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
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
Per page 10 20 50 100 | Total 139

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.

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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?

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


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Function Cross reference Weighted score Related literatures

What lipids are associated with trichostatin A?

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

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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
Sawa H et al. Histone deacetylase inhibitors such as sodium butyrate and trichostatin A inhibit vascular endothelial growth factor (VEGF) secretion from human glioblastoma cells. 2002 Brain Tumor Pathol pmid:12622137
Handumrongkul C et al. Distinct sets of cellular genes control the expression of transfected, nuclear-localized genes. 2002 Mol. Ther. pmid:11829526
Herold C et al. The histone-deacetylase inhibitor Trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells. 2002 J. Hepatol. pmid:11830335
Yamashita K et al. Pharmacologic unmasking of epigenetically silenced tumor suppressor genes in esophageal squamous cell carcinoma. 2002 Cancer Cell pmid:12498717
Zhou DC et al. Frequent mutations in the ligand-binding domain of PML-RARalpha after multiple relapses of acute promyelocytic leukemia: analysis for functional relationship to response to all-trans retinoic acid and histone deacetylase inhibitors in vitro and in vivo. 2002 Blood pmid:11830487
Fahrner JA et al. Dependence of histone modifications and gene expression on DNA hypermethylation in cancer. 2002 Cancer Res. pmid:12499261
Rombouts K et al. Trichostatin A, a histone deacetylase inhibitor, suppresses collagen synthesis and prevents TGF-beta(1)-induced fibrogenesis in skin fibroblasts. 2002 Exp. Cell Res. pmid:12169274
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
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
Petti MC et al. Complete remission through blast cell differentiation in PLZF/RARalpha-positive acute promyelocytic leukemia: in vitro and in vivo studies. 2002 Blood pmid:12130525
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
Qiu P and Li L Histone acetylation and recruitment of serum responsive factor and CREB-binding protein onto SM22 promoter during SM22 gene expression. 2002 Circ. Res. pmid:11988486
Mai A et al. Binding mode analysis of 3-(4-benzoyl-1-methyl-1H-2-pyrrolyl)-N-hydroxy-2-propenamide: a new synthetic histone deacetylase inhibitor inducing histone hyperacetylation, growth inhibition, and terminal cell differentiation. 2002 J. Med. Chem. pmid:11960489
Merezak C et al. Inhibition of histone deacetylases induces bovine leukemia virus expression in vitro and in vivo. 2002 J. Virol. pmid:11967319
Weston AD et al. Requirement for RAR-mediated gene repression in skeletal progenitor differentiation. 2002 J. Cell Biol. pmid:12105181
Toyooka S et al. Progressive aberrant methylation of the RASSF1A gene in simian virus 40 infected human mesothelial cells. 2002 Oncogene pmid:12082623
Choy JS and Kron SJ NuA4 subunit Yng2 function in intra-S-phase DNA damage response. 2002 Mol. Cell. Biol. pmid:12417725
Ghoshal K et al. Inhibitors of histone deacetylase and DNA methyltransferase synergistically activate the methylated metallothionein I promoter by activating the transcription factor MTF-1 and forming an open chromatin structure. 2002 Mol. Cell. Biol. pmid:12417732
Hauser C et al. Activation of the mouse histone deacetylase 1 gene by cooperative histone phosphorylation and acetylation. 2002 Mol. Cell. Biol. pmid:12391151
Westendorf JJ et al. Runx2 (Cbfa1, AML-3) interacts with histone deacetylase 6 and represses the p21(CIP1/WAF1) promoter. 2002 Mol. Cell. Biol. pmid:12391164