Wednesday 16th July 2008
Syngene is delighted to announce that its revolutionary Dymension 2D image analysis software is being used by scientists at the world renowned, Georgetown University Medical Center (GUMC) in Washington DC to rapidly assess molecular mechanisms of novel pro-drugs on breast cancer cells.
Researchers in the Lombardi Comprehensive Cancer Center at GUMC are using Dymension, currently the fastest 2D protein gel analysis software on the market, to analyse images of Coomassie Blue stained proteins derived from breast cancer cell lines (MCF7 and MDA MB231) after treatment with an 8-Quinolinyl histone deacetylase inhibitor. From the analysis, GUMC scientists have isolated many proteins that are significantly up or down-regulated, which could provide information about the drug’s molecular targets and molecular mechanisms in cancer treatment.
Dr Amrita Cheema, Research Instructor, in the Department of Oncology, GUMC commented: “Many studies show that inhibition of histone deacetylase can lead to the histone-deacetylase-mediated transcriptional repression of tumor suppressor genes and we have used 2D gels to see the protein profile from breast cancer cells at different time points of treatment with a 8-Quinolinyl histone deacetylase inhibitor.”
“We chose to use Dymension for analyzing our 2D gels because of the software packages we tested, this is the easiest to use and also represents the best value for money as it is capable of better performance than the more expensive software we looked at. Using Dymension we have detected hundreds of interesting proteins, which we are now validating by Western blot and MS analysis,” added Dr Cheema.
Paula Maia, Vice President of Sales, Syngene US stated: "We are pleased to see our software being utilized by such a prestigious cancer center to accelerate their search for new breast cancer drug targets. The use of the software at GUMC shows it is an unrivalled, quick and simple method of analyzing complex 2D gels and is a great endorsement of Dymension’s capabilities in proteomics studies.”
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