Mass Spectrometry Facility

Lauren Ball and Baylye Boxall-Burnette in Mass Spectrometry Core Facility

The MUSC Mass Spectrometry Facility provides expertise, services, education, and state-of-the-art instrumentation to enhance biomedical research endeavors through LC-MS/MS-based proteomics. Services are offered for protein identification; characterization of post-translational modifications; and quantitative proteomics to identify differentially expressed/degraded proteins, regulated sites of post-translational modification, protein-protein interactions, and protein targets of drugs identified in phenotypic screens. Analyses include sample preparation, LC-MS/MS, database searching, generation of reports, and assistance with data interpretation. Faculty and staff assist with experimental design and the development/optimization of customized methodology for analysis of post-translationally modified peptides (e.g. phosphorylation and O-GlcNAc modification, N- and O-linked glycosylation, Cys modifications including S-glutathionylation, and glycation of Lys and Arg). Quantitative approaches including metabolic labeling (SILAC), isobaric tagging (iTRAQ/TMT), and label free proteomics (LFQ) are performed on the Orbitrap Elite or Orbitrap Fusion Lumos Mass Spectrometers. We are developing methodology to identify alterations in post-translational modifications that impact signal transduction, transcription, translation, and the response to therapeutics with the goal of enabling investigators to discover molecular mechanisms underlying disease progression and therapeutic response.

Recent Publications

The following are recent publications that utilized the Orbitrap Elite ETD or the *Orbitrap Fusion Lumos Mass Spectrometer:

Nimitvilai, S., Uys, J. D., Woodward, J. J., Randall, P. K., Ball, L. E., Williams, R. W., Jones, B. C., Lu, L., Grant, K. A., & Mulholland, P. J. (2017). Orbitofrontal Neuroadaptations and Cross-Species Synaptic Biomarkers in Heavy-Drinking Macaques. The Journal of neuroscience : the official journal of the Society for Neuroscience, 37(13), 3646–3660.

Uys, J. D., McGuier, N. S., Gass, J. T., Griffin, W. C., 3rd, Ball, L. E., & Mulholland, P. J. (2016). Chronic intermittent ethanol exposure and withdrawal leads to adaptations in nucleus accumbens core postsynaptic density proteome and dendritic spines. Addiction biology, 21(3), 560–574.

Hurst, K. E., Lawrence, K. A., Robino, R. A., Ball, L. E., Chung, D., & Thaxton, J. E. (2020). Remodeling Translation Primes CD8+ T-cell Antitumor Immunity. Cancer immunology research, 8(5), 587–595.

Zhang, L., Zhang, J., Ye, Z., Manevich, Y., Ball, L. E., Bethard, J. R., Jiang, Y. L., Broome, A. M., Dalton, A. C., Wang, G. Y., Townsend, D. M., & Tew, K. D. (2019). Isoflavone ME-344 Disrupts Redox Homeostasis and Mitochondrial Function by Targeting Heme Oxygenase 1. Cancer research, 79(16), 4072–4085.

Angel, P. M., Schwamborn, K., Comte-Walters, S., Clift, C. L., Ball, L. E., Mehta, A. S., & Drake, R. R. (2019). Extracellular Matrix Imaging of Breast Tissue Pathologies by MALDI-Imaging Mass Spectrometry. Proteomics. Clinical applications, 13(1), e1700152.

Angel, P. M., Comte-Walters, S., Ball, L. E., Talbot, K., Mehta, A., Brockbank, K. G. M., & Drake, R. R. (2018). Mapping Extracellular Matrix Proteins in Formalin-Fixed, Paraffin-Embedded Tissues by MALDI Imaging Mass Spectrometry. Journal of proteome research, 17(1), 635–646.

Kim, M. J., Vargas, M. R., Harlan, B. A., Killoy, K. M., Ball, L. E., Comte-Walters, S., Gooz, M., Yamamoto, Y., Beckman, J. S., Barbeito, L., & Pehar, M. (2018). Nitration and Glycation Turn Mature NGF into a Toxic Factor for Motor Neurons: A Role for p75NTR and RAGE Signaling in ALS. Antioxidants & redox signaling, 28(18), 1587–1602.

Nagel, A. K., & Ball, L. E. (2014). O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells. Molecular & cellular proteomics : MCP, 13(12), 3381–3395. *Article featured on journal cover and website.

Nagel, A. K., Schilling, M., Comte-Walters, S., Berkaw, M. N., & Ball, L. E. (2013). Identification of O-linked N-acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation. Molecular & cellular proteomics : MCP, 12(4), 945–955.

Song, J. H., Padi, S. K., Luevano, L. A., Minden, M. D., DeAngelo, D. J., Hardiman, G., Ball, L. E., Warfel, N. A., & Kraft, A. S. (2016). Insulin receptor substrate 1 is a substrate of the Pim protein kinases. Oncotarget, 7(15), 20152–20165.

Kruyer, A., Ball, L. E., Townsend, D. M., Kalivas, P. W., & Uys, J. D. (2019). Post-translational S-glutathionylation of cofilin increases actin cycling during cocaine seeking. PloS one, 14(9), e0223037.

Zhang, J., Ye, Z. W., Chen, W., Manevich, Y., Mehrotra, S., Ball, L., Janssen-Heininger, Y., Tew, K. D., & Townsend, D. M. (2018). S-Glutathionylation of estrogen receptor α affects dendritic cell function. The Journal of biological chemistry, 293(12), 4366–4380.

Pehar, M., Ball, L. E., Sharma, D. R., Harlan, B. A., Comte-Walters, S., Neely, B. A., & Vargas, M. R. (2016). Changes in Protein Expression and Lysine Acetylation Induced by Decreased Glutathione Levels in Astrocytes. Molecular & cellular proteomics : MCP, 15(2), 493–505.

Williams, G. R., Bethard, J. R., Berkaw, M. N., Nagel, A. K., Luttrell, L. M., & Ball, L. E. (2016). Exploring G protein-coupled receptor signaling networks using SILAC-based phosphoproteomics. Methods (San Diego, Calif.), 92, 36–50.