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Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Gene References into Functions
IL17A and HPSE may promote tumor angiogenesis and cell proliferation and invasion in cervical cancer, possibly via the NF-kappaB signaling pathway. PMID: 30066843
Data report that mammary gland branching morphogenesis is increased in MMTV-HSPE and MMTV-8c (HSPE c-terminal)mice. Also, the growth of tumors generated by mouse breast cancer cells and the resulting lung metastases are enhanced in MMTV-HPSE mice, thus supporting the notion that HPSE contributed by the tumor microenvironment plays a decisive role in tumorigenesis. PMID: 28916201
Results find that anti-myeloma chemotherapy dramatically stimulates secretion of exosomes and alters exosome composition. Exosomes secreted during therapy contain high levels of heparanase on their surface that can degrade ECM and also can be transferred to both tumor and host cells, altering their behavior in ways that may enhance tumor survival and progression. PMID: 28888912
Knockdown of heparanase suppressed proliferation, invasion, and tube formation but induced apoptosis in trophoblasts. PMID: 29849826
This study showed that heparanase mRNA in PBMC and activity in plasma are closely correlated with therapeutic responsiveness and survival time; therefore, heparanase level in blood might be a sensitive but non-specific marker to monitor patients' response to anticancer treatment and to predict survival. PMID: 29153700
this is the first study to demonstrate that heparanase is involved in the pathogenesis of AP. PMID: 28386074
Heparanase procoagulant activity decreases during sepsis and returns to normal levels as soon as the patient recovers. Hence, it can be potentially used to predict the risk of severe sepsis. PMID: 29120525
Plasma heparanase is not significantly associated with urinary microalbumin/creatinine, while it is correlated positively with blood glucose levels in the early stage of diabetic nephropathy PMID: 28994624
These results demonstrate that Smad4 suppresses the tumorigenesis and aggressiveness of neuroblastoma through repressing the HPSE expression. PMID: 27595937
the results of this study suggest that the use of HPSE as a predictive factor for clinical prognosis and as a treatment target would benefit breast cancer patients. PMID: 28388549
The results of this study shown the Upregulated Expression of Heparanase in the Brains of Alzheimer's Disease. PMID: 28387673
Heparanase has a role in upregulating platelet adhesion activity and thrombogenicity PMID: 27129145
Results show that all tested inhibitors reduced heparanase (HPA) enzyme activity and inhibited the growth of HeLa cells. PMID: 27166252
Data demonstrate that the mesenchymal features induced by HPSE in MM cells contribute to enhanced tumor cell motility and bone-dissemination. PMID: 26849235
c-Myc and heparanase expression was positively correlated with hTERT levels, and was also an independent predictor of metastasis and survival. PMID: 26689987
miR-558 facilitates the progression of gastric cancer through directly targeting the HPSE promoter to attenuate Smad4-mediated repression of HPSE expression. PMID: 27685626
High HPSE expression is associated with breast carcinoma. PMID: 28038446
data suggest that heparanase plays a critical role in NK cell invasion into tumors and thereby tumor progression and metastases. PMID: 28581441
The heparanase/syndecan1 axis in gallbladder carcinoma cells plays an important role in the invasion and metastasis, thus providing a new therapeutic target. PMID: 28351285
Results show that HPSE is upregulated in human glioma and seems to confer a growth advantage on glioma cells. PMID: 27565180
under physiological pH and low levels of tissue factor, heparanase may exert a non-enzymatic function interacting and activating the inhibitory function of antithrombin. PMID: 27322195
Heparanase has emerged as a major regulator of cancer by degrading heparan sulfate thereby influencing multiple signaling pathways that control gene expression, syndecan shedding and cell behavior. (Review) PMID: 27758044
The most common HPA genotypes among Saudis were HPA-1 a + b- (75%), HPA-2 a + b- (62%), HPA-3 a + b- (51.5%), HPA-4 a + b- (99%), HPA-5 a + b- (76.5%), HPA-6 a + b- (100%) and HPA-15 a + b + (50%). The prevalent allele among the HPA systems was (a), except in the HPA-15 system where the (b) allele was found in 52% of the subjects. PMID: 27019315
