Sunday November 22 2009 | Biotechnology feed | All feeds
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Sunday November 22 2009 | Biotechnology feed | All feeds
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Metastatic control by histone deacetylase inhibitors The drive to develop improved treatments of cancer has resulted in the birth of a number of highly exciting therapeutic fields, apoptosis and angiogenesis offering just two recent examples. The field of histone deacetylation represents one of the most recent therapeutic targets to fall under the oncology spotlight. Information relating histone deacetylation is emerging with breathtaking rapidity with over 1 new article currently being published every day. In response to this activity, we recently published one of the most comprehensive overview of the pharmaceutical potential of the histone deacetylase (HDAC) inhibitors to date (Click here to access "Histone deacetylase inhibitors: Redefining pharmaceutical approaches to the treatment of cancer"). One feature of HDACs described in this report is their ability to impinge on multiple aspects of tumor progression including cell cycling, differentiation and proliferation, angiogenesis and apoptosis. A further component of tumor progression is extracellular matrix degradation, which contributes to both metastasis and angiogenesis. Matrix metalloproteinases (MMPs) are a family of zinc-dependent neutral endopeptidases collectively capable of degrading essentially all matrix components. Over 20 MMP modulating agents are in pharmaceutical develop, almost half of which are indicated for cancer. Most recently, University of Toronto researchers have reported that HDACs regulate MMP expression and activity in 3T3 cells. In particular, inhibition of HDAC by trichostatin A (TSA), which has been shown to prevent tumorigenesis and metastasis, decreases mRNA as well as zymographic activity of gelatinase A (MMP2; Type IV collagenase), a matrix metalloproteinase, which is itself, implicated in tumorigenesis and metastasis. Furthermore, TSA inhibits cytochalasin D-induced activation of gelatinase A, but TSA does not affect other members of the gelatinase A activation complex, MT1-MMP and TIMP-2. Thus, TSA is a selective and potent inhibitor of expression and activation of gelatinase A. This finding strengthens the rationale for continuing to investigate the therapeutic utility of TSA and other HDAC inhibitors in cancer.
November, 2002 Adapted from Ailenberg & Silverman, Biochem Biophys Res Commun 2002 Oct 18;298(1):110 Interested in collaborating with this group? Contact leaddiscovery@bioportfolio.co.uk LeadDiscovery and BioPortfolio aims to provide reliable, insightful analysis on the biotechnology industry. However, this information is provided "as is" and no representations or warranties either express or implied of completeness, accuracy, or of any other nature are made with respect to this information. This information is neither an offer to sell nor a solicitation to buy the securities of any company. This information contains forward-looking statements, which involve risks and uncertainties which may not be listed. The biotechnology industry is an emerging industry and the securities of the companies mentioned in this report have a very high degree of risk and volatility. For this reason, this information is supplied on the condition that the reader will make his or her own determination as to its suitability for any purpose prior to any use of this information. The employees and officers of LeadDiscovery and BioPortfolio may hold positions in some or all of the stocks discussed in this report. This abstract has been produced by LeadDiscovery Ltd. Founded by life scientists for life scientists we aim to help industry identify cutting edge drug discovery options and academic/biotech institutions maximize the potential of their research. Abstracts strictly reflect the opinion of LeadDiscovery's editorial panel. While all reasonable efforts are made to ensure the accuracy of information provided LeadDiscovery and the publisher BioPortfolio, takes no responsibility for incorrect or misleading information. LeadDiscovery is designed for educational and drug development purposes only and is not intended or designed to offer medical advice or advice of any sort, and must not be used for such purpose. The information provided through LeadDiscovery and BioPortfolio should not be used for diagnosing or treating a health problem or a disease and no reliance should be placed on any information contained in this abstract or elsewhere on LeadDiscovery's and BioPortfolio's website. It is not intended to be a substitute for professional care. If you have or suspect you may have a health problem, you should consult your physician or other health care provider. |
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