Journal
CONNECTIVE TISSUE RESEARCH
Volume 49, Issue 3-4, Pages 207-210Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/03008200802143281
Keywords
heparanase; heparan sulfate; metastasis; angiogenesis; enzymatic and nonenzymatic functions
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Funding
- NCI NIH HHS [R01-CA106456] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA106456] Funding Source: NIH RePORTER
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Mammalian heparanase, an endoglycosidase-degrading heparan sulfate, is synthesized as a latent 65 kDa precursor that undergoes proteolytic processing, primarily by cathepsin-L, yielding 8 kDa and 50 kDa subunits that heterodimerize to form a highly active enzyme. Enhanced heparanase expression in human tumors correlates with metastatic potential, tumor vascularity, and reduced postoperative survival of cancer patients, attributed to enzymatic and nonenzymatic activities of the heparanase protein. Urinary and plasma levels of heparanase are elevated in cancer patients and suppressed in response to effective anticancer treatments. These observations and the anticancerous effect of heparanase gene silencing and of heparanase-inhibiting molecules suggest that the enzyme is a promising target for anticancer drug development.
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