Cited by 131Neuroinflammation and Neurodegeneration MechanismsTryptophan and brain disordersNeuroscience and Neuropharmacology Research

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Acetate reduces microglia inflammatory signaling in vitro

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Soliman, Mahmoud L., Puig, Kendra L., Combs, Colin K., Rosenberger, Thad A.·2012·Journal of Neurochemistry

DOI 10.1111/j.1471-4159.2012.07955.xPMC PMC3472042

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Abstract

Acetate supplementation increases brain acetyl‐CoA and histone acetylation and reduces lipopolysaccharide ( LPS )‐induced neuroglial activation and interleukin ( IL )‐1β expression in vivo . To determine how acetate imparts these properties, we tested the hypothesis that acetate metabolism reduces inflammatory signaling in microglia. To test this, we measured the effect acetate treatment had on cytokine expression, mitogen‐activated protein kinase ( MAPK ) signaling, histone H3 at lysine 9 acetylation, and alterations of nuclear factor‐kappa B ( NF‐κB ) in primary and BV‐2 cultured microglia. We found that treatment induced H3K9 hyperacetylation and reversed LPS‐induced H3K9 hypoacetylation similar to that found in vivo . LPS also increased IL‐1β, IL‐6, and tumor necrosis factor‐alpha ( TNF ‐α) mRNA and protein, whereas treatment returned the protein to control levels and only partially attenuated IL‐6 mRNA . In contrast, treatment increased mRNA levels of transforming growth factor‐β1 ( TGF ‐β1) and both IL‐4 mRNA and protein. LPS increased p38 MAPK and JNK phosphorylation at 4 and 2–4 h, respectively, whereas treatment reduced p38 MAPK and JNK phosphorylation only at 2 h. In addition, treatment reversed the LPS‐induced elevation of NF‐κB p65 protein and phosphorylation at serine 468 and induced acetylation at lysine 310. These data suggest that acetate metabolism reduces inflammatory signaling and alters histone and non‐histone protein acetylation.

