Journal of Proteomics & Bioinformatics
Open Access
ISSN: 0974-276X
+44 1223 790975
ISSN: 0974-276X
+44 1223 790975
Alan Tackett
Scientific Tracks Abstracts: J Proteomics Bioinform
Melanoma accounts for the vast majority of skin cancer related deaths. The discovery of new markers for diagnosis and prognosis of this disease has been hampered by the inefficient analysis of primary human tissue. We have developed an unbiased, high throughput and quantitative approach for the identification of proteins that are differentially expressed in metastatic melanoma from human tissue. Using quantitative label-free mass spectrometry of laser microdissected samples, we have identified 390 proteins differentially expressed in melanoma. Immunohistochemistry was used to validate a subset of these proteins. Furthermore, we have used this quantitative mass spectrometry approach to uncover a panel of histone posttranslational modifications that are differentially regulated in metastatic melanoma. The former has allowed us to explore epigenetic mechanisms that regulate melanoma progression. Our studies lay the foundation for an extensive analysis of archived human melanoma tissues for the discovery of biomarkers that will help clinicians with diagnosis, prognosis and treatment of this cancer.
Alan Tackett completed PhD. From University of Arkansas for Medical Sciences, Little Rock, AR and Post doctoral study from The Rockefeller University, New York, NY .Now working as an Associate Professor of Biochemistry and Molecular Biology in University of Arkansas for Medical Sciences, USA. My laboratory focuses on technology development for the high resolution analysis of chromatin and the elucidation of proteinprotein interactions that direct the posttranslational modification of histones. Additionally, I direct the UAMS Proteomics Facility and have extensive experience in collaborative research projects involving various areas of mass spectrometry. My group has expertise in using mass spectrometry to identify proteins in complex mixtures as well as quantifying protein abundance using various procedures (e.g., label-free, spectral counting, stable isotope tags & SILAC). We also perform various quantitative analyses of posttranslational modifications.