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Glycosylation plays essential roles in many neurological functions including brain development, synaptic formation, and synaptic transmission. Previous studies have shown that aberrant glycosylation is associated with neurodegenerative diseases, including Parkinson's disease (PD) and Alzheimer's disease (AD). However, brain glycome is not well explored due to the lack of sensitive analytical tools in spite of its biological significance. The AGRS has developed a novel analytical platform for rapid profiling and quantitation of glyco-conjugates such as protein-bound glycans and lipid-bound glycans found in brain tissues. Ultimately, the AGRS will achieve the construction of organ (or tissue) specific brain glycome map and library for better understanding of brain function related to aging, development, and neurological disorders.

Research highlights:
  • Development of analytical techniques for extraction and enrichment of glyco-conjugates from brain tissues
  • Comprehensive glycome profiling of organ (or tissue)-specific brain
  • Discovery and identification of novel glycans found in human brain
  • Structure characterization of isomer-specific LC/MS/MS analysis
  • Construction of brain glycome library (database)
  • Regional mouse brain glycome mapping
  • Monitoring the change of glycosylation according to human developmental stages
Relevant publications:
  • Kim, J.A., Kim, D., Won, S.Y., Han, K.A., Park, D., Cho, E., Yun, N., An, H.J., Um, J.W., Kim, E., Lee, J.O., Ko, J., Kim, H.M., “Structural Insights into Modulation of Neurexin-Neuroligin Trans-synaptic Adhesion by MDGA1/Neuroligin-2 Complex”, Neuron, 2017, 94(6), 1121–1131.
  • Park, J.S., Ji, I.J., Kim, D.H., An, H.J., Yoon, S.Y., “The Alzheimer's Disease-Associated R47H Variant of TREM2 Has an Altered Glycosylation Pattern and Protein Stability”, Frontiers in Neuroscience, 2017, 10.
  • Ji, I.J., Hua, S., Shin, D.H., Seo, N.R., Hwang, J.Y., Jang, I.S., Kang, M.G., Choi, J.S., and An, H.J., “Spatially-Resolved Exploration of the Mouse Brain Glycome by Tissue Glyco-Capture (TGC) and Nano-LC/MS”, Analytical Chemistry, 2015, 87(5), 2869–2877.
  • Park, J.S., Ji, I.J., An, H.J., Kang, M.J., Kang, S.W., Kim, D.H., Yoon, S.Y., “Disease-Associated Mutations of TREM2 Alter the Processing of N-Linked Oligosaccharides in the Golgi Apparatus”, Traffic, 2015, 16(5), 510-518.
  • Hua, S., Saunders, M., Dimapasoc, L.M., Jeong, S.H., Kim, B.J., Kim, S., So, M., Lee, K.S., Kim, J.H., Lam, K.S., Lebrilla, C.B., An, H.J., “Differentiation of Cancer Cell Origin and Molecular Subtype by Plasma Membrane N-glycan Profiling”, Journal of Proteome Research, 2014, 13(2), 961–968.