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The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
Microglia: Active sensor and versatile effector cells in the normal and pathologic brain
Hanisch, U.-K., & Kettenmann, H. (2007) · Nature Neuroscience · doi:10.1038/nn1997 · Cited by 3,676
Microglial physiology: unique stimuli, specialized responses
Ransohoff, R. M., & Perry, V. H. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132528 · Cited by 1,858
Acetylation and deacetylation of non-histone proteins
Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E. (2005) · Gene · doi:10.1016/j.gene.2005.09.010 · Cited by 1,584
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions
Pearson, G. (2001) · Endocrine Reviews · doi:10.1210/er.22.2.153 · Cited by 1,406
Duration of Nuclear NF-κB Action Regulated by Reversible Acetylation
Chen, L., Fischle, W., Verdin, E. M., & Greene, W. C. (2001) · Science · doi:10.1126/science.1062374 · Cited by 1,231
p38 MAP kinases: key signalling molecules as therapeutic targets for inflammatory diseases
Kumar, S., Boehm, J. C., & Lee, J. C. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1177 · Cited by 1,199
Reactive microgliosis
Streit, W. J., Walter, S. A., & Pennell, N. A. (1999) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00069-0 · Cited by 1,096
Immortalization of murine microglial cells by a v-raf / v-myc carrying retrovirus
Blasi, E., Barluzzi, R., Bocchini, V., Mazzolla, R., & Bistoni, F. (1990) · Journal of Neuroimmunology · doi:10.1016/0165-5728(90)90073-v · Cited by 1,076
Cytokines and the nervous system II: actions and mechanisms of action
Rothwell, N. J., & Hopkins, S. J. (1995) · Trends in Neurosciences · doi:10.1016/0166-2236(95)93890-a · Cited by 922
Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF‐κB
Chen, L., Mu, Y., & Greene, W. C. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf660 · Cited by 827
Cytokines and the nervous system I: expression and recognition
Hopkins, S. J., & Rothwell, N. J. (1995) · Trends in Neurosciences · doi:10.1016/0166-2236(95)80029-2 · Cited by 793
MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis
Kotlyarov, A., Neininger, A., Schubert, C., Eckert, R., Birchmeier, C., Volk, H.-D., & Gaestel, M. (1999) · Nature Cell Biology · doi:10.1038/10061 · Cited by 763
SIRT1 Protects against Microglia-dependent Amyloid-β Toxicity through Inhibiting NF-κB Signaling
Chen, J., Zhou, Y., Mueller-Steiner, S., Chen, L.-F., Kwon, H., Yi, S., Mucke, L., & Gan, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509329200 · Cited by 740
Regulation of NF-κB by Cyclin-Dependent Kinases Associated with the p300 Coactivator
Perkins, N. D., Felzien, L. K., Betts, J. C., Leung, K., Beach, D., & Nabel, G. J. (1997) · Science · doi:10.1126/science.275.5299.523 · Cited by 720
Regulation and Destabilization of HIF-1α by ARD1-Mediated Acetylation
Jeong, J.-W., Bae, M.-K., Ahn, M.-Y., Kim, S.-H., Sohn, T.-K., Bae, M.-H., Yoo, M.-A., Song, E. J., Lee, K.-J., & Kim, K.-W. (2002) · Cell · doi:10.1016/s0092-8674(02)01085-1 · Cited by 716
Histone methylation versus histone acetylation: new insights into epigenetic regulation
Rice, J. C., & Allis, C. D. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00208-8 · Cited by 701
The p38/RK mitogen‐activated protein kinase pathway regulates interleukin‐6 synthesis response to tumor necrosis factor.
Beyaert, R., Cuenda, A., Berghe, W. V., Plaisance, S., Lee, J. C., Haegeman, G., Cohen, P., & Fiers, W. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00542.x · Cited by 650
Innate immunity and neuroinflammation in the CNS: The role of microglia in Toll‐like receptor‐mediated neuronal injury
Lehnardt, S. (2009) · Glia · doi:10.1002/glia.20928 · Cited by 612
Translational control by CPEB: a means to the end
Méndez, R., & Richter, J. D. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35080081 · Cited by 609
Interleukin-1 Mediates Pathological Effects of Microglia on Tau Phosphorylation and on Synaptophysin Synthesis in Cortical Neurons through a p38-MAPK Pathway
Li, Y., Liu, L., Barger, S. W., & Griffin, W. S. T. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-05-01605.2003 · Cited by 563
Post-activation Turn-off of NF-κB-dependent Transcription Is Regulated by Acetylation of p65
Kiernan, R. E., Brès, V., Ng, R. W. M., Coudart, M.-P., Messaoudi, S. E., Sardet, C., Jin, D., Emiliani, S., & Benkirane, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209572200 · Cited by 545
Hypusine-containing protein eIF5A promotes translation elongation
Saini, P., Eyler, D. E., Green, R., & Dever, T. E. (2009) · Nature · doi:10.1038/nature08034 · Cited by 425
Sodium butyrate improves memory function in an Alzheimer's disease mouse model when administered at an advanced stage of disease progression
Govindarajan, N., Agis-Balboa, R. C., Walter, J., Sananbenesi, F., & Fischer, A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110080 · Cited by 405
An immortalized cell line expresses properties of activated microglial cells
Bocchini, V., Mazzolla, R., Barluzzi, R., Blasi, E., Sick, P., & Kettenmann, H. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310405 · Cited by 367
Posttranslational modifications of NF-κB: Another layer of regulation for NF-κB signaling pathway
Huang, B., Yang, X., Lamb, A., & Chen, L. F. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.03.017 · Cited by 357
Inflammation and brain injury: Acute cerebral ischaemia, peripheral and central inflammation
Dénes, Á., Thornton, P., Rothwell, N. J., & Allan, S. M. (2009) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2009.09.010 · Cited by 307
Regulation of DNA binding by Rel/NF-κB transcription factors: structural views
Chen, F. E., & Ghosh, G. (1999) · Oncogene · doi:10.1038/sj.onc.1203224 · Cited by 303
