Peptide mass mapping of acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with histone deacetylase (HDACs) inhibitors

J Am Soc Mass Spectrom. 2005 Oct;16(10):1641-53. doi: 10.1016/j.jasms.2005.06.001.

Abstract

The acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with HDAC inhibitors trichostatin A (TSA) and depsipeptide (DDP) were separated by acetic acid urea-polyacrylamide gel electrophoresis (AU-PAGE), in-gel digested, and analyzed by matrix assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and liquid chromatography tandem mass spectrometry (LC-MS/MS). The acetylation pattern of histone H4 in mouse lymphosarcoma cells induced by TSA was established in which acetylation initially occurred at K16 followed by K12 and then K8 and/or K5. An identical order of acetylation was found for cells treated with DDP.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Amino Acid Sequence
  • Animals
  • Antineoplastic Agents / administration & dosage
  • Cell Line, Tumor
  • Depsipeptides / administration & dosage*
  • Histone Deacetylase Inhibitors*
  • Histones / chemistry
  • Histones / metabolism*
  • Hydroxamic Acids / administration & dosage*
  • Lymphoma, Non-Hodgkin / drug therapy*
  • Lymphoma, Non-Hodgkin / metabolism*
  • Mice
  • Molecular Sequence Data
  • Peptide Mapping / methods*
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism

Substances

  • Antineoplastic Agents
  • Depsipeptides
  • Histone Deacetylase Inhibitors
  • Histones
  • Hydroxamic Acids
  • Protein Isoforms
  • trichostatin A