Publication / Source: Bioanalysis 5(3)
Authors: Wang W, Xu L, Kong J, Fan H, Yang P
Background: Core histone H3 is a highly conserved protein in the cell nucleus, it goes through various post-translational modifications easily, and the state of the acetylation has clinical diagnostic significance in prostate cancer, breast cancer, lung cancer and other diseases. Results: In this work, the combinatorial method of chromatographic separation, methylation isotope labeling and LTQ-Orbitrap MS was employed to quantify the acetylation sites of histone H3 separately within normal liver cells L02 and hepatocellular carcinoma (HCC) cells HepG2, HCC metastasis cells 97H and HCC cells HepG2, high HCC metastasis potential cells LM3 and low HCC metastasis potential cells 97L. In comparison with the quantitative results of HepG2 and L02, the amounts of five acetylated and methylated peptides were found decreased. Similarly, when comparing the 97H with HepG2, the amounts of eight acetylated and methylated peptides were found decreased, and when comparing the LM3 with 97L, the amounts of six acetylated and methylated peptides were found decreased. Conclusion: These results provide some fundamental reference information for the research into post-translational modifications of histones in human liver cancer and other related diseases.