022) · Nutrients · doi:10.3390/nu14081605 · Cited by 48 · see citing works
Fungal KATs/KDACs: A New Highway to Better Antifungal Drugs?
Kuchler, K., Jenull, S., Shivarathri, R., & Chauhan, N. (2016) · PLOS Pathogens · doi:10.1371/journal.ppat.1005938 · Cited by 40 · see citing works
Do Bacteria Provide an Alternative to Cancer Treatment and What Role Does Lactic Acid Bacteria Play?
Dicks, L. M. T., & Vermeulen, W. (2022) · Microorganisms · doi:10.3390/microorganisms10091733 · Cited by 25 · see citing works

Regulation of HDAC1 Histone Deacetylase Activity During Hematopoesis
Yang, T., Lou, Y., Jian, W., Bungert, J., Noguchi, C. T., Huang, S., & Qiu, Y. (2010) · Blood · doi:10.1182/blood.v116.21.3869.3869
Selective regulation of class I and class II histone deacetylases expression by inhibitors of histone deacetylases in cultured mouse neural cells
Ajamian, F., Salminen, A., & Reeben, M. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.04.087 · Cited by 43 · see citing works
The histone deacetylase-3 complex contains nuclear receptor corepressors
Wen, Y.-D., Perissi, V., Staszewski, L. M., Yang, W.-M., Krones, A., Glass, C. K., Rosenfeld, M. G., & Seto, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7202 · Cited by 378 · see citing works
Update of histone deacetylase inhibitors
Ma, X. (2008) · Chinese Journal of New Drugs and Clinical Remedies
HDAC4 deacetylase associates with and represses the MEF2 transcription factor
Miska, E. A., Karlsson, C., Langley, E., Nielsen, S. J., Pines, J., & Kouzarides, T. (1999) · The EMBO Journal · doi:10.1093/emboj/18.18.5099 · Cited by 551 · see citing works

Authors: Davie, J. R.
Affiliations: University of Manitoba (CA)
Corresponding author: Davie, James R.
ORCID: Davie, James R.
Venue: The Journal of Nutrition
Publisher: Elsevier BV
Published: 2003-07
Volume: 133
Issue: 7
Pages: 2485S-2493S
ISSN: 0022-3166 (ISSN-L)
DOI: 10.1093/jn/133.7.2485s
OpenAlex: W2140937256
Cited by: 1,515
References: 91
Citations by year: 2026: 132 · 2025: 124 · 2024: 89 · 2023: 92 · 2022: 104 · 2021: 96 · 2020: 74 · 2019: 76 · 2018: 79 · 2017: 73 · 2016: 79 · 2015: 65 · 2014: 69 · 2013: 63 · 2012: 53
FWCI: 1.85
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 7161 d)
Locations: Journal of Nutrition (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: butyrate, histone deacetylase inhibition, histone hyperacetylation, Sp1, Sp3, HDAC1, HDAC2, CK2 phosphorylation, p21, CDK2, cell cycle arrest, cell differentiation, gene expression regulation, chromatin structure, histone deacetylase inhibitors, cancer prevention
MeSH terms: Acetyltransferases, Breast Neoplasms, Butyrates, Enzyme Inhibitors, Female, Gene Expression Regulation, Histone Deacetylases, Humans, Tumor Cells, Cultured, Saccharomyces cerevisiae Proteins, Histone Acetyltransferases, Histone Deacetylase Inhibitors

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Inhibition of Histone Deacetylase Activity by Butyrate

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