Thrombin is a selective inducer of heparanase release from platelets and granulocytes via protease-activated receptor-1.

Heparanase, known to be involved in angiogenesis and metastasis, was shown to form a complex with tissue factor (TF) and to enhance the generation of factor Xa. Platelets and granulocytes contain abundant amounts of heparanase that may enhance the coagulation system upon discharge. It was the aim of this study to identify the inducer and pathway of heparanase release from these cells.

Peptides inhibiting heparanase procoagulant activity significantly reduce tumour growth and vascularisation in a mouse model.

Heparanase is implicated in angiogenesis and tumour progression. We previously demonstrated that heparanase might also affect the haemostatic system in a non-enzymatic manner. It forms a complex and enhances the activity of the blood coagulation initiator tissue factor (TF).

Heparanase procoagulant activity as a predictor of wound necrosis following diabetic foot amputation.

Background: Trans-metatarsal operation to diabetic foot necrosis is a common procedure although only half of the patients do not need a second amputation due to surgery wound ischemia. No current tools are available for early prediction of surgery success and the clinical decision for a second operation may take weeks. Heparanase protein is involved in inflammation, angiogenesis and coagulation activation.

JAK-2 V617F mutation increases heparanase procoagulant activity.

Patients with polycythaemia vera (PV), essential thrombocythaemia (ET) and primary myelofibrosis (PMF) are at increased risk of arterial and venous thrombosis. In patients with ET a positive correlation was observed between JAK-2 V617F mutation, that facilitates erythropoietin receptor signalling, and thrombotic events, although the mechanism involved is not clear. We previously demonstrated that heparanase protein forms a complex and enhances the activity of the blood coagulation initiator tissue factor (TF) which leads to increased factor Xa production and subsequent activation of the coagulation system.

Nephroprotective effect of heparanase in experimental nephrotic syndrome.

Background: Heparanase, an endoglycosidase that cleaves heparan sulfate (HS), is involved in various biologic processes. Recently, an association between heparanase and glomerular injury was suggested. The present study examines the involvement of heparanase in the pathogenesis of Adriamycin-induced nephrotic syndrome (ADR-NS) in a mouse model.

Heparanase procoagulant activity is elevated and predicts survival in non-small cell lung cancer patients.

Background: Heparanase is implicated in angiogenesis and tumor progression. We had earlier demonstrated that heparanase may also affect the hemostatic system in a non-enzymatic manner. It forms a complex and enhances the activity of the blood coagulation initiator- tissue factor (TF).

Novel peptides that inhibit heparanase activation of the coagulation system.

Heparanase is implicated in cell invasion, tumour metastasis and angiogenesis. It forms a complex and enhances the activity of the blood coagulation initiator - tissue factor (TF). We describe new peptides derived from the solvent accessible surface of TF pathway inhibitor 2 (TFPI-2) that inhibit the heparanase procoagulant activity.

New England salt marsh recovery: opportunistic colonization of an invasive species and its non-consumptive effects.

Predator depletion on Cape Cod (USA) has released the herbivorous crab Sesarmareticulatum from predator control leading to the loss of cordgrass from salt marsh creek banks. After more than three decades of die-off, cordgrass is recovering at heavily damaged sites coincident with the invasion of green crabs (Carcinusmaenas) into intertidal Sesarma burrows. We hypothesized that Carcinus is dependent on Sesarma burrows for refuge from physical and biotic stress in the salt marsh intertidal and reduces Sesarma functional density and herbivory through consumptive and non-consumptive effects, mediated by both visual and olfactory cues.

Feedbacks underlie the resilience of salt marshes and rapid reversal of consumer-driven die-off.

Understanding ecosystem resilience to human impacts is critical for conservation and restoration. The large-scale die-off of New England salt marshes was triggered by overfishing and resulted from decades of runaway crab grazing. In 2009, however, cordgrass began to recover, decreasing die-off -40% by 2010.

Heparanase procoagulant activity is elevated in women using oral contraceptives.

Study Question: What is the effect of estrogen on heparanase procogulant activity?

Summary Answer: Estrogen increases heparanase procoagulant activity.

What Is Known Already: Estrogen therapy increases the risk of thrombosis and was previously found to up-regulate heparanase expression. Heparanase is involved in angiogenesis and metastasis, and has been shown to form a complex with tissue factor (TF) and also shown to enhance the generation of factor Xa.

Heparanase role in the treatment of avascular necrosis of femur head.

Background: Idiopathic avascular necrosis (AVN) of bone causes significant morbidity in adults although the pathophysiology is unknown. The present treatment options include systemic biphosphonate therapy and local bone drilling decompression, ameliorating the healing process and their by render the weight bearing femur head less vulnerable to collapse. In the present study we demonstrate the involvement of heparanase in AVN and in the acceptable treatments.

Increased heparanase level and procoagulant activity in orthopedic surgery patients receiving prophylactic dose of enoxaparin.

Background: Orthopedic hip and knee surgeries are followed by a hypercoagulable state. Heparanase is implicated in inflammation, coagulation activation and angiogenesis. Recently, heparanase was shown to directly interact with tissue factor (TF) and to enhance the generation of factor Xa (Nadir et al.