MassIVE MSV000093608

Partial Public PXD047659

Decrypting lysine deacetylase inhibitor action and protein modifications by dose-resolved proteomics

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Description

Lysine deacetylase inhibitors (KDACis) are approved for cutaneous T-cell lymphoma (CTCL) and multiple myeloma. Nevertheless, their mechanisms of action (MoA) remain elusive. To characterize the MoA of these drugs in more detail, we systematically measured dose-dependent changes in protein expression, acetylation, and phosphorylation in response to 21 clinical and pre-clinical KDACis. MV4-11 cells were treated for 6 h with vehicle control and 10 increasing doses of the respective drug (from 100 pM to 30 mM). PTM-carrying and unmodified peptides were analyzed separately by liquid chromatography tandem mass spectrometry (LC-MS/MS) for peptide and protein identification and quantification. Furthermore, time-dependent experiments were carried out for Vorinostat and Panobinostat at their respective pEC50 concentrations from the cell viability data. In an independent experiment, the subcellular proteomes of Panobinostat-treated cells were measured. [doi:10.25345/C51Z4242K] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: HDACs ; Lysine deacetylase inhibitors ; Acetylome ; Phosphoproteome ; Proteomic pharmacology ; Chemical proteomics ; Dose-dependent response

Contact

Principal Investigators:
(in alphabetical order) 		Bernhard Kuster, Chair of Proteomics and Bioanalytics, Technical University of Munich, Germany
Submitting User: ychang123
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