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
Abnormalities, Multiple D000015 13 associated lipids
Adenocarcinoma D000230 166 associated lipids
Adenocarcinoma, Papillary D000231 2 associated lipids
Adrenoleukodystrophy D000326 29 associated lipids
Alzheimer Disease D000544 76 associated lipids
Arthritis, Experimental D001169 24 associated lipids
Asthma D001249 52 associated lipids
Autoimmune Diseases D001327 27 associated lipids
Biliary Tract Neoplasms D001661 7 associated lipids
Body Weight D001835 333 associated lipids
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
Conjunctival Neoplasms D003230 3 associated lipids
Coronary Artery Disease D003324 47 associated lipids
Cystic Fibrosis D003550 65 associated lipids
Cytomegalovirus Infections D003586 7 associated lipids
Diabetes Mellitus, Experimental D003921 85 associated lipids
Encephalomyelitis, Autoimmune, Experimental D004681 26 associated lipids
Endometriosis D004715 29 associated lipids
Enteritis D004751 8 associated lipids
Leukemia, Erythroblastic, Acute D004915 41 associated lipids
Fetal Growth Retardation D005317 9 associated lipids
Fibrosis D005355 23 associated lipids
Fragile X Syndrome D005600 5 associated lipids
Ganglioneuroma D005729 2 associated lipids
Glioblastoma D005909 27 associated lipids
Glioma D005910 112 associated lipids
Goldenhar Syndrome D006053 1 associated lipids
Cardiomegaly D006332 31 associated lipids
Carcinoma, Hepatocellular D006528 140 associated lipids
von Hippel-Lindau Disease D006623 1 associated lipids
Hypersensitivity D006967 22 associated lipids
Hypertension D006973 115 associated lipids
Hypertension, Pulmonary D006976 32 associated lipids
Hypesthesia D006987 1 associated lipids
Immunologic Deficiency Syndromes D007153 8 associated lipids
Inflammation D007249 119 associated lipids
Chromosome Inversion D007446 1 associated lipids
Keloid D007627 12 associated lipids
Leishmaniasis D007896 19 associated lipids
Leukemia D007938 74 associated lipids
Leukemia, Myeloid D007951 52 associated lipids
Liver Cirrhosis D008103 67 associated lipids
Lung Neoplasms D008175 171 associated lipids
Lupus Vulgaris D008177 1 associated lipids
Lupus Erythematosus, Systemic D008180 43 associated lipids
Lymphatic Metastasis D008207 10 associated lipids
Lymphoma, Follicular D008224 3 associated lipids
Mammary Neoplasms, Experimental D008325 67 associated lipids
Medulloblastoma D008527 22 associated lipids
Melanoma D008545 69 associated lipids
Intellectual Disability D008607 13 associated lipids
Muscular Dystrophies D009136 10 associated lipids
Myeloproliferative Disorders D009196 5 associated lipids
Opioid-Related Disorders D009293 5 associated lipids
Nasal Polyps D009298 26 associated lipids
Nasopharyngeal Neoplasms D009303 4 associated lipids
Neoplasms D009369 13 associated lipids
Neoplasms, Hormone-Dependent D009376 23 associated lipids
Neovascularization, Pathologic D009389 39 associated lipids
Nerve Degeneration D009410 53 associated lipids
Neuroblastoma D009447 66 associated lipids
Osteomalacia D010018 5 associated lipids
Pancreatic Neoplasms D010190 77 associated lipids
Progeria D011371 3 associated lipids
Prostatic Hyperplasia D011470 20 associated lipids
Prostatic Neoplasms D011471 126 associated lipids
Pulmonary Fibrosis D011658 24 associated lipids
Radiation Injuries D011832 14 associated lipids
Retinoblastoma D012175 12 associated lipids
Rubinstein-Taybi Syndrome D012415 1 associated lipids
Mast-Cell Sarcoma D012515 9 associated lipids
Osteosarcoma D012516 50 associated lipids
Thyroid Neoplasms D013964 33 associated lipids
Tongue Neoplasms D014062 15 associated lipids
Translocation, Genetic D014178 20 associated lipids
Ureteral Obstruction D014517 10 associated lipids
Uterine Neoplasms D014594 18 associated lipids
Uveal Neoplasms D014604 3 associated lipids
