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 (HPSE) is the only functional mammalian endoglycosidase whose activity correlates with cancer metastasis, angiogenesis, and the reduced postoperative survival of cancer patients, making it an active target for anticancer therapeutics.
Endoglycosidic heparanase degrades heparan sulfate glycosaminoglycans, and may be important in cancer invasion and metastasis, although its expression in human epithelial ovarian cancer has not been characterized.
Heparanase, a mammalian endo‑D‑glucuronidase, is involved in degradation of the extracellular matrix (ECM), and thus promotes tumor progression and metastasis.
Over-expression of circHIPK3 effectively inhibits migration, invasion, and angiogenesis of bladder cancer cells <i>in vitro</i> and suppresses bladder cancer growth and metastasis <i>in vivo</i> Mechanistic studies reveal that circHIPK3 contains two critical binding sites for the microRNA miR-558 and can abundantly sponge miR-558 to suppress the expression of heparanase (HPSE).