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
Rubinstein-Taybi Syndrome D012415 1 associated lipids
Goldenhar Syndrome D006053 1 associated lipids
Classical Lissencephalies and Subcortical Band Heterotopias D054221 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
Supratentorial Neoplasms D015173 1 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Intervertebral Disc Degeneration D055959 1 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
Chen T et al. Histone acetylation is involved in hsp70 gene transcription regulation in Drosophila melanogaster. 2002 Arch. Biochem. Biophys. pmid:12464268
Rombouts K et al. Actin filament formation, reorganization and migration are impaired in hepatic stellate cells under influence of trichostatin A, a histone deacetylase inhibitor. 2002 J. Hepatol. pmid:12445420
Guo WH et al. Inhibition of growth of mouse gastric cancer cells by Runx3, a novel tumor suppressor. 2002 Oncogene pmid:12447699
Marin-Husstege M et al. Histone deacetylase activity is necessary for oligodendrocyte lineage progression. 2002 J. Neurosci. pmid:12451133
Taniura S et al. Transcriptional regulation of cyclooxygenase-1 by histone deacetylase inhibitors in normal human astrocyte cells. 2002 J. Biol. Chem. pmid:11877441
Heltweg B and Jung M A microplate reader-based nonisotopic histone deacetylase activity assay. 2002 Anal. Biochem. pmid:11878795
Kamitani H et al. Histone acetylation may suppress human glioma cell proliferation when p21 WAF/Cip1 and gelsolin are induced. 2002 Neuro-oncology pmid:11916500
Kishikawa S et al. Roles of histone acetylation in the Dnmt1 gene expression. 2002 Nucleic Acids Res. Suppl. pmid:12903179
Zschocke J et al. Estrogen receptor alpha-mediated silencing of caveolin gene expression in neuronal cells. 2002 J. Biol. Chem. pmid:12138116
Yu Z et al. Histone deacetylases augment cytokine induction of the iNOS gene. 2002 J. Am. Soc. Nephrol. pmid:12138131
Li J et al. Involvement of histone methylation and phosphorylation in regulation of transcription by thyroid hormone receptor. 2002 Mol. Cell. Biol. pmid:12138181
Aapola U et al. Imprinting regulator DNMT3L is a transcriptional repressor associated with histone deacetylase activity. 2002 Nucleic Acids Res. pmid:12177302
Ito K et al. A molecular mechanism of action of theophylline: Induction of histone deacetylase activity to decrease inflammatory gene expression. 2002 Proc. Natl. Acad. Sci. U.S.A. pmid:12070353
Katula KS et al. Cell cycle specific changes in the human cyclin B1 gene regulatory region as revealed by response to trichostatin A. 2002 Arch. Biochem. Biophys. pmid:12054478
Wang XQ et al. Histone deacetylase inhibition results in decreased macrophage CD9 expression. 2002 Biochem. Biophys. Res. Commun. pmid:12056820
Rahmani M et al. The histone deacetylase inhibitor sodium butyrate interacts synergistically with phorbol myristate acetate (PMA) to induce mitochondrial damage and apoptosis in human myeloid leukemia cells through a tumor necrosis factor-alpha-mediated process. 2002 Exp. Cell Res. pmid:12061815
Woo SH et al. Structurally simple trichostatin A-like straight chain hydroxamates as potent histone deacetylase inhibitors. 2002 J. Med. Chem. pmid:12061890
Im H et al. Histone deacetylase-dependent establishment and maintenance of broad low-level histone acetylation within a tissue-specific chromatin domain. 2002 Biochemistry pmid:12484752
Gong XQ and Li L Dermo-1, a multifunctional basic helix-loop-helix protein, represses MyoD transactivation via the HLH domain, MEF2 interaction, and chromatin deacetylation. 2002 J. Biol. Chem. pmid:11809751
Rössig L et al. Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis. 2002 Circ. Res. pmid:12411399