Related Experiment Video
Updated: Apr 25, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
Synthesis, Processing, and Function of N-glycans in N-glycoproteins
1Department of Neuroscience and Regenerative Medicine, Medical College of Georgia, Georgia Regents University, 1120 15th Street Room CA4012, Augusta, GA, 30912, USA, ebieberich@gru.edu.
Abstract:
Many membrane-resident and secrected proteins, including growth factors and their receptors, are N-glycosylated. The initial N-glycan structure is synthesized in the endoplasmic reticulum (ER) as a branched structure on a lipid anchor (dolichol pyrophosphate) and then co-translationally, "en bloc" transferred and linked via N-acetylglucosamine to asparagine within a specific N-glycosylation acceptor sequence of the nascent recipient protein. In the ER and then the Golgi apparatus, the N-linked glycan structure is modified by hydrolytic removal of sugar residues ("trimming") followed by re-glycosylation with additional sugar residues ("processing") such as galactose, fucose, or sialic acid to form complex N-glycoproteins. While the sequence of the reactions leading to biosynthesis, "en bloc" transfer and processing of N-glycans is well investigated, it is still not completely understood how N-glycans affect the biological fate and function of N-glycoproteins. This review discusses the biology of N-glycoprotein synthesis, processing, and function with specific reference to the physiology and pathophysiology of the nervous system.
Related Concept Videos
Protein Glycosylation
Glycosylation occurs in...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Proteoglycans
Biosynthesis of Polysaccharides
Matrix Proteoglycans and Glycoproteins
Glycosaminoglycans
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...

