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
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
Rhabdoid Tumor D018335 1 associated lipids
Visceral Pain D059265 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
Cystadenoma, Serous D018293 1 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Intervertebral Disc Degeneration D055959 1 associated lipids
Supratentorial Neoplasms D015173 1 associated lipids
Hypesthesia D006987 1 associated lipids
Cystadenocarcinoma, Mucinous D018282 1 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
Inflammatory Breast Neoplasms D058922 2 associated lipids
Ganglioneuroma D005729 2 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
Lymphoma, Large-Cell, Anaplastic D017728 3 associated lipids
Retinal Neoplasms D019572 3 associated lipids
Progeria D011371 3 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
Cicatrix, Hypertrophic D017439 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
Chiocca S et al. Histone deacetylase 1 inactivation by an adenovirus early gene product. 2002 Curr. Biol. pmid:11937030
Milutinovic S et al. Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification. 2002 J. Biol. Chem. pmid:11929879
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
Sawa H et al. Histone deacetylase inhibitors such as sodium butyrate and trichostatin A induce apoptosis through an increase of the bcl-2-related protein Bad. 2001 Brain Tumor Pathol pmid:11908866
Heltweg B and Jung M A microplate reader-based nonisotopic histone deacetylase activity assay. 2002 Anal. Biochem. pmid:11878795
Taniura S et al. Transcriptional regulation of cyclooxygenase-1 by histone deacetylase inhibitors in normal human astrocyte cells. 2002 J. Biol. Chem. pmid:11877441
Murphy JC et al. Control of cytomegalovirus lytic gene expression by histone acetylation. 2002 EMBO J. pmid:11867539
Drewell RA et al. Methylation-dependent silencing at the H19 imprinting control region by MeCP2. 2002 Nucleic Acids Res. pmid:11861904
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
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
Valapour M et al. Histone deacetylation inhibits IL4 gene expression in T cells. 2002 J. Allergy Clin. Immunol. pmid:11842291
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
Kiefer SM et al. Murine Sall1 represses transcription by recruiting a histone deacetylase complex. 2002 J. Biol. Chem. pmid:11836251
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
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
Herold C et al. The histone-deacetylase inhibitor Trichostatin A blocks proliferation and triggers apoptotic programs in hepatoma cells. 2002 J. Hepatol. pmid:11830335
Handumrongkul C et al. Distinct sets of cellular genes control the expression of transfected, nuclear-localized genes. 2002 Mol. Ther. pmid:11829526
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
Deroanne CF et al. Histone deacetylases inhibitors as anti-angiogenic agents altering vascular endothelial growth factor signaling. 2002 Oncogene pmid:11821955
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