RRC ID 40060
Author Simizu S, Ishida K, Wierzba MK, Osada H.
Title Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
Journal J Biol Chem
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.
Volume 279(4)
Pages 2697-703
Published 2004-1-23
DOI 10.1074/jbc.M300541200
PII M300541200
PMID 14573609
MeSH Cell Line, Tumor Glucuronidase / metabolism* Glycosylation Humans Neoplasms / enzymology* Neoplasms / metabolism Protein Transport
IF 4.238
Times Cited 51
DNA material pcDNA3.1/Myc-His(+)-Heparanase(HP) (RDB14252) pcDNA3.1/Myc-His(+)-HP/N162Q (RDB14253) pcDNA3.1/Myc-His(+)-HP/N178Q (RDB14254) pcDNA3.1/Myc-His(+)-HP/N200Q (RDB14255) pcDNA3.1/Myc-His(+)-HP/N217Q (RDB14256) pcDNA3.1/Myc-His(+)-HP/N238Q (RDB14257) pcDNA3.1/Myc-His(+)-HP/N459Q (RDB14258.