Research Description
Work in our group involves the development and application of mass spectrometry-based tools to study proteins and proteomes. The goal of this work is to provide the necessary tools to enable the comprehensive characterization of the entire complement of proteins expressed within a cell, tissue or organism, in order to better understand basic mechanisms of biological function and disease. These tools must be capable of measuring the many properties of proteins that collectively determine their function. These properties include the quantitative levels of expressed proteins, sub-cellular localization, post-translational modifications, associations in non-covalent complexes and biochemical activity. Mass spectrometry provides a highly powerful tool that is capable of measuring these various protein properties, in a high-throughput manner. The development of these tools is highly interdisciplinary in nature, integrating front-end molecular biology and biochemical methods, protein and peptide chemistry, analytical separations, instrumental analysis, and back-end computational software for data processing.
Ongoing research projects in the laboratory include:
- Studies of oral cancer progression and the salivary proteome using a variety of quantitative proteomic strategies, in collaboration with researchers from the Dental, Medical and Computer Science Departments
- Studies of oxidative stress-induced protein damage and modification, and the effects of these modifications in the aging process and disease. One ongoing project focuses on the effect of these protein modifications on muscle function during the aging process, through a collaboration with researchers in the Chemistry and Physical Medicine and Rehabilitation Departments
- Studying the biochemistry of cellular growth regulation via proteomic strategies, in both human cell lines and model organisms (yeast). This work is undertaken through an ongoing collaboration with Dr. Do-Hyung Kim, also of the Department of Biochemistry, Molecular Biology and Biophysics
Recent Publications
Meany, D., Xie, H., Thompson, L.V., Arriaga, E.A. and Griffin, T.J. (2007) Identification of carbonylated mitochondrial proteins from rat muscle using affinity chromatography-stable isotope labeling and tandem mass spectrometry, Proteomics 7, 1150-1163.
Roe, M.R. Xie, H., Bandhakavi, S. and Griffin, T.J. (2007) Proteomic Mapping of 4-Hydroxynonenal Protein Modification Sites by Solid-Phase Hydrazide Chemistry and Mass Spectrometry, Anal Chem, 79, 3747-3756.
Vander Haar, E., Lee, S., Bandhakavi, S., Griffin, T.J. and Kim, D.H. (2007) Integration of Nutrient and Insulin Signaling Through the mTOR-raptor Complex, Nature Cell Biology 9, 316-23.
Grimsrud, P.A., Griffin, T.J., Picklo, M.J. and Bernlohr, D.A. (2007) Aldehyde Modification of Proteins in Obesity and Insulin Resistance, Mol Cellular Proteomics, 6, 624-637.
Xie, H, Bandhakavi, S., Roe, M.R. and Griffin, T.J. (2007) Preparative peptide isoelectric focusing as a tool for improving the identification of lysine acetylated peptides from complex mixtures, J Proteome Res, 6, 2019-2026.
Roe, M.R. and Griffin, T.J. (2006) Gel-Free Mass Spectrometry-Based High Throughput Proteomics: Tools for Studying Biological Response of Proteins and Proteomes. Review Article. Proteomics, (2006) 6, 4678-4687.
Xie, H. and Griffin, T.J. (2006) The Trade-Off Between Sensitivity and False Positive Peptide Sequence Matches Using a 2-D Linear Ion Trap for Tandem Mass Spectrometry-Based Proteomics, J Proteome Res 5, 1003-9.
Xie, H., Rhodus, N.L., Griffin, R.J., Carlis, J.V. and Griffin, T.J. (2005) A catalogue of human saliva proteins identified using Free Flow Electrophoresis and Tandem Mass Spectrometry. Mol. Cellular Proteomics 4 , 1826-1830.
Xie, H., Bandhakavi, S. and Griffin, T.J. (2005) Evaluating Preparative Isoelectric Focusing of Complex Peptide Mixtures for Mass Spectrometry-Based Proteomics: A Case Study in Profiling Chromatin-Enriched Subcellular Fractions in S. cerevisiae. Anal. Chem. 77 , 3198-3207.
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