Title : Secretion of
heparanase protein is regulated by glycosylation in human tumor cell lines
Abstract :
- The endo-beta-d-glucuronidase, heparanase , is capable of specifically degrading heparan sulfate, and this activity is associated with the metastatic potential of tumor cells
- The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites ; however, the precise biochemical role of glycosylated heparanase remains unknown
- In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines
- Heparanase protein was glycosylated at six Asn residues in human tumor cell lines
- Treatment with a glycosylation inhibitor demonstrated that glycosylation was not required for the activity of heparanase
- However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. N-glycosylation, , -, -, sites
- 2. glycosylated, , heparanase, -, -
- 3. glycosylation, , heparanase, -, -
- 4. glycosylated, , Heparanase protein, -, Asn residues
- 5. glycosylation, , heparanase, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):