Boone M. Prentice received his B.S. degree in Chemistry with Honors and Distinction from Longwood University (Farmville, VA) in 2008 with minors in Biology and Mathematics. At Longwood, he conducted electroanalytical research focused on developing biosensors under the supervision of Professor Melissa C. Rhoten. He attended graduate school at Purdue University (West Lafayette, IN) under the mentorship of Professor Scott A. McLuckey and received a Ph.D. in Chemistry in 2013. His Ph.D. research focused on ion trap mass spectrometry (MS) instrumentation development as well as gas-phase ion/ion and ion/molecule reactions involving biopolymers. Boone then worked as a postdoctoral research fellow in Professor Richard Caprioli’s laboratory at Vanderbilt University (Nashville, TN) where he studied matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) instrumentation and applications. Specifically, he worked on Fourier transform ion cyclotron resonance (FT-ICR) and time-of-flight (TOF) MS systems and applied IMS to the study of diabetes, cancer, drug delivery, and infectious disease. Boone joined the Department of Chemistry at the University of Florida as an Assistant Professor in the fall of 2018. His research focuses on developing next-generation bioanalytical mass spectrometry to better understand the molecular basis of health and disease.

Imaging mass spectrometry is a powerful technology that enables the visualization of biochemical processes directly in tissues by combining the molecular specificity of mass spectrometry with the spatial fidelity of microscopic imaging. Especially when studying lipids, there are many isobaric and isomeric molecules that complicate spectral analysis, with each isoform having a potentially unique cellular function. While traditional tandem mass spectrometry (MS/MS) approaches can distinguish amongst these compounds in select instances, this is often not the case. Our group is developing gas-phase reactions that afford the ability to provide improved molecular specificity without manipulating the sample. These gas-phase transformations are fast, efficient, and specific, making them ideally suited for implementation into imaging mass spectrometry workflows to enable novel structural identification and separation based on chemical reactivity. While traditional analytical analyses oftentimes simply use the mass spectrometer as a detector of molecular mass, we instead use the mass spectrometer as a reaction vessel to perform unique gas-phase transformations to provide unparalleled levels of chemical resolution.

Dr. Stefani Thomas earned her BA in Biological Sciences from Dartmouth College and her PhD in Pharmaceutical Sciences from the University of Southern California. She pursued postdoctoral training in Dr. Robert Cotter’s Middle Atlantic Mass Spectrometry laboratory, conducted clinical proteomics research in the Center for Biomarker Discovery and Translation, and completed a Clinical Chemistry postdoctoral fellowship at Johns Hopkins University. She is currently an Assistant Professor, a faculty member of the Advanced Research and Diagnostics Laboratory (ARDL) and a member of the Masonic Cancer Center at the University of Minnesota. She is also the Associate Medical Director of the M Health Fairview West Bank Laboratory. Stefani's research laboratory applies discovery and targeted mass spectrometry-based proteomics methods to elucidate the biology of ovarian cancer and to identify proteome-level mechanisms of improved ovarian cancer treatment response.

I am a researcher in the Thomas lab working on identifying PARP inhibitor-induced autophagosome-associated proteins to determine the means of resistance during PARPi treatment in high-grade serous ovarian cancers.

I am a PhD student in the Microbiology, Immunology, and Cancer Biology (MICaB) program at the University of Minnesota. The goal of my research is to study the molecular mechanisms of PARP inhibition in HGSOCs containing BRCA1/2 mutations and comparing these responses to wild-type BRCA1/2 ovarian cancers. By studying the differential responses that HGSOCs have on PARP inhibition at the level of the proteome, we can ascertain which type of HGSOCs would benefit most with PARP inhibition with minimal risk of relapse. Finally, studying changes in the proteome upon PARP inhibition will reveal other sets of genes besides BRCA1/2 that are involved in homologous recombination dysfunction.

I received my Ph.D. in Biology from Kongju National University in South Korea. During my Ph.D. program, I studied in the Medical Proteomic Research Center at the Korea Research Institute of Bioscience and Biotechnology (KRIBB). In Medical Proteomics Research Center, KRIBB, I performed proteome-based approaches for mining the molecular targets and susceptibility markers of various diseases such as cancers, senescence, neurodegenerative disorder, leukemia, psoriasis and rheumatism and investigated the molecular mechanisms for deeper understanding of diseases. After I received my Ph.D., I obtained as position of a Postdoctoral Researcher in the Division of Molecular and Cellular Biology at the Hormel Institute, University of Minnesota. At the Hormel Institute, I was a proteomics and mass spectrometry specialist, and I have worked on studying the analysis of protein modification and proteome quantification for drug discovery and molecular targeting in a variety of cancers for medical research as well as on structural analysis of protein complexes with cross-linking mass spectrometry. In addition, I have studied the epigenetic modifications to understand the regulatory mechanism of epigenetic marks in the chromatin and cancer biology fields. Currently, I am a Researcher 5 in Dr. Stefani Thomas Lab at University of Minnesota. My research is focused on ovarian cancer biology using discovery and targeted mass spectrometry-based proteomics.

