Abstract
The spatial and temporal aspects of molecular processes in cells and tissues play an enormous part in the biology that defines living systems. Profiling and Imaging MALDI MS provides an effective means to measure and assess those dimensions on a molecular basis, including peptides, proteins, lipids, metabolite as well as others. The technology is extraordinarily high throughput with high molecular specificity and is an excellent discovery tool. It provides the capability of mapping the location of specific molecules such as drugs, lipids, peptides and proteins directly from fresh frozen tissue sections. For example, utilization of this technology provides spatial information across a tissue section for a target protein expression or for a signature of multiple proteins and can be used to correlate changes in expression levels with specific disease states or drug response. Protein patterns can be directly correlated to known histological regions within the tissue, allowing for the direct monitoring of proteins specific to these regions within a tissue sample. Profiling and imaging MS have been used to characterize many tissue types, including human gliomas and lung cancers, as well as tumor response to specific therapeutics, suggesting the use of proteomic information in assessing disease progression as well as predicting patient response to specific treatments.

Frozen tissues specimens are sectioned (~10 µm thick), thaw-mounted on flat metallic target plates, and matrix automatically deposited. This can be done in a histology-directed manner to bring into play the expertise and experience of pathologists to obtain molecular profiles from discrete areas of tissue. This represents a profiling approach where only specific areas of interest are being interrogated. In the imaging mode, high density laser ablation of an ordered array of spots over the entire tissue gives rise to a 2-dimensional ion density map (or image) with 30-80 µm lateral resolution in which location and relative abundance of a given analyte is displayed. From the analysis of a single section, images at virtually any molecular weight may be obtained.

This presentation will discuss both the technology and methods involved in analyzing molecules directly from tissue samples, including examples of discovery in mouse developmental models and the profiling of human tumors, characterizing protein differences between tumor grades, and monitoring protein changes due to drug therapy. We have applied this technology for the creation of 3-D protein images of substructures of mouse brain, to drug targeting and metabolic studies and the measurement of concomitant protein changes in specific tissues after systemic drug administration. Finally, we explore the correlation of lipid and protein changes in several systems in both health and disease.


Speaker Background
Richard M. Caprioli is the Stanley Cohen Professor of 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 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.

Meeting details

Date:	Tuesday	June 24, 2008
Time:	6:00 pm	Social hour, registration (no-host cocktails)
	7:00 pm	Dinner
	8:00 pm	Presentation
Dinner:	featuring:	Herb marinated breast of chicken
		Sliced bistro filet of beef
		Mediterranean farfalle pasta
Cost:	$40	BAMS members*
	$50	Non-members
	$60	BAMS membership plus dinner cost
	$30	Students only
	$300	2008 Corporate Sponsors
		Dinner reservations required by noon on Friday June 20, 2008

*Note:  BAMS memberships are for the calendar year and should be renewed with the first event you attend in 2008.  Dues ($30.00) may be paid while registering for dinner.  If you are unsure of your Membership status, please email Tim Hawkins.

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