Dwight E. Matthews |
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Analytical Chemistry and Mass SpectrometryProfessor & ChairDwight.Matthews@uvm.edu |
| Dr. Matthews received his Ph.D. from Indiana University with John Hayes in 1977. He pursued his research career first at Washington University School of Medicine in St. Louis in the Department of Medicine then at Cornell University Medical College in New York City in the Departments of Medicine and Surgery before arriving at Vermont in 1996. Dr. Matthews has a joint appointment in the Department of Medicine and is involved in the Clinical Research Center (CRC) program in the College of Medicine. Dr. Matthews' primary research interest is in mass spectrometry and heads mass spectrometry in the CRC and biomedical mass spectrometry for proteomics studies at UVM. Dr. Matthews was appointed the Chair of the Department of Chemistry in July 2002 and named a UVM University Scholar for 2004-05. He has been an NIH study section member and chair of an NIH Study Section. He was elected to the Vermont Academy of Science and Engineering in 2007. |
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My research has used stable isotopically labeled tracers and kinetic models to answer questions of human physiology and biochemistry. The research program of my group in chemistry focuses on developing new methods and techniques of mass spectrometry to measure stable isotopes in biological molecules and mathematical and computer models to interpret the stable isotope tracer kinetic data obtained from biological samples. Much of our research is focused upon amino acid and protein metabolism in humans. Students are encouraged as part of their thesis work to apply methods developed to clinical studies of metabolism in humans. Many simple metabolic questions have never been answered in humans. For example, we do not know which pathways regulate the metabolism of several important amino acids in humans. Mass spectrometry has been widely applied for compound identification, but precise measurement of isotopes in biological compounds has received less attention. Gas chromatography-mass spectrometry, liquid chromatography-mass spectrometry, and isotope ratio mass spectrometry are all used for research in our group for research in stable isotope tracer measurement. More recent work has been to bring stable isotope methodology to proteomics for quantiation of proteins and protein modifications. |
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An example of in vivo stable isotope tracer work is shown in the figure below from a 2001 paper where we were able to trace intracellular metabolism of methionine in humans through production of intracellular homocysteine and homocysteine in blood, including measurement of homocysteine covalent-binding to plasma proteins. This work give us a tool for studying homocysteine metabolism in humans. The importance of these studies is that elevated levels of blood homocysteine translate into greatly increased risks of cardiovascular disease. |
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Our 2005 A-pages article in Analytical Chemistry highlights some of the work done in proteomics and provides an overview of the current status of quantitative methods in proteomics today. |
 August 1, 2005 cover of Analytical Chemistry |
Selected PublicationsPrevis, M.J.; VanBuren, P.; Begin, K.J.; Vigoreaux, J.O.; LeWinter, M.M.; & Matthews, D.E. "Quantification of Protein Phosphorylation by Liquid Chromatography Mass Spectrometry", Anal. Chem. 2008, 80, 5864-5872, 2008. McCarthy, S.M.; Bove, P.F.; Matthews, D.E.; Akaike, T.; & van der Vliet, A. "Nitric Oxide Regulation of MMP-9 Activation and Its Relationship to Modifications of the Cysteine Switch", Biochemistry 2008, 47, 5832-40. Thornton, T.M.; Pedraza-Alva, G.; Deng, B.; Wood, C.D.; Aronshtam, A.; Clements, J.L.; Sabio, G.; Davis, R.J.; Matthews, D.E.; Doble, B.; & Rincon, M. "Phosphorylation by p38 MAPK as an Alternative Pathway for GSK3β Inactivation", Science 2008, 320, 667-70. Reynaert, N.L.; van der Vliet, A.; Guala, A.S.; McGovern, T.; Hristova, M.; Pantano, C.; Heintz, N.H.; Heim, J.; Ho, Y.S.; Matthews, D.E.; Wouters, E.F. & Janssen-Heininger, Y.M.: "Dynamic Redox Control of NF-κB Through Glutaredoxin-regulated S-Glutathionylation of Inhibitory κB Kinase β," Proc. Natl. Acad. Sci. U. S. A. 2006, 103, 13086-91. Jennings, M.E., II & Matthews, D.E.: "Determination of Complex Isotopomer Patterns in Isotopically Labeled Compounds by Mass Spectrometry," Anal. Chem. 2005, 77, 6435-44. MacCoss, M.J.; Wu, C.C.; Matthews, D.E. & Yates, J.R., III: "Measurement of the Isotope Enrichment of Stable Isotope-Labeled Proteins Using High-Resolution Mass Spectra of Peptides," Anal. Chem. 2005, 77, 7646-53. MacCoss, M.J. & Matthews, D.E.: "Quantitative Mass Spectrometry for Proteomics: Teaching a New Dog Old Tricks," Anal. Chem. 2005, 77, 294A-302A. Wu, C. C.; MacCoss, M. J.; Howell, K. E.; Matthews, D. E.; Yates, J. R., III: "Metabolic Labeling of Mammalian Organisms with Stable Isotopes for Quantitative Proteomic Analysis," Anal. Chem. 2004, 76, 4951-9. |
Last modified August 28 2008 09:38 PM
