Back to your search result

Description

Heparanase (UniProt: Q9Y251, also known as EC: 3.2.1.166, Endo-glucuronidase, Heparanase-1, Hpa1) is encoded by the HPSE (also known as HEP, HPA, HPA1, HPR1, HPSE1, HSE1) gene (Gene ID: 10855) in human. Heparanase is a heterodimeric, glycosylated, endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans and participates in extracellular matrix (ECM) degradation and remodeling. It is known to selectively cleave 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. It is also shown to 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. Heparanase is 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. Heparanase is synthesized with a signal peptide (aa 1-35) and a propeptide chain (110-157), which are cleaved off to produce the heterodimeric mature form of 8 kDa and 50 kDa subunits. This active 8/50 kDa heterodimer is resistant to degradation. Heparanase is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Heparanase activity is inhibited by EDTA and laminarian sulfate. Four isoforms of heparanase have been described that are produced by alternative splicing.