Quantitative N-Glycoproteomic Analysis of Cattle-Yak and Yak Longissimus Thoracis

In this study, the N-glycosylated protein profiles ofcattle-yak longissimus thoracis (CYLT) and yak longissimusthoracis (YLT) were comparatively analyzed using quantitativeproteomics techniques. A total of 76 differential N-glycosylated proteins(DGPs) were screened from 181 quantified N-glycoproteins, indicatingthat differences in N-glycosylation levels are key to the differencesbetween CYLT and YLT. In particular, a variety of N-glycoproteinsinvolved in the extracellular matrix were differentially N-glycosylatedbetween CYLT and YLT, mainly including fibrillin-1, fibromodulin,collagen, and laminins. In addition, the N-glycosylation levels ofseveral lysosomal-related proteolytic enzymes (cathepsin D, dipeptidylpeptidase 1, legumain, and aminopeptidases, etc.) were significantlyhigher in CYLT. These results indicated that the N-glycosylation ofCYLT and YLT proteins plays a crucial role in the regulation of extracellularmatrix organization (muscle fiber structure) and lysosomal activity(postmortem meat tenderness). The results remind us that posttranslationmodifications, especially N-glycosylation, are still icebergs beneaththe surface.

Automated summary

In this study, the N-glycosylated protein profiles of cattle-yak longissimus thoracis (CYLT) and yak longissimus thoracis (YLT) were compared using quantitative proteomics techniques. Differential N-glycosylated proteins (DGPs) were screened from the quantified N-glycoproteins, indicating the key role of N-glycosylation levels in the differences between CYLT and YLT. The findings highlight the importance of N-glycosylation in regulating extracellular matrix organization and lysosomal activity.