The mission of the Mass Spectrometry Research Center (MSRC) is to bring state-of-the-art mass spectrometry expertise, methodology, and instrumentation to the research and clinical infrastructure of the Vanderbilt University Medical Center.
The MSRC is located on the 9th floor in Medical Research Building III. Support for the facility comes from service cores affiliated with seven NIH-funded Program Projects and Research Centers, service fees charged to unaffiliated investigators and direct institutional support from Vanderbilt University.
The MSRC is located at the corner of Hillsboro Road/21st Avenue and Edgehill Avenue, across the street from The University School of Nashville.
The Mass Spectrometry (small molecule) Core provides collaboration, consultation, and equipment to research investigators throughout the University. The Mass Spectrometry Research and Development Lab continues to provide the Medical Center with cutting-edge instrumentation and methods, including close collaborations with clinicians through translational research. Proteome profiling identifies mass spectral patterns derived from multiple proteins in a tissue or biofluid sample. Proteome imaging can be done by analyzing mass spectral data acquired across a grid within a tissue section. The Tissue/Serum Proteomics Core laboratory provides direct proteome profiling and protein imaging of intact tissues by MALDI-MS. There is now in place a Bioinformatics section of the MSRC to address the growing biocomputational needs of the MSRC for mining data. Because of the huge data load generated in the facility, we have begun to implement system to run complex and time-consuming programs for correlation mass spectral data with clinical data, as well as archive and search data.
The MSRC conducts collaborative research programs with investigators in nearly every Center and department in the Medical Center as well as many trans-Institutional initiatives in the Over 200 investigators currently use the facilities, most as an on-going part of their research programs. In particular, the Proteomics Core facility plays major roles not only in the Cancer Center (VICC), but also in the three funded SPORES (GI, Lung and Breast). It is also a major part of the facilities available to the newly formed Chemical Biology Instituteand has many collaborative arrangements with faculty members at the Meharry Medical College.
In September 2003 the MSRC moved into new facilities in Medical Research Building III that provided a more than 2-fold increase in space. The Mass Spectrometry Core Lab currently occupies about 3,800 square feet of laboratory space on the 9th floor of the MRB III that is contiguous with that occupied by the Proteomics Core (3,600 sq ft). The Tissue Profiling/Imaging Laboratory was established in 2004 to provide expertise in molecular analysis of tissues and biological fluids, where it is housed within the National Resource for Imaging Mass Spectrometry. The mission of this Core is to provide expertise for the analysis of complex proteomes of tissue samples to provide information that can facilitate the detection of disease states, responses to therapy and drug toxicity. Proteome profiling identifies mass spectral patterns derived from multiple proteins in a tissue sample. Proteome imaging can be done by analyzing mass spectral data acquired across a grid within a tissue section. Proteomic patterns can be analyzed with bioinformatics and biostatistical methods to identify sets of diagnostic spectral markers. Identification of the proteins and protein fragments that account for biomarker signals is done in collaboration with the Proteomics Core Laboratory.
Support for these facilities comes from service cores affiliated with seven NIH-funded Program Projects and Research Centers, service fees charged to unaffiliated investigators and direct institutional support from Vanderbilt University .
The MSRC has protocols and instrumentation to form a critical mass in proteomics with established support from the Vanderbilt Ingram Cancer Center , the Molecular Toxicology Center , the Breast SPORE Grant and the Vanderbilt Vision Research Center .
The amount and complexity of the data generated by the MSRC requires both an active development and support staff to be available to address the needs of the mass spectrometry-based research enterprise at Vanderbilt. The MSRC's bioinformatics core is actively engaged in both systems and algorithm development to facilitate the analysis and correlation of mass spectral data and clinical information. The core's support component provides systems support and storage management to members of the facility.
In addition, contracts to Vanderbilt University for research in drug metabolism include some of the largest and most prestigious pharmaceutical companies. The basic goal of most of these projects is the measurement of the site of arrival of a drug, a measure of its relative metabolism, and its effect on the protein concentrations at the site of arrival as compared to other areas.
The current configuration of the MSRC, with four core laboratories, two research and development laboratories, and the National Research Resource for Imaging Mass Spectrometry, currently houses 40 mass spectrometers and has served over 400 users over the past 12 months, making it one of the premier Mass Spectrometry centers in the United States.
Richard M. Caprioli is the Stanford Moore Chair in Biochemistry and Director of the Mass Spectrometry Research Center at Vanderbilt University School of Medicine. He is also currently Professor in the Departments of Chemistry, Medicine and Pharmacology at Vanderbilt University. Dr. Caprioli received his B.S. in 1965 from Columbia University in New York, N.Y., his Ph.D. in 1969 in Biochemistry, also at Columbia University with Professor David Rittenberg. He did a one-year postdoctoral fellowship at Purdue University with Professor John H. Beynon. In 1970, he was appointed as Assistant Professor of Biochemistry at Purdue. In 1975, Dr. Caprioli moved to the University of Texas Medical School in Houston where he was Professor of Biochemistry and Molecular Biology and Director of the Analytical Chemistry Center until his move to Nashville in early 1998.
Professor Caprioli is interested in the use of mass spectrometry for the analysis of compounds in biological systems. Current work includes the use of electrospray and laser desorption ionization methods with biological tissues and samples. Applications have focused on the development of this instrumentation and associated methodologies to achieve ultra-high sensitivity detection of endogenous compounds (e.g., neuropeptides) in live animal systems. Recent work involves the development of Imaging Mass Spectrometry, a technique whereby molecular images of peptides, proteins, drugs and other compounds are localized in tissue sections with molecular weight specificity. This method involves molecular mapping of animal tissue through the production of ion images obtained from the analysis of mammalian tissue. Applications to specific research areas involve questions about certain spatial distributions of molecules within specific tissues, e.g., mapping proteins in cancer tissue. Specific applications include human glioblastomas, breast cancer, colorectal cancer and lung cancer.
Dr. Caprioli has been a member of the American Society for Mass Spectrometry since 1975; he served two years each as President of the Society and Vice-President for Programs. He is a member of the American Society for Biochemistry and Molecular Biology, the American Association for Cancer Research, and the American Chemical Society. Professor Caprioli has been the Editor-in-Chief of the Journal of Mass Spectrometry since 1990. He is currently co-editing several volumes and is Series Editor of Encyclopedia of Mass Spectrometry. He has published over 300 scientific papers, including three books. In 2003, Dr. Caprioli received the Thomson Medal Award from the International Mass Spectrometry Society for “for outstanding achievements in mass spectrometry and for distinguished service to international mass spectrometry.” He received the Field and Franklin Award from the American Chemical Society in April, 2006 for Outstanding Achievement in Mass Spectrometry.