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

Research output: Contribution to journalArticlepeer-review

Abstract

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 PXD002669.

Original languageEnglish
Pages (from-to)188-194
Number of pages7
JournalData in Brief
Volume7
DOIs
Publication statusPublished - Jun 1 2016

Keywords

  • Biomarker
  • Breast cancer
  • Epigenetics
  • Formalin-fixed paraffin embedded tissues
  • Histone posttranslational modifications
  • Mass spectrometry
  • Proteomics

ASJC Scopus subject areas

  • General
  • Education

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