trichostatin A

Trichostatin is a lipid of Polyketides (PK) class. Trichostatin is associated with abnormalities such as Dentatorubral-Pallidoluysian Atrophy, PARAGANGLIOMAS 3, abnormal fragmented structure, Disintegration (morphologic abnormality) and Hyperostosis, Diffuse Idiopathic Skeletal. The involved functions are known as Acetylation, Cell Differentiation process, histone modification, Gene Silencing and Transcriptional Activation. Trichostatin often locates in CD41a, Hematopoietic System, Chromatin Structure, Blood and Endothelium. The associated genes with Trichostatin are SPI1 gene, CELL Gene, Chromatin, CXCR4 gene and DNMT1 gene. The related lipids are Butyrates, Promega, butyrate, Lipopolysaccharides and Steroids. The related experimental models are Knock-out, Mouse Model, Xenograft Model and Cancer Model.

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Introduction

To understand associated biological information of trichostatin A, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.

What diseases are associated with trichostatin A?

trichostatin A is suspected in Infection, Morphologically altered structure, Ureteral obstruction, Photosensitization, Atherosclerosis, Hypertrophic Cardiomyopathy and other diseases in descending order of the highest number of associated sentences.

Related references are mostly published in these journals:

Disease Cross reference Weighted score Related literature
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Possible diseases from mapped MeSH terms on references

We collected disease MeSH terms mapped to the references associated with trichostatin A

MeSH term MeSH ID Detail
Abnormalities, Multiple D000015 13 associated lipids
Adenocarcinoma D000230 166 associated lipids
Adenocarcinoma, Papillary D000231 2 associated lipids
Adrenoleukodystrophy D000326 29 associated lipids
Alzheimer Disease D000544 76 associated lipids
Arthritis, Experimental D001169 24 associated lipids
Asthma D001249 52 associated lipids
Autoimmune Diseases D001327 27 associated lipids
Biliary Tract Neoplasms D001661 7 associated lipids
Body Weight D001835 333 associated lipids
Brain Neoplasms D001932 15 associated lipids
Breast Neoplasms D001943 24 associated lipids
Carcinoma D002277 18 associated lipids
Carcinoma, Non-Small-Cell Lung D002289 72 associated lipids
Carcinoma, Renal Cell D002292 12 associated lipids
Cat Diseases D002371 12 associated lipids
Cell Transformation, Neoplastic D002471 126 associated lipids
Cell Transformation, Viral D002472 26 associated lipids
Chondrosarcoma D002813 9 associated lipids
Colonic Neoplasms D003110 161 associated lipids
Conjunctival Neoplasms D003230 3 associated lipids
Coronary Artery Disease D003324 47 associated lipids
Cystic Fibrosis D003550 65 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Diabetes Mellitus, Experimental D003921 85 associated lipids
Encephalomyelitis, Autoimmune, Experimental D004681 26 associated lipids
Endometriosis D004715 29 associated lipids
Enteritis D004751 8 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Fetal Growth Retardation D005317 9 associated lipids
Fibrosis D005355 23 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Ganglioneuroma D005729 2 associated lipids
Glioblastoma D005909 27 associated lipids
Glioma D005910 112 associated lipids
Goldenhar Syndrome D006053 1 associated lipids
Cardiomegaly D006332 31 associated lipids
Carcinoma, Hepatocellular D006528 140 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Hypersensitivity D006967 22 associated lipids
Hypertension D006973 115 associated lipids
Hypertension, Pulmonary D006976 32 associated lipids
Hypesthesia D006987 1 associated lipids
Immunologic Deficiency Syndromes D007153 8 associated lipids
Inflammation D007249 119 associated lipids
Chromosome Inversion D007446 1 associated lipids
Keloid D007627 12 associated lipids
Leishmaniasis D007896 19 associated lipids
Leukemia D007938 74 associated lipids
Leukemia, Myeloid D007951 52 associated lipids
Liver Cirrhosis D008103 67 associated lipids
Lung Neoplasms D008175 171 associated lipids
Lupus Vulgaris D008177 1 associated lipids
Lupus Erythematosus, Systemic D008180 43 associated lipids
Lymphatic Metastasis D008207 10 associated lipids
Lymphoma, Follicular D008224 3 associated lipids
Mammary Neoplasms, Experimental D008325 67 associated lipids
Medulloblastoma D008527 22 associated lipids
Melanoma D008545 69 associated lipids
Intellectual Disability D008607 13 associated lipids
Muscular Dystrophies D009136 10 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Nasal Polyps D009298 26 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Neoplasms D009369 13 associated lipids
Neoplasms, Hormone-Dependent D009376 23 associated lipids
Neovascularization, Pathologic D009389 39 associated lipids
Nerve Degeneration D009410 53 associated lipids
Neuroblastoma D009447 66 associated lipids
Osteomalacia D010018 5 associated lipids
Pancreatic Neoplasms D010190 77 associated lipids
Progeria D011371 3 associated lipids
Prostatic Hyperplasia D011470 20 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Pulmonary Fibrosis D011658 24 associated lipids
Radiation Injuries D011832 14 associated lipids
Retinoblastoma D012175 12 associated lipids
Rubinstein-Taybi Syndrome D012415 1 associated lipids
Mast-Cell Sarcoma D012515 9 associated lipids
Osteosarcoma D012516 50 associated lipids
Thyroid Neoplasms D013964 33 associated lipids
Tongue Neoplasms D014062 15 associated lipids
Translocation, Genetic D014178 20 associated lipids
Ureteral Obstruction D014517 10 associated lipids
Uterine Neoplasms D014594 18 associated lipids
Uveal Neoplasms D014604 3 associated lipids
Supratentorial Neoplasms D015173 1 associated lipids
Reperfusion Injury D015427 65 associated lipids
Leukemia, Lymphocytic, Chronic, B-Cell D015451 25 associated lipids
Leukemia, T-Cell D015458 23 associated lipids
Leukemia-Lymphoma, Adult T-Cell D015459 25 associated lipids
Leukemia, Myeloid, Acute D015470 19 associated lipids
Leukemia, Promyelocytic, Acute D015473 3 associated lipids
Leukemia, Myelomonocytic, Acute D015479 6 associated lipids
Endometrial Neoplasms D016889 30 associated lipids
Polycystic Kidney, Autosomal Dominant D016891 6 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Dermatitis, Allergic Contact D017449 20 associated lipids
Hypereosinophilic Syndrome D017681 3 associated lipids
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PubChem Associated disorders and diseases