Acetyl-CoA Synthetase 2, a Mitochondrial Matrix Enzyme Involved in the Oxidation of Acetate
Fujino, T., Kondo, J., Ishikawa, M., Morikawa, K., & Yamamoto, T. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008782200 · Cited by 298
Neuroinflammation is a key player in Parkinson’s disease and a prime target for therapy
Li, Q., Flood, P. M., & Hong, J. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0428-1 · Cited by 295
Osmotic regulation of cytokine synthesis in vitro.
Shapiro, L., & Dinarello, C. A. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.26.12230 · Cited by 280
Ambivalent Aspects of Interleukin-6 in Cerebral Ischemia: Inflammatory versus Neurotrophic Aspects
Suzuki, S., Tanaka, K., & Suzuki, N. (2008) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2008.141 · Cited by 241
Interleukin-10, interleukin-4, and transforming growth factor-? differentially regulate lipopolysaccharide-induced production of pro-inflammatory cytokines and nitric oxide in co-cultures of rat astroglial and microglial cells
Ledeboer, A., Brev�, J. J. P., Poole, S., Tilders, F. J. H., & van Dam, A. (2000) · Glia · doi:10.1002/(sici)1098-1136(200004)30:2 · Cited by 233
Interleukin‐10 Inhibits Both Production of Cytokines and Expression of Cytokine Receptors in Microglia
Sawada, M., Suzumura, A., Hosoya, H., Marunouchi, T., & Nagatsu, T. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.721466.x · Cited by 223
Regulation of protein turnover by acetyltransferases and deacetylases
Sadoul, K., Boyault, C., Pabion, M., & Khochbin, S. (2007) · Biochimie · doi:10.1016/j.biochi.2007.06.009 · Cited by 222
HDAC inhibitors as anti‐inflammatory agents
Adcock, I. M. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707166 · Cited by 217
Cytokines and innate inflammation in the pathogenesis of human traumatic brain injury.
Helmy, A., Simoni, M. D., Guilfoyle, M., Carpenter, K., & Hutchinson, P. (2011) · Progress in neurobiology · doi:10.1016/j.pneurobio.2011.09.003 · Cited by 208
Two previously undescribed members of the mouse CPEB family of genes and their inducible expression in the principal cell layers of the hippocampus
Theis, M., Si, K., & Kandel, E. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1133424100 · Cited by 193
Acetylation of mitogen-activated protein kinase phosphatase-1 inhibits Toll-like receptor signaling
Cao, W., Bao, C., Padalko, E. Y., & Lowenstein, C. J. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071728 · Cited by 188
Suppression of acute proinflammatory cytokine and chemokine upregulation by post-injury administration of a novel small molecule improves long-term neurologic outcome in a mouse model of traumatic brain injury
Lloyd, E., Somera-Molina, K., Eldik, L. J. V., Watterson, D. M., & Wainwright, M. S. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-28 · Cited by 183
Remodeling Chromatin and Stress Resistance in the Central Nervous System: Histone Deacetylase Inhibitors as Novel and Broadly Effective Neuroprotective Agents
Langley, B. C., Gensert, J. M., Beal, M. F., & Ratan, R. R. (2005) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007053005091 · Cited by 169
Chronic High-Fat Diet Drives Postnatal Epigenetic Regulation of μ-Opioid Receptor in the Brain
Vucetic, Z., Kimmel, J. N., & Reyes, T. M. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2011.4 · Cited by 166
Acetate supplementation increases brain histone acetylation and inhibits histone deacetylase activity and expression
Soliman, M. L., & Rosenberger, T. A. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0751-3 · Cited by 161
Self-citation
Cytoplasmic Polyadenylation Element Binding Protein-Dependent Protein Synthesis Is Regulated by Calcium/Calmodulin-Dependent Protein Kinase II
Atkins, C. M., Nozaki, N., Shigeri, Y., & Soderling, T. R. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0854-04.2004 · Cited by 156
HDAC inhibitor increases histone H3 acetylation and reduces microglia inflammatory response following traumatic brain injury in rats.
Zhang, B., West, E., Van, K. C., Gurkoff, G. G., Zhou, J., Zhang, X.-M., Kozikowski, A., & Lyeth, B. G. (2008) · Brain Research · doi:10.1016/j.brainres.2008.05.085 · Cited by 138
eIF5A has a function in the elongation step of translation in yeast
Gregio, A. P. B., Cano, V. S. P., Avaca, J. S., Valentini, S. R., & Zanelli, C. F. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.148 · Cited by 127
Anti-Inflammatory Cytokines: Expression and Action in the Brain
Vitković, L., Maeda, S., & STERNBERG, E. M. (2001) · NeuroImmunoModulation · doi:10.1159/000059387 · Cited by 117
Assessing the contribution of inflammation in models of Alzheimer's disease
Johnston, H. R., Boutin, H., & Allan, S. M. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390886 · Cited by 114
Transforming Growth Factor-β: A Neuroprotective Factor in Cerebral Ischemia
Dhandapani, K. M., & Brann, D. W. (2003) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:39:1:13 · Cited by 113
eIF5A binds to translational machinery components and affects translation in yeast
Zanelli, C. F., Maragno, A. L. C., Gregio, A. P. B., Komili, S., Pandolfi, J. R. C., Mestriner, C. A., Lustri, W. R., & Valentini, S. R. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.07.195 · Cited by 112
Amyloid-β oligomers stimulate microglia through a tyrosine kinase dependent mechanism
Manocha, G. D., Floden, A. M., & Combs, C. K. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.10.027 · Cited by 110
Self-citation
Lipopolysaccharide induces the rapid tyrosine phosphorylation of the mitogen-activated protein kinases erk-1 and p38 in cultured human vascular endothelial cells requiring the presence of soluble CD14
