Background
Novel findings in biochemical characteristics of placenta can bring new insight for further studies on the potential markers of physiological/pathological pregnancy or function of placenta. In this study, we compared the proteome of dairy cow placenta enzymatic hydrolysis by different proteases using a label-free mass spectrometry approach.
Results
In total, 541, 136 and 86 proteins were identified in trypsin group (TRY), pepsin group (PEP) and papain group (PAP), respectively. 432 differentially expressed proteins (DEPs) were identified between the proteomes of PAP and TRY. 421 DEPs were identified between PEP and TRY, while 136 DEPs were identified between PEP and PAP. Further analysis of the up-regulated DEPs and down-regulated DEPs of each comparison showed the proteins identified by papain are mostly derived from extracellular matrix and collagen and enriched in relaxin signaling pathway, advanced glycation end products-receptor of advanced glycation end products (AGE-RAGE) signaling pathway in diabetic complications. Moreover, pepsin digestion resulted in more muscle-related proteins, which enriched in lysosome, platelet activation, cardiac muscle contraction,bacterial invasion of epithelial cell and small cell lung cancer. Trypsin mainly enzymatically degrades extracellular matrix, blood particles, and cell surface proteins which enriched in arginine and proline metabolism, olfactory transduction proteasome, protein processing in endoplasmic reticulum, pyruvate metabolism and arrhythmogenic right ventricular cardiomyopathy (ARVC).
Conclusions
In summary, these data provide insights into the selection of protease in dairy cow placenta proteomics.