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
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
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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.

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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?

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
Huang X et al. Nitric oxide (NO), methylation and TIMP-1 expression in BL6 melanoma cells transfected with MHC class I genes. 2000 Clin. Exp. Metastasis pmid:11448064
Chang LK and Liu ST Activation of the BRLF1 promoter and lytic cycle of Epstein-Barr virus by histone acetylation. 2000 Nucleic Acids Res. pmid:11024171
Suzuki T et al. Effect of trichostatin A on cell growth and expression of cell cycle- and apoptosis-related molecules in human gastric and oral carcinoma cell lines. 2000 Int. J. Cancer pmid:11093826
Sutcliffe JE et al. Retinoblastoma protein disrupts interactions required for RNA polymerase III transcription. 2000 Mol. Cell. Biol. pmid:11094071
Yu J et al. Transcriptional repression by blimp-1 (PRDI-BF1) involves recruitment of histone deacetylase. 2000 Mol. Cell. Biol. pmid:10713181
Adachi N et al. Cell-cycle regulation of the DNA topoisomerase IIalpha promoter is mediated by proximal CCAAT boxes: possible involvement of acetylation. 2000 Gene pmid:10713444
Stöckel B et al. Characterization of the 5'-flanking region of the human multidrug resistance protein 2 (MRP2) gene and its regulation in comparison withthe multidrug resistance protein 3 (MRP3) gene. 2000 Eur. J. Biochem. pmid:10691972
Imai S et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. 2000 Nature pmid:10693811
Sirchia SM et al. Evidence of epigenetic changes affecting the chromatin state of the retinoic acid receptor beta2 promoter in breast cancer cells. 2000 Oncogene pmid:10734315
Kim YB et al. Mechanism of cell cycle arrest caused by histone deacetylase inhibitors in human carcinoma cells. 2000 J. Antibiot. pmid:11132966
Fukuda K Apoptosis-associated cleavage of beta-catenin in human colon cancer and rat hepatoma cells. 1999 Mar-Apr Int. J. Biochem. Cell Biol. pmid:10224675
Schmidt K et al. Inhibitors of histone deacetylase suppress the growth of MCF-7 breast cancer cells. 1999 Arch. Pharm. (Weinheim) pmid:10575368
Jung M et al. Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. 1999 J. Med. Chem. pmid:10579829
Chien PY et al. A fusion protein of the estrogen receptor (ER) and nuclear receptor corepressor (NCoR) strongly inhibits estrogen-dependent responses in breast cancer cells. 1999 Mol. Endocrinol. pmid:10598586
Taddei A et al. Duplication and maintenance of heterochromatin domains. 1999 J. Cell Biol. pmid:10601331
Gray SG et al. IGF-II enhances trichostatin A-induced TGFbeta1 and p21(Waf1,Cip1, sdi1) expression in Hep3B cells. 1999 Exp. Cell Res. pmid:10585285
Gobl AE et al. Menin represses JunD-activated transcription by a histone deacetylase-dependent mechanism. 1999 Biochim. Biophys. Acta pmid:10500243
Kosugi H et al. Histone deacetylase inhibitors are the potent inducer/enhancer of differentiation in acute myeloid leukemia: a new approach to anti-leukemia therapy. 1999 Leukemia pmid:10482980
Carmen AA et al. Yeast HOS3 forms a novel trichostatin A-insensitive homodimer with intrinsic histone deacetylase activity. 1999 Proc. Natl. Acad. Sci. U.S.A. pmid:10535926
Rüller S et al. Sensitization of tumor cells to ribotoxic stress-induced apoptotic cell death: a new therapeutic strategy. 1999 Clin. Cancer Res. pmid:10537334