Mass-spectrometry analysis of histone post-translational modifications in pathology tissue using the PAT-H-MS approach

• Main Authors: Roberta Noberini, Giancarlo Pruneri, Saverio Minucci, Tiziana Bonaldi
• Format: Article
• Language: English
• Published: Elsevier 2016-06-01
• Series: Data in Brief
• Online Access: http://www.sciencedirect.com/science/article/pii/S2352340916300506

Aberrant histone post-translational modifications (hPTMs) have been implicated with various pathologies, including cancer, and may represent useful epigenetic biomarkers. The data described here provide a mass spectrometry-based quantitative analysis of hPTMs from formalin-fixed paraffin-embedded (FFPE) tissues, from which histones were extracted through the recently developed PAT-H-MS method. First, we analyzed FFPE samples from mouse spleen and liver or human breast cancer up to six years old, together with their corresponding fresh frozen tissue. We then combined the PAT-H-MS approach with a histone-focused version of the super-SILAC strategy-using a mix of histones from four breast cancer cell lines as a spike-in standard- to accurately quantify hPTMs from breast cancer specimens belonging to different subtypes. The data, which are associated with a recent publication (Pathology tissue-quantitative mass spectrometry analysis to profile histone post-translational modification patterns in patient samples (Noberini, 2015) [1]), are deposited at the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier http://www.ebi.ac.uk/pride/archive/projects/PXD002669. Keywords: Mass spectrometry, Proteomics, Epigenetics, Histone posttranslational modifications, Formalin-fixed paraffin embedded tissues, Biomarker, Breast cancer