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Literature summary for 3.2.1.166 extracted from

  • Goldberg, R.; Meirovitz, A.; Hirshoren, N.; Bulvik, R.; Binder, A.; Rubinstein, A.M.; Elkin, M.
    Versatile role of heparanase in inflammation (2013), Matrix Biol., 32, 234-240.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
heparin
-
Mammalia

Localization

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 [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

Organism UniProt Comment Textmining
Mammalia
-
-
-

Posttranslational Modification

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

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

Subunits Comment Organism
heterodimer 1 * 50000 + 1 * 8000, SDS-PAGE Mammalia
monomer 1 * 65000, precursor polypeptide, SDS-PAGE Mammalia

Synonyms

Synonyms Comment Organism
heparanase-1
-
Mammalia

Expression

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

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