Seer's Proteograph™ Product Suite identifies undiscovered links between protein variants and lung cancer progression
REDWOOD CITY, Calif., March 29, 2023 (GLOBE NEWSWIRE) -- Seer Inc. (NASDAQ: SEER), a life sciences company commercializing a disruptive new platform for proteomics, today announced a new scientific publication in PLOS One demonstrating the unmatched utility of the Proteograph Product Suite to uncover novel insights in human health and disease with deep, unbiased proteomics.
Scientists from Seer in collaboration with Luis Diaz, M.D. from Memorial Sloan Kettering Cancer Center found previously unknown associations between four protein isoforms and non-small cell lung cancer (NSCLC) progression, constituting potential novel, disease-relevant biomarkers, or therapeutic targets. Importantly, the identified NSCLC-associated protein isoforms comprise structural variants of proteins that arise from distinct but related mRNAs produced from the same gene through the process of alternative splicing. Different protein isoforms can have distinct roles in biology, influencing disease predisposition and progression. Notably, discovery and quantification of such protein variants in a complex biological sample requires deep, unbiased interrogation of the proteome at peptide-level resolution.
“These findings demonstrate that distinct protein isoforms may differentially contribute to diverse biological mechanisms and to the pathogenesis of cancers, potentially paving the road to identify new diagnostic markers or new therapeutic targets,” said Dr. Diaz, Head of the Division of Solid Tumor Oncology at Memorial Sloan Kettering Cancer Center. “What is especially encouraging here is that these protein isoforms were detected in plasma, a readily accessible sample type, enabling cancer detection and monitoring through liquid biopsy evaluation of patients.”
The researchers found that the short protein isoform of bone morphogenetic protein 1 (BMP1) occurred more frequently in NSCLC patients compared with healthy participants, and with even greater abundance in patients with late-stage cancer, suggesting that this isoform of BMP1 may play a role in NSCLC progression. BMP1 is involved in collagen processing, and the short isoform of the protein lacks the ability to release collagen, which could impact the tumor microenvironment.
The study analyzed 188 plasma proteomes from NSCLC patients and controls to identify disease-associated protein isoforms. In addition to BMP1, the analysis revealed three other protein isoforms with significant diffeential behavior in NSCLC when compared to healthy controls: complement component 4a (C4a), complement component 1r (C1r) and lactate dehydrogenase B (LDHB).
“This study, which found disease-associated protein isoforms in NSCLC, could only have been achieved using an unbiased peptide-level approach that provides a deeper, more nuanced view of the human proteome,” said Asim Siddiqui, Senior Vice President of Research at Seer. “These findings demonstrate the power of unbiased proteomics to discover novel biology, especially in the context of cancer, that may otherwise be missed by genomics or targeted proteomics.”
Further research is necessary to validate the utility of these protein isoforms as novel biomarkers for NSCLC, or even new therapeutic targets.
Seer’s Proteograph Product Suite enables proteomics studies with an unprecedented combination of speed, scale, depth, and breadth of data, allowing an unbiased interrogation of the proteome to allow studies not previously possible. Seer’s proprietary engineered nanoparticles deliver reproducible performance across samples, labs, and experiments, providing peptide level information that is key to identifying protein variants. The accompanying Proteograph Analysis Suite offers cloud-scalable software for proteomic data analysis, visualization, and generation of biological insights. The Proteograph Product Suite makes it easy to add unbiased, deep, rapid proteomics studies at scale to any lab.
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