Key result
Automated in-solution proteolysis identified 92 Lipoprotein(a)-associated proteins compared to 55 with in-gel digestion, revealing a shared core proteome of 34 proteins.
Absolute Event Rate: 92% vs 55%
The identified proteome of Lipoprotein(a) is highly dependent on the analytical method used, though a core set of 34 proteins is consistently detected across methods.
Background: Lipoprotein(a) [Lp(a)] is a genetically determined risk factor for atherosclerotic cardiovascular disease (ASCVD). Proteomic studies suggest that Lp(a)-associated proteins mediate inflammation, thrombosis, and vascular calcification, but methodological variability may influence proteome definition. Methods: Lp(a) was immunoprecipitated from human plasma using an apo(a)-specific monoclonal antibody and analyzed by mass spectrometry following either in-gel digestion or automated in-solution proteolysis. Proteins identified by ≥3 unique peptides and consistently detected across all samples by both methods were considered high confidence. Functional enrichment and interaction networks were assessed using STRING. Results: In-solution proteolysis identified 92 proteins and in-gel digestion identified 55 proteins, with 34 proteins shared between methods. These high-confidence proteins were enriched for pathways involved in lipoprotein remodeling, coagulation regulation, vesicle-mediated transport, lipid binding, and extracellular matrix organization, providing biological insight into mechanisms linking Lp(a) to inflammation, thrombosis, and calcification. Conclusions: Proteome composition of Lp(a) is method-dependent; however, a rigorously defined core proteome of 34 proteins was consistently identified across analytical approaches, highlighting biologically relevant pathways that may underlie Lp(a)-mediated ASCVD risk.
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Matienzo et al. (2026) studied Atherosclerotic cardiovascular disease. Automated in-solution proteolysis vs. In-gel digestion was evaluated on Proteins identified. Automated in-solution proteolysis identified 92 Lipoprotein(a)-associated proteins compared to 55 with in-gel digestion, revealing a shared core proteome of 34 proteins.
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