Literature DB >> 16099169

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

Chen Ren1, Liwen Zhang, Michael A Freitas, Kalpana Ghoshal, Mark R Parthun, Samson T Jacob.   

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.

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Year:  2005        PMID: 16099169      PMCID: PMC2749475          DOI: 10.1016/j.jasms.2005.06.001

Source DB:  PubMed          Journal:  J Am Soc Mass Spectrom        ISSN: 1044-0305            Impact factor:   3.109


  48 in total

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Journal:  Mol Cell Biol       Date:  2002-12       Impact factor: 4.272

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  24 in total

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Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2007-01-07       Impact factor: 3.205

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7.  Histone H4 acetylation dynamics determined by stable isotope labeling with amino acids in cell culture and mass spectrometry.

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