Title : Identification of N-glycosylation
sites on secreted
proteins of human hepatocellular carcinoma cells with a complementary proteomics approach
Abstract :
- N-linked glycosylation is prevalent in proteins destined for extracellular environments; nearly all secreted proteins are glycosylated
- However, with respect to their glycosylation sites , little attention has been paid
- Here, we report the analysis of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells
- For the enrichment of glycopeptides , capture methods with hydrophilic affinity (HA) and hydrazide chemistry (HC) were used complementarily
- With the use of both methods in combination with nano-LC- ESI-MS/MS analysis, 300 different glycosylation sites within 194 unique glycoproteins were identified, and 172 glycosites have not been determined experimentally previously
- A direct comparison between HA and HC methods was also investigated for the first time
- In brief, in terms of selectivity for glycopeptides , HC is superior to HA (92.9% vs 51.3%); however, based on the number of glycosites identified, HA outweighs HC (265 vs 159)
- Furthermore, unavoidable contaminants such as actin and bovine serum albumin which are not N-glycosylated could be easily depleted by using this glycoproteomic strategy
- As a consequence, more low-abundance and genuinely secreted proteins were identified
- Among the glycoproteins identified, alpha-fetoprotein , CD44 and laminin have been reported to be implicated in HCC and its metastasis
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. N-glycosylation, , -, -, sites
- 1. glycosylated, , -, all secreted proteins, -
- 10. glycoproteins, , glycoproteins, -, -
- 2. glycosylation, , -, -, sites
- 3. N-glycosylation, , -, -, sites
- 4. glycopeptides, , -, -, glycopeptides
- 5. glycoproteins, , glycoproteins, -, -
- 5. glycosites, , -, -, glycosites
- 5. glycosylation, , -, -, sites
- 7. glycopeptides, , -, -, glycopeptides
- 7. glycosites, , -, -, glycosites
- 8. N-glycosylated, , albumin, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):