Richard Caprioli (Presenter)
Vanderbilt University
Bio: Richard M. Caprioli is the Stanford Moore Professor of Biochemistry and Director of the Mass Spectrometry Research Center at Vanderbilt University School of Medicine. He is Principal Investigator of the NIH Imaging Mass Spectrometry National Resource. He is Professor in the Departments of Chemistry, Medicine and Pharmacology at Vanderbilt University. Dr. Caprioli received his B.S. in 1965 from Columbia University, his Ph.D. in 1969 in Biochemistry, also at Columbia University with Professor David Rittenberg. After a one-year postdoctoral fellowship at Purdue University with Professor John H. Beynon, he was appointed as Assistant Professor of Biochemistry at Purdue in 1970. Dr. Caprioli moved to the University of Texas Medical School in Houston in 1975 where he was Professor of Biochemistry and Molecular Biology and Director of the Analytical Chemistry Center. He moved to Vanderbilt University in 1998. Professor Caprioli’s general research interests lie in discovery of temporal and spatial processes in biological systems using mass spectrometry. This work has included technology developments in the areas of electrospray and laser desorption ionization mass spectrometry and their applications to intact tissues as well as other biological samples. Recent work involves the development of Imaging Mass Spectrometry, a technology whereby molecular images of peptides, proteins, drugs and other compounds are localized in tissue sections with molecular weight specificity. Dr. Caprioli has been a member of the American Society for Mass Spectrometry (ASMS) since 1975; he served two years each as President of the Society and Vice-President for Programs. He is currently Series Editor of The Encyclopedia of Mass Spectrometry. He has published over 300 scientific papers and holds 12 US patents involving mass spectrometry technologies. In 2003, Dr. Caprioli received the Thomson Medal Award from the International Mass Spectrometry Society, the Field and Franklin Award from ACS in 2006 and the HUPO Distinguished Achievement Award in Proteomic Sciences for 2010. Dr. Caprioli is a Fellow of the AAAS and received the “Distinguished Contribution to Mass Spectrometry” Award from ASMS in June, 2014.
| Short Abstract We have employed IMS in studies of a variety of biologically and medically relevant research projects. One area of interest is the molecular mapping of molecular changes occurring in diabetes in both a mouse model and in the human disease. Major molecular alterations have been recorded in advanced diabetic nephropathy involving both proteins and lipids. Other applications include developmental studies of embryo implantation is mouse, assessment of margins in renal cancers as well as that in other organs, and neurodegenerative disease. Molecular signatures have been identified that are differentially expressed in diseased tissue compared to normal tissue and also in differentiating different stages of disease. These signatures typically consist of 10-20 or more different proteins and peptides, each identified using classical proteomics methods. |
Long Abstract
MALDI Imaging Mass Spectrometry (IMS) produces molecular maps of peptides, proteins, lipids and metabolites present in intact tissue sections. It employs desorption of molecules by direct laser irradiation to map the location of specific molecules from fresh frozen and formalin fixed tissue sections without the need of target specific reagents such as antibodies. Molecular images of this nature are produced in specific m/z (mass-to-charge) values, or ranges of values. Thus, each specimen gives rise to many hundreds of specific molecular images from a single raster of the tissue. In a complementary approach where only discrete areas within the tissue are of interest, we have developed a histology-directed approach that integrates mass spectrometry and microscopy. Thus, mass spectra are collected from only selected areas of cells within the tissue following laser ablation and analysis.
We have employed IMS in studies of a variety of biologically and medically relevant research projects. One area of interest is the molecular mapping of molecular changes occurring in diabetes in both a mouse model and in the human disease. Major molecular alterations have been recorded in advanced diabetic nephropathy involving both proteins and lipids. Other applications include developmental studies of embryo implantation is mouse, assessment of margins in renal cancers as well as that in other organs, and neurodegenerative disease. Molecular signatures have been identified that are differentially expressed in diseased tissue compared to normal tissue and also in differentiating different stages of disease. These signatures typically consist of 10-20 or more different proteins and peptides, each identified using classical proteomics methods. One such application described is that concerning the differentiation of benign skin lesions from melanomas. Our PIMS (Pathology Interface for Mass Spectrometry) will be demonstrated. In addition, Imaging MS has been applied to drug targeting and metabolic studies both in specific organs and also in intact whole animal sections following drug administration.
This presentation will also describe recent technological advances both in sample preparation and instrumental performance to achieve images at high spatial resolution (1-10 microns) and at high speeds so that a typical sample tissue once prepared can be imaged in just a few minutes. Applications will include the use of MS/MS, ultra-high mass resolution, ion mobility, and ion accumulation devices for IMS. Finally, new biocomputational approaches will be discussed that deals with the high data dimensionality of Imaging MS and our implementation of ‘image fusion’ in terms of predictive integration of MS images with microscopy and other imaging modalities.
References & Acknowledgements:
NIH/NIGMS 5R01 GM058008; NIH/NIGMS 2P41 GM103391
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IP Royalty: no
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