Small-molecule-based inhibition of histone demethylation in cells assessed by quantitative mass spectrometry.

ABSTRACT: Post-translational modifications on histones are an important mechanism for the regulation of gene expression and are involved in all aspects of cell growth and differentiation, as well as pathological processes including neurodegeneration, autoimmunity, and cancer. A major challenge within the chromatin field is to develop methods for the quantitative analysis of histone modifications. Here we report a mass spectrometry (MS) approach based on ultraperformance liquid chromatography high/low collision switching (UPLC-MS(E)) to monitor histone modifications in cells. This approach is exemplified by the analysis of trimethylated lysine-9 levels in histone H3, following a simple chemical derivatization procedure with d(6)-acetic anhydride. This method was used to study the inhibition of histon

SUBMITTER: Mackeen MM 

PROVIDER: S-EPMC4681095 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature