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
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
Supratentorial Neoplasms D015173 1 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Intervertebral Disc Degeneration D055959 1 associated lipids
Hypesthesia D006987 1 associated lipids
Cystadenocarcinoma, Mucinous D018282 1 associated lipids
Myopathy, Central Core D020512 1 associated lipids
Roseolovirus Infections D019349 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
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
Cystadenocarcinoma, Serous D018284 2 associated lipids
Fibromatosis, Aggressive D018222 2 associated lipids
Rhabdomyosarcoma, Alveolar D018232 2 associated lipids
Small Cell Lung Carcinoma D055752 2 associated lipids
Adenocarcinoma, Follicular D018263 3 associated lipids
Lymphoma, Follicular D008224 3 associated lipids
Hypereosinophilic Syndrome D017681 3 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
Porcine Reproductive and Respiratory Syndrome D019318 4 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
Myeloproliferative Disorders D009196 5 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Osteomalacia D010018 5 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Carcinoma, Pancreatic Ductal D021441 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
Amin HM et al. Histone deacetylase inhibitors induce caspase-dependent apoptosis and downregulation of daxx in acute promyelocytic leukaemia with t(15;17). 2001 Br. J. Haematol. pmid:11703323
Xu D et al. Switch from Myc/Max to Mad1/Max binding and decrease in histone acetylation at the telomerase reverse transcriptase promoter during differentiation of HL60 cells. 2001 Proc. Natl. Acad. Sci. U.S.A. pmid:11274400
Seth KA and Majzoub JA Repressor element silencing transcription factor/neuron-restrictive silencing factor (REST/NRSF) can act as an enhancer as well as a repressor of corticotropin-releasing hormone gene transcription. 2001 J. Biol. Chem. pmid:11278361
Taddei A et al. Reversible disruption of pericentric heterochromatin and centromere function by inhibiting deacetylases. 2001 Nat. Cell Biol. pmid:11175742
He LZ et al. Histone deacetylase inhibitors induce remission in transgenic models of therapy-resistant acute promyelocytic leukemia. 2001 J. Clin. Invest. pmid:11696577
Steinbac OC et al. Histone deacetylase activity is required for the induction of the MyoD muscle cell lineage in Xenopus. 2000 Sep-Oct Biol. Chem. pmid:11076034
Dressel U et al. Promoter specific sensitivity to inhibition of histone deacetylases: implications for hormonal gene control, cellular differentiation and cancer. 2000 Mar-Apr Anticancer Res. pmid:10810390
Avram D et al. Isolation of a novel family of C(2)H(2) zinc finger proteins implicated in transcriptional repression mediated by chicken ovalbumin upstream promoter transcription factor (COUP-TF) orphan nuclear receptors. 2000 J. Biol. Chem. pmid:10744719
Eickhoff B et al. Trichostatin A modulates expression of p21waf1/cip1, Bcl-xL, ID1, ID2, ID3, CRAB2, GATA-2, hsp86 and TFIID/TAFII31 mRNA in human lung adenocarcinoma cells. 2000 Biol. Chem. pmid:10746741
Lee SK et al. Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor. 2000 J. Biol. Chem. pmid:10777532
Zhang HS et al. Exit from G1 and S phase of the cell cycle is regulated by repressor complexes containing HDAC-Rb-hSWI/SNF and Rb-hSWI/SNF. 2000 Cell pmid:10778858
Fu M et al. p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. 2000 J. Biol. Chem. pmid:10779504
Wharton W et al. Inhibition of mitogenesis in Balb/c-3T3 cells by Trichostatin A. Multiple alterations in the induction and activation of cyclin-cyclin-dependent kinase complexes. 2000 J. Biol. Chem. pmid:10945992
Zhou Q et al. Rapid induction of histone hyperacetylation and cellular differentiation in human breast tumor cell lines following degradation of histone deacetylase-1. 2000 J. Biol. Chem. pmid:10938272
Xu RH et al. Histone acetylation is a checkpoint in FGF-stimulated mesoderm induction. 2000 Dev. Dyn. pmid:10906781
Gray SG et al. IGF-II and IL-2 act synergistically to alter HDAC1 expression following treatments with trichostatin a. 2000 Cytokine pmid:10880258
Su GH et al. A novel histone deacetylase inhibitor identified by high-throughput transcriptional screening of a compound library. 2000 Cancer Res. pmid:10866300
DiRenzo J et al. BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation. 2000 Mol. Cell. Biol. pmid:11003650
Kim YB et al. Mechanism of cell cycle arrest caused by histone deacetylase inhibitors in human carcinoma cells. 2000 J. Antibiot. pmid:11132966
Pender SL et al. Butyrate upregulates stromelysin-1 production by intestinal mesenchymal cells. 2000 Am. J. Physiol. Gastrointest. Liver Physiol. pmid:11052988