Non-small cell lung cancer (NSCLC) is the leading cause of cancer-related deaths worldwide. Although immunotherapy has improved the treatment of NSCLC, a significant number of patients still fail to respond or develop resistance.
Veronica G. Anania, Kebing Yu, Francesco Pingitore, Qingling Li, Christopher M. Rose, Peter Liu, Wendy Sandoval, Ann E. Herman, Jennie R. Lill, and W. Rodney Mathews. Journal of Proteome Research.
Lupus nephritis (LN) is a severe clinical manifestation of systemic lupus erythematosus (SLE) associated with significant morbidity and mortality. Assessment of severity and activity of renal involvement in SLE requires a kidney biopsy, an invasive procedure with limited prognostic value. Noninvasive biomarkers are needed to inform treatment decisions and to monitor disease activity. Proteinuria is associated with disease progression in LN; however, the composition of the LN urinary proteome remains incompletely characterized. To address this, we profiled LN urine samples using complementary mass spectrometry-based methods: protein gel fractionation, chemical labeling using tandem mass tags, and data-independent acquisition. Combining results from these approaches yielded quantitative information on 2573 unique proteins in urine from LN patients. A multiple-reaction monitoring (MRM) method was established to confirm eight proteins in an independent cohort of LN patients, and seven proteins (transferrin, α-2-macroglobulin, haptoglobin, afamin, α-1-antitrypsin, vimentin, and ceruloplasmin) were confirmed to be elevated in LN urine compared to healthy controls. In this study, we demonstrate that deep mass spectrometry profiling of a small number of patient samples can identify high-quality biomarkers that replicate in an independent LN disease cohort. These biomarkers are being used to inform clinical biomarker strategies to support longitudinal and interventional studies focused on evaluating disease progression and treatment efficacy of novel LN therapeutics.
The novel particle-based P2 Plasma Enrichment System achieves the highest reported proteome enrichment with greater reproducibility than any other protein corona-based workflow. The optimized single-well sample preparation, combined with optimized particle surface, stabilizes the labile protein corona and provides exceptional quantitative accuracy.
The brochure provides an overview of the key features and benefits of our next-generation TrueDiscovery™ platform. In addition, it elaborates on our deep and reproducible proteome, phospho- and immune-proteome quantification and analysis. Finally, it digs into how we identify the most promising and actionable biomarkers for research and clinical decision-making.
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