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
Hypertension, Pulmonary D006976 32 associated lipids
Endometriosis D004715 29 associated lipids
Uterine Neoplasms D014594 18 associated lipids
Adrenoleukodystrophy D000326 29 associated lipids
Prostatic Hyperplasia D011470 20 associated lipids
Alzheimer Disease D000544 76 associated lipids
Thyroid Neoplasms D013964 33 associated lipids
Leukemia D007938 74 associated lipids
Neuroblastoma D009447 66 associated lipids
Carcinoma, Hepatocellular D006528 140 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?

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?


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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
Nielsen AL et al. Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. 1999 EMBO J. pmid:10562550
Habeck M Gelsolin: a new marker for breast cancer? 1999 Mol Med Today pmid:10562712
O'Neill LP et al. A developmental switch in H4 acetylation upstream of Xist plays a role in X chromosome inactivation. 1999 EMBO J. pmid:10329635
Strouboulis J et al. Transcriptional repression by XPc1, a new Polycomb homolog in Xenopus laevis embryos, is independent of histone deacetylase. 1999 Mol. Cell. Biol. pmid:10330136
Verdel A and Khochbin S Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers. 1999 J. Biol. Chem. pmid:9891014
Coffee B et al. Acetylated histones are associated with FMR1 in normal but not fragile X-syndrome cells. 1999 Nat. Genet. pmid:10319871
Xiao H et al. Both Sp1 and Sp3 are responsible for p21waf1 promoter activity induced by histone deacetylase inhibitor in NIH3T3 cells. 1999 J. Cell. Biochem. pmid:10321829
Mielnicki LM et al. Epigenetic regulation of gelsolin expression in human breast cancer cells. 1999 Exp. Cell Res. pmid:10328963
Krajewski WA Effect of in vivo histone hyperacetylation on the state of chromatin fibers. 1999 J. Biomol. Struct. Dyn. pmid:10333179
Yoshida M [Discovery of cell cycle inhibitors and their application to molecular biology]. 1999 Jpn J Antibiot pmid:10221182
Feng YQ et al. Enhancer-dependent transcriptional oscillations in mouse erythroleukemia cells. 1999 Mol. Cell. Biol. pmid:10373540
Böger H and Gruss P Functional determinants for the tetracycline-dependent transactivator tTA in transgenic mouse embryos. 1999 Mech. Dev. pmid:10381574
Finnin MS et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. 1999 Nature pmid:10490031
Huang Y et al. Transcriptional repression by REST: recruitment of Sin3A and histone deacetylase to neuronal genes. 1999 Nat. Neurosci. pmid:10491605
List HJ et al. Inhibition of histone deacetylation augments dihydrotestosterone induction of androgen receptor levels: an explanation for trichostatin A effects on androgen-induced chromatin remodeling and transcription of the mouse mammary tumor virus promoter. 1999 Exp. Cell Res. pmid:10527637
Bordonaro M et al. Butyrate-induced apoptotic cascade in colonic carcinoma cells: modulation of the beta-catenin-Tcf pathway and concordance with effects of sulindac and trichostatin A but not curcumin. 1999 Cell Growth Differ. pmid:10547075
KraevskiÄ­ VA and Prasolov VS [Comparative analysis of higher levels of organization of normal and hyperacetylated chromatin]. 1999 Dokl. Akad. Nauk. pmid:10439916
Zabel MD et al. Lymphoid transcription of the murine CD21 gene is positively regulated by histone acetylation. 1999 J. Immunol. pmid:10453011
Bernhard D et al. Interaction between dexamethasone and butyrate in apoptosis induction: non-additive in thymocytes and synergistic in a T cell-derived leukemia cell line. 1999 Cell Death Differ. pmid:10453071
Liu Z et al. Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and receptor-dependent cell-free transcription of chromatin. 1999 Proc. Natl. Acad. Sci. U.S.A. pmid:10449719