What pathways are associated with trichostatin A

Lipid pathways are not clear in current pathway databases. We organized associated pathways with trichostatin A through full-text articles, including metabolic pathways or pathways of biological mechanisms.

Related references are published most in these journals:

Pathway name Related literatures
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PubChem Biomolecular Interactions and Pathways

Link to PubChem Biomolecular Interactions and Pathways

What cellular locations are associated with trichostatin A?

Related references are published most in these journals:

Location Cross reference Weighted score Related literatures
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What functions are associated with trichostatin A?


Related references are published most in these journals:

Function Cross reference Weighted score Related literatures

What lipids are associated with trichostatin A?

Related references are published most in these journals:

Lipid concept Cross reference Weighted score Related literatures
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What genes are associated with trichostatin A?

Related references are published most in these journals:


Gene Cross reference Weighted score Related literatures

What common seen animal models are associated with trichostatin A?

Mouse Model

Mouse Model are used in the study 'Regulation of minichromosome maintenance gene family by microRNA-1296 and genistein in prostate cancer.' (Majid S et al., 2010), Mouse Model are used in the study 'Reversal of hypermethylation and reactivation of p16INK4a, RARbeta, and MGMT genes by genistein and other isoflavones from soy.' (Fang MZ et al., 2005) and Mouse Model are used in the study 'Histone deacetylase 3 mediates allergic skin inflammation by regulating expression of MCP1 protein.' (Kim Y et al., 2012).

Xenograft Model

Xenograft Model are used in the study 'Histone deacetylase inhibitors induce growth arrest and differentiation in uveal melanoma.' (Landreville S et al., 2012), Xenograft Model are used in the study 'Extended treatment with physiologic concentrations of dietary phytochemicals results in altered gene expression, reduced growth, and apoptosis of cancer cells.' (Moiseeva EP et al., 2007) and Xenograft Model are used in the study 'Retinoic acid and the histone deacetylase inhibitor trichostatin a inhibit the proliferation of human renal cell carcinoma in a xenograft tumor model.' (Touma SE et al., 2005).

Cancer Model

Cancer Model are used in the study 'Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin a after intraperitoneal administration to mice.' (Sanderson L et al., 2004).