heparanase activity is increased without changes in superoxide dismutase activity in the granulocytes from patients with lupus nephritis and membranous nephropathy PMID: 27091112
Heparanase up-regulated the expression of the blood coagulation initiator-tissue factor (TF) and interacted with the tissue factor pathway inhibitor (TFPI) on the cell surface membrane of endothelial and tumor cells, leading to dissociation of TFPI and resulting in increased cell surface coagulation activity. [review] PMID: 27067977
Suggest heparanase is a promising, novel target for overcoming myeloma resistance to therapy and that targeting heparanase has the potential to prevent relapse in myeloma and possibly other cancers. PMID: 26624982
expression of BRMS1 and/or HPA might be closely related to the carcinogenesis, clinical biological behaviors, and prognosis of gallbladder adenocarcinoma PMID: 26200836
in colorectal adenomas, the heparanase-1 does not participate in syndecan-1 degradation; the heparanase-2 does not stimulate syndecan-1 degradation by the action of heparanase-1, and the heparanase-2 may be involved in the modulation of the heparanase-1 activity. PMID: 26972718
higher heparanase expression in gastric cancer is associated with clinicopathologic features of depth of invasion, lymph node metastasis. PMID: 26745132
JAK-2 V617F mutation results in heparanase up-regulation via the erythropoietin receptor. PMID: 26489695
Studies indicate that heparanase (HPSE) has been a potential target of medical treatment. PMID: 26552066
our results suggest that HPSE contributes to the proliferation and metastasis of Ovarian cancer and HPSE might be a potent molecular target for Ovarian cancer treatment PMID: 25586097
Heparanase is over expressed in preeclamptic placentas compared to normal healthy controls, suggesting its role in the development of preeclampsia. PMID: 25189635
Taken together, it is concluded that colon 26 cells transduce the heparanase-mediated signal through heparan sulfate binding. PMID: 26713365
Report FGF23/klotho/heparanase signaling axis active in multiple myeloma. PMID: 25944690
Elevated heparanase procoagulant activity in patients with lung cancer reveals a new mechanism of coagulation system activation in malignancy. Heparanase procoagulant activity can potentially be used as a predictor for survival. PMID: 25065557
heparanase contributes to allergen-induced eosinophil recruitment to the lung. PMID: 26039697
Our findings suggest a link between heparanase, syndecan-1, and VEGF in the progression of PDR and that heparanase is a potential target for therapy of diabetic retinopathy. PMID: 26720478
The authors present crystal structures of human HPSE at 1.6-A to 1.9-A resolution that reveal how an endo-acting binding cleft is exposed by proteolytic activation of latent proHPSE. PMID: 26575439
upregulated through NF-kB and translocated to the cell surface upon herpes simplex virus-1 infection for the removal of heparan sulfate to facilitate viral release PMID: 25912399
Findings identify a dual function for HPSE in malignant melanoma with a protumorigenic extracellular activity and a tumor-suppressive nuclear action. PMID: 25745999
Heparanase resides within autophagosomes. Heparanase-overexpressing cells were more resistant to stress and chemotherapy in a manner associated with increased autophagy. PMID: 26249176
miRNA-558 promotes tumorigenesis and aggressiveness of neuroblastoma cells through activating the transcription of heparanase PMID: 25616966
Since blockade of heparanase by LMWH has functional consequences for reduced VLA-4 binding, latent heparanase appears as a novel, so far unnoticed target of heparin, underlying its antimetastatic activity. PMID: 25682080
The close correlation between heparanase and COX-2 expression in lymphangiogenesis of cervical cancer. PMID: 25370734
Polymorphisms in the heparanase gene in multiple myeloma association with bone morbidity and survival PMID: 24954766
Heparanase 1 is more intensely expressed in the glandular tissue of high-grade compared with type I endometrial carcinomas. PMID: 25423319
HPSE deficiency in in vitro-engineered and cultured tumor-specific LTE-T cells may limit their antitumor activity in stroma-rich solid tumors PMID: 25849134
Heparanase procoagulant activity was significantly higher in shift work nurses compared to daytime work nurses. PMID: 25743687
Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's lay