Proteomics analysis of porcine endothelial cells revealed 29 proteins highly expressed and 25 less expressed in the aortic valve compared to the endocardial endothelium.
The variations in the protein profile of aortic-valvular (AVE) and endocardial endothelial (EE) cells are currently unknown. The current study’s objective is to identify differentially expressed proteins and associated pathways in both the endothelial cells. We used endothelial cells isolated from the porcine (Sus scrofa) aortic valve and endocardium for the profiling of proteins. Label-free proteomics was performed by liquid chromatography-tandem mass spectrometry (LC-MS/MS). Our proteomics analysis revealed that 29 proteins were highly expressed, and 25 proteins were less expressed in the valve than the endocardial endothelium. The cell surface markers, such as CD63, ICAM1, PECAM1, PROCR, and TFRC, were highly expressed in EE. In contrast, CD44 was highly expressed in AVE. The pathway analysis showed that metabolic process-related proteins and extracellular matrix-related proteins were enriched in valves. Differential enrichment of signaling pathways was observed in the endocardium. The hemostasis function-related proteins were increased in both endothelial cells. The proteins and pathways enriched in aortic-valvular and endocardial endothelial cells revealed the distinct phenotype of these two closely related cells.
Kumar et al. (Tue,) reported a other. Label-free proteomics by LC-MS/MS vs. Aortic-valvular endothelium vs endocardial endothelium was evaluated on Differentially expressed proteins and associated pathways. Proteomics analysis of porcine endothelial cells revealed 29 proteins highly expressed and 25 less expressed in the aortic valve compared to the endocardial endothelium.