Related references are published most in these journals:

Model Cross reference Weighted score Related literatures
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NCBI Entrez Crosslinks

All references with trichostatin A

Download all related citations
Per page 10 20 50 100 | Total 3126
Authors Title Published Journal PubMed Link
Ou JN et al. Histone deacetylase inhibitor Trichostatin A induces global and gene-specific DNA demethylation in human cancer cell lines. 2007 Biochem. Pharmacol. pmid:17276411
McBain JA et al. Apoptotic death in adenocarcinoma cell lines induced by butyrate and other histone deacetylase inhibitors. 1997 Biochem. Pharmacol. pmid:9214697
Mikkelsen IM et al. Activation of the gamma-glutamyltransferase promoter 2 in the rat colon carcinoma cell line CC531 by histone deacetylase inhibitors is mediated through the Sp1 binding motif. 2002 Biochem. Pharmacol. pmid:12123752
Kohge T et al. Promotion of antigen-specific antibody production in murine B cells by a moderate increase in histone acetylation. 1998 Biochem. Pharmacol. pmid:9825735
Jalonen U et al. Inhibition of tristetraprolin expression by dexamethasone in activated macrophages. 2005 Biochem. Pharmacol. pmid:15710351
Brieger A et al. In bcr-abl-positive myeloid cells resistant to conventional chemotherapeutic agents, expression of Par-4 increases sensitivity to imatinib (STI571) and histone deacetylase-inhibitors. 2004 Biochem. Pharmacol. pmid:15183120
Place RF et al. HDAC inhibition prevents NF-kappa B activation by suppressing proteasome activity: down-regulation of proteasome subunit expression stabilizes I kappa B alpha. 2005 Biochem. Pharmacol. pmid:15950952
Wagner S and Roemer K Retinoblastoma protein is required for efficient colorectal carcinoma cell apoptosis by histone deacetylase inhibitors in the absence of p21Waf. 2005 Biochem. Pharmacol. pmid:15763542
Vandergeeten C et al. HIV-1 protease inhibitors do not interfere with provirus transcription and host cell apoptosis induced by combined treatment TNF-alpha + TSA. 2007 Biochem. Pharmacol. pmid:17386923
Carbajal A et al. A novel method for purification of polymerizable tubulin with a high content of the acetylated isotype. 2013 Biochem. J. pmid:23140207
Aapola U et al. Epigenetic modifications affect Dnmt3L expression. 2004 Biochem. J. pmid:15015937
Swingler TE et al. MMP28 gene expression is regulated by Sp1 transcription factor acetylation. 2010 Biochem. J. pmid:20144149
Sanchez del Pino MM et al. Properties of the yeast nuclear histone deacetylase. 1994 Biochem. J. pmid:7980438
Mehra-Chaudhary R et al. Msx3 protein recruits histone deacetylase to down-regulate the Msx1 promoter. 2001 Biochem. J. pmid:11115394
Avram D et al. COUP-TF (chicken ovalbumin upstream promoter transcription factor)-interacting protein 1 (CTIP1) is a sequence-specific DNA binding protein. 2002 Biochem. J. pmid:12196208
Arts J et al. Stimulation of tissue-type plasminogen activator gene expression by sodium butyrate and trichostatin A in human endothelial cells involves histone acetylation. 1995 Biochem. J. pmid:7646441
Yang L et al. An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B. 2003 Biochem. J. pmid:12398767
Hodny Z et al. Sp1 and chromatin environment are important contributors to the formation of repressive chromatin structures on the transfected human adenine nucleotide translocase-2 promoter. 2000 Biochem. J. pmid:10657244
Zhang X et al. Suppression of DPYD expression in RKO cells via DNA methylation in the regulatory region of the DPYD promoter: a potentially important epigenetic mechanism regulating DPYD expression. 2007 Biochem. Cell Biol. pmid:17612628
Sekhavat A et al. Competitive inhibition of histone deacetylase activity by trichostatin A and butyrate. 2007 Biochem. Cell Biol. pmid:18059533
Waterborg JH and Kapros T Kinetic analysis of histone acetylation turnover and Trichostatin A induced hyper- and hypoacetylation in alfalfa. 2002 Biochem. Cell Biol. pmid:12123281
Hosseinkhani M et al. Trichostatin A induces myocardial differentiation of monkey ES cells. 2007 Biochem. Biophys. Res. Commun. pmid:17368572
Oger F et al. The class I histone deacetylases of the platyhelminth parasite Schistosoma mansoni. 2008 Biochem. Biophys. Res. Commun. pmid:18977200
Deltour S et al. Characterization of HRG22, a human homologue of the putative tumor suppressor gene HIC1. 2001 Biochem. Biophys. Res. Commun. pmid:11554746
