Secretion of Heparanase Protein Is Regulated by Glycosylation in Human Tumor Cell Lines

Siro Simizu, Keisuke Ishida, Michal K. Wierzba, Hiroyuki Osada

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

The endo-β-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.

Original languageEnglish
Pages (from-to)2697-2703
Number of pages7
JournalJournal of Biological Chemistry
Volume279
Issue number4
DOIs
Publication statusPublished - 2004 Jan 23
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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