Heparanase is an endoglycosidase that degrades heparan sulfate (HS) in the extracellular matrix (ECM) and cell surfaces, and fulfills a significant role in cancer metastasis and angiogenesis.
Heparanase (HPSE), as the only enzyme which can degrade the extracellular matrix and heparin sulfate in basement membrane, plays an important role in invasion and metastasis of tumor cells.
Heparanase, the sole heparan sulfate (HS) degrading endoglycosidase, regulates multiple biological activities that enhance tumor growth, metastasis, angiogenesis, and inflammation.
Heparanase is an endoglycosidase that can degrade extracellular matrix by cleaving heparan sulfate chains of heparan sulfate proteoglycan, thus playing important roles in the invasion and metastasis of human cancers.
Multivariate analyzes revealed that heparanase mRNA overexpression was a significant independent risk factor for hematogenous metastasis in colorectal cancer.
In conclusion, our results suggest that HPSE contributes to the proliferation and metastasis of NPC, and HPSE may be a potent molecular target for NPC treatment.
Cloning of the heparanase gene enables the development of specific molecular probes for early detection and treatment of cancer metastasis and autoimmune disorders.
In colon carcinoma, heparanase shows increased expression in tumor compared to normal tissue and its expression correlates with the presence of metastasis.
Our study demonstrated that high-level expression of HPA in cervical cancer was involved in LN metastasis, further impacting on patients' long-term survival.
Heparanase is overexpressed by tumor cells and degrades the extracellular matrix proteoglycans through cleavage of heparan sulfates (HS), allowing pro-angiogenic factor release and thus playing a key role in tumor angiogenesis and metastasis.
Our study implies that the expression of heparanase protein and mRNA is associated with bladder cancer invasion and metastasis, and heparanase may have a role in disease progression.
We analyzed the rate of apoptosis using TDT-mediated dUTP-biotin nick end-labeling (TUNEL), p53 and heparanase in 73 patients with tongue cancer by immonohistochemistry, and tested data for correlation with survival, tumor size, grade and metastasis.
Notably, although heparanase inhibitors attenuated tumor progression and metastasis in several experimental systems, other studies revealed that heparanase also functions in an enzymatic activity-independent manner.
Preclinical experiments have found heparanase inhibitors to substantially reduce tumor growth and metastasis, leading to clinical trials with heparan sulfate mimetics.
Heparanase is an endo-beta-D-glucuronidase involved in extracellular matrix remodeling and degradation and implicated in tumor metastasis, angiogenesis, inflammation, and autoimmunity.