Title : Biological Importance of Glycosylation
Abstract :
- Glycosylation is key for the stability and solubility of secreted and membrane proteins
- It is the most complex post-translational modification (31) and mediates extracellular matrix network assembly, cell–cell interactions, and cell–matrix interactions
- Unlike polynucleotides and polypeptides , which have a linear structure, sugars tend to be arranged in branched polymers, resulting in an exponential increase of possible polysaccharide combinations
- Theoretically, just six monosaccharides can give rise to 1012 different glycan structures
- This high diversity of protein-bound glycans requires a combination of different techniques
- For example, new MS-based methods were developed to profile the cell surface N-glycoproteome as a differentiation marker for stem cells (32)
- We applied a combination of different glycoproteomics techniques to further enrich for secreted and shed membrane proteins and reveal potential glycosylation sites within the endothelial secretome
- Glyco proteins play important roles in many biological processes related to ECs, such as angiogenesis, in which the structural change of the glycans will determine the attachment property of cells and influence cell-to-cell interactions (33)
- Interestingly, vWF is a glycoprotein produced uniquely by ECs and megakaryocytes
- Previous publications investigating vWF isolated from plasma failed to identify glycosylation sites within the propeptide (29)
- In plasma, the concentration of the propeptide is about one-tenth of the concentration of mature vWF (34, 35)
- In the conditioned medium of ECs, however, we observed several glycopeptides of the propeptide
- Thus, the endothelial secretome allowed us to interrogate the glycosylation sites of von Willebrand antigen 2, the N-terminal cleavage product of vWF that aids N-terminal multimerization and protein compartmentalization of mature vWF in storage granules
Output (sent_index, trigger,
protein,
sugar,
site):
- 10. glycosylation, , -, -, sites
- 12. glycopeptides, , -, -, glycopeptides
- 12. glycopeptides, , -, -, propeptide
- 13. glycosylation, , -, -, sites
- 7. glycosylation, , -, -, sites
- 9. glycoprotein, , Interestingly, vWF, -, -
- 9. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):