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
Gurova KV et al. Expression of prostate specific antigen (PSA) is negatively regulated by p53. 2002 Oncogene pmid:11791186
Suenaga M et al. Histone deacetylase inhibitors suppress telomerase reverse transcriptase mRNA expression in prostate cancer cells. 2002 Int. J. Cancer pmid:11807787
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
Maeda Y et al. Repression of hepatocyte nuclear factor 4alpha tumor suppressor p53: involvement of the ligand-binding domain and histone deacetylase activity. 2002 Mol. Endocrinol. pmid:11818510
Gregory RI et al. Inhibition of histone deacetylases alters allelic chromatin conformation at the imprinted U2af1-rs1 locus in mouse embryonic stem cells. 2002 J. Biol. Chem. pmid:11821379
Lim Y et al. Trichostatin A-induced detransformation correlates with decreased focal adhesion kinase phosphorylation at tyrosine 861 in ras-transformed fibroblasts. 2002 J. Biol. Chem. pmid:11821402
Wilson MA et al. The histone deacetylase inhibitor trichostatin A blocks progesterone receptor-mediated transactivation of the mouse mammary tumor virus promoter in vivo. 2002 J. Biol. Chem. pmid:11821430
Deroanne CF et al. Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. 2002 Oncogene pmid:11821955
Sourlingas TG et al. Histone deacetylase inhibitors induce apoptosis in peripheral blood lymphocytes along with histone H4 acetylation and the expression of the linker histone variant, H1 degrees. 2001 Eur. J. Cell Biol. pmid:11824792
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
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
Remiszewski SW et al. Inhibitors of human histone deacetylase: synthesis and enzyme and cellular activity of straight chain hydroxamates. 2002 J. Med. Chem. pmid:11831887
Kiefer SM et al. Murine Sall1 represses transcription by recruiting a histone deacetylase complex. 2002 J. Biol. Chem. pmid:11836251
Roddie PH et al. Primary acute myeloid leukaemia blasts resistant to cytokine-induced differentiation to dendritic-like leukaemia cells can be forced to differentiate by the addition of bryostatin-1. 2002 Leukemia pmid:11840267
Valapour M et al. Histone deacetylation inhibits IL4 gene expression in T cells. 2002 J. Allergy Clin. Immunol. pmid:11842291
McBurney MW et al. Evidence for repeat-induced gene silencing in cultured Mammalian cells: inactivation of tandem repeats of transfected genes. 2002 Exp. Cell Res. pmid:11855851
Hou M et al. The histone deacetylase inhibitor trichostatin A derepresses the telomerase reverse transcriptase (hTERT) gene in human cells. 2002 Exp. Cell Res. pmid:11855854
Drewell RA et al. Methylation-dependent silencing at the H19 imprinting control region by MeCP2. 2002 Nucleic Acids Res. pmid:11861904
Murphy JC et al. Control of cytomegalovirus lytic gene expression by histone acetylation. 2002 EMBO J. pmid:11867539