I am a graduate student at the University of Minnesota in the department of Biochemistry, Molecular Biology, and Biophysics under the mentorship of Dr. Stefani Thomas. My initial project is focused on a mass-spectrometry based approach to evaluate the utility of HDAC and PARP inhibitors in ovarian cancer treatment with an emphasis on determining how epigenetic modifications confer treatment sensitivity in the context of homologous recombination proficiency or deficiency. Overall, I believe my current research plan will support the development of biomedical breakthroughs improving treatment opportunities for patients with this lethal gynecological malignancy.

Lab Showcase meetings are opportunities for lab PIs and Directors to share their scientific goals and ambitions, and introduce the labs' current projects and scientists to our community.

The Thomas lab applies discovery and targeted mass spectrometry-based proteomics methods to elucidate the biology of ovarian cancer. The common theme among the current research projects in the lab is the determination of protein-based signatures of sensitivity to ovarian cancer treatment. We are excited to share summaries of the following research projects during the Lab Showcase: "Proteome-level determinants of response to PARP inhibitor treatment in ovarian cancer," "HDAC inhibitor sensitization of high-grade serous ovarian cancer cells to PARP inhibitor treatment," "Development and validation of targeted mass spectrometry assays to detect ovarian cancer protein biomarkers," and "Longitudinal proteome alterations in high-grade serous ovarian cancer patient-derived xenografts."

I grew up in San Diego, CA and Arlington, VA. I attended Santa Clara University where I received a B.S. in chemistry. I joined the MD PhD program at UCSD in 2007 and completed a PhD in Biomedical Sciences with a specialization in Anthropogeny. I continued at UCSD for residency training in internal medicine and completed a year as chief resident in 2019-2020. In June of 2020, I started my Endocrinology Fellowship. I plan to pursue a career in academic medicine that combines clinical endocrinology with outcomes research in Vitamin D metabolism.

Using the MrOS database and mass spectrometry, we demonstrate that 1,25(OH)2 Vitamin D, 24,25(OH)2 Vitamin D, and their associated metabolite ratios are associated with gut microbial diversity in older community dwelling men. Notably, 25(OH) Vitamin D levels did not show this association. We also demonstrate that firmicutes which frequently produce butyrate are associated with higher levels of activated Vitamin D. Overall, the project demonstrates that quantifying Vitamin D metabolites may provide more clinically relevant measures of Vitamin D metabolism.

Vitamin D metabolites and the gut microbiome in older men

Chris Shuford, Ph.D., is Associate Vice President and Technical Director for research and development at Laboratory Corporation of America in Burlington, North Carolina. Chris received his B.S. in Chemistry & Physics at Longwood University and obtained his Ph.D. in Bioanalytical Chemistry from North Carolina State University under the tutelage of Professor David Muddiman, where his research focused on applications of nano-flow chromatography for multiplexed peptide quantification using protein cleavage coupled with isotope dilution mass spectrometry (PC-IDMS). In 2012, Chris joined LabCorp’s research and development team where his efforts have focused on development of high-flow chromatographic methods (>1 mL/min) for multiplexed and single protein assays for clinical diagnostics.

The Michael S. Bereman Award for Innovative Clinical Proteomics recognizes recent innovations in clinical proteomics from early- and mid-career scientists. The awardee is honored at the annual meeting of MSACL, where they will be invited to give a lecture. Nominees will be reviewed annually by a rolling award committee.

The 2021 Awardee of the Michael S. Bereman Award for Innovative Clinical Proteomics is Christopher Shuford, Ph.D. for groundbreaking work on calibration and sensitivity.

Dr. Shuford will accept this award with a presentation : Breakthrough or Bust? Thyroglobulin Measurement by LC-MS/MS.

Proteolysis-aided workflows can effectively eliminate autoantibody complexes and allow for interference-free protein quantification by mass spectrometry with surrogate peptides. Owing to the prevalence of autoantibodies in thyroid cancer patients and associated interference among immunoassay platforms, the purported poster child for mass spectrometry-based protein measurements has been Thyroglobulin (Tg). However, many other factors contribute to the utility of measurement procedures for tumor makers such as Tg, including throughput, ruggedness, trueness, and sensitivity. This presentation will focus on these limitations – real or perceived – as it pertains to application of mass spectrometry measurements for Tg.

This year's Michael S. Bereman Award for Innovative Clinical Proteomics is proudly sponsored by Agilent with an MSACL Open Educational Grant Fund donation of $10,000. The MSACL Open Educational Grant program provides awards to early and mid-career community members to fund conference and short course attendance.