Inhibitors | Comment | Organism | Structure |
---|---|---|---|
heparin | - |
Mammalia |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | heparanase is the only known mammalian endoglycosidase capable of degrading heparan sulfate glycosaminoglycan, both in extracellular space and within the cells | Mammalia | - |
- |
intracellular | heparanase is the only known mammalian endoglycosidase capable of degrading heparan sulfate glycosaminoglycan, both in extracellular space and within the cells | Mammalia | 5622 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
8000 | - |
1 * 50000 + 1 * 8000, SDS-PAGE | Mammalia |
50000 | - |
1 * 50000 + 1 * 8000, SDS-PAGE | Mammalia |
65000 | - |
1 * 65000, precursor polypeptide, SDS-PAGE | Mammalia |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mammalia | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the 65 kDa precursor polypeptide that is enzymatically inactive. Proteolytic activation by cleavage into two fragments | Mammalia |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
carcinoma cell | enhanced growth/aggressiveness of numerous cancer cell types following overexpression of heparanase and inhibition of the tumorigenic/metastatic abilities of cancer cells following heparanase gene silencing | Mammalia | - |
colon | - |
Mammalia | - |
colonic mucosa | - |
Mammalia | - |
lung | - |
Mammalia | - |
lung epithelial cell | - |
Mammalia | - |
neutrophil | - |
Mammalia | - |
T-lymphocyte | activated | Mammalia | - |
Subunits | Comment | Organism |
---|---|---|
heterodimer | 1 * 50000 + 1 * 8000, SDS-PAGE | Mammalia |
monomer | 1 * 65000, precursor polypeptide, SDS-PAGE | Mammalia |
Synonyms | Comment | Organism |
---|---|---|
heparanase-1 | - |
Mammalia |
Organism | Comment | Expression |
---|---|---|
Mammalia | sepsis-associated inflammatory lung disease causes rapid induction of heparanase activity through a TNFlpha-dependent mechanism in pulmonary microvascular endothelial cells. Heparanase induction is also found in biopsies of human inflammatory lung disease | up |
General Information | Comment | Organism |
---|---|---|
malfunction | enhanced growth/aggressiveness of numerous cancer cell types following overexpression of heparanase and inhibition of the tumorigenic/metastatic abilities of cancer cells following heparanase gene silencing | Mammalia |
physiological function | the enzyme degrades side chains of heparan sulfate. Versatile role of heparanase in inflammation, detailed overview. In light of the potential tissue damage as a consequence of inappropriate cleavage of heparan sulfate, under physiological conditions heparanase is tightly regulated. Along with posttranslational proteolytic processing regulation of heparanase gene transcription represents an important control mechanism. Role for heparanase located within the cell nuclei in regulating expression of genes involved in shaping of inflammatory phenotype in endothelial and T cells. Key role of heparan sulfate in glycocalyx structure during acute inflammatory lung injury heparanase-mediated degradation and loss of pulmonary endothelial glycocalyx facilitating neutrophil recruitment. The enzyme is involved in colon inflammatory bowel disease through exposure of the endothelial surface and increased availability of adhesion molecules | Mammalia |