Schumann, R., Pfeil, D., Lamping, N., Kirschning, C. J., Scherzinger, G., Schlag, P., Karawajew, L., & Herrmann, F. (1996) · Blood · doi:10.1182/blood.v87.7.2805.bloodjournal8772805 · Cited by 109
Expression of mutant alpha-synuclein modulates microglial phenotype in vitro
Rojanathammanee, L., Murphy, E. J., & Combs, C. K. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-44 · Cited by 106
Self-citation
Acetate supplementation modulates brain histone acetylation and decreases interleukin-1β expression in a rat model of neuroinflammation
Soliman, M. L., Smith, M. D., Houdek, H. M., & Rosenberger, T. A. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-51 · Cited by 105
Self-citation
Role of Cytokines as Mediators and Regulators of Microglial Activity in Inflammatory Demyelination of the CNS
Merson, T. D., Binder, M. D., & Kilpatrick, T. J. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8112-z · Cited by 84
Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A)
Ishfaq, M., Maeta, K., Maeda, S., Natsume, T., Ito, A., & Yoshida, M. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.06.042 · Cited by 82
Selective modulation of lipopolysaccharide-stimulated cytokine expression and mitogen-activated protein kinase pathways by dibutyryl-cAMP in BV2 microglial cells.
Woo, M.-S., Jang, P., Park, J.-S., Kim, W.-K., Joh, T., & Kim, H.-S. (2003) · Brain Research. Molecular Brain Research · doi:10.1016/s0169-328x(03)00095-0 · Cited by 78
Selective Modulation of BV-2 Microglial Activation by Prostaglandin E2
Petrova, T. V., Akama, K. T., & Eldik, L. J. V. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28823 · Cited by 77
RNA-Binding Proteins: A Lesson in Repression
Wells, D. G. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1795-06.2006 · Cited by 76
Acetate supplementation attenuates lipopolysaccharide‐induced neuroinflammation
Reisenauer, C. J., Bhatt, D. P., Mitteness, D. J., Slanczka, E. R., Gienger, H. M., Watt, J. A., & Rosenberger, T. A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07198.x · Cited by 73
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Metabolic Acetate Therapy for the Treatment of Traumatic Brain Injury
Arun, P., Ariyannur, P. S., Moffett, J. R., Xing, G., Hamilton, K. R., Grunberg, N. E., Ives, J. A., & Namboodiri, A. M. A. (2009) · Journal of Neurotrauma · doi:10.1089/neu.2009.0994 · Cited by 73
Interferon-β treatment in multiple sclerosis patients decreases the number of circulating T cells producing interferon-γ and interleukin-4
Furlan, R., Bergami, A., Lang, R., Brambilla, E., Franciotta, D. M., Martinelli, V., Comı, G., Panina‐Bordignon, P., & Martino, G. (2000) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(00)00377-5 · Cited by 72
Metabolic acetate therapy improves phenotype in the tremor rat model of Canavan disease
Arun, P., Madhavarao, C. N., Moffett, J. R., Hamilton, K. R., Grunberg, N. E., Ariyannur, P. S., Gahl, W. A., Anikster, Y., Mog, S. R., Hallows, W. C., et al. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9100-z · Cited by 71
Relationship between Methylation and Acetylation of Arginine-Rich Histones in Cycling and Arrested HeLa Cells
Annunziato, A. T., Eason, M. B., & Perry, C. A. (1995) · Biochemistry · doi:10.1021/bi00009a023 · Cited by 70
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Development of a novel therapeutic suppressor of brain proinflammatory cytokine up-regulation that attenuates synaptic dysfunction and behavioral deficits
Hu, W., Ranaivo, H. R., Roy, S. M., Behanna, H. A., Wing, L. K., Munoz, L., Guo, L., Eldik, L. J. V., & Watterson, D. M. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.10.028 · Cited by 65
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Nuclear‐cytoplasmic localization of acetyl coenzyme a synthetase‐1 in the rat brain
Ariyannur, P. S., Moffett, J. R., Madhavarao, C. N., Arun, P., Vishnu, N., Jacobowitz, D. M., Hallows, W. C., Denu, J. M., & Namboodiri, A. M. A. (2010) · The Journal of Comparative Neurology · doi:10.1002/cne.22373 · Cited by 63
Memory impairment induced by brain iron overload is accompanied by reduced H3K9 acetylation and ameliorated by sodium butyrate
da Silva, P. F., Garcia, V. A., Dornelles, A. D. S., da Silva, V. K., Maurmann, N., Portal, B. C. D., Ferreira, R. D. P., Piazza, F. C., Roesler, R., & Schröder, N. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.10.038 · Cited by 59
Interleukin-10 expression in lipopolysaccharide-activated microglia is mediated by extracellular ATP in an autocrine fashion
Seo, D. R., Kim, K. Y., & Lee, Y. B. (2004) · Neuroreport · doi:10.1097/00001756-200405190-00015 · Cited by 58
Role of highly conserved pyrimidine-rich sequences in the 3′ untranslated region of the GAP-43 mRNA in mRNA stability and RNA-protein interactions
Kohn, D. T., Tsai, K.-C., Cansino, V. V., Neve, R. L., & Perrone‐Bizzozero, N. I. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00239-o · Cited by 45
Genome-wide ChIP-seq mapping and analysis reveal butyrate-induced acetylation of H3K9 and H3K27 correlated with transcription activity in bovine cells
Shin, J. H., Li, R. W., Gao, Y., Baldwin, R. L., & Li, C. (2012) · Functional & Integrative Genomics · doi:10.1007/s10142-012-0263-6 · Cited by 41
Inactivation of eukaryotic initiation factor 5A (eIF5A) by specific acetylation of its hypusine residue by spermidine/spermine acetyltransferase 1 (SSAT1)
Lee, S. B., Park, J. H., Folk, J. E., Deck, J. A., Pegg, A. E., Sokabe, M., Fraser, C. S., & Park, M. H. (2010) · Biochemical Journal · doi:10.1042/bj20101322 · Cited by 34
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Kraatz, J. J., Clair, L., Bellingham, J. M., Wahlstrom, K., Rodriguez, J. L., & West, M. A. (1998) · doi:10.1097/00005373-199810000-00008 · Cited by 14