Supratentorial Neoplasms D015173 1 associated lipids
Reperfusion Injury D015427 65 associated lipids
Leukemia, Lymphocytic, Chronic, B-Cell D015451 25 associated lipids
Leukemia, T-Cell D015458 23 associated lipids
Leukemia-Lymphoma, Adult T-Cell D015459 25 associated lipids
Leukemia, Myeloid, Acute D015470 19 associated lipids
Leukemia, Promyelocytic, Acute D015473 3 associated lipids
Leukemia, Myelomonocytic, Acute D015479 6 associated lipids
Endometrial Neoplasms D016889 30 associated lipids
Polycystic Kidney, Autosomal Dominant D016891 6 associated lipids
Cicatrix, Hypertrophic D017439 4 associated lipids
Dermatitis, Allergic Contact D017449 20 associated lipids
Hypereosinophilic Syndrome D017681 3 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

Download all related citations
Per page 10 20 50 100 | Total 3126
Authors Title Published Journal PubMed Link
Ashburner BP et al. The p65 (RelA) subunit of NF-kappaB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. 2001 Mol. Cell. Biol. pmid:11564889
Sachs LM et al. Involvement of histone deacetylase at two distinct steps in gene regulation during intestinal development in Xenopus laevis. 2001 Dev. Dyn. pmid:11668605
Amann JM et al. ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain. 2001 Mol. Cell. Biol. pmid:11533236
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
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
Hatama S et al. Reactivation of feline foamy virus from a chronically infected feline renal cell line by trichostatin A. 2001 Virology pmid:11336556
Viollet B et al. Embryonic but not postnatal reexpression of hepatocyte nuclear factor 1alpha (HNF1alpha) can reactivate the silent phenylalanine hydroxylase gene in HNF1alpha-deficient hepatocytes. 2001 Mol. Cell. Biol. pmid:11340160
Nakamura M et al. Reduction of telomerase activity in human liver cancer cells by a histone deacetylase inhibitor. 2001 J. Cell. Physiol. pmid:11319763
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
Matsuda E et al. Targeting of Krüppel-associated box-containing zinc finger proteins to centromeric heterochromatin. Implication for the gene silencing mechanisms. 2001 J. Biol. Chem. pmid:11278721
Yang H et al. Role of promoter methylation in increased methionine adenosyltransferase 2A expression in human liver cancer. 2001 Am. J. Physiol. Gastrointest. Liver Physiol. pmid:11208539
Chen C et al. Evidence that silencing of the HPRT promoter by DNA methylation is mediated by critical CpG sites. 2001 J. Biol. Chem. pmid:11013250
Ullerås E et al. Inhibition of histone deacetylase activity causes cell type-specific induction of the PDGF-B promoter only in the absence of activation by its enhancer. 2001 Exp. Cell Res. pmid:11640883
Meier JL Reactivation of the human cytomegalovirus major immediate-early regulatory region and viral replication in embryonal NTera2 cells: role of trichostatin A, retinoic acid, and deletion of the 21-base-pair repeats and modulator. 2001 J. Virol. pmid:11160656
Kuusisto E et al. Ubiquitin-binding protein p62 expression is induced during apoptosis and proteasomal inhibition in neuronal cells. 2001 Biochem. Biophys. Res. Commun. pmid:11162503
Grandjean V et al. Relationship between DNA methylation, histone H4 acetylation and gene expression in the mouse imprinted Igf2-H19 domain. 2001 FEBS Lett. pmid:11163765
Lizcano F et al. Cell type-specific roles of histone deacetylase in TR ligand-independent transcriptional repression. 2001 Mol. Cell. Endocrinol. pmid:11165035
Nervi C et al. Inhibition of histone deacetylase activity by trichostatin A modulates gene expression during mouse embryogenesis without apparent toxicity. 2001 Cancer Res. pmid:11245412
Zhu WG et al. DNA methyltransferase inhibition enhances apoptosis induced by histone deacetylase inhibitors. 2001 Cancer Res. pmid:11245429