Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
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Simizu S, Ishida K, Wierzba MK, Osada H
Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
J Biol Chem. 2004 Jan 23;279(4):2697-703. Epub 2003 Oct 22.
- PubMed ID
- 14573609 [ View in PubMed]
- 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.