Shama Mirza, Ph.D.
Assistant Professor

Dr. Mirza received her Master of Science degree from Nagarjuna University, Andhra Pradesh, India in 1997 and her Doctorate degree in Chemistry (Mass Spectrometry) from the Indian Institute of Chemical Technology, Hyderabad, India in 2004. She was a postdoctoral fellow at the University of Texas Southwestern Medical Center in Dallas, TX from 2004-2005 and the Medical College of Wisconsin from 2005-2008 where she was involved in the technology development for the comprehensive characterization and quantification of cellular proteomes using mass spectrometry. Dr. Mirza joined the faculty of the Medical College of Wisconsin in 2008.
Contact Information
smirza@mcw.edu
Phone: (414) 955-2231
Fax: (414) 955-6568
Research Interests
Our primary research interest is to develop novel technologies for the comprehensive characterization of cellular proteomes in order to better understand protein functions and interactions under normal and disease states. Such understanding requires high-throughput technologies that allow running various experiments in parallel. The aim of our research is to develop such technologies and gain insight into the biological processes that would otherwise not be achieved using traditional methods.
The comprehensive proteomic analysis of complex biological systems and processes is currently very difficult due to the technical limitations and challenges. However, the potential for improving our understanding of biological processes using proteomic information is tremendous. One such biological system that would benefit from comprehensive proteomic profiling is the analysis of differential protein expression in vascular endothelial cells during hypoxia-induced angiogenesis. Angiogenesis describes the development of new capillaries from the endothelium of the pre-existing blood vessels. Although many studies have defined the properties of angiogenic regulators, little is known about the signaling pathways within vascular endothelial cells that govern angiogenic behavior. Hence, it has become imperative to bridge the gap by comprehensive characterization of the cellular proteome that mediates vessel formation. Thus, the development of precise protein characterization methods will significantly aid in the identification and characterization of proteomic changes in vascular endothelial cells during angiogenesis.
Below is the highlight of some of the current research activities:
1. Determine changes in protein phosphorylation and glycosylation during angiogenesis.
2. Develop peptoid arrays for high-throughput quantification of differentially expressed proteins and their posttranslational modifications.
3. Proteomics of Congestive Heart Defects.
Selected Publications
18O labeling over coffee break: A rapid strategy for quantitative proteomics. S.P. Mirza, A.S. Greene and M. Olivier. J. Proteom. Res. 7: 3042 (2008)
Methods and approaches for the comprehensive characterization and quantification of cellular proteomes using mass spectrometry. S.P. Mirza and M. Olivier. Physiological Genomics. 33: 3 (2007)
Visualizing quantitative proteomics datasets using Treemaps. B.D. Halligan, S.P. Mirza, M.C. Pellitteri-Hahn, M. Olivier, and A.S. Greene Information Visualization 527. (2007)
Improved method for the analysis of membrane proteins by mass spectrometry. S.P. Mirza, B.D. Halligan, A. S. Greene and M. Olivier Physiological Genomics 30: 89. (2007)
A clean, more efficient method for in-solution digestion of protein mixtures without detergent or urea. S.C. Kim, Y. Chen, S.P. Mirza, Y. Xu, J. Lee, P. Liu, and Y. Zhao J. Proteom. Res. 5: 3446. (2006)
Improved mass spectrometric proteomic profiling of the secretome of rat vascular endothelial cells. M.C. Pellitteri-Hahn, M.C. Warren, D.N. Didier, E.L. Winkler, S.P. Mirza, A.S. Greene, and M. Olivier J. Proteom. Res. 5: 2861. (2006)
Estimation of the proton affinity values of fifteen Matrix-assisted laser desorption/ionisation matrices under Electrospray ionisation conditions using the kinetic method. S.P. Mirza, N.P. Raju and M. Vairamani J. Am. Soc. Mass Spectrom. 15: 431. (2004)
5-Amino-2-mercapto-1,3,4-thiadiazole: a new matrix for the efficient matrix-assisted laser desorption/ionization of neutral carbohydrates. S.P. Mirza, N.P. Raju, S.S. Madhavendra and M. Vairamani Rapid Commun. Mass Spectrom. 18: 1666. (2004)
Electron Transfer Reaction of Oxo(salen)chromium(V) Ion with Anilines. S. Premsingh, N.S. Venkataramanan, S. Rajagopal, S.P. Mirza, M. Vairamani, P.S. Rao and K. Velavan Inorg. Chem. 43: 5744. (2004)
Mass spectral study of meso-alkyl and meso-cycloalkyl calix(4)pyrroles under electron impact conditions. S. Prabhakar, M.R. Kishan, S.P. Mirza, K.V. Raghavan and M. Vairamani Rapid Commun. Mass Spectrom. 18: 2077. (2004)
The kinetic method reveals secondary deuterium isotope effects on the proton affinity and gas-phase basicity of glycine and alanine methyl esters. S.P. Mirza, P. Krishna, S. Prabhakar and M. Vairamani, D. Giblin and Michael L. GrossInt. J. Mass Spectrom, 230: 175. (2003)
Mass Spectral studies of N,N-dialkylaminoethanols. T.J. Reddy, S.P. Mirza, U.V.R. Vijaya Saradhi, V. Jayathirtha Rao and M. Vairamani Rapid Commun. Mass Spectrom. 17: 746. (2003)
Estimation of proton affinity of proline and tryptophan under electrospray ionization conditions using the extended kinetic method. S.P. Mirza, S. Prabhakar, M. Vairamani Rapid Commun. Mass Spectrom. 15: 957. (2001)
5-Ethyl-2-mercaptothiazole as matrix for matrix-assisted laser desorption/ionization of a broad spectrum of analytes in positive and negative ion mode. N.P. Raju, S.P. Mirza, M. Vairamani, A.R. Ramulu and M. Pardhasaradhi Rapid Commun. Mass Spectrom. 15: 1879. (2001)
Mass spectral study of O- and S-aryl dimethylthiocarbamates under electron impact conditions: Newman-Kwart rearrangement in the gas phase. S. Prabhakar, P. Kar, S.P. Mirza, V.V.S. Laxmi, K. Nagaiah and M. Vairamani Rapid Commun. Mass Spectrom. 15: 2127. (2001)
Claisen rearrangement of allyl phenyl ether and its sulfur and selenium analogues on electron impact. S. Prabhakar, S.P. Mirza, A. Kundu, S. Roy and M. Vairamani Rapid Commun. Mass Spectrom. 14: 1116. (2000)