TMP269 cas 1314890-29-3

TMP269 has no impact on the mitochondrial activity and/or the viability of human CD4+ T cells at 10 μM, and may be used as tools to identify the endogenous substrates of the class IIa HDAC enzymes. In IEC-18 intestinal epithelial cells, TMP269 prevents cell cycle progression, DNA synthesis, and proliferation induced in response to G protein-coupled receptor/PKD1 activation. As with HDAC4 knockdown, TMP269 significantly enhances cytotoxicity induced by CFZ in MM cell lines, upregulating ATF4 and CHOP and inducing apoptosis. TMP269 does not hyperacetylate histone H3K9 or α-tubulin in MM cell lines, confirming that it has no inhibitory effects on class I or IIb HDACs. In a dosedependent manner, TPM269-induced cytotoxicity is associated with cleavage of caspase-8, -9, -3 and PARP, consistent with apoptosis.

Related Prodcuts:

Etoposide; Etoposide phosphate; ML-323; BMH-21; Nexturastat A; GSK2606414; ELR510444; Chidamide; Inauhzin; CW069; Purvalanol A; Purvalanol B; JW55; Tenovin-6; Tenovin-6 HCL; RKI-1447; AZD2461; Tasquinimod

[1]. Lobera M, et al. Selective class IIa histone deacetylase inhibition via a nonchelating zinc-binding group. Nat Chem Biol. 2013 May;9(5):319-25.

[2]. Sinnett-Smith J, et al. Protein kinase D1 mediates class IIa histone deacetylase phosphorylation and nuclear extrusion in intestinal epithelial cells: role in mitogenic signaling. Am J Physiol Cell Physiol. 2014 May 15;306(10):C961-71.