Department of Biology

My research involves the application of proteomic techniques to the detection and analysis of protein expression in a variety of research paradigms. Specific projects include 1) the analysis of differential protein expression by cells and tissues exposed to toxic agents in vivo or in vitro, 2) the study of alcohol effects on protein expression in various brain cell types and regions, 3) the characterization of serum proteins associated with atherosclerosis, diabetic dyslipidemia, and alcoholism, and 4) assessment of altered protein expression in polycystic kidney disease fluids and epithelia. In conducting these studies, we apply various combinations of the proteomic technologies available to us, to address the unique analytical demands associated with each project. We use solution isoelectric focusing, large format one- and two-dimensional gel electrophoretic separations and image analysis coupled to peptide mass fingerprinting (MALDI-TOF MS) and tandem mass spectrometry (LC-MS/MS) to analyze and identify differential protein expression. As a non-gel-based alternative, we also have begun to employ quantitative mass spectrometric techniques along with single- and multi-dimensional liquid chromatographic approaches. Using both statistical and bioinformatic strategies, alterations in either the quantitative expression or post-translational modification of individual proteins or altered protein expression “patterns” from tissues, cells and cell fractions detected by these various approaches can then be assessed. Protein expression information obtained in this way can be used as indicators or “molecular biomarkers” of primary or secondary cellular effects, or used to better understand the molecular mechanisms, as represented by the altered proteome, that trigger altered or impaired physiological function.