Trichostatin A (TSA) is an organic compound that serves as an antifungal antibiotic and selectively inhibits the class I and II mammalian histone deacetylase (HDAC) families of enzymes, but not class III HDACs (i.e., sirtuins).[1] However, there are recent reports of the interactions of this molecule with Sirt 6 protein.[2] TSA inhibits the eukaryoticcell cycle during the beginning of the growth stage. TSA can be used to alter gene expression by interfering with the removal of acetyl groups from histones (histone deacetylases, HDAC) and therefore altering the ability of DNAtranscription factors to access the DNA molecules inside chromatin. It is a member of a larger class of histone deacetylase inhibitors (HDIs or HDACIs) that have a broad spectrum of epigenetic activities. Thus, TSA has some potential as an anti-cancer drug.[3] One suggested mechanism is that TSA promotes the expression of apoptosis-related genes, leading to cancerous cells surviving at lower rates, thus slowing the progression of cancer.[4] Other mechanisms may include the activity of HDIs to induce cell differentiation, thus acting to "mature" some of the de-differentiated cells found in tumors. HDIs have multiple effects on non-histone effector molecules, so the anti-cancer mechanisms are truly not understood at this time.[5][6]
TSA inhibits HDACs 1, 3, 4, 6 and 10 with IC50 values around 20 nM.[7]
^Vanhaecke T, Papeleu P, Elaut G, Rogiers V (June 2004). "Trichostatin A-like hydroxamate histone deacetylase inhibitors as therapeutic agents: toxicological point of view". Current Medicinal Chemistry. 11 (12): 1629–1643. doi:10.2174/0929867043365099. PMID15180568.
^You W, Steegborn C (December 2018). "Structural Basis of Sirtuin 6 Inhibition by the Hydroxamate Trichostatin A: Implications for Protein Deacylase Drug Development". Journal of Medicinal Chemistry. 61 (23): 10922–10928. doi:10.1021/acs.jmedchem.8b01455. PMID30395713.
^Drummond DC, Noble CO, Kirpotin DB, Guo Z, Scott GK, Benz CC (2005). "Clinical development of histone deacetylase inhibitors as anticancer agents". Annual Review of Pharmacology and Toxicology. 45: 495–528. doi:10.1146/annurev.pharmtox.45.120403.095825. PMID15822187.
^Shankar S, Srivastava RK (2008). "Histone Deacetylase Inhibitors: Mechanisms and Clinical Significance in Cancer: HDAC Inhibitor-Induced Apoptosis". Programmed Cell Death in Cancer Progression and Therapy. Advances in Experimental Medicine and Biology. Vol. 615. pp. 261–98. doi:10.1007/978-1-4020-6554-5_13. ISBN978-1-4020-6553-8. PMID18437899.
^Movafagh S, Munson A (January 2019). "Chapter 4 - Histone Deacetylase Inhibitors in Cancer Prevention and Therapy". In Bishayee A, Bhatia D (eds.). Epigenetics of Cancer Prevention. Translational Epigenetics. Vol. 8. Academic Press. pp. 75–105. doi:10.1016/b978-0-12-812494-9.00004-4. ISBN978-0-12-812494-9.
^US 8232297, Maier T, Beckers T, Hummel RP, Feth M, Muller M, Bar T, Volz J, "Novel Sulphonylpyrroles as Inhibitors of Hdac S Novel Sulphonylpyrroles", issued 31 July 2012, assigned to 4SC AG