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
Cystadenocarcinoma, Mucinous D018282 1 associated lipids
Roseolovirus Infections D019349 1 associated lipids
Myopathy, Central Core D020512 1 associated lipids
Thyroid Hormone Resistance Syndrome D018382 1 associated lipids
Chromosome Inversion D007446 1 associated lipids
Rhabdomyosarcoma, Embryonal D018233 1 associated lipids
Carcinoma, Papillary, Follicular D018265 1 associated lipids
Gestational Trophoblastic Disease D031901 1 associated lipids
Rhabdoid Tumor D018335 1 associated lipids
Visceral Pain D059265 1 associated lipids
Lupus Vulgaris D008177 1 associated lipids
Rubinstein-Taybi Syndrome D012415 1 associated lipids
Classical Lissencephalies and Subcortical Band Heterotopias D054221 1 associated lipids
Goldenhar Syndrome D006053 1 associated lipids
Adenomyosis D062788 1 associated lipids
Capsule Opacification D058442 1 associated lipids
Neoplasm Micrometastasis D061206 1 associated lipids
Cystadenoma, Serous D018293 1 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Intervertebral Disc Degeneration D055959 1 associated lipids
Supratentorial Neoplasms D015173 1 associated lipids
Hypesthesia D006987 1 associated lipids
Ganglioneuroma D005729 2 associated lipids
Cystadenocarcinoma, Serous D018284 2 associated lipids
Fibromatosis, Aggressive D018222 2 associated lipids
Rhabdomyosarcoma, Alveolar D018232 2 associated lipids
Small Cell Lung Carcinoma D055752 2 associated lipids
Bone Marrow Neoplasms D019046 2 associated lipids
Adenocarcinoma, Papillary D000231 2 associated lipids
Inflammatory Breast Neoplasms D058922 2 associated lipids
Progeria D011371 3 associated lipids
Mastocytoma D034801 3 associated lipids
Uveal Neoplasms D014604 3 associated lipids
Leukemia, Promyelocytic, Acute D015473 3 associated lipids
Conjunctival Neoplasms D003230 3 associated lipids
Adenocarcinoma, Follicular D018263 3 associated lipids
Hypereosinophilic Syndrome D017681 3 associated lipids
Lymphoma, Follicular D008224 3 associated lipids
Lymphoma, Large-Cell, Anaplastic D017728 3 associated lipids
Retinal Neoplasms D019572 3 associated lipids
Spinocerebellar Ataxias D020754 4 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Neuroendocrine Tumors D018358 4 associated lipids
Porcine Reproductive and Respiratory Syndrome D019318 4 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Osteomalacia D010018 5 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Primary Myelofibrosis D055728 6 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

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Per page 10 20 50 100 | Total 3126
Authors Title Published Journal PubMed Link
Wong J et al. Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. 1998 EMBO J. pmid:9430643
Magnaghi-Jaulin L et al. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. 1998 Nature pmid:9468140
Svensson K et al. The paternal allele of the H19 gene is progressively silenced during early mouse development: the acetylation status of histones may be involved in the generation of variegated expression patterns. 1998 Development pmid:9389664
El Kharroubi A et al. Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. 1998 Mol. Cell. Biol. pmid:9566873
Gray SG and Ekström TJ Effects of cell density and trichostatin A on the expression of HDAC1 and p57Kip2 in Hep 3B cells. 1998 Biochem. Biophys. Res. Commun. pmid:9571167
Belyaev ND et al. The acetylation patterns of histones H3 and H4 along Vicia faba chromosomes are different. 1998 Chromosome Res. pmid:9510512
Richon VM et al. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. 1998 Proc. Natl. Acad. Sci. U.S.A. pmid:9501205
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
Phelan MW et al. Hypoxia increases thrombospondin-1 transcript and protein in cultured endothelial cells. 1998 J. Lab. Clin. Med. pmid:9851743
Ciana P et al. Leukemic transformation by the v-ErbA oncoprotein entails constitutive binding to and repression of an erythroid enhancer in vivo. 1998 EMBO J. pmid:9857194
De Luca P et al. Retinoblastoma protein tethered to promoter DNA represses TBP-mediated transcription. 1998 J. Cell. Biochem. pmid:9671233
Selker EU Trichostatin A causes selective loss of DNA methylation in Neurospora. 1998 Proc. Natl. Acad. Sci. U.S.A. pmid:9689097
Jin S and Scotto KW Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y. 1998 Mol. Cell. Biol. pmid:9632821