Kishigami S et al. Significant improvement of mouse cloning technique by treatment with trichostatin A after somatic nuclear transfer. 2006 Biochem. Biophys. Res. Commun. pmid:16356478
Hagiwara H et al. Histone deacetylase inhibitor trichostatin A enhances myogenesis by coordinating muscle regulatory factors and myogenic repressors. 2011 Biochem. Biophys. Res. Commun. pmid:22019851
Park KS et al. Histone modification-mediated Lhx2 gene expression. 2012 Biochem. Biophys. Res. Commun. pmid:23036195
Heo H et al. Suppression of caspase-11 expression by histone deacetylase inhibitors. 2009 Biochem. Biophys. Res. Commun. pmid:19013432
Liu Z et al. Deacetylase inhibitor trichostatin A down-regulates Foxp3 expression and reduces CD4+CD25+ regulatory T cells. 2010 Biochem. Biophys. Res. Commun. pmid:20801101
Akiba Y et al. Histone deacetylase inhibitors de-repress tyrosine hydroxylase expression in the olfactory bulb and rostral migratory stream. 2010 Biochem. Biophys. Res. Commun. pmid:20170631
Bigl M et al. Aberrant methylation of human L- and M-fructose 1,6-bisphosphatase genes in cancer. 2008 Biochem. Biophys. Res. Commun. pmid:18938139
Benny Klimek ME et al. Acute inhibition of myostatin-family proteins preserves skeletal muscle in mouse models of cancer cachexia. 2010 Biochem. Biophys. Res. Commun. pmid:20036643
Li H and Wu X Histone deacetylase inhibitor, Trichostatin A, activates p21WAF1/CIP1 expression through downregulation of c-myc and release of the repression of c-myc from the promoter in human cervical cancer cells. 2004 Biochem. Biophys. Res. Commun. pmid:15474507
Choi HS et al. Trichostatin A, a histone deacetylase inhibitor, activates the IGFBP-3 promoter by upregulating Sp1 activity in hepatoma cells: alteration of the Sp1/Sp3/HDAC1 multiprotein complex. 2002 Biochem. Biophys. Res. Commun. pmid:12200149
Sowa Y et al. Histone deacetylase inhibitor activates the WAF1/Cip1 gene promoter through the Sp1 sites. 1997 Biochem. Biophys. Res. Commun. pmid:9405248
Sayan BS et al. Induction of TAp63 by histone deacetylase inhibitors. 2010 Biochem. Biophys. Res. Commun. pmid:20043870
Ghosh AK et al. Trichostatin A blocks TGF-beta-induced collagen gene expression in skin fibroblasts: involvement of Sp1. 2007 Biochem. Biophys. Res. Commun. pmid:17234156
Matsubara K et al. Dynamics and regulation of lysine-acetylation during one-cell stage mouse embryos. 2013 Biochem. Biophys. Res. Commun. pmid:23567968
Zhou X et al. Preclinical evaluation of combined antineoplastic effect of DLC1 tumor suppressor protein and suberoylanilide hydroxamic acid on prostate cancer cells. 2012 Biochem. Biophys. Res. Commun. pmid:22425986
Choi S et al. Histone deacetylases inhibitor trichostatin A modulates the extracellular release of APE1/Ref-1. 2013 Biochem. Biophys. Res. Commun. pmid:23665318
Maehara K et al. Effects of histone acetylation on transcriptional regulation of manganese superoxide dismutase gene. 2002 Biochem. Biophys. Res. Commun. pmid:12083788
Wang XQ et al. Histone deacetylase inhibition results in decreased macrophage CD9 expression. 2002 Biochem. Biophys. Res. Commun. pmid:12056820
Hu JF et al. The role of histone acetylation in the allelic expression of the imprinted human insulin-like growth factor II gene. 1998 Biochem. Biophys. Res. Commun. pmid:9792787
Korhonen P et al. Expression of transcriptional repressor protein mSin3A but not mSin3B is induced during neuronal apoptosis. 1998 Biochem. Biophys. Res. Commun. pmid:9813182
Hirose N et al. ATF-2 regulates lipopolysaccharide-induced transcription in macrophage cells. 2009 Biochem. Biophys. Res. Commun. pmid:19422799
Kim HS et al. Regulation of the tyrosine hydroxylase gene promoter by histone deacetylase inhibitors. 2003 Biochem. Biophys. Res. Commun. pmid:14651963
Sun P et al. Effect of trichostatin A on Burkitt's lymphoma cells: Inhibition of EPS8 activity through Phospho-Erk1/2 pathway. 2018 Biochem. Biophys. Res. Commun. pmid:29462617
Kusakabe M et al. Impact of DNA demethylation of the G0S2 gene on the transcription of G0S2 in squamous lung cancer cell lines with or without nuclear receptor agonists. 2009 Biochem. Biophys. Res. Commun. pmid:19878646
Lu ZP et al. Histone deacetylase inhibitor Trichostatin A reduces anti-DNA autoantibody production and represses IgH gene transcription. 2005 Biochem. Biophys. Res. Commun. pmid:15781251
Iacobazzi V et al. Epigenetic mechanisms and Sp1 regulate mitochondrial citrate carrier gene expression. 2008 Biochem. Biophys. Res. Commun. pmid:18706393