For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
441
views
123
references
 Top references
cited by
8
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    32
    shares
      1,940
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      HDAC6 and Ovarian Cancer

      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

          The special class IIb histone deacetylase, HDAC6, plays a prominent role in many cellular processes related to cancer, including oncogenesis, the cell stress response, motility, and myriad signaling pathways. Many of the lessons learned from other cancers can be applied to ovarian cancer as well. HDAC6 interacts with diverse proteins such as HSP90, cortactin, tubulin, dynein, p300, Bax, and GRK2 in both the nucleus and cytoplasm to carry out these cancerous functions. Not all pro-cancer interactions of HDAC6 involve deacetylation. The idea of using HDAC6 as a target for cancer treatment continues to expand in recent years, and more potent and specific HDAC6 inhibitors are required to effectively down-regulate the tumor-prone cell signaling pathways responsible for ovarian cancer.

          Related collections

          Most cited references123

          • Record: found
          • Abstract: found
          • Article: not found

          Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes.

          Zhibin Wang, Chongzhi Zang, Kairong Cui … (2009)
          Histone acetyltransferases (HATs) and deacetylases (HDACs) function antagonistically to control histone acetylation. As acetylation is a histone mark for active transcription, HATs have been associated with active and HDACs with inactive genes. We describe here genome-wide mapping of HATs and HDACs binding on chromatin and find that both are found at active genes with acetylated histones. Our data provide evidence that HATs and HDACs are both targeted to transcribed regions of active genes by phosphorylated RNA Pol II. Furthermore, the majority of HDACs in the human genome function to reset chromatin by removing acetylation at active genes. Inactive genes that are primed by MLL-mediated histone H3K4 methylation are subject to a dynamic cycle of acetylation and deacetylation by transient HAT/HDAC binding, preventing Pol II from binding to these genes but poising them for future activation. Silent genes without any H3K4 methylation signal show no evidence of being bound by HDACs.
          Article 0 comments Cited 474 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men.

            Xiang-Jiao Yang, Edward Seto (2008)
            Protein lysine deacetylases have a pivotal role in numerous biological processes and can be divided into the Rpd3/Hda1 and sirtuin families, each having members in diverse organisms including prokaryotes. In vertebrates, the Rpd3/Hda1 family contains 11 members, traditionally referred to as histone deacetylases (HDAC) 1-11, which are further grouped into classes I, II and IV. Whereas most class I HDACs are subunits of multiprotein nuclear complexes that are crucial for transcriptional repression and epigenetic landscaping, class II members regulate cytoplasmic processes or function as signal transducers that shuttle between the cytoplasm and the nucleus. Little is known about class IV HDAC11, although its evolutionary conservation implies a fundamental role in various organisms.
            Article 0 comments Cited 344 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Histone deacetylases and cancer: causes and therapies.

              P. Marks, R A Rifkind, V M Richon … (2001)
              Together, histone acetyltransferases and histone deacetylases (HDACs) determine the acetylation status of histones. This acetylation affects the regulation of gene expression, and inhibitors of HDACs have been found to cause growth arrest, differentiation and/or apoptosis of many tumours cells by altering the transcription of a small number of genes. HDAC inhibitors are proving to be an exciting therapeutic approach to cancer, but how do they exert this effect?
              Article 0 comments Cited 305 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: Molecular Diversity Preservation International (MDPI)
                ISSN (Electronic): 1422-0067
                Publication date Collection: May 2013
                Publication date (Electronic): 02 May 2013
                Volume: 14
                Issue: 5
                Pages: 9514-9535
                Affiliations
                [1 ]Department of Pathology and Cell Biology, University of South Florida Morsani College of Medicine, 12901 Bruce B. Downs Blvd., Tampa, FL 33612, USA; E-Mail: jhaakens@ 123456health.usf.edu
                [2 ]Program of Molecular Oncology, H. Lee Moffitt Cancer Center and Research Institute, 12902 Magnolia Dr., Tampa, FL 33612, USA
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: xzhang1@ 123456health.usf.edu ; Tel.: +1-813-974-1288; Fax: +1-813-974-5536.
                Article
                Publisher ID: ijms-14-09514
                DOI: 10.3390/ijms14059514
                PMC ID: 3676797
                PubMed ID: 23644884
                SO-VID: 7b76eeb6-1684-4369-9976-f6afe11f3e3d
                Copyright © © 2013 by the authors; licensee MDPI, Basel, Switzerland
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 02 April 2013
                Date revision received : 23 April 2013
                Date accepted : 24 April 2013
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: hdac6,ovarian cancer,cancer-related signaling pathways,hdac6 inhibitors,cell stress response,motility,oncogenesis,histone deacetylase
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: hdac6, ovarian cancer, cancer-related signaling pathways, hdac6 inhibitors, cell stress response, motility, oncogenesis, histone deacetylase

                Comments

                Comment on this article

                scite_

                Similar content1,940

                See all similar

                Cited by7

                See all cited by

                Most referenced authors3,046

                See all reference authors