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Authors: Soliman, M. L., Puig, K. L., Combs, C. K., & Rosenberger, T. A.
Affiliations: University of North Dakota (US)
Corresponding author: Rosenberger, Thad A.
ORCID: Combs, Colin K.
Rosenberger, Thad A.
Venue: Journal of Neurochemistry
Publisher: Wiley
Published: 2012-09-28
Volume: 123
Issue: 4
Pages: 555-567
ISSN: 0022-3042 (ISSN-L)
1471-4159
DOI: 10.1111/j.1471-4159.2012.07955.x
PMC: PMC3472042
OpenAlex: W2090091665
Cited by: 131
References: 75
Citations by year: 2026: 12 · 2025: 12 · 2024: 21 · 2023: 12 · 2022: 15 · 2021: 14 · 2020: 12 · 2019: 3 · 2018: 5 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 7 · 2013: 7 · 2012: 3
FWCI: 3.06
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Neurochemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Center for Research Resources
component of the National Institutes of Health
Topics: Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Neuroscience › Biological Psychiatry › Tryptophan and brain disorders
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords: acetate, microglia, neuroinflammation, histone H3K9 acetylation, NF-κB, MAPK signaling, p38 MAPK, JNK, lipopolysaccharide, IL-1β, acetyl-CoA, histone acetylation, non-histone protein acetylation, acetate metabolism, cytokine expression, TGF-β1
MeSH terms: Acetates, Acetylation, Analysis of Variance, Animals, Brain, Cells, Cultured, Dose-Response Relationship, Drug, Histones, L-Lactate Dehydrogenase, Lipopolysaccharides, Lysine, Mice, Inbred C57BL, Phosphorylation, RNA, Messenger, Time Factors, Signal Transduction, Cytokines, Microglia, Mitogen-Activated Protein Kinases, Mice

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Acetate reduces microglia inflammatory signaling in vitro

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