Nakajima H et al. FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor. 1998 Exp. Cell Res. pmid:9633520
Thompson EM and Renard JP Preferential nuclear location of a transgene does not depend on its transcriptional activity during early mouse development. 1998 Chromosoma pmid:9880765
Durum SK et al. Interleukin 7 receptor control of T cell receptor gamma gene rearrangement: role of receptor-associated chains and locus accessibility. 1998 J. Exp. Med. pmid:9858510
McBain JA et al. Apoptotic death in adenocarcinoma cell lines induced by butyrate and other histone deacetylase inhibitors. 1997 Biochem. Pharmacol. pmid:9214697
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Sheridan PL et al. Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. 1997 Genes Dev. pmid:9407026
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Ekwall K et al. Transient inhibition of histone deacetylation alters the structural and functional imprint at fission yeast centromeres. 1997 Cell pmid:9428524
Xu L et al. Effect of the histone deacetylase inhibitor trichostatin A on the responsiveness of rat hepatocytes to dioxin. 1997 Biochem. Pharmacol. pmid:9174108
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Dion LD et al. Amplification of recombinant adenoviral transgene products occurs by inhibition of histone deacetylase. 1997 Virology pmid:9168882
Chen ZJ and Pikaard CS Epigenetic silencing of RNA polymerase I transcription: a role for DNA methylation and histone modification in nucleolar dominance. 1997 Genes Dev. pmid:9284051
Medina V et al. Induction of caspase-3 protease activity and apoptosis by butyrate and trichostatin A (inhibitors of histone deacetylase): dependence on protein synthesis and synergy with a mitochondrial/cytochrome c-dependent pathway. 1997 Cancer Res. pmid:9288776
Koguchi Y et al. Trichostatin A and herboxidiene up-regulate the gene expression of low density lipoprotein receptor. 1997 J. Antibiot. pmid:9592573
Lee E et al. Involvement of histone hyperacetylation in triggering DNA fragmentation of rat thymocytes undergoing apoptosis. 1996 FEBS Lett. pmid:8898091
Taunton J et al. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. 1996 Science pmid:8602529
Van Lint C et al. Transcriptional activation and chromatin remodeling of the HIV-1 promoter in response to histone acetylation. 1996 EMBO J. pmid:8605881
Carmen AA et al. HDA1 and HDA3 are components of a yeast histone deacetylase (HDA) complex. 1996 J. Biol. Chem. pmid:8663039
Van Lint C et al. The expression of a small fraction of cellular genes is changed in response to histone hyperacetylation. 1996 Gene Expr. pmid:8723390
Takahashi I et al. Selective inhibition of IL-2 gene expression by trichostatin A, a potent inhibitor of mammalian histone deacetylase. 1996 J. Antibiot. pmid:8682722
Zhang J et al. Basis for the loss of aryl hydrocarbon receptor gene expression in clones of a mouse hepatoma cell line. 1996 Mol. Pharmacol. pmid:8967965
Yoshida M [Molecular targets of cell cycle inhibitors and their mode of action]. 1996 Tanpakushitsu Kakusan Koso pmid:8890633
Sano M and Kitajima S Inhibition of the nerve growth factor-induced outgrowth of neurites by trichostatin A requires protein synthesis de novo in PC12D cells. 1996 Brain Res. pmid:9117395
Bartsch J et al. Moderate increase in histone acetylation activates the mouse mammary tumor virus promoter and remodels its nucleosome structure. 1996 Proc. Natl. Acad. Sci. U.S.A. pmid:8855250
Ogryzko VV et al. Human fibroblast commitment to a senescence-like state in response to histone deacetylase inhibitors is cell cycle dependent. 1996 Mol. Cell. Biol. pmid:8756678
Yamamoto I et al. Histone hyperacetylation plays a role in augmentation of IL-4-induced IgE production in LPS-stimulated murine B-lymphocytes by sodium butyrate. 1996 J. Biochem. pmid:8827437
Okabe M et al. Competence effect of PDGF on Ki-67 antigen and DNA contents, and its inhibition by trichostatin-A and a butylydene phthalide BP-421 in primary smooth muscle cells of rat aorta by flow cytometry. 1995 Biol. Pharm. Bull. pmid:8787785
Worrad DM et al. Temporally restricted spatial localization of acetylated isoforms of histone H4 and RNA polymerase II in the 2-cell mouse embryo. 1995 Development pmid:7555721
O'Neill LP and Turner BM Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. 1995 EMBO J. pmid:7664735