Poster Presentation HUPO 2019 - 18th Human Proteome Organization World Congress

Profiling of intact N-linked glycopeptides in the rat brain (#701)

Jialin Liu 1 , Yi Wan 2 , Pengyuan Yang 1 , Xing Chen 2
  1. IBS, Fudan university, Shanghai, China
  2. College of Chemistry and Molecular Engineering, Peking university, Beijing, China

Protein N-linked glycosylation plays a key role in various biological and pathological processes in the brain. Interestingly, different brain cells such as neurons and astrocytes can have distinct N-glycosylation patterns. However, it remains challenging to analyze brain N-glycosylation in a cell-type specific manner. Here we report the glycoproteomic studies of N-linked glycosylation in primary rat neurons and astrocytes. By combining primary brain cell culture and mass spectrometry-based analysis of intact glycopepties, we identified 6461 glycopeptides, 1684 glycosides and 770 glycoproteins, including 144 sialic acid glycoproteins.  These N-linked glycosylated proteins are highly enriched in cell communication and adhesion. Profiling of intact glycopeptides provides a powerful tool for investing the biological function of brain glycosylation.

  1. P. Fang, X. Wang, Y. Xue, M. Liu, et al., In-depth mapping of the mouse brain Nglycoproteome reveals widespread N-glycosylation of diverse brain proteins, Oncotarget 7 (2016) 38796–38809