Heparanase (HPSE) cleaves heparan sulfate from its proteoglycan (lysosome)

Stable Identifier
Reaction [transition]
Homo sapiens
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Heparanase (HPSE) is an endoglycosidase that cleaves heparan sulfate (HS) from its HS proteoglycan (HSPG) (Toyoshima & Nakajima 1999; Okada et al. 2002). The formation of a heterodimer of 8kDa and 50kDa subunits cleaved from the 65kDa form is required for enzyme activity (Levy-Adam et al. 2003) and this proteolytic cleavage occurs in the lysosome (Goldshmidt et al. 2002). Acidic conditions within the lysosome optimises HPSE activity.

Literature References
PubMed ID Title Journal Year
12213822 Structural recognition by recombinant human heparanase that plays critical roles in tumor metastasis. Hierarchical sulfate groups with different effects and the essential target disulfated trisaccharide sequence

Okada, Y, Sugahara, K, Yamada, S, Toyoshima, M, Dong, J, Nakajima, M

J Biol Chem 2002
12927802 Heterodimer formation is essential for heparanase enzymatic activity

Ilan, N, Heinrikson, RL, Vlodavsky, I, Levy-Adam, F, Miao, HQ

Biochem Biophys Res Commun 2003
12441129 Human heparanase is localized within lysosomes in a stable form

Geiger, B, Ilan, N, Irit, C, Vlodavsky, I, Feinstein, N, Katz, BZ, Aingorn, H, Goldshmidt, O, Zamir, E, Nadav, L

Exp Cell Res 2002
10446189 Human heparanase. Purification, characterization, cloning, and expression

Nakajima, M, Toyoshima, M

J Biol Chem 1999
Catalyst Activity

heparanase activity of HPSE dimer [lysosomal lumen]

Orthologous Events
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