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
Cystadenoma, Serous D018293 1 associated lipids
Intervertebral Disc Degeneration D055959 1 associated lipids
Supratentorial Neoplasms D015173 1 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Hypesthesia D006987 1 associated lipids
Cystadenocarcinoma, Mucinous D018282 1 associated lipids
Roseolovirus Infections D019349 1 associated lipids
Myopathy, Central Core D020512 1 associated lipids
Thyroid Hormone Resistance Syndrome D018382 1 associated lipids
Chromosome Inversion D007446 1 associated lipids
Rhabdomyosarcoma, Embryonal D018233 1 associated lipids
Carcinoma, Papillary, Follicular D018265 1 associated lipids
Gestational Trophoblastic Disease D031901 1 associated lipids
Visceral Pain D059265 1 associated lipids
Rhabdoid Tumor D018335 1 associated lipids
Lupus Vulgaris D008177 1 associated lipids
Rubinstein-Taybi Syndrome D012415 1 associated lipids
Classical Lissencephalies and Subcortical Band Heterotopias D054221 1 associated lipids
Goldenhar Syndrome D006053 1 associated lipids
Adenomyosis D062788 1 associated lipids
Capsule Opacification D058442 1 associated lipids
Neoplasm Micrometastasis D061206 1 associated lipids
Inflammatory Breast Neoplasms D058922 2 associated lipids
Ganglioneuroma D005729 2 associated lipids
Cystadenocarcinoma, Serous D018284 2 associated lipids
Fibromatosis, Aggressive D018222 2 associated lipids
Small Cell Lung Carcinoma D055752 2 associated lipids
Rhabdomyosarcoma, Alveolar D018232 2 associated lipids
Bone Marrow Neoplasms D019046 2 associated lipids
Adenocarcinoma, Papillary D000231 2 associated lipids
Lymphoma, Large-Cell, Anaplastic D017728 3 associated lipids
Retinal Neoplasms D019572 3 associated lipids
Progeria D011371 3 associated lipids
Mastocytoma D034801 3 associated lipids
Uveal Neoplasms D014604 3 associated lipids
Leukemia, Promyelocytic, Acute D015473 3 associated lipids
Conjunctival Neoplasms D003230 3 associated lipids
Adenocarcinoma, Follicular D018263 3 associated lipids
Hypereosinophilic Syndrome D017681 3 associated lipids
Lymphoma, Follicular D008224 3 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Spinocerebellar Ataxias D020754 4 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Neuroendocrine Tumors D018358 4 associated lipids
Porcine Reproductive and Respiratory Syndrome D019318 4 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Osteomalacia D010018 5 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Primary Myelofibrosis D055728 6 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
Inoue H et al. Histone deacetylase inhibitors sensitize human colonic adenocarcinoma cell lines to TNF-related apoptosis inducing ligand-mediated apoptosis. 2002 Int. J. Mol. Med. pmid:11956660
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
Suzuki-Mizushima Y et al. Enhancement of NGF- and cholera toxin-induced neurite outgrowth by butyrate in PC12 cells. 2002 Brain Res. pmid:12270499
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
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
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
Guo Y et al. Regulation of DNA methylation in human breast cancer. Effect on the urokinase-type plasminogen activator gene production and tumor invasion. 2002 J. Biol. Chem. pmid:12198113
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
Maehara K et al. Effects of histone acetylation on transcriptional regulation of manganese superoxide dismutase gene. 2002 Biochem. Biophys. Res. Commun. pmid:12083788
Iezzi S et al. Stage-specific modulation of skeletal myogenesis by inhibitors of nuclear deacetylases. 2002 Proc. Natl. Acad. Sci. U.S.A. pmid:12032356
Scott GK et al. Transcriptional repression of ErbB2 by histone deacetylase inhibitors detected by a genomically integrated ErbB2 promoter-reporting cell screen. 2002 Mol. Cancer Ther. pmid:12477051
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
Hoshimoto A et al. Caprylic acid and medium-chain triglycerides inhibit IL-8 gene transcription in Caco-2 cells: comparison with the potent histone deacetylase inhibitor trichostatin A. 2002 Br. J. Pharmacol. pmid:12010777