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Heparanase inhibition is a potent anti-lymphoma strategy.
HPSE activity increased in the plasma of patients with liver fibrosis but it inversely correlated with liver stiffness.
H. pylori may promote the invasion and metastasis of gastric cancer (GC) by increasing HPA expression that may associate with MAPK activation, thus causing a poorer prognosis of GC.
IL17A and HPSE may promote tumor angiogenesis and cell proliferation and invasion in cervical cancer, possibly via the NF-kappaB signaling pathway.
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.
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.
Knockdown of heparanase suppressed proliferation, invasion, and tube formation but induced apoptosis in trophoblasts.
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.
this is the first study to demonstrate that heparanase is involved in the pathogenesis of AP.
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.
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
These results demonstrate that Smad4 suppresses the tumorigenesis and aggressiveness of neuroblastoma through repressing the HPSE expression.
Over-expression of circHIPK3 effectively inhibits migration, invasion, and angiogenesis of bladder cancer cells in vitro and suppresses bladder cancer growth and metastasis in vivo 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).
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.
The results of this study shown the Upregulated Expression of Heparanase in the Brains of Alzheimer's Disease.
Heparanase has a role in upregulating platelet adhesion activity and thrombogenicity
Results show that all tested inhibitors reduced heparanase (HPA) enzyme activity and inhibited the growth of HeLa cells.
Data demonstrate that the mesenchymal features induced by HPSE in MM cells contribute to enhanced tumor cell motility and bone-dissemination.
c-Myc and heparanase expression was positively correlated with hTERT levels, and was also an independent predictor of metastasis and survival.
miR-558 facilitates the progression of gastric cancer through directly targeting the HPSE promoter to attenuate Smad4-mediated repression of HPSE expression.
HPSE expression increased in mouse livers after carbon tetrachloride (CCl4)-mediated chronic induction of fibrosis, but with a trend to decline during progression of the disease.
AGEs and RAGE interaction increases podocyte heparanase expression by activating NF-kappaB signal pathway.
rHpse was taken up into mast cells and the uptake was not a mere internalization but a process by which proheparanase was properly processed and sorted into secretory granules. Hpse was incorporated at least partly into secretory granules, which was supported by release of Hpse as a result of degranulation.
elevated expression of heparanase augmented both the innate and adaptive immune system and propagated inflammatory reactions in the murine rheumatoid arthritis model.
These results show for the first time that HPSE regulates macrophage polarization as well as renal damage and repair after I/R. HPSE inhibitors could therefore provide a new pharmacologic approach to minimize acute kidney injury and to prevent the chronic profibrotic damages induced by I/R.
Study reveals that HPSE stimulates the proliferation of ES cells as well as the expansion of emerging progenitors during neural differentiation.
heparanase as a key mediator of macrophage activation and function in tumorigenesis and cross-talk with the tumor microenvironment.
Results demonstrate that acute ischemic injury up-regulates renal heparanase expression and suggest that heparanase plays a deleterious role in the development of renal injury and kidney dysfunction.
eNOS prevents heparanase induction and the development of proteinuria
Data show that heparanase-1 (HPA-1) induced shedding of heparan sulfate chain from syndecan-1 (SDC-1) facilitated the release of vascular endothelial growth factor C (VEGF-C) from SDC-1/VEGF-C complex into the medium of hepatocarcinoma cell.
the activation of intestinal heparanase contributes to intestinal injury during early sepsis by facilitating the destruction of mucosal epithelial glycocalyx and promoting inflammatory responses.
Heparanase increases the inflammation in AGEs-stimulated macrophages through activating the RAGE-NF-kappaB pathway. Heparanase driven inflammation from AGEs-stimulated macrophages increases the adherence of glomerular endothelial cells (GEnCs) and augments the permeability of GEnCs.
heparanase contributes to allergen-induced eosinophil recruitment to the lung.
Unfractionated heparin inhibits heparanase, and reverses the activation of NF-kappaB and MAPK P38 signaling pathways to attenuate inflammatory responses induced by sepsis. These results suggest that UFH
Results show a critical role for heparanase in regulating the branching and invasive behavior of normal mammary epithelia which could be the result of its mutually reciprocal feedback with MMP-14.
Data suggest a potential mechanism of diabetic enteropathy, which is depending remarkably on syndecan-1 (Sdc1) and -beta-D-glucuronidase heparanase (HPSE).
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
Findings identify a dual function for HPSE in malignant melanoma with a protumorigenic extracellular activity and a tumor-suppressive nuclear action.
Studies in heparanase-deficient mice established its contributions to autophagy.
These data suggest that porcine reproductive and respiratory syndrome virus activates NF-kappaB and cathepsin L to upregulate and process heparanase, and then the active heparanase cleaves heparan sulfate, resulting in viral release.
during late gestation, the mRNA and HPSE levels were higher in Meishan placentae than Yorkshire pigs
study of tissue expression profiles, polymorphisms of HPSE and HPSE2 genes and changes of their mRNA levels in porcine alveolar macrophages (PAMs) induced by PRRSV; upon stimulation in healthy piglets with PRRSV, HPSE mRNA was obviously upregulated, while HPSE2 mRNA did not induce a prominent change in PAMs
our results support a critical role for heparanase in the development of vulnerable atherosclerotic plaques
report molecular cloning and characterisation of heparanase mRNA in the porcine placenta throughout gestation.
changing placental expression indicates possible involvement in fetomaternal communication and placental maturation
Suggest that high glucose is a potent stimulator of endothelial heparanase secretion.
Lutropin induces a transient increase in HPSE mRNA at specific times after its addition.
Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. The protein encoded by this gene is an enzyme that cleaves heparan sulfate proteoglycans to permit cell movement through remodeling of the extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene.
, endoglycosidase heparanase