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      Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer.

      Author(s): 1 ,
      Publication date (Electronic):
      Journal: Nature reviews. Cancer
      Publisher: Springer Nature

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          Abstract

          Histone deacetylases (HDACs) are considered to be among the most promising targets in drug development for cancer therapy, and first-generation histone deacetylase inhibitors (HDACi) are currently being tested in phase I/II clinical trials. A wide-ranging knowledge of the role of HDACs in tumorigenesis, and of the action of HDACi, has been achieved. However, several basic aspects are not yet fully understood. Investigating these aspects in the context of what we now understand about HDACi action both in vitro and in vivo will further improve the design of optimized clinical protocols.

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          The history of cancer epigenetics.

          Andrew Feinberg, Benjamin Tycko (2004)
          Article 0 comments Cited 551 times – based on 0 reviews     Review now
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            Loss of acetylation at Lys16 and trimethylation at Lys20 of histone H4 is a common hallmark of human cancer.

            Mario Fraga, Esteban Ballestar, Ana Villar-Garea … (2005)
            CpG island hypermethylation and global genomic hypomethylation are common epigenetic features of cancer cells. Less attention has been focused on histone modifications in cancer cells. We characterized post-translational modifications to histone H4 in a comprehensive panel of normal tissues, cancer cell lines and primary tumors. Using immunodetection, high-performance capillary electrophoresis and mass spectrometry, we found that cancer cells had a loss of monoacetylated and trimethylated forms of histone H4. These changes appeared early and accumulated during the tumorigenic process, as we showed in a mouse model of multistage skin carcinogenesis. The losses occurred predominantly at the acetylated Lys16 and trimethylated Lys20 residues of histone H4 and were associated with the hypomethylation of DNA repetitive sequences, a well-known characteristic of cancer cells. Our data suggest that the global loss of monoacetylation and trimethylation of histone H4 is a common hallmark of human tumor cells.
            Article 0 comments Cited 440 times – based on 0 reviews     Review now
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              Proteomic analysis of post-translational modifications.

              Matthias Mann, Ole N. Jensen (2003)
              Post-translational modifications modulate the activity of most eukaryote proteins. Analysis of these modifications presents formidable challenges but their determination generates indispensable insight into biological function. Strategies developed to characterize individual proteins are now systematically applied to protein populations. The combination of function- or structure-based purification of modified 'subproteomes', such as phosphorylated proteins or modified membrane proteins, with mass spectrometry is proving particularly successful. To map modification sites in molecular detail, novel mass spectrometric peptide sequencing and analysis technologies hold tremendous potential. Finally, stable isotope labeling strategies in combination with mass spectrometry have been applied successfully to study the dynamics of modifications.
              Article 0 comments Cited 404 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Nat. Rev. Cancer
                Title: Nature reviews. Cancer
                Publisher: Springer Nature
                ISSN: 1474-175X
                ISSN (Print): 1474-175X
                Publication date (Electronic): Jan 2006
                Volume: 6
                Issue: 1
                Affiliations
                [1 ] Department of Experimental Oncology, European Institute of Oncology, Via Ripamanti 435, 20141, Milan, Italy. saverio.minucci@ifom-ieo-campus.it
                Article
                Publisher Item ID: nrc1779
                DOI: 10.1038/nrc1779
                PubMed ID: 16397526
                SO-VID: e9e4f953-ee16-41fa-85c4-7318b1682b09
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