For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
7
views
130
references
 Top references
cited by
17
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      223
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      H3K18Ac as a Marker of Cancer Progression and Potential Target of Anti-Cancer Therapy

      review-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Acetylation and deacetylation are posttranslational modifications (PTMs) which affect the regulation of chromatin structure and its remodeling. Acetylation of histone 3 at lysine placed on position 18 (H3K18Ac) plays an important role in driving progression of many types of cancer, including breast, colon, lung, hepatocellular, pancreatic, prostate, and thyroid cancer. The aim of this review is to analyze and discuss the newest findings regarding the role of H3K18Ac and acetylation of other histones in carcinogenesis. We summarize the level of H3K18Ac in different cancer cell lines and analyze its association with patients’ outcomes, including overall survival (OS), progression-free survival (PFS), and disease-free survival (DFS). Finally, we describe future perspectives of cancer therapeutic strategies based on H3K18 modifications.

          Related collections

          Most cited references130

          • Record: found
          • Abstract: found
          • Article: found
          Is Open Access

          Targeting oncogenic Myc as a strategy for cancer treatment

          Hui Chen, Hudan Liu, Guoliang Qing (2018)
          The MYC family oncogene is deregulated in >50% of human cancers, and this deregulation is frequently associated with poor prognosis and unfavorable patient survival. Myc has a central role in almost every aspect of the oncogenic process, orchestrating proliferation, apoptosis, differentiation, and metabolism. Although Myc inhibition would be a powerful approach for the treatment of many types of cancers, direct targeting of Myc has been a challenge for decades owing to its “undruggable” protein structure. Hence, alternatives to Myc blockade have been widely explored to achieve desirable anti-tumor effects, including Myc/Max complex disruption, MYC transcription and/or translation inhibition, and Myc destabilization as well as the synthetic lethality associated with Myc overexpression. In this review, we summarize the latest advances in targeting oncogenic Myc, particularly for cancer therapeutic purposes.
          Article 0 comments Cited 337 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: not found
            • Article: not found

            CBP/p300 in cell growth, transformation, and development.

            Richard H. Goodman, Sarah Smolik (2000)
            Article 0 comments Cited 290 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention.

              X-J. Yang, E Seto (2007)
              Acetylation of the epsilon-amino group of a lysine residue was first discovered with histones in 1968, but the responsible enzymes, histone acetyltransferases and deacetylases, were not identified until the mid-1990s. In the past decade, knowledge about this modification has exploded, with targets rapidly expanding from histones to transcription factors and other nuclear proteins, and then to cytoskeleton, metabolic enzymes, and signaling regulators in the cytoplasm. Thus, protein lysine acetylation has emerged as a major post-translational modification to rival phosphorylation. In this issue of Oncogene, 19 articles review various aspects of the enzymes governing lysine acetylation, especially about their intimate links to cancer. To introduce the articles, we highlight here four central themes: (i) multisubunit enzymatic complexes; (ii) non-histone substrates in diverse cellular processes; (iii) interplay of lysine acetylation with other regulatory mechanisms, such as noncoding RNA-mediated gene silencing and activation; and (iv) novel therapeutic strategies and preventive measures to combat cancer and other human diseases.
              Article 0 comments Cited 276 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Cells
                Journal ID (iso-abbrev): Cells
                Journal ID (publisher-id): cells
                Title: Cells
                Publisher: MDPI
                ISSN (Electronic): 2073-4409
                Publication date (Electronic): 22 May 2019
                Publication date Collection: May 2019
                Volume: 8
                Issue: 5
                Electronic Location Identifier: 485
                Affiliations
                [1 ]Department of Biochemistry and Molecular Biology, Medical University of Lublin, Chodzki 1 St., 20-093 Lublin, Poland; anna.wawruszak@ 123456umlub.pl (A.W.); alicja.przybyszewska@ 123456umlub.pl (A.P.); anna.jaruga@ 123456umlub.pl (A.J.); malgorzata.guz@ 123456umlub.pl (M.G.); joanna.kalafut@ 123456umlub.pl (J.K.); andrzej.stepulak@ 123456umlub.pl (A.S.); marek.cybulski@ 123456umlub.pl (M.C.)
                [2 ]Postgraduate School of Molecular Medicine, Medical University of Warsaw, Trojdena 2a St., 02-091 Warsaw, Poland; anna.jaruga@ 123456umlub.pl
                Author notes
                [* ]Correspondence: martahalasa@ 123456umlub.pl or marta.halasa@ 123456umlub.pl ; Tel.: +48-81-448-6350
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0003-2388-4577
                Article
                Publisher ID: cells-08-00485
                DOI: 10.3390/cells8050485
                PMC ID: 6562857
                PubMed ID: 31121824
                SO-VID: e7687952-8628-4c50-af32-4b1993394d29
                Copyright © © 2019 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 15 April 2019
                Date accepted : 16 May 2019
                Categories
                Subject: Review

                Keywords: histone acetylation,histone deacetylation,hats,hdacs,h3k18ac,cancer hallmarks
                Data availability:
                Keywords: histone acetylation, histone deacetylation, hats, hdacs, h3k18ac, cancer hallmarks

                Comments

                Comment on this article

                scite_

                Similar content223

                See all similar

                Cited by17

                See all cited by

                Most referenced authors1,949

                See all reference authors